HEADER    MEMBRANE PROTEIN                        23-MAY-24   8ZMG              
TITLE     CRYSTAL STRUCTURE OF AN INVERSE AGONIST ANTIPSYCHOTIC DRUG            
TITLE    2 PIMAVANSERIN-BOUND 5-HT2A                                            
KEYWDS    CLASS A G PROTEIN-COUPLED RECEPTOR, INVERSE AGONIST, MEMBRANE         
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 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 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            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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  8ZMG A   70   265  UNP    P28223   5HT2A_HUMAN     70    265             
DBREF  8ZMG A 1001  1040  UNP    P0ABE7   C562_ECOLX      23     62             
DBREF  8ZMG A 1046  1086  UNP    P0ABE7   C562_ECOLX      88    128             
DBREF  8ZMG A  313   403  UNP    P28223   5HT2A_HUMAN    313    403             
DBREF  8ZMG B   70   265  UNP    P28223   5HT2A_HUMAN     70    265             
DBREF  8ZMG B 1001  1040  UNP    P0ABE7   C562_ECOLX      23     62             
DBREF  8ZMG B 1046  1086  UNP    P0ABE7   C562_ECOLX      88    128             
DBREF  8ZMG B  313   403  UNP    P28223   5HT2A_HUMAN    313    403             
SEQRES   1 A  414  MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU          
SEQRES   2 A  414  VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP LYS GLU ASN          
SEQRES   3 A  414  LEU TYR PHE GLN GLY THR SER HIS LEU GLN GLU LYS ASN          
SEQRES   4 A  414  TRP SER ALA LEU LEU THR ALA VAL VAL ILE ILE LEU THR          
SEQRES   5 A  414  ILE ALA GLY ASN ILE LEU VAL ILE MET ALA VAL SER LEU          
SEQRES   6 A  414  GLU LYS LYS LEU GLN ASN ALA THR ASN TYR PHE LEU MET          
SEQRES   7 A  414  SER LEU ALA ILE ALA ASP MET LEU LEU GLY PHE LEU VAL          
SEQRES   8 A  414  MET PRO VAL SER MET LEU THR ILE LEU TYR GLY TYR ARG          
SEQRES   9 A  414  TRP PRO LEU PRO SER LYS LEU CYS ALA VAL TRP ILE TYR          
SEQRES  10 A  414  LEU ASP VAL LEU PHE SER THR ALA LYS ILE TRP HIS LEU          
SEQRES  11 A  414  CYS ALA ILE SER LEU ASP ARG TYR VAL ALA ILE GLN ASN          
SEQRES  12 A  414  PRO ILE HIS HIS SER ARG PHE ASN SER ARG THR LYS ALA          
SEQRES  13 A  414  PHE LEU LYS ILE ILE ALA VAL TRP THR ILE SER VAL GLY          
SEQRES  14 A  414  ILE SER MET PRO ILE PRO VAL PHE GLY LEU GLN ASP ASP          
SEQRES  15 A  414  SER LYS VAL PHE LYS GLU GLY SER CYS LEU LEU ALA ASP          
SEQRES  16 A  414  ASP ASN PHE VAL LEU ILE GLY SER PHE VAL SER PHE PHE          
SEQRES  17 A  414  ILE PRO LEU THR ILE MET VAL ILE THR TYR PHE LEU THR          
SEQRES  18 A  414  ILE LYS SER LEU GLN LYS GLU ALA ALA ASP LEU GLU ASP          
SEQRES  19 A  414  ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE GLU          
SEQRES  20 A  414  LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU THR          
SEQRES  21 A  414  LYS MET ARG ALA ALA ALA LEU ASP ALA GLY SER GLY SER          
SEQRES  22 A  414  GLY ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS          
SEQRES  23 A  414  LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA          
SEQRES  24 A  414  ALA GLU GLN LEU LYS THR THR ILE ASN ALA TYR ILE GLN          
SEQRES  25 A  414  LYS TYR GLY GLN SER ILE SER ASN GLU GLN LYS ALA CYS          
SEQRES  26 A  414  LYS VAL LEU GLY ILE VAL PHE PHE LEU PHE VAL VAL MET          
SEQRES  27 A  414  TRP CYS PRO PHE PHE ILE THR ASN ILE MET ALA VAL ILE          
SEQRES  28 A  414  CYS LYS GLU SER CYS ASN GLU ASP VAL ILE GLY ALA LEU          
SEQRES  29 A  414  LEU ASN VAL PHE VAL TRP ILE GLY TYR LEU SER SER ALA          
SEQRES  30 A  414  VAL ASN PRO LEU VAL TYR THR LEU PHE ASN LYS THR TYR          
SEQRES  31 A  414  ARG SER ALA PHE SER ARG TYR ILE GLN CYS GLN TYR LYS          
SEQRES  32 A  414  GLU ASN LYS LEU GLU GLU ASN LEU TYR PHE GLN                  
SEQRES   1 B  414  MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU          
SEQRES   2 B  414  VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP LYS GLU ASN          
SEQRES   3 B  414  LEU TYR PHE GLN GLY THR SER HIS LEU GLN GLU LYS ASN          
SEQRES   4 B  414  TRP SER ALA LEU LEU THR ALA VAL VAL ILE ILE LEU THR          
SEQRES   5 B  414  ILE ALA GLY ASN ILE LEU VAL ILE MET ALA VAL SER LEU          
SEQRES   6 B  414  GLU LYS LYS LEU GLN ASN ALA THR ASN TYR PHE LEU MET          
SEQRES   7 B  414  SER LEU ALA ILE ALA ASP MET LEU LEU GLY PHE LEU VAL          
SEQRES   8 B  414  MET PRO VAL SER MET LEU THR ILE LEU TYR GLY TYR ARG          
SEQRES   9 B  414  TRP PRO LEU PRO SER LYS LEU CYS ALA VAL TRP ILE TYR          
SEQRES  10 B  414  LEU ASP VAL LEU PHE SER THR ALA LYS ILE TRP HIS LEU          
SEQRES  11 B  414  CYS ALA ILE SER LEU ASP ARG TYR VAL ALA ILE GLN ASN          
SEQRES  12 B  414  PRO ILE HIS HIS SER ARG PHE ASN SER ARG THR LYS ALA          
SEQRES  13 B  414  PHE LEU LYS ILE ILE ALA VAL TRP THR ILE SER VAL GLY          
SEQRES  14 B  414  ILE SER MET PRO ILE PRO VAL PHE GLY LEU GLN ASP ASP          
SEQRES  15 B  414  SER LYS VAL PHE LYS GLU GLY SER CYS LEU LEU ALA ASP          
SEQRES  16 B  414  ASP ASN PHE VAL LEU ILE GLY SER PHE VAL SER PHE PHE          
SEQRES  17 B  414  ILE PRO LEU THR ILE MET VAL ILE THR TYR PHE LEU THR          
SEQRES  18 B  414  ILE LYS SER LEU GLN LYS GLU ALA ALA ASP LEU GLU ASP          
SEQRES  19 B  414  ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE GLU          
SEQRES  20 B  414  LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU THR          
SEQRES  21 B  414  LYS MET ARG ALA ALA ALA LEU ASP ALA GLY SER GLY SER          
SEQRES  22 B  414  GLY ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS          
SEQRES  23 B  414  LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA          
SEQRES  24 B  414  ALA GLU GLN LEU LYS THR THR ILE ASN ALA TYR ILE GLN          
SEQRES  25 B  414  LYS TYR GLY GLN SER ILE SER ASN GLU GLN LYS ALA CYS          
SEQRES  26 B  414  LYS VAL LEU GLY ILE VAL PHE PHE LEU PHE VAL VAL MET          
SEQRES  27 B  414  TRP CYS PRO PHE PHE ILE THR ASN ILE MET ALA VAL ILE          
SEQRES  28 B  414  CYS LYS GLU SER CYS ASN GLU ASP VAL ILE GLY ALA LEU          
SEQRES  29 B  414  LEU ASN VAL PHE VAL TRP ILE GLY TYR LEU SER SER ALA          
SEQRES  30 B  414  VAL ASN PRO LEU VAL TYR THR LEU PHE ASN LYS THR TYR          
SEQRES  31 B  414  ARG SER ALA PHE SER ARG TYR ILE GLN CYS GLN TYR LYS          
SEQRES  32 B  414  GLU ASN LYS LEU GLU GLU ASN LEU TYR PHE GLN                  
HELIX    1   1 SER A   77  GLU A  102  1                                  26    
HELIX    2   2 LYS A  103  GLN A  106  5                                   4    
HELIX    3   3 ASN A  107  TYR A  137  1                                  31    
HELIX    4   4 PRO A  144  LYS A  146  5                                   3    
HELIX    5   5 LEU A  147  ALA A  176  1                                  30    
HELIX    6   6 SER A  188  MET A  208  1                                  21    
HELIX    7   7 MET A  208  ASP A  217  1                                  10    
HELIX    8   8 ASP A  231  PHE A  243  1                                  13    
HELIX    9   9 PHE A  243  LYS A 1019  1                                  42    
HELIX   10  10 ALA A 1023  ASP A 1039  1                                  17    
HELIX   11  11 SER A 1044  GLY A 1062  1                                  19    
HELIX   12  12 LYS A 1063  CYS A  349  1                                  61    
HELIX   13  13 VAL A  357  ASN A  384  1                                  28    
HELIX   14  14 ASN A  384  TYR A  394  1                                  11    
HELIX   15  15 ASN B   75  GLU B  102  1                                  28    
HELIX   16  16 ASN B  107  TYR B  137  1                                  31    
HELIX   17  17 PRO B  144  ASN B  179  1                                  36    
HELIX   18  18 SER B  188  MET B  208  1                                  21    
HELIX   19  19 MET B  208  ASP B  217  1                                  10    
HELIX   20  20 ASP B  217  PHE B  222  1                                   6    
HELIX   21  21 ASP B  231  PHE B  243  1                                  13    
HELIX   22  22 PHE B  243  LYS B 1019  1                                  42    
HELIX   23  23 ALA B 1023  LEU B 1038  1                                  16    
HELIX   24  24 ILE B 1047  GLY B 1062  1                                  16    
HELIX   25  25 LYS B 1063  CYS B  349  1                                  61    
HELIX   26  26 VAL B  357  ASN B  384  1                                  28    
HELIX   27  27 ASN B  384  TYR B  394  1                                  11    
SHEET    1 AA1 2 PHE A 222  LYS A 223  0                                        
SHEET    2 AA1 2 SER A 226  CYS A 227 -1  O  SER A 226   N  LYS A 223           
SSBOND   1 CYS A  148    CYS A  227                          1555   1555  2.03  
SSBOND   2 CYS A  349    CYS A  353                          1555   1555  2.03  
SSBOND   3 CYS B  148    CYS B  227                          1555   1555  2.03  
SSBOND   4 CYS B  349    CYS B  353                          1555   1555  2.03  
CRYST1  276.260   42.040   90.410  90.00  93.15  90.00 C 1 2 1       8          
ATOM      1  N   LYS A  74      -7.431   4.129  13.831  1.00161.33           N  
ANISOU    1  N   LYS A  74    10714  26012  24572  -2941    703   3531       N  
ATOM      2  CA  LYS A  74      -7.281   4.828  12.561  1.00156.15           C  
ANISOU    2  CA  LYS A  74    10091  25666  23574  -3089    920   3193       C  
ATOM      3  C   LYS A  74      -8.598   5.505  12.179  1.00147.62           C  
ANISOU    3  C   LYS A  74     9446  24600  22045  -3274    934   3180       C  
ATOM      4  O   LYS A  74      -9.411   5.824  13.046  1.00135.26           O  
ANISOU    4  O   LYS A  74     8202  22859  20333  -3302    754   3466       O  
ATOM      5  CB  LYS A  74      -6.825   3.858  11.467  1.00153.78           C  
ANISOU    5  CB  LYS A  74     9331  25465  23632  -3010   1213   2759       C  
ATOM      6  CG  LYS A  74      -5.967   4.483  10.372  1.00151.51           C  
ANISOU    6  CG  LYS A  74     8924  25514  23129  -3129   1414   2449       C  
ATOM      7  CD  LYS A  74      -4.698   5.096  10.940  1.00138.77           C  
ANISOU    7  CD  LYS A  74     7217  24010  21500  -3083   1274   2627       C  
ATOM      8  CE  LYS A  74      -3.814   4.042  11.583  1.00142.53           C  
ANISOU    8  CE  LYS A  74     7224  24342  22590  -2808   1223   2680       C  
ATOM      9  NZ  LYS A  74      -2.578   4.640  12.159  1.00143.79           N  
ANISOU    9  NZ  LYS A  74     7287  24624  22722  -2777   1067   2870       N  
ATOM     10  N   ASN A  75      -8.807   5.721  10.881  1.00140.73           N  
ANISOU   10  N   ASN A  75     8574  23935  20961  -3405   1146   2852       N  
ATOM     11  CA  ASN A  75      -9.980   6.435  10.396  1.00154.13           C  
ANISOU   11  CA  ASN A  75    10659  25673  22232  -3576   1138   2850       C  
ATOM     12  C   ASN A  75     -11.203   5.545  10.211  1.00168.37           C  
ANISOU   12  C   ASN A  75    12478  27318  24179  -3575   1211   2747       C  
ATOM     13  O   ASN A  75     -12.304   6.072  10.013  1.00146.31           O  
ANISOU   13  O   ASN A  75    10003  24513  21073  -3689   1161   2799       O  
ATOM     14  CB  ASN A  75      -9.660   7.138   9.073  1.00137.39           C  
ANISOU   14  CB  ASN A  75     8568  23858  19776  -3755   1290   2602       C  
ATOM     15  CG  ASN A  75      -8.667   8.270   9.242  1.00135.38           C  
ANISOU   15  CG  ASN A  75     8405  23773  19259  -3812   1190   2747       C  
ATOM     16  OD1 ASN A  75      -8.614   8.912  10.291  1.00141.76           O  
ANISOU   16  OD1 ASN A  75     9420  24481  19962  -3779    979   3074       O  
ATOM     17  ND2 ASN A  75      -7.875   8.523   8.207  1.00134.32           N  
ANISOU   17  ND2 ASN A  75     8126  23907  19004  -3924   1350   2503       N  
ATOM     18  N   TRP A  76     -11.051   4.220  10.272  1.00186.75           N  
ANISOU   18  N   TRP A  76    14454  29519  26982  -3447   1321   2613       N  
ATOM     19  CA  TRP A  76     -12.214   3.350  10.136  1.00163.81           C  
ANISOU   19  CA  TRP A  76    11567  26462  24212  -3469   1389   2530       C  
ATOM     20  C   TRP A  76     -13.110   3.368  11.368  1.00159.92           C  
ANISOU   20  C   TRP A  76    11350  25690  23721  -3427   1156   2886       C  
ATOM     21  O   TRP A  76     -14.214   2.816  11.315  1.00167.55           O  
ANISOU   21  O   TRP A  76    12402  26533  24726  -3477   1187   2850       O  
ATOM     22  CB  TRP A  76     -11.785   1.912   9.825  1.00181.76           C  
ANISOU   22  CB  TRP A  76    13368  28666  27027  -3349   1591   2289       C  
ATOM     23  CG  TRP A  76     -10.412   1.542  10.298  1.00197.12           C  
ANISOU   23  CG  TRP A  76    14945  30568  29385  -3138   1568   2343       C  
ATOM     24  CD1 TRP A  76      -9.255   1.602   9.576  1.00180.17           C  
ANISOU   24  CD1 TRP A  76    12486  28653  27318  -3114   1749   2073       C  
ATOM     25  CD2 TRP A  76     -10.052   1.034  11.589  1.00186.58           C  
ANISOU   25  CD2 TRP A  76    13509  28926  28458  -2925   1343   2694       C  
ATOM     26  NE1 TRP A  76      -8.198   1.169  10.338  1.00180.31           N  
ANISOU   26  NE1 TRP A  76    12194  28536  27780  -2873   1647   2228       N  
ATOM     27  CE2 TRP A  76      -8.660   0.817  11.579  1.00188.15           C  
ANISOU   27  CE2 TRP A  76    13321  29186  28981  -2754   1382   2629       C  
ATOM     28  CE3 TRP A  76     -10.772   0.747  12.753  1.00173.05           C  
ANISOU   28  CE3 TRP A  76    12001  26888  26864  -2879   1105   3061       C  
ATOM     29  CZ2 TRP A  76      -7.973   0.326  12.688  1.00190.26           C  
ANISOU   29  CZ2 TRP A  76    13408  29186  29696  -2524   1161   2944       C  
ATOM     30  CZ3 TRP A  76     -10.088   0.260  13.853  1.00158.20           C  
ANISOU   30  CZ3 TRP A  76     9954  24745  25408  -2685    893   3375       C  
ATOM     31  CH2 TRP A  76      -8.703   0.054  13.812  1.00179.43           C  
ANISOU   31  CH2 TRP A  76    12263  27488  28424  -2502    909   3327       C  
ATOM     32  N   SER A  77     -12.667   3.983  12.465  1.00168.87           N  
ANISOU   32  N   SER A  77    12627  26735  24801  -3365    937   3218       N  
ATOM     33  CA  SER A  77     -13.501   4.170  13.642  1.00168.17           C  
ANISOU   33  CA  SER A  77    12841  26414  24643  -3372    731   3546       C  
ATOM     34  C   SER A  77     -13.889   5.623  13.874  1.00162.13           C  
ANISOU   34  C   SER A  77    12479  25735  23387  -3484    618   3704       C  
ATOM     35  O   SER A  77     -14.796   5.883  14.672  1.00148.31           O  
ANISOU   35  O   SER A  77    11003  23822  21525  -3520    498   3905       O  
ATOM     36  CB  SER A  77     -12.790   3.629  14.892  1.00173.80           C  
ANISOU   36  CB  SER A  77    13411  26911  25714  -3241    551   3848       C  
ATOM     37  OG  SER A  77     -11.554   4.289  15.102  1.00173.36           O  
ANISOU   37  OG  SER A  77    13281  27001  25588  -3206    479   3944       O  
ATOM     38  N   ALA A  78     -13.227   6.573  13.207  1.00150.54           N  
ANISOU   38  N   ALA A  78    11043  24512  21644  -3544    658   3618       N  
ATOM     39  CA  ALA A  78     -13.595   7.977  13.352  1.00134.51           C  
ANISOU   39  CA  ALA A  78     9376  22552  19179  -3647    554   3775       C  
ATOM     40  C   ALA A  78     -14.980   8.248  12.780  1.00134.34           C  
ANISOU   40  C   ALA A  78     9574  22525  18945  -3731    590   3691       C  
ATOM     41  O   ALA A  78     -15.757   9.019  13.356  1.00134.59           O  
ANISOU   41  O   ALA A  78     9898  22467  18775  -3765    476   3879       O  
ATOM     42  CB  ALA A  78     -12.549   8.866  12.679  1.00151.70           C  
ANISOU   42  CB  ALA A  78    11520  24994  21126  -3712    588   3706       C  
ATOM     43  N   LEU A  79     -15.305   7.630  11.641  1.00143.13           N  
ANISOU   43  N   LEU A  79    10533  23742  20107  -3775    751   3405       N  
ATOM     44  CA  LEU A  79     -16.634   7.793  11.059  1.00138.99           C  
ANISOU   44  CA  LEU A  79    10185  23228  19396  -3865    770   3334       C  
ATOM     45  C   LEU A  79     -17.703   7.158  11.940  1.00142.49           C  
ANISOU   45  C   LEU A  79    10717  23413  20010  -3814    713   3443       C  
ATOM     46  O   LEU A  79     -18.816   7.684  12.051  1.00139.90           O  
ANISOU   46  O   LEU A  79    10620  23036  19499  -3858    646   3526       O  
ATOM     47  CB  LEU A  79     -16.662   7.197   9.648  1.00126.22           C  
ANISOU   47  CB  LEU A  79     8376  21801  17783  -3961    961   3000       C  
ATOM     48  CG  LEU A  79     -17.887   7.421   8.752  1.00130.02           C  
ANISOU   48  CG  LEU A  79     9009  22376  18018  -4099    977   2909       C  
ATOM     49  CD1 LEU A  79     -18.956   6.352   8.963  1.00132.32           C  
ANISOU   49  CD1 LEU A  79     9262  22496  18518  -4086   1023   2838       C  
ATOM     50  CD2 LEU A  79     -18.468   8.815   8.960  1.00123.85           C  
ANISOU   50  CD2 LEU A  79     8538  21616  16904  -4135    797   3155       C  
ATOM     51  N   LEU A  80     -17.385   6.023  12.567  1.00147.68           N  
ANISOU   51  N   LEU A  80    11175  23904  21033  -3728    734   3453       N  
ATOM     52  CA  LEU A  80     -18.361   5.341  13.411  1.00145.24           C  
ANISOU   52  CA  LEU A  80    10947  23348  20889  -3712    678   3565       C  
ATOM     53  C   LEU A  80     -18.745   6.195  14.614  1.00142.57           C  
ANISOU   53  C   LEU A  80    10906  22873  20390  -3710    508   3859       C  
ATOM     54  O   LEU A  80     -19.910   6.205  15.031  1.00139.43           O  
ANISOU   54  O   LEU A  80    10689  22352  19936  -3749    475   3914       O  
ATOM     55  CB  LEU A  80     -17.806   3.991  13.865  1.00144.77           C  
ANISOU   55  CB  LEU A  80    10599  23126  21281  -3628    704   3570       C  
ATOM     56  CG  LEU A  80     -17.280   3.075  12.758  1.00145.05           C  
ANISOU   56  CG  LEU A  80    10279  23281  21551  -3616    907   3259       C  
ATOM     57  CD1 LEU A  80     -16.762   1.766  13.335  1.00139.62           C  
ANISOU   57  CD1 LEU A  80     9286  22370  21393  -3498    907   3322       C  
ATOM     58  CD2 LEU A  80     -18.359   2.817  11.717  1.00138.65           C  
ANISOU   58  CD2 LEU A  80     9514  22573  20595  -3750   1051   3001       C  
ATOM     59  N   THR A  81     -17.781   6.915  15.185  1.00156.35           N  
ANISOU   59  N   THR A  81    12698  24651  22058  -3682    412   4036       N  
ATOM     60  CA  THR A  81     -18.032   7.762  16.343  1.00155.80           C  
ANISOU   60  CA  THR A  81    12903  24469  21826  -3710    271   4300       C  
ATOM     61  C   THR A  81     -18.524   9.155  15.975  1.00143.03           C  
ANISOU   61  C   THR A  81    11527  22968  19850  -3768    255   4312       C  
ATOM     62  O   THR A  81     -18.850   9.935  16.877  1.00151.16           O  
ANISOU   62  O   THR A  81    12784  23904  20744  -3800    168   4494       O  
ATOM     63  CB  THR A  81     -16.762   7.890  17.195  1.00144.78           C  
ANISOU   63  CB  THR A  81    11447  23056  20505  -3683    161   4509       C  
ATOM     64  OG1 THR A  81     -15.717   8.479  16.411  1.00141.84           O  
ANISOU   64  OG1 THR A  81    10968  22916  20011  -3675    201   4421       O  
ATOM     65  CG2 THR A  81     -16.307   6.520  17.686  1.00155.12           C  
ANISOU   65  CG2 THR A  81    12502  24213  22225  -3616    131   4567       C  
ATOM     66  N   ALA A  82     -18.584   9.487  14.686  1.00129.06           N  
ANISOU   66  N   ALA A  82     9706  21398  17935  -3797    335   4130       N  
ATOM     67  CA  ALA A  82     -19.021  10.809  14.256  1.00121.20           C  
ANISOU   67  CA  ALA A  82     8909  20513  16626  -3859    293   4179       C  
ATOM     68  C   ALA A  82     -20.519  10.886  14.003  1.00107.37           C  
ANISOU   68  C   ALA A  82     7266  18706  14823  -3882    301   4138       C  
ATOM     69  O   ALA A  82     -21.107  11.965  14.140  1.00103.15           O  
ANISOU   69  O   ALA A  82     6912  18168  14111  -3909    234   4257       O  
ATOM     70  CB  ALA A  82     -18.272  11.225  12.987  1.00116.39           C  
ANISOU   70  CB  ALA A  82     8201  20170  15853  -3917    344   4046       C  
ATOM     71  N   VAL A  83     -21.149   9.769  13.630  1.00112.93           N  
ANISOU   71  N   VAL A  83     7844  19370  15695  -3877    382   3974       N  
ATOM     72  CA  VAL A  83     -22.584   9.774  13.363  1.00122.98           C  
ANISOU   72  CA  VAL A  83     9194  20610  16923  -3908    386   3930       C  
ATOM     73  C   VAL A  83     -23.375   9.988  14.647  1.00119.34           C  
ANISOU   73  C   VAL A  83     8901  19930  16513  -3880    329   4087       C  
ATOM     74  O   VAL A  83     -24.492  10.521  14.615  1.00105.45           O  
ANISOU   74  O   VAL A  83     7241  18152  14672  -3896    308   4113       O  
ATOM     75  CB  VAL A  83     -22.996   8.469  12.655  1.00120.52           C  
ANISOU   75  CB  VAL A  83     8703  20321  16768  -3941    496   3704       C  
ATOM     76  CG1 VAL A  83     -24.431   8.555  12.157  1.00105.66           C  
ANISOU   76  CG1 VAL A  83     6883  18470  14795  -3998    491   3650       C  
ATOM     77  CG2 VAL A  83     -22.045   8.164  11.509  1.00129.82           C  
ANISOU   77  CG2 VAL A  83     9691  21708  17926  -3985    589   3517       C  
ATOM     78  N   VAL A  84     -22.822   9.570  15.789  1.00122.67           N  
ANISOU   78  N   VAL A  84     9341  20192  17076  -3853    304   4194       N  
ATOM     79  CA  VAL A  84     -23.539   9.676  17.057  1.00107.05           C  
ANISOU   79  CA  VAL A  84     7528  18012  15135  -3869    267   4322       C  
ATOM     80  C   VAL A  84     -23.826  11.134  17.391  1.00100.99           C  
ANISOU   80  C   VAL A  84     6949  17253  14168  -3883    219   4444       C  
ATOM     81  O   VAL A  84     -24.910  11.471  17.882  1.00111.94           O  
ANISOU   81  O   VAL A  84     8446  18541  15547  -3901    233   4461       O  
ATOM     82  CB  VAL A  84     -22.739   8.985  18.178  1.00103.35           C  
ANISOU   82  CB  VAL A  84     7043  17396  14828  -3874    220   4451       C  
ATOM     83  CG1 VAL A  84     -23.567   8.899  19.450  1.00114.83           C  
ANISOU   83  CG1 VAL A  84     8670  18649  16312  -3937    196   4550       C  
ATOM     84  CG2 VAL A  84     -22.283   7.604  17.732  1.00104.49           C  
ANISOU   84  CG2 VAL A  84     6947  17535  15221  -3849    264   4346       C  
ATOM     85  N   ILE A  85     -22.863  12.019  17.130  1.00109.35           N  
ANISOU   85  N   ILE A  85     8035  18433  15079  -3884    174   4522       N  
ATOM     86  CA  ILE A  85     -23.030  13.434  17.458  1.00113.06           C  
ANISOU   86  CA  ILE A  85     8677  18901  15378  -3913    130   4650       C  
ATOM     87  C   ILE A  85     -24.204  14.026  16.688  1.00108.85           C  
ANISOU   87  C   ILE A  85     8147  18424  14785  -3911    140   4608       C  
ATOM     88  O   ILE A  85     -25.102  14.655  17.266  1.00110.93           O  
ANISOU   88  O   ILE A  85     8512  18578  15058  -3920    149   4666       O  
ATOM     89  CB  ILE A  85     -21.726  14.198  17.167  1.00114.32           C  
ANISOU   89  CB  ILE A  85     8849  19205  15381  -3937     76   4732       C  
ATOM     90  CG1 ILE A  85     -20.558  13.558  17.920  1.00103.32           C  
ANISOU   90  CG1 ILE A  85     7409  17773  14075  -3936     49   4792       C  
ATOM     91  CG2 ILE A  85     -21.870  15.666  17.525  1.00100.96           C  
ANISOU   91  CG2 ILE A  85     7339  17497  13525  -3987     32   4868       C  
ATOM     92  CD1 ILE A  85     -19.211  14.103  17.526  1.00101.11           C  
ANISOU   92  CD1 ILE A  85     7088  17668  13663  -3961      8   4841       C  
ATOM     93  N   ILE A  86     -24.220  13.822  15.368  1.00146.24           N  
ANISOU   93  N   ILE A  86    12755  23340  19468  -3914    142   4508       N  
ATOM     94  CA  ILE A  86     -25.272  14.408  14.549  1.00146.47           C  
ANISOU   94  CA  ILE A  86    12767  23457  19428  -3933    114   4511       C  
ATOM     95  C   ILE A  86     -26.616  13.748  14.838  1.00153.39           C  
ANISOU   95  C   ILE A  86    13608  24217  20455  -3909    162   4430       C  
ATOM     96  O   ILE A  86     -27.656  14.415  14.807  1.00147.25           O  
ANISOU   96  O   ILE A  86    12844  23421  19681  -3906    139   4491       O  
ATOM     97  CB  ILE A  86     -24.897  14.343  13.054  1.00147.62           C  
ANISOU   97  CB  ILE A  86    12799  23853  19439  -3989     93   4429       C  
ATOM     98  CG1 ILE A  86     -25.905  15.131  12.214  1.00172.64           C  
ANISOU   98  CG1 ILE A  86    15954  27134  22506  -4036     16   4504       C  
ATOM     99  CG2 ILE A  86     -24.791  12.905  12.569  1.00148.50           C  
ANISOU   99  CG2 ILE A  86    12760  24002  19660  -3991    181   4214       C  
ATOM    100  CD1 ILE A  86     -25.977  16.601  12.571  1.00171.57           C  
ANISOU  100  CD1 ILE A  86    15932  26962  22293  -4046    -69   4727       C  
ATOM    101  N   LEU A  87     -26.629  12.442  15.131  1.00134.81           N  
ANISOU  101  N   LEU A  87    11193  21786  18244  -3900    228   4302       N  
ATOM    102  CA  LEU A  87     -27.885  11.790  15.486  1.00100.72           C  
ANISOU  102  CA  LEU A  87     6856  17359  14054  -3902    277   4224       C  
ATOM    103  C   LEU A  87     -28.451  12.354  16.783  1.00 99.92           C  
ANISOU  103  C   LEU A  87     6888  17073  14002  -3899    293   4321       C  
ATOM    104  O   LEU A  87     -29.653  12.629  16.873  1.00122.02           O  
ANISOU  104  O   LEU A  87     9675  19839  16846  -3900    316   4306       O  
ATOM    105  CB  LEU A  87     -27.689  10.279  15.597  1.00101.31           C  
ANISOU  105  CB  LEU A  87     6844  17373  14275  -3920    340   4090       C  
ATOM    106  CG  LEU A  87     -27.554   9.518  14.277  1.00102.57           C  
ANISOU  106  CG  LEU A  87     6841  17702  14427  -3954    375   3922       C  
ATOM    107  CD1 LEU A  87     -27.562   8.016  14.516  1.00103.40           C  
ANISOU  107  CD1 LEU A  87     6853  17706  14728  -3983    452   3795       C  
ATOM    108  CD2 LEU A  87     -28.658   9.920  13.313  1.00103.04           C  
ANISOU  108  CD2 LEU A  87     6863  17906  14382  -3993    348   3879       C  
ATOM    109  N   THR A  88     -27.599  12.540  17.795  1.00 99.35           N  
ANISOU  109  N   THR A  88     6933  16892  13925  -3910    288   4414       N  
ATOM    110  CA  THR A  88     -28.046  13.159  19.040  1.00 98.85           C  
ANISOU  110  CA  THR A  88     7015  16665  13877  -3945    322   4487       C  
ATOM    111  C   THR A  88     -28.613  14.546  18.778  1.00 98.83           C  
ANISOU  111  C   THR A  88     7034  16700  13816  -3930    316   4560       C  
ATOM    112  O   THR A  88     -29.715  14.880  19.236  1.00114.91           O  
ANISOU  112  O   THR A  88     9077  18649  15935  -3941    382   4538       O  
ATOM    113  CB  THR A  88     -26.883  13.240  20.034  1.00 98.89           C  
ANISOU  113  CB  THR A  88     7147  16589  13839  -3988    292   4593       C  
ATOM    114  OG1 THR A  88     -26.519  11.924  20.469  1.00 98.92           O  
ANISOU  114  OG1 THR A  88     7113  16520  13950  -4013    287   4568       O  
ATOM    115  CG2 THR A  88     -27.264  14.084  21.242  1.00 99.02           C  
ANISOU  115  CG2 THR A  88     7337  16460  13825  -4058    341   4652       C  
ATOM    116  N   ILE A  89     -27.876  15.359  18.016  1.00 98.87           N  
ANISOU  116  N   ILE A  89     7032  16838  13694  -3915    241   4652       N  
ATOM    117  CA  ILE A  89     -28.310  16.726  17.744  1.00108.76           C  
ANISOU  117  CA  ILE A  89     8298  18119  14907  -3916    214   4767       C  
ATOM    118  C   ILE A  89     -29.670  16.727  17.056  1.00 99.97           C  
ANISOU  118  C   ILE A  89     7036  17057  13891  -3883    212   4734       C  
ATOM    119  O   ILE A  89     -30.608  17.402  17.498  1.00101.56           O  
ANISOU  119  O   ILE A  89     7220  17165  14204  -3877    260   4776       O  
ATOM    120  CB  ILE A  89     -27.252  17.462  16.901  1.00111.86           C  
ANISOU  120  CB  ILE A  89     8702  18674  15126  -3936    116   4876       C  
ATOM    121  CG1 ILE A  89     -26.016  17.775  17.748  1.00 98.75           C  
ANISOU  121  CG1 ILE A  89     7192  16954  13373  -3979    115   4939       C  
ATOM    122  CG2 ILE A  89     -27.839  18.723  16.286  1.00112.56           C  
ANISOU  122  CG2 ILE A  89     8755  18822  15192  -3949     55   5019       C  
ATOM    123  CD1 ILE A  89     -24.886  18.406  16.968  1.00113.42           C  
ANISOU  123  CD1 ILE A  89     9061  18987  15047  -4017     27   5024       C  
ATOM    124  N   ALA A  90     -29.803  15.946  15.982  1.00100.43           N  
ANISOU  124  N   ALA A  90     6971  17268  13921  -3873    167   4649       N  
ATOM    125  CA  ALA A  90     -31.036  15.956  15.201  1.00122.22           C  
ANISOU  125  CA  ALA A  90     9580  20116  16740  -3862    133   4635       C  
ATOM    126  C   ALA A  90     -32.212  15.425  16.012  1.00109.19           C  
ANISOU  126  C   ALA A  90     7895  18326  15266  -3846    234   4530       C  
ATOM    127  O   ALA A  90     -33.288  16.034  16.028  1.00102.44           O  
ANISOU  127  O   ALA A  90     6945  17456  14523  -3823    237   4580       O  
ATOM    128  CB  ALA A  90     -30.849  15.142  13.920  1.00126.65           C  
ANISOU  128  CB  ALA A  90    10042  20879  17202  -3896     79   4538       C  
ATOM    129  N   GLY A  91     -32.024  14.297  16.701  1.00100.97           N  
ANISOU  129  N   GLY A  91     6913  17184  14265  -3868    316   4393       N  
ATOM    130  CA  GLY A  91     -33.116  13.725  17.468  1.00101.22           C  
ANISOU  130  CA  GLY A  91     6925  17098  14436  -3890    415   4282       C  
ATOM    131  C   GLY A  91     -33.586  14.632  18.587  1.00105.63           C  
ANISOU  131  C   GLY A  91     7550  17505  15081  -3900    503   4333       C  
ATOM    132  O   GLY A  91     -34.790  14.803  18.798  1.00124.58           O  
ANISOU  132  O   GLY A  91     9849  19876  17608  -3899    568   4283       O  
ATOM    133  N   ASN A  92     -32.648  15.239  19.317  1.00100.53           N  
ANISOU  133  N   ASN A  92     7061  16766  14369  -3924    517   4420       N  
ATOM    134  CA  ASN A  92     -33.065  16.081  20.429  1.00100.81           C  
ANISOU  134  CA  ASN A  92     7176  16648  14479  -3970    634   4437       C  
ATOM    135  C   ASN A  92     -33.623  17.419  19.962  1.00101.80           C  
ANISOU  135  C   ASN A  92     7187  16806  14687  -3919    622   4555       C  
ATOM    136  O   ASN A  92     -34.510  17.972  20.622  1.00106.92           O  
ANISOU  136  O   ASN A  92     7788  17350  15488  -3939    749   4524       O  
ATOM    137  CB  ASN A  92     -31.904  16.268  21.400  1.00103.05           C  
ANISOU  137  CB  ASN A  92     7678  16824  14651  -4044    653   4486       C  
ATOM    138  CG  ASN A  92     -31.576  14.990  22.142  1.00 99.56           C  
ANISOU  138  CG  ASN A  92     7332  16309  14189  -4115    671   4401       C  
ATOM    139  OD1 ASN A  92     -32.268  14.615  23.088  1.00 99.98           O  
ANISOU  139  OD1 ASN A  92     7439  16245  14303  -4206    783   4305       O  
ATOM    140  ND2 ASN A  92     -30.526  14.304  21.707  1.00102.33           N  
ANISOU  140  ND2 ASN A  92     7687  16730  14465  -4089    564   4442       N  
ATOM    141  N   ILE A  93     -33.159  17.943  18.824  1.00101.93           N  
ANISOU  141  N   ILE A  93     7138  16967  14623  -3866    476   4695       N  
ATOM    142  CA  ILE A  93     -33.810  19.118  18.255  1.00103.53           C  
ANISOU  142  CA  ILE A  93     7191  17209  14938  -3822    428   4850       C  
ATOM    143  C   ILE A  93     -35.231  18.775  17.822  1.00112.76           C  
ANISOU  143  C   ILE A  93     8127  18435  16281  -3770    429   4789       C  
ATOM    144  O   ILE A  93     -36.162  19.572  18.007  1.00113.98           O  
ANISOU  144  O   ILE A  93     8129  18530  16648  -3733    478   4852       O  
ATOM    145  CB  ILE A  93     -32.972  19.688  17.096  1.00108.92           C  
ANISOU  145  CB  ILE A  93     7869  18053  15461  -3818    249   5028       C  
ATOM    146  CG1 ILE A  93     -31.704  20.348  17.637  1.00102.51           C  
ANISOU  146  CG1 ILE A  93     7267  17172  14511  -3877    262   5109       C  
ATOM    147  CG2 ILE A  93     -33.776  20.694  16.290  1.00117.14           C  
ANISOU  147  CG2 ILE A  93     8713  19163  16634  -3782    145   5224       C  
ATOM    148  CD1 ILE A  93     -30.845  20.981  16.570  1.00102.74           C  
ANISOU  148  CD1 ILE A  93     7305  17366  14366  -3904     99   5278       C  
ATOM    149  N   LEU A  94     -35.426  17.579  17.258  1.00124.34           N  
ANISOU  149  N   LEU A  94     9548  20015  17678  -3770    383   4661       N  
ATOM    150  CA  LEU A  94     -36.775  17.123  16.937  1.00121.19           C  
ANISOU  150  CA  LEU A  94     8948  19678  17420  -3744    391   4575       C  
ATOM    151  C   LEU A  94     -37.646  17.063  18.185  1.00121.90           C  
ANISOU  151  C   LEU A  94     9020  19604  17693  -3765    585   4440       C  
ATOM    152  O   LEU A  94     -38.803  17.496  18.162  1.00125.28           O  
ANISOU  152  O   LEU A  94     9239  20039  18324  -3721    619   4444       O  
ATOM    153  CB  LEU A  94     -36.723  15.749  16.265  1.00122.30           C  
ANISOU  153  CB  LEU A  94     9088  19944  17436  -3781    342   4432       C  
ATOM    154  CG  LEU A  94     -36.286  15.647  14.803  1.00125.91           C  
ANISOU  154  CG  LEU A  94     9492  20618  17730  -3793    172   4508       C  
ATOM    155  CD1 LEU A  94     -36.153  14.188  14.400  1.00126.00           C  
ANISOU  155  CD1 LEU A  94     9524  20703  17648  -3855    193   4318       C  
ATOM    156  CD2 LEU A  94     -37.273  16.356  13.898  1.00121.50           C  
ANISOU  156  CD2 LEU A  94     8717  20199  17248  -3766     40   4652       C  
ATOM    157  N   VAL A  95     -37.108  16.522  19.280  1.00106.45           N  
ANISOU  157  N   VAL A  95     7268  17508  15669  -3846    711   4320       N  
ATOM    158  CA  VAL A  95     -37.874  16.425  20.522  1.00110.01           C  
ANISOU  158  CA  VAL A  95     7734  17815  16250  -3919    913   4173       C  
ATOM    159  C   VAL A  95     -38.238  17.813  21.038  1.00116.09           C  
ANISOU  159  C   VAL A  95     8435  18483  17191  -3903   1021   4251       C  
ATOM    160  O   VAL A  95     -39.369  18.051  21.486  1.00135.88           O  
ANISOU  160  O   VAL A  95    10777  20947  19905  -3908   1164   4156       O  
ATOM    161  CB  VAL A  95     -37.091  15.616  21.574  1.00104.13           C  
ANISOU  161  CB  VAL A  95     7247  16946  15370  -4040    991   4075       C  
ATOM    162  CG1 VAL A  95     -37.800  15.661  22.920  1.00104.96           C  
ANISOU  162  CG1 VAL A  95     7405  16906  15571  -4164   1209   3930       C  
ATOM    163  CG2 VAL A  95     -36.922  14.182  21.113  1.00103.47           C  
ANISOU  163  CG2 VAL A  95     7180  16937  15197  -4058    911   3994       C  
ATOM    164  N   ILE A  96     -37.285  18.747  20.988  1.00106.21           N  
ANISOU  164  N   ILE A  96     7294  17189  15870  -3892    971   4418       N  
ATOM    165  CA  ILE A  96     -37.548  20.114  21.434  1.00111.76           C  
ANISOU  165  CA  ILE A  96     7937  17773  16754  -3889   1083   4512       C  
ATOM    166  C   ILE A  96     -38.665  20.736  20.605  1.00112.79           C  
ANISOU  166  C   ILE A  96     7725  17977  17154  -3759   1018   4622       C  
ATOM    167  O   ILE A  96     -39.589  21.362  21.142  1.00111.78           O  
ANISOU  167  O   ILE A  96     7420  17747  17305  -3742   1183   4583       O  
ATOM    168  CB  ILE A  96     -36.262  20.957  21.367  1.00107.89           C  
ANISOU  168  CB  ILE A  96     7638  17243  16113  -3916   1009   4691       C  
ATOM    169  CG1 ILE A  96     -35.253  20.485  22.416  1.00105.14           C  
ANISOU  169  CG1 ILE A  96     7607  16798  15546  -4049   1090   4583       C  
ATOM    170  CG2 ILE A  96     -36.578  22.436  21.545  1.00108.59           C  
ANISOU  170  CG2 ILE A  96     7627  17210  16422  -3904   1096   4836       C  
ATOM    171  CD1 ILE A  96     -33.925  21.206  22.353  1.00104.30           C  
ANISOU  171  CD1 ILE A  96     7695  16677  15258  -4083   1005   4737       C  
ATOM    172  N   MET A  97     -38.596  20.570  19.280  1.00109.79           N  
ANISOU  172  N   MET A  97     7233  17778  16705  -3674    778   4763       N  
ATOM    173  CA  MET A  97     -39.630  21.125  18.410  1.00116.80           C  
ANISOU  173  CA  MET A  97     7790  18752  17836  -3556    661   4907       C  
ATOM    174  C   MET A  97     -40.987  20.492  18.687  1.00123.19           C  
ANISOU  174  C   MET A  97     8388  19585  18832  -3527    768   4709       C  
ATOM    175  O   MET A  97     -42.010  21.186  18.710  1.00121.95           O  
ANISOU  175  O   MET A  97     7942  19389  19002  -3433    809   4760       O  
ATOM    176  CB  MET A  97     -39.244  20.936  16.943  1.00114.84           C  
ANISOU  176  CB  MET A  97     7508  18719  17405  -3528    378   5075       C  
ATOM    177  CG  MET A  97     -38.009  21.709  16.514  1.00115.20           C  
ANISOU  177  CG  MET A  97     7711  18777  17283  -3566    255   5294       C  
ATOM    178  SD  MET A  97     -37.748  21.656  14.731  1.00117.57           S  
ANISOU  178  SD  MET A  97     7930  19356  17386  -3577    -66   5499       S  
ATOM    179  CE  MET A  97     -37.827  19.894  14.427  1.00110.41           C  
ANISOU  179  CE  MET A  97     7093  18595  16262  -3621    -45   5205       C  
ATOM    180  N   ALA A  98     -41.019  19.174  18.895  1.00120.53           N  
ANISOU  180  N   ALA A  98     8175  19307  18316  -3607    812   4486       N  
ATOM    181  CA  ALA A  98     -42.284  18.498  19.159  1.00113.51           C  
ANISOU  181  CA  ALA A  98     7106  18456  17566  -3615    915   4284       C  
ATOM    182  C   ALA A  98     -42.909  18.983  20.459  1.00114.79           C  
ANISOU  182  C   ALA A  98     7208  18450  17957  -3657   1195   4139       C  
ATOM    183  O   ALA A  98     -44.124  19.207  20.526  1.00142.42           O  
ANISOU  183  O   ALA A  98    10415  21971  21727  -3596   1274   4070       O  
ATOM    184  CB  ALA A  98     -42.076  16.986  19.196  1.00111.85           C  
ANISOU  184  CB  ALA A  98     7071  18309  17117  -3723    917   4093       C  
ATOM    185  N   VAL A  99     -42.098  19.151  21.507  1.00113.48           N  
ANISOU  185  N   VAL A  99     7310  18124  17685  -3774   1357   4080       N  
ATOM    186  CA  VAL A  99     -42.643  19.614  22.780  1.00114.91           C  
ANISOU  186  CA  VAL A  99     7464  18149  18047  -3867   1657   3916       C  
ATOM    187  C   VAL A  99     -43.108  21.062  22.675  1.00119.07           C  
ANISOU  187  C   VAL A  99     7725  18588  18929  -3738   1717   4066       C  
ATOM    188  O   VAL A  99     -44.182  21.420  23.174  1.00132.05           O  
ANISOU  188  O   VAL A  99     9116  20179  20878  -3715   1919   3935       O  
ATOM    189  CB  VAL A  99     -41.616  19.432  23.911  1.00113.13           C  
ANISOU  189  CB  VAL A  99     7621  17778  17584  -4059   1796   3828       C  
ATOM    190  CG1 VAL A  99     -42.172  19.983  25.216  1.00114.95           C  
ANISOU  190  CG1 VAL A  99     7843  17856  17975  -4202   2130   3643       C  
ATOM    191  CG2 VAL A  99     -41.257  17.967  24.070  1.00111.24           C  
ANISOU  191  CG2 VAL A  99     7596  17589  17081  -4165   1735   3703       C  
ATOM    192  N   SER A 100     -42.319  21.917  22.020  1.00117.88           N  
ANISOU  192  N   SER A 100     7609  18410  18770  -3652   1549   4344       N  
ATOM    193  CA  SER A 100     -42.638  23.339  21.965  1.00119.52           C  
ANISOU  193  CA  SER A 100     7583  18477  19351  -3536   1604   4528       C  
ATOM    194  C   SER A 100     -43.703  23.685  20.931  1.00122.18           C  
ANISOU  194  C   SER A 100     7490  18906  20027  -3315   1425   4685       C  
ATOM    195  O   SER A 100     -44.227  24.804  20.965  1.00125.03           O  
ANISOU  195  O   SER A 100     7574  19112  20819  -3181   1493   4816       O  
ATOM    196  CB  SER A 100     -41.368  24.146  21.681  1.00121.01           C  
ANISOU  196  CB  SER A 100     7989  18593  19397  -3562   1485   4785       C  
ATOM    197  OG  SER A 100     -40.736  23.702  20.493  1.00116.65           O  
ANISOU  197  OG  SER A 100     7507  18236  18578  -3520   1163   4955       O  
ATOM    198  N   LEU A 101     -44.038  22.769  20.022  1.00121.64           N  
ANISOU  198  N   LEU A 101     7354  19065  19799  -3275   1199   4679       N  
ATOM    199  CA  LEU A 101     -45.012  23.040  18.970  1.00128.54           C  
ANISOU  199  CA  LEU A 101     7848  20056  20934  -3092    980   4844       C  
ATOM    200  C   LEU A 101     -46.370  22.401  19.234  1.00127.40           C  
ANISOU  200  C   LEU A 101     7450  19992  20965  -3058   1096   4593       C  
ATOM    201  O   LEU A 101     -47.399  23.075  19.130  1.00131.77           O  
ANISOU  201  O   LEU A 101     7622  20497  21947  -2886   1109   4645       O  
ATOM    202  CB  LEU A 101     -44.473  22.561  17.615  1.00124.87           C  
ANISOU  202  CB  LEU A 101     7478  19814  20151  -3103    630   5033       C  
ATOM    203  CG  LEU A 101     -43.421  23.436  16.931  1.00122.96           C  
ANISOU  203  CG  LEU A 101     7346  19554  19819  -3099    426   5364       C  
ATOM    204  CD1 LEU A 101     -42.982  22.811  15.615  1.00121.35           C  
ANISOU  204  CD1 LEU A 101     7233  19605  19268  -3153    123   5481       C  
ATOM    205  CD2 LEU A 101     -43.956  24.842  16.709  1.00125.80           C  
ANISOU  205  CD2 LEU A 101     7379  19768  20651  -2934    353   5650       C  
ATOM    206  N   GLU A 102     -46.395  21.113  19.567  1.00142.16           N  
ANISOU  206  N   GLU A 102     9510  21971  22533  -3215   1176   4326       N  
ATOM    207  CA  GLU A 102     -47.660  20.411  19.744  1.00155.29           C  
ANISOU  207  CA  GLU A 102    10951  23743  24311  -3223   1269   4087       C  
ATOM    208  C   GLU A 102     -48.401  20.944  20.964  1.00156.07           C  
ANISOU  208  C   GLU A 102    10875  23684  24742  -3225   1618   3875       C  
ATOM    209  O   GLU A 102     -47.837  21.036  22.058  1.00167.46           O  
ANISOU  209  O   GLU A 102    12557  24973  26097  -3376   1872   3737       O  
ATOM    210  CB  GLU A 102     -47.418  18.910  19.883  1.00146.58           C  
ANISOU  210  CB  GLU A 102    10121  22752  22820  -3418   1287   3866       C  
ATOM    211  CG  GLU A 102     -46.704  18.287  18.694  1.00154.47           C  
ANISOU  211  CG  GLU A 102    11283  23902  23506  -3429    993   4022       C  
ATOM    212  CD  GLU A 102     -47.502  18.400  17.410  1.00160.61           C  
ANISOU  212  CD  GLU A 102    11764  24873  24387  -3312    733   4183       C  
ATOM    213  OE1 GLU A 102     -48.749  18.369  17.475  1.00168.59           O  
ANISOU  213  OE1 GLU A 102    12474  25948  25633  -3261    780   4082       O  
ATOM    214  OE2 GLU A 102     -46.880  18.521  16.333  1.00164.18           O  
ANISOU  214  OE2 GLU A 102    12284  25426  24672  -3290    478   4410       O  
ATOM    215  N   LYS A 103     -49.674  21.291  20.772  1.00135.06           N  
ANISOU  215  N   LYS A 103     7793  21067  22458  -3069   1634   3841       N  
ATOM    216  CA  LYS A 103     -50.496  21.806  21.859  1.00134.69           C  
ANISOU  216  CA  LYS A 103     7521  20882  22774  -3053   1990   3605       C  
ATOM    217  C   LYS A 103     -50.966  20.710  22.805  1.00138.07           C  
ANISOU  217  C   LYS A 103     8064  21407  22990  -3305   2250   3212       C  
ATOM    218  O   LYS A 103     -51.425  21.020  23.910  1.00135.97           O  
ANISOU  218  O   LYS A 103     7718  21036  22907  -3388   2601   2964       O  
ATOM    219  CB  LYS A 103     -51.716  22.545  21.299  1.00143.74           C  
ANISOU  219  CB  LYS A 103     8145  22036  24434  -2768   1906   3696       C  
ATOM    220  CG  LYS A 103     -51.553  23.059  19.873  1.00139.85           C  
ANISOU  220  CG  LYS A 103     7514  21598  24026  -2557   1475   4111       C  
ATOM    221  CD  LYS A 103     -50.609  24.247  19.792  1.00139.53           C  
ANISOU  221  CD  LYS A 103     7555  21312  24148  -2456   1427   4410       C  
ATOM    222  CE  LYS A 103     -50.482  24.738  18.359  1.00140.53           C  
ANISOU  222  CE  LYS A 103     7548  21516  24330  -2290    976   4836       C  
ATOM    223  NZ  LYS A 103     -49.570  25.908  18.246  1.00151.33           N  
ANISOU  223  NZ  LYS A 103     8986  22652  25861  -2216    911   5149       N  
ATOM    224  N   LYS A 104     -50.864  19.445  22.396  1.00139.70           N  
ANISOU  224  N   LYS A 104     8457  21796  22826  -3445   2097   3148       N  
ATOM    225  CA  LYS A 104     -51.334  18.326  23.200  1.00131.67           C  
ANISOU  225  CA  LYS A 104     7549  20857  21622  -3696   2307   2808       C  
ATOM    226  C   LYS A 104     -50.320  17.870  24.240  1.00128.81           C  
ANISOU  226  C   LYS A 104     7641  20354  20945  -3956   2485   2690       C  
ATOM    227  O   LYS A 104     -50.673  17.074  25.117  1.00128.88           O  
ANISOU  227  O   LYS A 104     7763  20372  20835  -4193   2699   2414       O  
ATOM    228  CB  LYS A 104     -51.692  17.150  22.288  1.00130.96           C  
ANISOU  228  CB  LYS A 104     7458  20975  21326  -3729   2071   2804       C  
ATOM    229  CG  LYS A 104     -52.352  17.568  20.983  1.00133.17           C  
ANISOU  229  CG  LYS A 104     7384  21406  21809  -3488   1781   3022       C  
ATOM    230  CD  LYS A 104     -52.511  16.394  20.032  1.00132.21           C  
ANISOU  230  CD  LYS A 104     7332  21483  21418  -3566   1548   3035       C  
ATOM    231  CE  LYS A 104     -52.966  16.860  18.656  1.00134.95           C  
ANISOU  231  CE  LYS A 104     7394  21985  21898  -3367   1219   3304       C  
ATOM    232  NZ  LYS A 104     -54.249  17.614  18.711  1.00138.62           N  
ANISOU  232  NZ  LYS A 104     7380  22494  22796  -3196   1264   3276       N  
ATOM    233  N   LEU A 105     -49.081  18.350  24.166  1.00140.81           N  
ANISOU  233  N   LEU A 105     9426  21742  22332  -3928   2392   2901       N  
ATOM    234  CA  LEU A 105     -48.018  17.937  25.072  1.00140.55           C  
ANISOU  234  CA  LEU A 105     9834  21576  21991  -4156   2506   2833       C  
ATOM    235  C   LEU A 105     -47.818  18.905  26.230  1.00143.91           C  
ANISOU  235  C   LEU A 105    10324  21820  22534  -4265   2812   2745       C  
ATOM    236  O   LEU A 105     -46.875  18.735  27.007  1.00139.36           O  
ANISOU  236  O   LEU A 105    10124  21120  21706  -4460   2896   2717       O  
ATOM    237  CB  LEU A 105     -46.705  17.773  24.303  1.00120.80           C  
ANISOU  237  CB  LEU A 105     7606  19064  19229  -4087   2216   3096       C  
ATOM    238  CG  LEU A 105     -46.649  16.691  23.225  1.00119.41           C  
ANISOU  238  CG  LEU A 105     7456  19050  18862  -4040   1942   3161       C  
ATOM    239  CD1 LEU A 105     -45.324  16.745  22.480  1.00116.87           C  
ANISOU  239  CD1 LEU A 105     7360  18722  18321  -3968   1700   3404       C  
ATOM    240  CD2 LEU A 105     -46.866  15.314  23.832  1.00118.67           C  
ANISOU  240  CD2 LEU A 105     7540  18966  18584  -4251   2040   2933       C  
ATOM    241  N   GLN A 106     -48.679  19.910  26.370  1.00161.02           N  
ANISOU  241  N   GLN A 106    12132  23956  25094  -4143   2986   2701       N  
ATOM    242  CA  GLN A 106     -48.448  20.946  27.369  1.00156.21           C  
ANISOU  242  CA  GLN A 106    11575  23145  24632  -4231   3293   2633       C  
ATOM    243  C   GLN A 106     -48.743  20.442  28.778  1.00152.97           C  
ANISOU  243  C   GLN A 106    11341  22737  24045  -4593   3643   2274       C  
ATOM    244  O   GLN A 106     -49.880  20.533  29.254  1.00156.60           O  
ANISOU  244  O   GLN A 106    11520  23274  24708  -4635   3885   2034       O  
ATOM    245  CB  GLN A 106     -49.291  22.183  27.053  1.00164.61           C  
ANISOU  245  CB  GLN A 106    12177  24108  26260  -3943   3386   2696       C  
ATOM    246  CG  GLN A 106     -49.205  22.650  25.600  1.00167.73           C  
ANISOU  246  CG  GLN A 106    12347  24527  26855  -3603   3008   3063       C  
ATOM    247  CD  GLN A 106     -47.801  23.060  25.180  1.00162.11           C  
ANISOU  247  CD  GLN A 106    11945  23719  25930  -3595   2802   3371       C  
ATOM    248  OE1 GLN A 106     -46.936  22.215  24.944  1.00152.29           O  
ANISOU  248  OE1 GLN A 106    11038  22586  24240  -3723   2611   3426       O  
ATOM    249  NE2 GLN A 106     -47.573  24.363  25.075  1.00170.42           N  
ANISOU  249  NE2 GLN A 106    12874  24548  27331  -3437   2848   3567       N  
ATOM    250  N   ASN A 107     -47.723  19.904  29.442  1.00133.91           N  
ANISOU  250  N   ASN A 107     9392  20239  21249  -4853   3659   2247       N  
ATOM    251  CA  ASN A 107     -47.826  19.465  30.829  1.00128.54           C  
ANISOU  251  CA  ASN A 107     8952  19492  20393  -5231   3983   1939       C  
ATOM    252  C   ASN A 107     -46.416  19.377  31.404  1.00125.91           C  
ANISOU  252  C   ASN A 107     9121  18932  19787  -5374   3945   2063       C  
ATOM    253  O   ASN A 107     -45.424  19.584  30.701  1.00123.55           O  
ANISOU  253  O   ASN A 107     8960  18628  19356  -5219   3661   2337       O  
ATOM    254  CB  ASN A 107     -48.577  18.134  30.941  1.00128.65           C  
ANISOU  254  CB  ASN A 107     8936  19541  20403  -5312   4002   1767       C  
ATOM    255  CG  ASN A 107     -48.077  17.092  29.959  1.00125.63           C  
ANISOU  255  CG  ASN A 107     8684  19240  19808  -5170   3601   1984       C  
ATOM    256  OD1 ASN A 107     -46.942  17.156  29.488  1.00123.01           O  
ANISOU  256  OD1 ASN A 107     8580  18875  19284  -5079   3356   2225       O  
ATOM    257  ND2 ASN A 107     -48.929  16.122  29.645  1.00126.21           N  
ANISOU  257  ND2 ASN A 107     8608  19425  19921  -5163   3550   1890       N  
ATOM    258  N   ALA A 108     -46.338  19.064  32.701  1.00102.12           N  
ANISOU  258  N   ALA A 108    10371  13051  15381  -1139  -1359   3642       N  
ATOM    259  CA  ALA A 108     -45.055  19.083  33.400  1.00 98.03           C  
ANISOU  259  CA  ALA A 108     9869  12555  14824  -1145  -1399   3789       C  
ATOM    260  C   ALA A 108     -44.087  18.046  32.841  1.00 95.26           C  
ANISOU  260  C   ALA A 108     9517  12205  14473  -1085  -1425   4031       C  
ATOM    261  O   ALA A 108     -42.889  18.322  32.689  1.00 97.66           O  
ANISOU  261  O   ALA A 108     9815  12541  14751  -1055  -1392   4079       O  
ATOM    262  CB  ALA A 108     -45.274  18.854  34.896  1.00103.55           C  
ANISOU  262  CB  ALA A 108    10586  13319  15440  -1272  -1408   3631       C  
ATOM    263  N   THR A 109     -44.584  16.843  32.542  1.00 89.26           N  
ANISOU  263  N   THR A 109     8750  11440  13724  -1088  -1422   4015       N  
ATOM    264  CA  THR A 109     -43.703  15.770  32.092  1.00 87.36           C  
ANISOU  264  CA  THR A 109     8480  11206  13507  -1051  -1397   4103       C  
ATOM    265  C   THR A 109     -43.020  16.125  30.777  1.00 86.95           C  
ANISOU  265  C   THR A 109     8394  11181  13460   -988  -1308   4135       C  
ATOM    266  O   THR A 109     -41.813  15.910  30.617  1.00 78.69           O  
ANISOU  266  O   THR A 109     7321  10165  12414   -966  -1272   4193       O  
ATOM    267  CB  THR A 109     -44.490  14.466  31.954  1.00 96.33           C  
ANISOU  267  CB  THR A 109     9585  12302  14715  -1069  -1428   4123       C  
ATOM    268  OG1 THR A 109     -45.072  14.122  33.218  1.00 92.91           O  
ANISOU  268  OG1 THR A 109     9178  11885  14238  -1163  -1488   4032       O  
ATOM    269  CG2 THR A 109     -43.577  13.336  31.501  1.00 83.75           C  
ANISOU  269  CG2 THR A 109     7926  10687  13209  -1032  -1396   4207       C  
ATOM    270  N   ASN A 110     -43.768  16.690  29.828  1.00 95.66           N  
ANISOU  270  N   ASN A 110     9482  12292  14570   -970  -1279   4123       N  
ATOM    271  CA  ASN A 110     -43.158  17.049  28.553  1.00 92.58           C  
ANISOU  271  CA  ASN A 110     9040  11973  14164   -932  -1210   4192       C  
ATOM    272  C   ASN A 110     -42.246  18.261  28.684  1.00 80.27           C  
ANISOU  272  C   ASN A 110     7499  10433  12566   -923  -1192   4200       C  
ATOM    273  O   ASN A 110     -41.276  18.379  27.933  1.00 74.86           O  
ANISOU  273  O   ASN A 110     6766   9820  11857   -903  -1143   4277       O  
ATOM    274  CB  ASN A 110     -44.234  17.296  27.499  1.00105.76           C  
ANISOU  274  CB  ASN A 110    10665  13679  15839   -930  -1198   4211       C  
ATOM    275  CG  ASN A 110     -44.929  16.019  27.069  1.00101.79           C  
ANISOU  275  CG  ASN A 110    10100  13236  15338   -919  -1179   4062       C  
ATOM    276  OD1 ASN A 110     -44.490  15.343  26.138  1.00108.27           O  
ANISOU  276  OD1 ASN A 110    10828  14160  16149   -882  -1134   4065       O  
ATOM    277  ND2 ASN A 110     -46.018  15.680  27.748  1.00113.97           N  
ANISOU  277  ND2 ASN A 110    11671  14734  16898   -953  -1212   3902       N  
ATOM    278  N   TYR A 111     -42.528  19.167  29.624  1.00 78.73           N  
ANISOU  278  N   TYR A 111     7349  10181  12382   -944  -1238   4144       N  
ATOM    279  CA  TYR A 111     -41.589  20.255  29.886  1.00 80.45           C  
ANISOU  279  CA  TYR A 111     7565  10408  12594   -939  -1235   4170       C  
ATOM    280  C   TYR A 111     -40.264  19.714  30.411  1.00 84.57           C  
ANISOU  280  C   TYR A 111     8084  10978  13071   -944  -1228   4205       C  
ATOM    281  O   TYR A 111     -39.186  20.152  29.984  1.00 77.33           O  
ANISOU  281  O   TYR A 111     7133  10112  12138   -929  -1194   4269       O  
ATOM    282  CB  TYR A 111     -42.193  21.250  30.878  1.00 85.58           C  
ANISOU  282  CB  TYR A 111     8226  10983  13306   -969  -1298   4129       C  
ATOM    283  CG  TYR A 111     -43.447  21.939  30.385  1.00101.64           C  
ANISOU  283  CG  TYR A 111    10237  12945  15437   -964  -1311   4118       C  
ATOM    284  CD1 TYR A 111     -43.705  22.070  29.026  1.00 97.67           C  
ANISOU  284  CD1 TYR A 111     9699  12472  14939   -937  -1265   4172       C  
ATOM    285  CD2 TYR A 111     -44.372  22.461  31.280  1.00116.65           C  
ANISOU  285  CD2 TYR A 111    12127  14765  17430  -1000  -1365   4046       C  
ATOM    286  CE1 TYR A 111     -44.851  22.698  28.573  1.00116.89           C  
ANISOU  286  CE1 TYR A 111    12093  14845  17476   -940  -1286   4191       C  
ATOM    287  CE2 TYR A 111     -45.520  23.089  30.837  1.00121.33           C  
ANISOU  287  CE2 TYR A 111    12677  15299  18125   -998  -1354   3953       C  
ATOM    288  CZ  TYR A 111     -45.754  23.207  29.483  1.00124.19           C  
ANISOU  288  CZ  TYR A 111    13008  15656  18522   -960  -1342   4116       C  
ATOM    289  OH  TYR A 111     -46.896  23.834  29.039  1.00120.28           O  
ANISOU  289  OH  TYR A 111    12449  15110  18141   -959  -1347   4050       O  
ATOM    290  N   PHE A 112     -40.327  18.754  31.336  1.00 83.60           N  
ANISOU  290  N   PHE A 112     7982  10846  12937   -971  -1269   4188       N  
ATOM    291  CA  PHE A 112     -39.106  18.120  31.824  1.00 80.41           C  
ANISOU  291  CA  PHE A 112     7555  10483  12516   -981  -1269   4253       C  
ATOM    292  C   PHE A 112     -38.391  17.372  30.706  1.00 75.28           C  
ANISOU  292  C   PHE A 112     6840   9861  11903   -944  -1199   4327       C  
ATOM    293  O   PHE A 112     -37.158  17.376  30.637  1.00 73.50           O  
ANISOU  293  O   PHE A 112     6564   9683  11680   -940  -1175   4407       O  
ATOM    294  CB  PHE A 112     -39.428  17.180  32.983  1.00 79.16           C  
ANISOU  294  CB  PHE A 112     7411  10312  12355  -1030  -1340   4255       C  
ATOM    295  CG  PHE A 112     -39.322  17.823  34.335  1.00 92.44           C  
ANISOU  295  CG  PHE A 112     9107  12039  13979  -1098  -1416   4264       C  
ATOM    296  CD1 PHE A 112     -38.103  17.889  34.990  1.00 83.01           C  
ANISOU  296  CD1 PHE A 112     7879  10913  12748  -1129  -1434   4350       C  
ATOM    297  CD2 PHE A 112     -40.440  18.355  34.957  1.00101.71           C  
ANISOU  297  CD2 PHE A 112    10306  13198  15143  -1150  -1472   4213       C  
ATOM    298  CE1 PHE A 112     -37.999  18.478  36.236  1.00 82.98           C  
ANISOU  298  CE1 PHE A 112     7866  10982  12679  -1217  -1511   4389       C  
ATOM    299  CE2 PHE A 112     -40.343  18.945  36.204  1.00 93.02           C  
ANISOU  299  CE2 PHE A 112     9192  12159  13991  -1242  -1548   4256       C  
ATOM    300  CZ  PHE A 112     -39.120  19.006  36.844  1.00 85.70           C  
ANISOU  300  CZ  PHE A 112     8232  11321  13009  -1280  -1568   4345       C  
ATOM    301  N   LEU A 113     -39.149  16.717  29.824  1.00 87.70           N  
ANISOU  301  N   LEU A 113     8387  11417  13518   -923  -1174   4325       N  
ATOM    302  CA  LEU A 113     -38.538  16.028  28.691  1.00 77.63           C  
ANISOU  302  CA  LEU A 113     7009  10190  12297   -890  -1117   4428       C  
ATOM    303  C   LEU A 113     -37.875  17.010  27.731  1.00 73.71           C  
ANISOU  303  C   LEU A 113     6472   9794  11740   -872  -1068   4487       C  
ATOM    304  O   LEU A 113     -36.835  16.702  27.142  1.00 64.88           O  
ANISOU  304  O   LEU A 113     5258   8750  10645   -852  -1032   4601       O  
ATOM    305  CB  LEU A 113     -39.580  15.183  27.960  1.00 86.65           C  
ANISOU  305  CB  LEU A 113     8110  11313  13499   -876  -1113   4436       C  
ATOM    306  CG  LEU A 113     -40.030  13.911  28.681  1.00 82.34           C  
ANISOU  306  CG  LEU A 113     7557  10664  13064   -891  -1160   4429       C  
ATOM    307  CD1 LEU A 113     -41.003  13.118  27.823  1.00 83.87           C  
ANISOU  307  CD1 LEU A 113     7682  10846  13339   -872  -1153   4437       C  
ATOM    308  CD2 LEU A 113     -38.826  13.061  29.061  1.00 54.12           C  
ANISOU  308  CD2 LEU A 113     3904   7056   9605   -885  -1159   4531       C  
ATOM    309  N   MET A 114     -38.465  18.194  27.552  1.00 84.49           N  
ANISOU  309  N   MET A 114     7889  11165  13049   -879  -1075   4437       N  
ATOM    310  CA  MET A 114     -37.840  19.207  26.708  1.00 79.06           C  
ANISOU  310  CA  MET A 114     7155  10566  12317   -871  -1044   4515       C  
ATOM    311  C   MET A 114     -36.564  19.739  27.344  1.00 79.20           C  
ANISOU  311  C   MET A 114     7172  10595  12326   -879  -1051   4544       C  
ATOM    312  O   MET A 114     -35.582  20.007  26.645  1.00 78.03           O  
ANISOU  312  O   MET A 114     6947  10547  12155   -870  -1021   4652       O  
ATOM    313  CB  MET A 114     -38.813  20.352  26.432  1.00 73.64           C  
ANISOU  313  CB  MET A 114     6503   9851  11628   -880  -1062   4483       C  
ATOM    314  CG  MET A 114     -38.276  21.381  25.448  1.00 70.09           C  
ANISOU  314  CG  MET A 114     5987   9495  11151   -881  -1041   4599       C  
ATOM    315  SD  MET A 114     -39.425  22.729  25.116  1.00 89.58           S  
ANISOU  315  SD  MET A 114     8460  11900  13678   -896  -1072   4609       S  
ATOM    316  CE  MET A 114     -39.605  23.428  26.754  1.00 50.08           C  
ANISOU  316  CE  MET A 114     3539   6719   8770   -896  -1132   4485       C  
ATOM    317  N   SER A 115     -36.559  19.906  28.667  1.00 75.95           N  
ANISOU  317  N   SER A 115     6826  10106  11924   -899  -1099   4471       N  
ATOM    318  CA  SER A 115     -35.322  20.278  29.349  1.00 72.64           C  
ANISOU  318  CA  SER A 115     6385   9722  11495   -914  -1114   4522       C  
ATOM    319  C   SER A 115     -34.267  19.185  29.200  1.00 74.94           C  
ANISOU  319  C   SER A 115     6596  10069  11808   -909  -1085   4618       C  
ATOM    320  O   SER A 115     -33.076  19.472  29.014  1.00 89.33           O  
ANISOU  320  O   SER A 115     8347  11970  13623   -909  -1070   4717       O  
ATOM    321  CB  SER A 115     -35.600  20.568  30.822  1.00 76.93           C  
ANISOU  321  CB  SER A 115     6985  10211  12034   -951  -1184   4458       C  
ATOM    322  OG  SER A 115     -34.417  20.965  31.494  1.00 54.01           O  
ANISOU  322  OG  SER A 115     4042   7366   9115   -978  -1208   4531       O  
ATOM    323  N   LEU A 116     -34.693  17.923  29.277  1.00 77.74           N  
ANISOU  323  N   LEU A 116     6939  10380  12218   -904  -1084   4611       N  
ATOM    324  CA  LEU A 116     -33.789  16.801  29.045  1.00 80.78           C  
ANISOU  324  CA  LEU A 116     7208  10790  12692   -888  -1062   4734       C  
ATOM    325  C   LEU A 116     -33.216  16.842  27.634  1.00 83.14           C  
ANISOU  325  C   LEU A 116     7394  11197  12997   -848  -1006   4851       C  
ATOM    326  O   LEU A 116     -32.022  16.595  27.428  1.00 83.84           O  
ANISOU  326  O   LEU A 116     7370  11356  13131   -834   -988   4985       O  
ATOM    327  CB  LEU A 116     -34.537  15.488  29.281  1.00 73.91           C  
ANISOU  327  CB  LEU A 116     6329   9826  11928   -886  -1081   4720       C  
ATOM    328  CG  LEU A 116     -33.743  14.187  29.383  1.00 65.38           C  
ANISOU  328  CG  LEU A 116     5113   8708  11022   -872  -1085   4861       C  
ATOM    329  CD1 LEU A 116     -33.298  13.965  30.814  1.00 67.12           C  
ANISOU  329  CD1 LEU A 116     5351   8897  11255   -929  -1146   4882       C  
ATOM    330  CD2 LEU A 116     -34.572  13.013  28.889  1.00 64.14           C  
ANISOU  330  CD2 LEU A 116     4902   8456  11014   -843  -1083   4877       C  
ATOM    331  N   ALA A 117     -34.061  17.146  26.648  1.00 85.55           N  
ANISOU  331  N   ALA A 117     7710  11542  13252   -833   -983   4828       N  
ATOM    332  CA  ALA A 117     -33.600  17.260  25.270  1.00 90.46           C  
ANISOU  332  CA  ALA A 117     8212  12321  13836   -807   -938   4967       C  
ATOM    333  C   ALA A 117     -32.656  18.441  25.092  1.00 89.91           C  
ANISOU  333  C   ALA A 117     8127  12351  13683   -823   -934   5024       C  
ATOM    334  O   ALA A 117     -31.722  18.365  24.292  1.00 87.94           O  
ANISOU  334  O   ALA A 117     7748  12261  13405   -798   -905   5124       O  
ATOM    335  CB  ALA A 117     -34.793  17.383  24.324  1.00110.42           C  
ANISOU  335  CB  ALA A 117    10747  14906  16303   -800   -928   4929       C  
ATOM    336  N   ILE A 118     -32.887  19.537  25.817  1.00100.11           N  
ANISOU  336  N   ILE A 118     9530  13567  14939   -851   -967   4921       N  
ATOM    337  CA  ILE A 118     -31.958  20.665  25.787  1.00 93.61           C  
ANISOU  337  CA  ILE A 118     8681  12812  14076   -868   -976   4987       C  
ATOM    338  C   ILE A 118     -30.600  20.246  26.331  1.00 93.02           C  
ANISOU  338  C   ILE A 118     8531  12782  14030   -870   -976   5074       C  
ATOM    339  O   ILE A 118     -29.553  20.581  25.760  1.00100.64           O  
ANISOU  339  O   ILE A 118     9391  13884  14965   -870   -962   5211       O  
ATOM    340  CB  ILE A 118     -32.537  21.857  26.572  1.00 91.08           C  
ANISOU  340  CB  ILE A 118     8465  12377  13762   -889  -1023   4881       C  
ATOM    341  CG1 ILE A 118     -33.724  22.467  25.826  1.00 91.72           C  
ANISOU  341  CG1 ILE A 118     8577  12434  13840   -886  -1023   4853       C  
ATOM    342  CG2 ILE A 118     -31.466  22.909  26.826  1.00 86.86           C  
ANISOU  342  CG2 ILE A 118     7886  11890  13228   -908  -1048   4961       C  
ATOM    343  CD1 ILE A 118     -34.395  23.595  26.576  1.00104.89           C  
ANISOU  343  CD1 ILE A 118    10313  13972  15569   -896  -1075   4774       C  
ATOM    344  N   ALA A 119     -30.595  19.513  27.446  1.00 83.01           N  
ANISOU  344  N   ALA A 119     7300  11420  12821   -879  -1000   5019       N  
ATOM    345  CA  ALA A 119     -29.335  19.025  28.002  1.00 97.29           C  
ANISOU  345  CA  ALA A 119     9016  13274  14677   -886  -1008   5131       C  
ATOM    346  C   ALA A 119     -28.626  18.093  27.026  1.00104.54           C  
ANISOU  346  C   ALA A 119     9769  14298  15654   -829   -963   5227       C  
ATOM    347  O   ALA A 119     -27.409  18.192  26.832  1.00103.42           O  
ANISOU  347  O   ALA A 119     9506  14291  15499   -799   -953   5229       O  
ATOM    348  CB  ALA A 119     -29.586  18.319  29.334  1.00 83.61           C  
ANISOU  348  CB  ALA A 119     7335  11436  12998   -913  -1052   5074       C  
ATOM    349  N   ASP A 120     -29.377  17.187  26.394  1.00110.30           N  
ANISOU  349  N   ASP A 120    10474  15006  16429   -773   -941   5126       N  
ATOM    350  CA  ASP A 120     -28.790  16.280  25.411  1.00106.48           C  
ANISOU  350  CA  ASP A 120     9809  14661  15989   -659   -910   5002       C  
ATOM    351  C   ASP A 120     -28.231  17.040  24.215  1.00111.55           C  
ANISOU  351  C   ASP A 120    10356  15528  16501   -650   -871   5005       C  
ATOM    352  O   ASP A 120     -27.149  16.715  23.712  1.00108.98           O  
ANISOU  352  O   ASP A 120     9855  15364  16188   -585   -851   4931       O  
ATOM    353  CB  ASP A 120     -29.835  15.269  24.947  1.00112.04           C  
ANISOU  353  CB  ASP A 120    10500  15308  16762   -601   -904   4878       C  
ATOM    354  CG  ASP A 120     -30.026  14.137  25.924  1.00115.54           C  
ANISOU  354  CG  ASP A 120    10950  15567  17385   -579   -945   4866       C  
ATOM    355  OD1 ASP A 120     -29.009  13.564  26.357  1.00108.25           O  
ANISOU  355  OD1 ASP A 120     9917  14638  16575   -525   -969   4877       O  
ATOM    356  OD2 ASP A 120     -31.188  13.820  26.258  1.00122.12           O  
ANISOU  356  OD2 ASP A 120    11882  16265  18252   -619   -961   4858       O  
ATOM    357  N   MET A 121     -28.968  18.042  23.733  1.00119.62           N  
ANISOU  357  N   MET A 121    11471  16572  17406   -716   -867   5097       N  
ATOM    358  CA  MET A 121     -28.526  18.831  22.592  1.00123.57           C  
ANISOU  358  CA  MET A 121    11878  17297  17775   -732   -842   5160       C  
ATOM    359  C   MET A 121     -27.261  19.610  22.920  1.00119.63           C  
ANISOU  359  C   MET A 121    11333  16868  17251   -768   -850   5253       C  
ATOM    360  O   MET A 121     -26.353  19.706  22.088  1.00121.02           O  
ANISOU  360  O   MET A 121    11348  17273  17360   -757   -819   5229       O  
ATOM    361  CB  MET A 121     -29.646  19.774  22.157  1.00122.60           C  
ANISOU  361  CB  MET A 121    11866  17148  17569   -795   -860   5294       C  
ATOM    362  CG  MET A 121     -29.355  20.562  20.899  1.00122.09           C  
ANISOU  362  CG  MET A 121    11697  17331  17361   -828   -850   5416       C  
ATOM    363  SD  MET A 121     -30.516  21.919  20.659  1.00139.64           S  
ANISOU  363  SD  MET A 121    14043  19469  19546   -897   -903   5620       S  
ATOM    364  CE  MET A 121     -30.201  22.890  22.131  1.00124.47           C  
ANISOU  364  CE  MET A 121    12254  17294  17744   -907   -946   5485       C  
ATOM    365  N   LEU A 122     -27.186  20.180  24.124  1.00105.85           N  
ANISOU  365  N   LEU A 122     9708  14955  15553   -818   -893   5337       N  
ATOM    366  CA  LEU A 122     -25.972  20.878  24.533  1.00105.17           C  
ANISOU  366  CA  LEU A 122     9564  14947  15450   -849   -907   5394       C  
ATOM    367  C   LEU A 122     -24.803  19.912  24.680  1.00 99.93           C  
ANISOU  367  C   LEU A 122     8738  14389  14841   -786   -884   5267       C  
ATOM    368  O   LEU A 122     -23.666  20.248  24.327  1.00 89.50           O  
ANISOU  368  O   LEU A 122     7278  13249  13478   -790   -865   5254       O  
ATOM    369  CB  LEU A 122     -26.214  21.634  25.838  1.00100.10           C  
ANISOU  369  CB  LEU A 122     9063  14128  14843   -906   -969   5469       C  
ATOM    370  CG  LEU A 122     -27.157  22.835  25.751  1.00 91.52           C  
ANISOU  370  CG  LEU A 122     8089  12949  13735   -933  -1004   5445       C  
ATOM    371  CD1 LEU A 122     -27.284  23.514  27.105  1.00 81.29           C  
ANISOU  371  CD1 LEU A 122     6882  11523  12482   -963  -1059   5347       C  
ATOM    372  CD2 LEU A 122     -26.675  23.818  24.693  1.00 67.58           C  
ANISOU  372  CD2 LEU A 122     4963  10072  10644   -954  -1007   5587       C  
ATOM    373  N   LEU A 123     -25.060  18.712  25.205  1.00104.74           N  
ANISOU  373  N   LEU A 123     9346  14885  15563   -724   -894   5174       N  
ATOM    374  CA  LEU A 123     -24.003  17.712  25.321  1.00 97.40           C  
ANISOU  374  CA  LEU A 123     8238  14033  14736   -630   -895   5058       C  
ATOM    375  C   LEU A 123     -23.483  17.300  23.950  1.00 97.71           C  
ANISOU  375  C   LEU A 123     8073  14294  14759   -550   -843   4910       C  
ATOM    376  O   LEU A 123     -22.273  17.137  23.757  1.00 95.78           O  
ANISOU  376  O   LEU A 123     7642  14209  14542   -503   -831   4824       O  
ATOM    377  CB  LEU A 123     -24.520  16.496  26.089  1.00104.28           C  
ANISOU  377  CB  LEU A 123     9143  14717  15762   -574   -934   5021       C  
ATOM    378  CG  LEU A 123     -23.498  15.434  26.500  1.00 92.35           C  
ANISOU  378  CG  LEU A 123     7456  13221  14410   -463   -972   4950       C  
ATOM    379  CD1 LEU A 123     -22.517  16.001  27.514  1.00 96.74           C  
ANISOU  379  CD1 LEU A 123     7998  13824  14933   -522  -1013   5049       C  
ATOM    380  CD2 LEU A 123     -24.197  14.201  27.056  1.00 93.68           C  
ANISOU  380  CD2 LEU A 123     7653  13187  14753   -406  -1016   4943       C  
ATOM    381  N   GLY A 124     -24.387  17.124  22.984  1.00106.63           N  
ANISOU  381  N   GLY A 124     9211  15462  15840   -539   -810   4860       N  
ATOM    382  CA  GLY A 124     -23.972  16.717  21.653  1.00 97.12           C  
ANISOU  382  CA  GLY A 124     7788  14512  14601   -484   -753   4694       C  
ATOM    383  C   GLY A 124     -23.335  17.831  20.849  1.00101.63           C  
ANISOU  383  C   GLY A 124     8288  15333  14995   -580   -713   4773       C  
ATOM    384  O   GLY A 124     -22.498  17.572  19.981  1.00103.22           O  
ANISOU  384  O   GLY A 124     8261  15787  15169   -559   -659   4624       O  
ATOM    385  N   PHE A 125     -23.721  19.080  21.115  1.00108.65           N  
ANISOU  385  N   PHE A 125     9350  16155  15776   -690   -740   5000       N  
ATOM    386  CA  PHE A 125     -23.156  20.208  20.384  1.00115.97           C  
ANISOU  386  CA  PHE A 125    10213  17299  16552   -790   -718   5122       C  
ATOM    387  C   PHE A 125     -21.766  20.589  20.875  1.00 99.81           C  
ANISOU  387  C   PHE A 125     8068  15330  14526   -815   -712   5105       C  
ATOM    388  O   PHE A 125     -20.951  21.076  20.083  1.00101.70           O  
ANISOU  388  O   PHE A 125     8155  15824  14662   -880   -667   5101       O  
ATOM    389  CB  PHE A 125     -24.081  21.421  20.478  1.00118.03           C  
ANISOU  389  CB  PHE A 125    10666  17438  16742   -876   -770   5375       C  
ATOM    390  CG  PHE A 125     -24.987  21.588  19.293  1.00132.91           C  
ANISOU  390  CG  PHE A 125    12538  19459  18501   -906   -763   5455       C  
ATOM    391  CD1 PHE A 125     -24.470  21.928  18.054  1.00134.54           C  
ANISOU  391  CD1 PHE A 125    12575  19998  18548   -972   -726   5494       C  
ATOM    392  CD2 PHE A 125     -26.355  21.425  19.420  1.00130.72           C  
ANISOU  392  CD2 PHE A 125    12407  19009  18252   -885   -794   5494       C  
ATOM    393  CE1 PHE A 125     -25.301  22.090  16.960  1.00139.52           C  
ANISOU  393  CE1 PHE A 125    13178  20801  19031  -1015   -731   5594       C  
ATOM    394  CE2 PHE A 125     -27.193  21.587  18.328  1.00132.56           C  
ANISOU  394  CE2 PHE A 125    12612  19398  18358   -916   -795   5575       C  
ATOM    395  CZ  PHE A 125     -26.664  21.921  17.098  1.00124.90           C  
ANISOU  395  CZ  PHE A 125    11468  18776  17213   -980   -770   5640       C  
ATOM    396  N   LEU A 126     -21.477  20.392  22.160  1.00100.33           N  
ANISOU  396  N   LEU A 126     8204  15208  14708   -782   -755   5096       N  
ATOM    397  CA  LEU A 126     -20.251  20.901  22.759  1.00 88.65           C  
ANISOU  397  CA  LEU A 126     6645  13802  13235   -821   -761   5097       C  
ATOM    398  C   LEU A 126     -19.274  19.794  23.137  1.00 77.03           C  
ANISOU  398  C   LEU A 126     4994  12384  11889   -712   -760   4906       C  
ATOM    399  O   LEU A 126     -18.128  19.800  22.681  1.00 87.51           O  
ANISOU  399  O   LEU A 126     6111  13935  13202   -710   -720   4790       O  
ATOM    400  CB  LEU A 126     -20.591  21.748  23.993  1.00 80.94           C  
ANISOU  400  CB  LEU A 126     5860  12618  12274   -887   -824   5245       C  
ATOM    401  CG  LEU A 126     -21.590  22.892  23.807  1.00 68.90           C  
ANISOU  401  CG  LEU A 126     4502  10987  10690   -964   -855   5422       C  
ATOM    402  CD1 LEU A 126     -21.740  23.690  25.094  1.00 65.07           C  
ANISOU  402  CD1 LEU A 126     4146  10325  10251  -1014   -918   5486       C  
ATOM    403  CD2 LEU A 126     -21.173  23.797  22.658  1.00 67.79           C  
ANISOU  403  CD2 LEU A 126     4257  11059  10440  -1038   -826   5506       C  
ATOM    404  N   VAL A 127     -19.699  18.833  23.956  1.00 72.76           N  
ANISOU  404  N   VAL A 127     4516  11646  11484   -621   -811   4874       N  
ATOM    405  CA  VAL A 127     -18.760  17.865  24.514  1.00 86.05           C  
ANISOU  405  CA  VAL A 127     6032  13346  13316   -506   -846   4747       C  
ATOM    406  C   VAL A 127     -18.417  16.785  23.495  1.00 94.73           C  
ANISOU  406  C   VAL A 127     6896  14576  14521   -371   -808   4515       C  
ATOM    407  O   VAL A 127     -17.246  16.423  23.321  1.00107.80           O  
ANISOU  407  O   VAL A 127     8312  16394  16253   -299   -801   4358       O  
ATOM    408  CB  VAL A 127     -19.334  17.260  25.808  1.00 93.47           C  
ANISOU  408  CB  VAL A 127     7116  14032  14366   -475   -925   4839       C  
ATOM    409  CG1 VAL A 127     -18.326  16.321  26.443  1.00 79.21           C  
ANISOU  409  CG1 VAL A 127     5131  12245  12719   -353   -987   4762       C  
ATOM    410  CG2 VAL A 127     -19.732  18.363  26.777  1.00 88.26           C  
ANISOU  410  CG2 VAL A 127     6662  13275  13599   -622   -951   5022       C  
ATOM    411  N   MET A 128     -19.432  16.246  22.822  1.00115.93           N  
ANISOU  411  N   MET A 128     9622  17203  17224   -334   -783   4461       N  
ATOM    412  CA  MET A 128     -19.210  15.140  21.893  1.00126.25           C  
ANISOU  412  CA  MET A 128    10684  18628  18659   -203   -744   4199       C  
ATOM    413  C   MET A 128     -18.283  15.492  20.733  1.00129.21           C  
ANISOU  413  C   MET A 128    10812  19341  18940   -246   -653   4032       C  
ATOM    414  O   MET A 128     -17.402  14.673  20.415  1.00136.46           O  
ANISOU  414  O   MET A 128    11452  20381  20016   -130   -633   3782       O  
ATOM    415  CB  MET A 128     -20.563  14.615  21.401  1.00123.18           C  
ANISOU  415  CB  MET A 128    10388  18134  18280   -183   -728   4171       C  
ATOM    416  CG  MET A 128     -21.417  14.015  22.511  1.00111.64           C  
ANISOU  416  CG  MET A 128     9120  16347  16953   -136   -807   4287       C  
ATOM    417  SD  MET A 128     -22.991  13.350  21.937  1.00112.99           S  
ANISOU  417  SD  MET A 128     9373  16407  17151   -115   -785   4221       S  
ATOM    418  CE  MET A 128     -22.432  12.111  20.774  1.00109.20           C  
ANISOU  418  CE  MET A 128     8525  16117  16851     42   -721   3859       C  
ATOM    419  N   PRO A 129     -18.422  16.635  20.045  1.00100.51           N  
ANISOU  419  N   PRO A 129     7241  15876  15071   -410   -595   4150       N  
ATOM    420  CA  PRO A 129     -17.453  16.944  18.978  1.00104.50           C  
ANISOU  420  CA  PRO A 129     7496  16729  15480   -480   -499   3998       C  
ATOM    421  C   PRO A 129     -16.032  17.126  19.486  1.00 97.84           C  
ANISOU  421  C   PRO A 129     6497  15977  14701   -469   -506   3928       C  
ATOM    422  O   PRO A 129     -15.077  16.752  18.792  1.00 83.53           O  
ANISOU  422  O   PRO A 129     4393  14408  12939   -447   -435   3675       O  
ATOM    423  CB  PRO A 129     -18.010  18.236  18.365  1.00101.38           C  
ANISOU  423  CB  PRO A 129     7258  16443  14819   -668   -468   4240       C  
ATOM    424  CG  PRO A 129     -18.785  18.857  19.459  1.00102.57           C  
ANISOU  424  CG  PRO A 129     7713  16290  14967   -689   -558   4510       C  
ATOM    425  CD  PRO A 129     -19.416  17.713  20.191  1.00 97.41           C  
ANISOU  425  CD  PRO A 129     7129  15378  14506   -541   -615   4429       C  
ATOM    426  N   VAL A 130     -15.864  17.695  20.682  1.00 98.45           N  
ANISOU  426  N   VAL A 130     6744  15883  14780   -492   -583   4123       N  
ATOM    427  CA  VAL A 130     -14.527  17.831  21.254  1.00 81.05           C  
ANISOU  427  CA  VAL A 130     4383  13776  12637   -478   -600   4049       C  
ATOM    428  C   VAL A 130     -13.932  16.459  21.538  1.00 83.01           C  
ANISOU  428  C   VAL A 130     4407  13990  13142   -267   -648   3815       C  
ATOM    429  O   VAL A 130     -12.751  16.210  21.266  1.00104.40           O  
ANISOU  429  O   VAL A 130     6834  16898  15934   -219   -620   3600       O  
ATOM    430  CB  VAL A 130     -14.569  18.709  22.519  1.00 79.25           C  
ANISOU  430  CB  VAL A 130     4374  13386  12350   -559   -671   4292       C  
ATOM    431  CG1 VAL A 130     -13.209  18.729  23.196  1.00 81.16           C  
ANISOU  431  CG1 VAL A 130     4437  13740  12659   -532   -701   4202       C  
ATOM    432  CG2 VAL A 130     -15.002  20.123  22.165  1.00 78.01           C  
ANISOU  432  CG2 VAL A 130     4385  13270  11987   -751   -628   4494       C  
ATOM    433  N   SER A 131     -14.740  15.544  22.079  1.00 83.21           N  
ANISOU  433  N   SER A 131     4540  13759  13316   -136   -724   3851       N  
ATOM    434  CA  SER A 131     -14.263  14.183  22.305  1.00 87.63           C  
ANISOU  434  CA  SER A 131     4885  14256  14156     84   -784   3654       C  
ATOM    435  C   SER A 131     -13.908  13.498  20.990  1.00104.36           C  
ANISOU  435  C   SER A 131     6686  16588  16377    158   -687   3308       C  
ATOM    436  O   SER A 131     -12.919  12.760  20.910  1.00112.84           O  
ANISOU  436  O   SER A 131     7461  17756  17659    306   -699   3063       O  
ATOM    437  CB  SER A 131     -15.315  13.377  23.067  1.00 99.36           C  
ANISOU  437  CB  SER A 131     6564  15415  15774    180   -873   3792       C  
ATOM    438  OG  SER A 131     -14.850  12.068  23.350  1.00 96.82           O  
ANISOU  438  OG  SER A 131     6041  14999  15746    402   -947   3650       O  
ATOM    439  N   MET A 132     -14.707  13.729  19.946  1.00103.95           N  
ANISOU  439  N   MET A 132     6676  16634  16186     54   -587   3268       N  
ATOM    440  CA  MET A 132     -14.425  13.135  18.641  1.00108.76           C  
ANISOU  440  CA  MET A 132     6968  17490  16867     80   -468   2914       C  
ATOM    441  C   MET A 132     -13.106  13.646  18.074  1.00109.11           C  
ANISOU  441  C   MET A 132     6751  17851  16854     -8   -380   2738       C  
ATOM    442  O   MET A 132     -12.296  12.869  17.553  1.00 94.44           O  
ANISOU  442  O   MET A 132     4538  16142  15202     94   -325   2381       O  
ATOM    443  CB  MET A 132     -15.573  13.430  17.676  1.00 98.20           C  
ANISOU  443  CB  MET A 132     5747  16231  15335    -54   -382   2952       C  
ATOM    444  CG  MET A 132     -15.354  12.892  16.272  1.00109.38           C  
ANISOU  444  CG  MET A 132     6833  17943  16785    -78   -235   2581       C  
ATOM    445  SD  MET A 132     -16.514  13.581  15.077  1.00109.03           S  
ANISOU  445  SD  MET A 132     6928  18098  16401   -297   -135   2698       S  
ATOM    446  CE  MET A 132     -16.090  15.319  15.163  1.00 93.82           C  
ANISOU  446  CE  MET A 132     5207  16311  14131   -520   -141   3069       C  
ATOM    447  N   LEU A 133     -12.877  14.960  18.158  1.00118.82           N  
ANISOU  447  N   LEU A 133     8137  19184  17823   -202   -359   2972       N  
ATOM    448  CA  LEU A 133     -11.622  15.525  17.669  1.00116.61           C  
ANISOU  448  CA  LEU A 133     7628  19202  17476   -313   -270   2835       C  
ATOM    449  C   LEU A 133     -10.437  15.067  18.507  1.00115.54           C  
ANISOU  449  C   LEU A 133     7294  19035  17569   -160   -347   2693       C  
ATOM    450  O   LEU A 133      -9.328  14.919  17.981  1.00118.66           O  
ANISOU  450  O   LEU A 133     7367  19663  18055   -162   -270   2413       O  
ATOM    451  CB  LEU A 133     -11.700  17.051  17.642  1.00119.57           C  
ANISOU  451  CB  LEU A 133     8230  19668  17534   -553   -240   3147       C  
ATOM    452  CG  LEU A 133     -12.280  17.656  16.362  1.00133.63           C  
ANISOU  452  CG  LEU A 133    10050  21672  19052   -747   -125   3215       C  
ATOM    453  CD1 LEU A 133     -12.370  19.170  16.472  1.00143.03           C  
ANISOU  453  CD1 LEU A 133    11468  22901  19975   -957   -128   3560       C  
ATOM    454  CD2 LEU A 133     -11.439  17.253  15.159  1.00127.22           C  
ANISOU  454  CD2 LEU A 133     8877  21210  18251   -803     24   2873       C  
ATOM    455  N   THR A 134     -10.645  14.851  19.808  1.00104.26           N  
ANISOU  455  N   THR A 134     6047  17335  16233    -37   -498   2888       N  
ATOM    456  CA  THR A 134      -9.601  14.261  20.636  1.00104.65           C  
ANISOU  456  CA  THR A 134     5902  17356  16506    137   -600   2774       C  
ATOM    457  C   THR A 134      -9.287  12.839  20.187  1.00112.92           C  
ANISOU  457  C   THR A 134     6619  18412  17874    373   -606   2419       C  
ATOM    458  O   THR A 134      -8.120  12.429  20.162  1.00120.80           O  
ANISOU  458  O   THR A 134     7292  19551  19057    485   -616   2162       O  
ATOM    459  CB  THR A 134     -10.027  14.285  22.105  1.00108.78           C  
ANISOU  459  CB  THR A 134     6703  17594  17035    196   -757   3092       C  
ATOM    460  OG1 THR A 134     -10.267  15.639  22.511  1.00105.85           O  
ANISOU  460  OG1 THR A 134     6594  17229  16394    -26   -737   3366       O  
ATOM    461  CG2 THR A 134      -8.950  13.685  22.992  1.00107.25           C  
ANISOU  461  CG2 THR A 134     6310  17394  17047    374   -881   3018       C  
ATOM    462  N   ILE A 135     -10.319  12.072  19.826  1.00122.96           N  
ANISOU  462  N   ILE A 135     7951  19537  19231    454   -597   2382       N  
ATOM    463  CA  ILE A 135     -10.106  10.714  19.325  1.00135.87           C  
ANISOU  463  CA  ILE A 135     9257  21184  21183    676   -582   2018       C  
ATOM    464  C   ILE A 135      -9.312  10.744  18.023  1.00140.54           C  
ANISOU  464  C   ILE A 135     9465  22120  21812    593   -407   1597       C  
ATOM    465  O   ILE A 135      -8.339  10.001  17.851  1.00115.88           O  
ANISOU  465  O   ILE A 135     5965  19109  18956    756   -401   1248       O  
ATOM    466  CB  ILE A 135     -11.451   9.987  19.144  1.00129.22           C  
ANISOU  466  CB  ILE A 135     8565  20129  20403    742   -582   2064       C  
ATOM    467  CG1 ILE A 135     -12.017   9.554  20.498  1.00140.52           C  
ANISOU  467  CG1 ILE A 135    10275  21179  21936    876   -759   2406       C  
ATOM    468  CG2 ILE A 135     -11.294   8.786  18.217  1.00130.59           C  
ANISOU  468  CG2 ILE A 135     8354  20419  20844    900   -491   1613       C  
ATOM    469  CD1 ILE A 135     -13.142   8.549  20.388  1.00129.17           C  
ANISOU  469  CD1 ILE A 135     8909  19501  20668    990   -766   2400       C  
ATOM    470  N   LEU A 136      -9.715  11.610  17.088  1.00138.34           N  
ANISOU  470  N   LEU A 136     9276  22017  21272    333   -258   1637       N  
ATOM    471  CA  LEU A 136      -9.020  11.683  15.806  1.00117.30           C  
ANISOU  471  CA  LEU A 136     6273  19658  18640    203    -66   1292       C  
ATOM    472  C   LEU A 136      -7.587  12.171  15.975  1.00107.62           C  
ANISOU  472  C   LEU A 136     4842  18596  17454    162    -50   1206       C  
ATOM    473  O   LEU A 136      -6.720  11.837  15.160  1.00117.45           O  
ANISOU  473  O   LEU A 136     5708  20013  18904    146     83    858       O  
ATOM    474  CB  LEU A 136      -9.788  12.583  14.836  1.00108.29           C  
ANISOU  474  CB  LEU A 136     5322  18689  17133    -78     70   1467       C  
ATOM    475  CG  LEU A 136      -9.415  12.478  13.354  1.00107.07           C  
ANISOU  475  CG  LEU A 136     4864  18844  16973   -230    291   1171       C  
ATOM    476  CD1 LEU A 136     -10.657  12.574  12.485  1.00105.78           C  
ANISOU  476  CD1 LEU A 136     4860  18769  16563   -369    373   1262       C  
ATOM    477  CD2 LEU A 136      -8.407  13.549  12.959  1.00111.56           C  
ANISOU  477  CD2 LEU A 136     5381  19714  17294   -452    386   1250       C  
ATOM    478  N   TYR A 137      -7.319  12.951  17.021  1.00107.37           N  
ANISOU  478  N   TYR A 137     5040  18494  17261    134   -171   1521       N  
ATOM    479  CA  TYR A 137      -5.958  13.364  17.336  1.00111.61           C  
ANISOU  479  CA  TYR A 137     5381  19176  17850    112   -176   1437       C  
ATOM    480  C   TYR A 137      -5.207  12.332  18.166  1.00110.28           C  
ANISOU  480  C   TYR A 137     4967  18895  18038    416   -329   1238       C  
ATOM    481  O   TYR A 137      -4.013  12.518  18.418  1.00112.64           O  
ANISOU  481  O   TYR A 137     5043  19316  18438    432   -344   1114       O  
ATOM    482  CB  TYR A 137      -5.965  14.711  18.070  1.00107.44           C  
ANISOU  482  CB  TYR A 137     5180  18650  16993    -72   -221   1837       C  
ATOM    483  CG  TYR A 137      -6.169  15.911  17.167  1.00104.38           C  
ANISOU  483  CG  TYR A 137     4924  18482  16253   -384    -62   1985       C  
ATOM    484  CD1 TYR A 137      -6.520  15.753  15.832  1.00105.58           C  
ANISOU  484  CD1 TYR A 137     4970  18814  16332   -494     96   1836       C  
ATOM    485  CD2 TYR A 137      -5.993  17.202  17.647  1.00102.81           C  
ANISOU  485  CD2 TYR A 137     4946  18327  15789   -572    -70   2279       C  
ATOM    486  CE1 TYR A 137      -6.702  16.847  15.005  1.00105.28           C  
ANISOU  486  CE1 TYR A 137     5062  19013  15927   -777    221   2014       C  
ATOM    487  CE2 TYR A 137      -6.172  18.302  16.827  1.00102.50           C  
ANISOU  487  CE2 TYR A 137     5025  18491  15431   -846     59   2436       C  
ATOM    488  CZ  TYR A 137      -6.526  18.119  15.508  1.00103.78           C  
ANISOU  488  CZ  TYR A 137     5095  18847  15489   -945    194   2321       C  
ATOM    489  OH  TYR A 137      -6.705  19.209  14.687  1.00103.87           O  
ANISOU  489  OH  TYR A 137     5228  19088  15150  -1220    300   2516       O  
ATOM    490  N   GLY A 138      -5.867  11.257  18.591  1.00129.54           N  
ANISOU  490  N   GLY A 138     7444  21122  20653    659   -447   1226       N  
ATOM    491  CA  GLY A 138      -5.200  10.198  19.324  1.00133.40           C  
ANISOU  491  CA  GLY A 138     7706  21541  21439    977   -604   1081       C  
ATOM    492  C   GLY A 138      -5.255  10.359  20.829  1.00153.76           C  
ANISOU  492  C   GLY A 138    10567  23902  23952   1067   -812   1499       C  
ATOM    493  O   GLY A 138      -4.248  10.157  21.515  1.00136.78           O  
ANISOU  493  O   GLY A 138     8239  21800  21930   1209   -929   1460       O  
ATOM    494  N   TYR A 139      -6.433  10.711  21.351  1.00213.51           N  
ANISOU  494  N   TYR A 139    18558  31231  31334    974   -857   1889       N  
ATOM    495  CA  TYR A 139      -6.642  10.918  22.786  1.00215.29           C  
ANISOU  495  CA  TYR A 139    19075  31230  31495   1002  -1028   2294       C  
ATOM    496  C   TYR A 139      -5.672  11.961  23.341  1.00200.64           C  
ANISOU  496  C   TYR A 139    17201  29553  29479    861  -1046   2373       C  
ATOM    497  O   TYR A 139      -5.058  11.780  24.394  1.00198.16           O  
ANISOU  497  O   TYR A 139    16851  29198  29241    974  -1196   2488       O  
ATOM    498  CB  TYR A 139      -6.536   9.598  23.556  1.00204.03           C  
ANISOU  498  CB  TYR A 139    17561  29584  30375   1316  -1200   2334       C  
ATOM    499  CG  TYR A 139      -7.467   8.522  23.045  1.00208.19           C  
ANISOU  499  CG  TYR A 139    18095  29914  31093   1461  -1173   2260       C  
ATOM    500  CD1 TYR A 139      -8.845   8.698  23.078  1.00213.79           C  
ANISOU  500  CD1 TYR A 139    19153  30404  31672   1335  -1143   2496       C  
ATOM    501  CD2 TYR A 139      -6.971   7.329  22.536  1.00203.42           C  
ANISOU  501  CD2 TYR A 139    17134  29353  30805   1726  -1169   1945       C  
ATOM    502  CE1 TYR A 139      -9.701   7.720  22.612  1.00205.62           C  
ANISOU  502  CE1 TYR A 139    18112  29190  30823   1455  -1110   2416       C  
ATOM    503  CE2 TYR A 139      -7.821   6.343  22.070  1.00204.20           C  
ANISOU  503  CE2 TYR A 139    17228  29267  31093   1852  -1124   1877       C  
ATOM    504  CZ  TYR A 139      -9.184   6.544  22.111  1.00204.17           C  
ANISOU  504  CZ  TYR A 139    17575  29038  30964   1709  -1097   2108       C  
ATOM    505  OH  TYR A 139     -10.035   5.566  21.647  1.00205.60           O  
ANISOU  505  OH  TYR A 139    17739  29030  31349   1822  -1045   2025       O  
ATOM    506  N   ARG A 140      -5.536  13.066  22.611  1.00141.99           N  
ANISOU  506  N   ARG A 140     9794  22332  21825    603   -888   2325       N  
ATOM    507  CA  ARG A 140      -4.654  14.162  22.986  1.00109.88           C  
ANISOU  507  CA  ARG A 140     5708  18448  17593    432   -867   2387       C  
ATOM    508  C   ARG A 140      -5.434  15.468  22.960  1.00113.53           C  
ANISOU  508  C   ARG A 140     6525  18892  17718    148   -779   2678       C  
ATOM    509  O   ARG A 140      -6.283  15.676  22.088  1.00114.86           O  
ANISOU  509  O   ARG A 140     6821  19049  17773     41   -670   2702       O  
ATOM    510  CB  ARG A 140      -3.446  14.237  22.045  1.00123.70           C  
ANISOU  510  CB  ARG A 140     7059  20497  19445    395   -745   2006       C  
ATOM    511  CG  ARG A 140      -2.713  12.914  21.903  1.00138.35           C  
ANISOU  511  CG  ARG A 140     8515  22376  21676    690   -818   1651       C  
ATOM    512  CD  ARG A 140      -1.818  12.897  20.680  1.00142.74           C  
ANISOU  512  CD  ARG A 140     8674  23182  22379    623   -644   1228       C  
ATOM    513  NE  ARG A 140      -0.501  13.461  20.947  1.00117.99           N  
ANISOU  513  NE  ARG A 140     5323  20232  19278    556   -640   1137       N  
ATOM    514  CZ  ARG A 140       0.424  13.664  20.019  1.00120.73           C  
ANISOU  514  CZ  ARG A 140     5345  20775  19754    443   -476    852       C  
ATOM    515  NH1 ARG A 140       0.195  13.392  18.745  1.00121.80           N  
ANISOU  515  NH1 ARG A 140     5336  20957  19986    366   -291    648       N  
ATOM    516  NH2 ARG A 140       1.608  14.150  20.380  1.00137.72           N  
ANISOU  516  NH2 ARG A 140     7310  23071  21945    391   -485    806       N  
ATOM    517  N   TRP A 141      -5.137  16.346  23.916  1.00112.75           N  
ANISOU  517  N   TRP A 141     6567  18804  17470     31   -829   2889       N  
ATOM    518  CA  TRP A 141      -5.904  17.575  24.100  1.00121.81           C  
ANISOU  518  CA  TRP A 141     8051  19893  18338   -210   -771   3174       C  
ATOM    519  C   TRP A 141      -5.371  18.665  23.179  1.00126.16           C  
ANISOU  519  C   TRP A 141     8523  20700  18714   -444   -604   3092       C  
ATOM    520  O   TRP A 141      -4.217  19.085  23.339  1.00137.52           O  
ANISOU  520  O   TRP A 141     9761  22337  20154   -505   -579   2972       O  
ATOM    521  CB  TRP A 141      -5.828  18.027  25.550  1.00108.43           C  
ANISOU  521  CB  TRP A 141     6513  18108  16577   -244   -886   3401       C  
ATOM    522  CG  TRP A 141      -6.654  19.233  25.875  1.00107.43           C  
ANISOU  522  CG  TRP A 141     6714  17888  16217   -467   -840   3663       C  
ATOM    523  CD1 TRP A 141      -6.194  20.473  26.209  1.00105.18           C  
ANISOU  523  CD1 TRP A 141     6465  17724  15774   -670   -789   3722       C  
ATOM    524  CD2 TRP A 141      -8.084  19.313  25.908  1.00124.01           C  
ANISOU  524  CD2 TRP A 141     9130  19743  18246   -502   -845   3875       C  
ATOM    525  NE1 TRP A 141      -7.249  21.322  26.443  1.00111.98           N  
ANISOU  525  NE1 TRP A 141     7639  18421  16488   -816   -768   3951       N  
ATOM    526  CE2 TRP A 141      -8.421  20.634  26.265  1.00118.50           C  
ANISOU  526  CE2 TRP A 141     8640  19025  17362   -715   -804   4052       C  
ATOM    527  CE3 TRP A 141      -9.113  18.397  25.665  1.00114.91           C  
ANISOU  527  CE3 TRP A 141     8090  18383  17187   -373   -878   3915       C  
ATOM    528  CZ2 TRP A 141      -9.742  21.060  26.387  1.00 97.28           C  
ANISOU  528  CZ2 TRP A 141     6258  16116  14588   -789   -804   4261       C  
ATOM    529  CZ3 TRP A 141     -10.422  18.822  25.788  1.00102.66           C  
ANISOU  529  CZ3 TRP A 141     6851  16625  15528   -464   -870   4131       C  
ATOM    530  CH2 TRP A 141     -10.725  20.142  26.144  1.00 96.00           C  
ANISOU  530  CH2 TRP A 141     6201  15767  14507   -664   -837   4301       C  
ATOM    531  N   PRO A 142      -6.162  19.152  22.213  1.00119.64           N  
ANISOU  531  N   PRO A 142     7843  19885  17730   -587   -490   3168       N  
ATOM    532  CA  PRO A 142      -5.654  20.175  21.289  1.00118.38           C  
ANISOU  532  CA  PRO A 142     7610  19980  17390   -823   -334   3128       C  
ATOM    533  C   PRO A 142      -6.003  21.600  21.695  1.00110.23           C  
ANISOU  533  C   PRO A 142     6848  18900  16136  -1044   -314   3411       C  
ATOM    534  O   PRO A 142      -5.476  22.559  21.123  1.00112.75           O  
ANISOU  534  O   PRO A 142     7115  19414  16310  -1252   -200   3410       O  
ATOM    535  CB  PRO A 142      -6.333  19.797  19.971  1.00107.06           C  
ANISOU  535  CB  PRO A 142     6158  18606  15914   -841   -236   3055       C  
ATOM    536  CG  PRO A 142      -7.670  19.270  20.416  1.00123.37           C  
ANISOU  536  CG  PRO A 142     8484  20371  18019   -715   -339   3232       C  
ATOM    537  CD  PRO A 142      -7.462  18.616  21.771  1.00119.76           C  
ANISOU  537  CD  PRO A 142     8036  19719  17749   -523   -497   3251       C  
ATOM    538  N   LEU A 143      -6.887  21.750  22.671  1.00102.28           N  
ANISOU  538  N   LEU A 143     6117  17629  15115  -1009   -421   3643       N  
ATOM    539  CA  LEU A 143      -7.344  23.056  23.121  1.00109.25           C  
ANISOU  539  CA  LEU A 143     7248  18418  15842  -1197   -413   3884       C  
ATOM    540  C   LEU A 143      -6.376  23.628  24.145  1.00 98.58           C  
ANISOU  540  C   LEU A 143     5815  17140  14499  -1263   -439   3845       C  
ATOM    541  O   LEU A 143      -5.495  22.928  24.647  1.00105.27           O  
ANISOU  541  O   LEU A 143     6449  18081  15470  -1138   -494   3680       O  
ATOM    542  CB  LEU A 143      -8.750  22.932  23.701  1.00120.74           C  
ANISOU  542  CB  LEU A 143     9010  19564  17300  -1135   -505   4109       C  
ATOM    543  CG  LEU A 143      -9.857  22.489  22.746  1.00113.05           C  
ANISOU  543  CG  LEU A 143     8146  18506  16303  -1089   -482   4169       C  
ATOM    544  CD1 LEU A 143     -11.204  22.481  23.453  1.00 86.41           C  
ANISOU  544  CD1 LEU A 143     5073  14821  12937  -1046   -571   4385       C  
ATOM    545  CD2 LEU A 143      -9.897  23.388  21.520  1.00101.88           C  
ANISOU  545  CD2 LEU A 143     6723  17265  14721  -1274   -368   4224       C  
ATOM    546  N   PRO A 144      -6.492  24.920  24.459  1.00 95.72           N  
ANISOU  546  N   PRO A 144     5599  16745  14024  -1460   -402   3978       N  
ATOM    547  CA  PRO A 144      -5.684  25.482  25.547  1.00 96.74           C  
ANISOU  547  CA  PRO A 144     5662  16934  14162  -1533   -426   3926       C  
ATOM    548  C   PRO A 144      -5.932  24.751  26.858  1.00 96.62           C  
ANISOU  548  C   PRO A 144     5701  16780  14230  -1376   -575   3970       C  
ATOM    549  O   PRO A 144      -7.045  24.304  27.149  1.00105.50           O  
ANISOU  549  O   PRO A 144     7033  17677  15374  -1285   -649   4120       O  
ATOM    550  CB  PRO A 144      -6.153  26.939  25.620  1.00 90.54           C  
ANISOU  550  CB  PRO A 144     5072  16050  13277  -1754   -365   4070       C  
ATOM    551  CG  PRO A 144      -6.593  27.247  24.234  1.00 93.42           C  
ANISOU  551  CG  PRO A 144     5486  16445  13565  -1834   -274   4149       C  
ATOM    552  CD  PRO A 144      -7.194  25.973  23.699  1.00 94.07           C  
ANISOU  552  CD  PRO A 144     5568  16486  13689  -1636   -324   4146       C  
ATOM    553  N   SER A 145      -4.864  24.628  27.652  1.00 99.17           N  
ANISOU  553  N   SER A 145     9097  11551  17032  -1492   -534   2150       N  
ATOM    554  CA  SER A 145      -4.910  23.818  28.865  1.00100.86           C  
ANISOU  554  CA  SER A 145     9407  11797  17115  -1475   -452   1869       C  
ATOM    555  C   SER A 145      -5.916  24.334  29.886  1.00 91.20           C  
ANISOU  555  C   SER A 145     8199  10375  16078  -1433   -451   1694       C  
ATOM    556  O   SER A 145      -6.381  23.556  30.726  1.00 89.10           O  
ANISOU  556  O   SER A 145     8014  10157  15682  -1401   -372   1486       O  
ATOM    557  CB  SER A 145      -3.516  23.747  29.495  1.00102.70           C  
ANISOU  557  CB  SER A 145     9639  12083  17300  -1537   -470   1802       C  
ATOM    558  OG  SER A 145      -2.978  25.042  29.701  1.00 98.19           O  
ANISOU  558  OG  SER A 145     8982  11337  16990  -1593   -575   1863       O  
ATOM    559  N   LYS A 146      -6.266  25.621  29.838  1.00 87.10           N  
ANISOU  559  N   LYS A 146     7595   9631  15868  -1430   -533   1776       N  
ATOM    560  CA  LYS A 146      -7.218  26.171  30.795  1.00 99.07           C  
ANISOU  560  CA  LYS A 146     9111  10944  17586  -1387   -527   1598       C  
ATOM    561  C   LYS A 146      -8.662  25.797  30.483  1.00101.13           C  
ANISOU  561  C   LYS A 146     9397  11213  17815  -1307   -471   1602       C  
ATOM    562  O   LYS A 146      -9.522  25.920  31.363  1.00 84.60           O  
ANISOU  562  O   LYS A 146     7326   9002  15816  -1261   -438   1416       O  
ATOM    563  CB  LYS A 146      -7.084  27.694  30.858  1.00 91.83           C  
ANISOU  563  CB  LYS A 146     8081   9761  17048  -1410   -623   1672       C  
ATOM    564  CG  LYS A 146      -5.934  28.171  31.727  1.00 66.86           C  
ANISOU  564  CG  LYS A 146     4902   6542  13959  -1503   -664   1536       C  
ATOM    565  CD  LYS A 146      -6.090  27.657  33.150  1.00 61.39           C  
ANISOU  565  CD  LYS A 146     4276   5862  13188  -1505   -609   1222       C  
ATOM    566  CE  LYS A 146      -4.942  28.104  34.037  1.00 77.12           C  
ANISOU  566  CE  LYS A 146     6234   7826  15243  -1618   -655   1086       C  
ATOM    567  NZ  LYS A 146      -5.101  27.600  35.429  1.00 62.02           N  
ANISOU  567  NZ  LYS A 146     4368   5955  13243  -1628   -608    791       N  
ATOM    568  N   LEU A 147      -8.950  25.347  29.263  1.00 95.96           N  
ANISOU  568  N   LEU A 147     8732  10708  17018  -1298   -457   1801       N  
ATOM    569  CA  LEU A 147     -10.309  24.992  28.878  1.00 82.99           C  
ANISOU  569  CA  LEU A 147     7102   9107  15325  -1243   -405   1817       C  
ATOM    570  C   LEU A 147     -10.674  23.551  29.212  1.00 88.94           C  
ANISOU  570  C   LEU A 147     7974  10059  15761  -1232   -290   1629       C  
ATOM    571  O   LEU A 147     -11.861  23.209  29.173  1.00101.58           O  
ANISOU  571  O   LEU A 147     9594  11685  17316  -1193   -236   1581       O  
ATOM    572  CB  LEU A 147     -10.515  25.233  27.379  1.00 66.63           C  
ANISOU  572  CB  LEU A 147     4944   7128  13243  -1257   -447   2122       C  
ATOM    573  CG  LEU A 147     -10.293  26.672  26.907  1.00 78.13           C  
ANISOU  573  CG  LEU A 147     6264   8386  15036  -1258   -563   2366       C  
ATOM    574  CD1 LEU A 147     -10.685  26.834  25.445  1.00 69.95           C  
ANISOU  574  CD1 LEU A 147     5135   7477  13965  -1267   -600   2686       C  
ATOM    575  CD2 LEU A 147     -11.057  27.653  27.787  1.00 85.07           C  
ANISOU  575  CD2 LEU A 147     7095   8967  16261  -1198   -584   2263       C  
ATOM    576  N   CYS A 148      -9.694  22.710  29.551  1.00 91.48           N  
ANISOU  576  N   CYS A 148     8364  10519  15876  -1267   -247   1530       N  
ATOM    577  CA  CYS A 148      -9.986  21.312  29.857  1.00 93.33           C  
ANISOU  577  CA  CYS A 148     8699  10928  15832  -1255   -132   1369       C  
ATOM    578  C   CYS A 148     -10.952  21.199  31.028  1.00 94.85           C  
ANISOU  578  C   CYS A 148     8943  11023  16074  -1201    -88   1156       C  
ATOM    579  O   CYS A 148     -11.937  20.453  30.967  1.00 94.44           O  
ANISOU  579  O   CYS A 148     8938  11054  15891  -1174    -11   1088       O  
ATOM    580  CB  CYS A 148      -8.688  20.559  30.149  1.00 94.87           C  
ANISOU  580  CB  CYS A 148     8939  11253  15854  -1291   -100   1313       C  
ATOM    581  SG  CYS A 148      -8.919  18.913  30.862  1.00 60.21           S  
ANISOU  581  SG  CYS A 148     4664   7024  11189  -1265     41   1104       S  
ATOM    582  N   ALA A 149     -10.699  21.961  32.096  1.00123.57           N  
ANISOU  582  N   ALA A 149    12561  14490  19899  -1195   -136   1042       N  
ATOM    583  CA  ALA A 149     -11.609  21.966  33.236  1.00126.58           C  
ANISOU  583  CA  ALA A 149    12975  14776  20344  -1147    -99    834       C  
ATOM    584  C   ALA A 149     -13.011  22.394  32.826  1.00122.09           C  
ANISOU  584  C   ALA A 149    12370  14112  19907  -1094    -95    880       C  
ATOM    585  O   ALA A 149     -13.996  21.957  33.433  1.00122.60           O  
ANISOU  585  O   ALA A 149    12479  14181  19925  -1049    -32    733       O  
ATOM    586  CB  ALA A 149     -11.071  22.882  34.335  1.00134.67           C  
ANISOU  586  CB  ALA A 149    13961  15637  21571  -1169   -160    701       C  
ATOM    587  N   VAL A 150     -13.123  23.244  31.804  1.00 88.19           N  
ANISOU  587  N   VAL A 150     7987   9742  15780  -1098   -163   1097       N  
ATOM    588  CA  VAL A 150     -14.439  23.588  31.274  1.00 83.55           C  
ANISOU  588  CA  VAL A 150     7347   9101  15298  -1053   -158   1184       C  
ATOM    589  C   VAL A 150     -15.091  22.361  30.649  1.00 84.19           C  
ANISOU  589  C   VAL A 150     7488   9426  15074  -1063    -71   1192       C  
ATOM    590  O   VAL A 150     -16.243  22.028  30.955  1.00 94.84           O  
ANISOU  590  O   VAL A 150     8859  10789  16388  -1026    -14   1093       O  
ATOM    591  CB  VAL A 150     -14.326  24.743  30.263  1.00 81.78           C  
ANISOU  591  CB  VAL A 150     6997   8762  15315  -1059   -253   1458       C  
ATOM    592  CG1 VAL A 150     -15.658  24.968  29.565  1.00 83.51           C  
ANISOU  592  CG1 VAL A 150     7145   8974  15612  -1019   -246   1597       C  
ATOM    593  CG2 VAL A 150     -13.863  26.013  30.959  1.00 75.96           C  
ANISOU  593  CG2 VAL A 150     6158   7703  15000  -1036   -336   1445       C  
ATOM    594  N   TRP A 151     -14.345  21.653  29.795  1.00 79.68           N  
ANISOU  594  N   TRP A 151     6940   9056  14280  -1120    -55   1292       N  
ATOM    595  CA  TRP A 151     -14.898  20.529  29.043  1.00 78.78           C  
ANISOU  595  CA  TRP A 151     6864   9184  13886  -1151     30   1294       C  
ATOM    596  C   TRP A 151     -15.572  19.526  29.970  1.00 89.93           C  
ANISOU  596  C   TRP A 151     8374  10647  15147  -1123    131   1060       C  
ATOM    597  O   TRP A 151     -16.782  19.283  29.875  1.00 92.19           O  
ANISOU  597  O   TRP A 151     8658  10979  15392  -1109    175   1024       O  
ATOM    598  CB  TRP A 151     -13.785  19.861  28.232  1.00 80.09           C  
ANISOU  598  CB  TRP A 151     7046   9538  13847  -1217     47   1371       C  
ATOM    599  CG  TRP A 151     -14.236  18.708  27.391  1.00 74.67           C  
ANISOU  599  CG  TRP A 151     6385   9105  12881  -1268    142   1348       C  
ATOM    600  CD1 TRP A 151     -14.942  18.771  26.225  1.00 64.34           C  
ANISOU  600  CD1 TRP A 151     5003   7934  11511  -1310    141   1479       C  
ATOM    601  CD2 TRP A 151     -13.994  17.317  27.638  1.00 81.27           C  
ANISOU  601  CD2 TRP A 151     7316  10094  13469  -1292    257   1177       C  
ATOM    602  NE1 TRP A 151     -15.161  17.506  25.735  1.00 74.74           N  
ANISOU  602  NE1 TRP A 151     6363   9485  12550  -1372    253   1367       N  
ATOM    603  CE2 TRP A 151     -14.589  16.595  26.584  1.00 84.34           C  
ANISOU  603  CE2 TRP A 151     7685  10700  13659  -1359    327   1184       C  
ATOM    604  CE3 TRP A 151     -13.335  16.611  28.650  1.00 79.57           C  
ANISOU  604  CE3 TRP A 151     7189   9855  13187  -1267    308   1025       C  
ATOM    605  CZ2 TRP A 151     -14.546  15.204  26.513  1.00 78.48           C  
ANISOU  605  CZ2 TRP A 151     7014  10129  12676  -1404    453   1028       C  
ATOM    606  CZ3 TRP A 151     -13.294  15.229  28.577  1.00 77.18           C  
ANISOU  606  CZ3 TRP A 151     6956   9717  12651  -1295    426    909       C  
ATOM    607  CH2 TRP A 151     -13.896  14.541  27.517  1.00 70.42           C  
ANISOU  607  CH2 TRP A 151     6084   9054  11618  -1365    499    905       C  
ATOM    608  N   ILE A 152     -14.804  18.983  30.919  1.00100.82           N  
ANISOU  608  N   ILE A 152     9831  12020  16455  -1115    163    913       N  
ATOM    609  CA  ILE A 152     -15.354  18.027  31.875  1.00100.33           C  
ANISOU  609  CA  ILE A 152     9858  12002  16261  -1083    255    714       C  
ATOM    610  C   ILE A 152     -16.565  18.622  32.576  1.00 97.43           C  
ANISOU  610  C   ILE A 152     9470  11490  16060  -1025    247    625       C  
ATOM    611  O   ILE A 152     -17.598  17.958  32.734  1.00108.62           O  
ANISOU  611  O   ILE A 152    10924  12980  17368  -1008    319    540       O  
ATOM    612  CB  ILE A 152     -14.273  17.598  32.886  1.00104.57           C  
ANISOU  612  CB  ILE A 152    10451  12533  16747  -1078    271    603       C  
ATOM    613  CG1 ILE A 152     -13.034  17.072  32.159  1.00 88.91           C  
ANISOU  613  CG1 ILE A 152     8473  10685  14623  -1131    279    702       C  
ATOM    614  CG2 ILE A 152     -14.822  16.546  33.838  1.00 95.81           C  
ANISOU  614  CG2 ILE A 152     9425  11480  15499  -1042    368    431       C  
ATOM    615  CD1 ILE A 152     -11.909  16.676  33.089  1.00 86.23           C  
ANISOU  615  CD1 ILE A 152     8168  10362  14234  -1130    291    624       C  
ATOM    616  N   TYR A 153     -16.469  19.897  32.972  1.00 73.11           N  
ANISOU  616  N   TYR A 153     6321   8202  13257   -997    162    640       N  
ATOM    617  CA  TYR A 153     -17.589  20.559  33.631  1.00 74.32           C  
ANISOU  617  CA  TYR A 153     6438   8198  13604   -938    158    546       C  
ATOM    618  C   TYR A 153     -18.860  20.414  32.808  1.00 77.86           C  
ANISOU  618  C   TYR A 153     6850   8724  14009   -931    188    637       C  
ATOM    619  O   TYR A 153     -19.895  19.962  33.314  1.00 87.16           O  
ANISOU  619  O   TYR A 153     8057   9932  15126   -899    251    512       O  
ATOM    620  CB  TYR A 153     -17.262  22.034  33.870  1.00 78.36           C  
ANISOU  620  CB  TYR A 153     6828   8417  14526   -909     60    594       C  
ATOM    621  CG  TYR A 153     -18.462  22.884  34.226  1.00 81.20           C  
ANISOU  621  CG  TYR A 153     7083   8535  15235   -830     52    555       C  
ATOM    622  CD1 TYR A 153     -19.042  22.809  35.485  1.00 81.85           C  
ANISOU  622  CD1 TYR A 153     7167   8501  15431   -774    102    303       C  
ATOM    623  CD2 TYR A 153     -19.010  23.768  33.305  1.00 82.02           C  
ANISOU  623  CD2 TYR A 153     7070   8527  15569   -810     -2    772       C  
ATOM    624  CE1 TYR A 153     -20.137  23.588  35.818  1.00 91.88           C  
ANISOU  624  CE1 TYR A 153     8329   9541  17040   -698    106    244       C  
ATOM    625  CE2 TYR A 153     -20.106  24.550  33.628  1.00 79.35           C  
ANISOU  625  CE2 TYR A 153     6616   7948  15584   -729     -3    749       C  
ATOM    626  CZ  TYR A 153     -20.665  24.456  34.885  1.00 87.43           C  
ANISOU  626  CZ  TYR A 153     7647   8850  16722   -673     54    470       C  
ATOM    627  OH  TYR A 153     -21.755  25.232  35.210  1.00 82.72           O  
ANISOU  627  OH  TYR A 153     6926   8006  16496   -590     65    424       O  
ATOM    628  N   LEU A 154     -18.785  20.741  31.514  1.00 70.31           N  
ANISOU  628  N   LEU A 154     5824   7832  13060   -970    144    860       N  
ATOM    629  CA  LEU A 154     -19.959  20.594  30.663  1.00 76.69           C  
ANISOU  629  CA  LEU A 154     6579   8761  13800   -981    170    959       C  
ATOM    630  C   LEU A 154     -20.406  19.142  30.616  1.00 82.02           C  
ANISOU  630  C   LEU A 154     7342   9676  14146  -1020    277    836       C  
ATOM    631  O   LEU A 154     -21.595  18.840  30.782  1.00 96.46           O  
ANISOU  631  O   LEU A 154     9167  11560  15924  -1006    327    767       O  
ATOM    632  CB  LEU A 154     -19.662  21.118  29.257  1.00 74.20           C  
ANISOU  632  CB  LEU A 154     6165   8515  13513  -1028    105   1230       C  
ATOM    633  CG  LEU A 154     -19.327  22.608  29.165  1.00 78.76           C  
ANISOU  633  CG  LEU A 154     6635   8843  14446   -989     -4   1400       C  
ATOM    634  CD1 LEU A 154     -19.211  23.038  27.713  1.00 88.61           C  
ANISOU  634  CD1 LEU A 154     7776  10194  15700  -1034    -64   1703       C  
ATOM    635  CD2 LEU A 154     -20.365  23.441  29.899  1.00 78.17           C  
ANISOU  635  CD2 LEU A 154     6484   8516  14700   -902    -15   1356       C  
ATOM    636  N   ASP A 155     -19.450  18.221  30.452  1.00 73.09           N  
ANISOU  636  N   ASP A 155     6287   8679  12804  -1070    317    800       N  
ATOM    637  CA  ASP A 155     -19.783  16.803  30.424  1.00 75.42           C  
ANISOU  637  CA  ASP A 155     6664   9176  12814  -1111    426    681       C  
ATOM    638  C   ASP A 155     -20.420  16.350  31.728  1.00 85.33           C  
ANISOU  638  C   ASP A 155     7994  10359  14069  -1048    484    490       C  
ATOM    639  O   ASP A 155     -21.155  15.356  31.739  1.00 88.26           O  
ANISOU  639  O   ASP A 155     8412  10866  14256  -1069    569    408       O  
ATOM    640  CB  ASP A 155     -18.531  15.978  30.127  1.00 80.69           C  
ANISOU  640  CB  ASP A 155     7392   9956  13311  -1160    461    676       C  
ATOM    641  CG  ASP A 155     -18.851  14.651  29.469  1.00 80.69           C  
ANISOU  641  CG  ASP A 155     7431  10196  13030  -1237    566    621       C  
ATOM    642  OD1 ASP A 155     -20.044  14.289  29.398  1.00 87.13           O  
ANISOU  642  OD1 ASP A 155     8242  11097  13767  -1253    613    567       O  
ATOM    643  OD2 ASP A 155     -17.908  13.976  29.009  1.00 90.67           O  
ANISOU  643  OD2 ASP A 155     8723  11567  14159  -1287    604    626       O  
ATOM    644  N   VAL A 156     -20.164  17.059  32.824  1.00 82.92           N  
ANISOU  644  N   VAL A 156     7693   9850  13964   -979    441    413       N  
ATOM    645  CA  VAL A 156     -20.857  16.774  34.073  1.00 77.32           C  
ANISOU  645  CA  VAL A 156     7032   9076  13270   -919    492    229       C  
ATOM    646  C   VAL A 156     -22.144  17.581  34.181  1.00 83.79           C  
ANISOU  646  C   VAL A 156     7775   9801  14259   -877    472    221       C  
ATOM    647  O   VAL A 156     -23.153  17.080  34.679  1.00 76.23           O  
ANISOU  647  O   VAL A 156     6844   8888  13231   -852    536    111       O  
ATOM    648  CB  VAL A 156     -19.919  17.035  35.269  1.00 70.93           C  
ANISOU  648  CB  VAL A 156     6255   8139  12558   -884    468    114       C  
ATOM    649  CG1 VAL A 156     -20.662  16.845  36.582  1.00 81.97           C  
ANISOU  649  CG1 VAL A 156     7677   9471  13998   -825    520    -84       C  
ATOM    650  CG2 VAL A 156     -18.713  16.113  35.204  1.00 73.86           C  
ANISOU  650  CG2 VAL A 156     6693   8624  12747   -921    500    130       C  
ATOM    651  N   LEU A 157     -22.138  18.824  33.690  1.00 85.61           N  
ANISOU  651  N   LEU A 157     7903   9901  14725   -866    386    351       N  
ATOM    652  CA  LEU A 157     -23.267  19.717  33.932  1.00 71.61           C  
ANISOU  652  CA  LEU A 157     6019   7947  13244   -799    370    348       C  
ATOM    653  C   LEU A 157     -24.546  19.185  33.301  1.00 83.95           C  
ANISOU  653  C   LEU A 157     7567   9718  14614   -825    421    392       C  
ATOM    654  O   LEU A 157     -25.612  19.203  33.929  1.00 98.11           O  
ANISOU  654  O   LEU A 157     9328  11449  16500   -772    463    287       O  
ATOM    655  CB  LEU A 157     -22.957  21.117  33.403  1.00 71.57           C  
ANISOU  655  CB  LEU A 157     5879   7721  13592   -776    271    529       C  
ATOM    656  CG  LEU A 157     -24.083  22.137  33.580  1.00 71.86           C  
ANISOU  656  CG  LEU A 157     5771   7522  14012   -696    253    559       C  
ATOM    657  CD1 LEU A 157     -24.401  22.318  35.054  1.00 58.96           C  
ANISOU  657  CD1 LEU A 157     4134   5669  12601   -620    295    282       C  
ATOM    658  CD2 LEU A 157     -23.722  23.467  32.936  1.00 86.78           C  
ANISOU  658  CD2 LEU A 157     7520   9185  16268   -674    155    789       C  
ATOM    659  N   PHE A 158     -24.460  18.702  32.064  1.00100.50           N  
ANISOU  659  N   PHE A 158     9654  12040  16490   -908    423    536       N  
ATOM    660  CA  PHE A 158     -25.658  18.263  31.360  1.00109.15           C  
ANISOU  660  CA  PHE A 158    10697  13344  17431   -950    467    582       C  
ATOM    661  C   PHE A 158     -26.109  16.887  31.834  1.00 99.72           C  
ANISOU  661  C   PHE A 158     9607  12314  15970   -978    570    410       C  
ATOM    662  O   PHE A 158     -27.285  16.691  32.163  1.00 99.80           O  
ANISOU  662  O   PHE A 158     9596  12376  15948   -959    612    342       O  
ATOM    663  CB  PHE A 158     -25.399  18.264  29.853  1.00119.63           C  
ANISOU  663  CB  PHE A 158    11950  14857  18647  -1039    438    780       C  
ATOM    664  CG  PHE A 158     -24.872  19.573  29.335  1.00114.66           C  
ANISOU  664  CG  PHE A 158    11220  14063  18285  -1009    333    991       C  
ATOM    665  CD1 PHE A 158     -25.367  20.774  29.819  1.00110.35           C  
ANISOU  665  CD1 PHE A 158    10589  13270  18068   -918    280   1043       C  
ATOM    666  CD2 PHE A 158     -23.872  19.603  28.380  1.00114.44           C  
ANISOU  666  CD2 PHE A 158    11175  14113  18195  -1071    293   1139       C  
ATOM    667  CE1 PHE A 158     -24.882  21.979  29.350  1.00111.15           C  
ANISOU  667  CE1 PHE A 158    10583  13180  18471   -888    185   1264       C  
ATOM    668  CE2 PHE A 158     -23.381  20.805  27.907  1.00122.22           C  
ANISOU  668  CE2 PHE A 158    12064  14941  19434  -1043    193   1359       C  
ATOM    669  CZ  PHE A 158     -23.887  21.995  28.395  1.00127.05           C  
ANISOU  669  CZ  PHE A 158    12593  15295  20386   -954    138   1424       C  
ATOM    670  N   SER A 159     -25.182  15.928  31.892  1.00 85.56           N  
ANISOU  670  N   SER A 159     7921  10592  13998  -1020    612    350       N  
ATOM    671  CA  SER A 159     -25.544  14.568  32.277  1.00 82.68           C  
ANISOU  671  CA  SER A 159     7654  10358  13403  -1045    712    218       C  
ATOM    672  C   SER A 159     -26.104  14.528  33.694  1.00 68.35           C  
ANISOU  672  C   SER A 159     5890   8401  11678   -952    747     56       C  
ATOM    673  O   SER A 159     -27.137  13.896  33.947  1.00 67.89           O  
ANISOU  673  O   SER A 159     5850   8433  11514   -954    812    -17       O  
ATOM    674  CB  SER A 159     -24.333  13.647  32.144  1.00 90.67           C  
ANISOU  674  CB  SER A 159     8761  11424  14266  -1085    750    200       C  
ATOM    675  OG  SER A 159     -23.889  13.579  30.801  1.00 86.94           O  
ANISOU  675  OG  SER A 159     8235  11118  13679  -1184    733    322       O  
ATOM    676  N   THR A 160     -25.445  15.219  34.632  1.00 72.53           N  
ANISOU  676  N   THR A 160     6435   8724  12400   -879    705     -8       N  
ATOM    677  CA  THR A 160     -25.979  15.307  35.987  1.00 76.62           C  
ANISOU  677  CA  THR A 160     6978   9126  13006   -802    736   -180       C  
ATOM    678  C   THR A 160     -27.370  15.925  35.989  1.00 73.12           C  
ANISOU  678  C   THR A 160     6436   8654  12692   -767    735   -188       C  
ATOM    679  O   THR A 160     -28.208  15.566  36.823  1.00 64.19           O  
ANISOU  679  O   THR A 160     5319   7511  11559   -726    799   -330       O  
ATOM    680  CB  THR A 160     -25.037  16.111  36.886  1.00 69.10           C  
ANISOU  680  CB  THR A 160     6007   7945  12302   -747    689   -262       C  
ATOM    681  OG1 THR A 160     -23.721  15.549  36.822  1.00 56.94           O  
ANISOU  681  OG1 THR A 160     4549   6474  10611   -785    683   -228       O  
ATOM    682  CG2 THR A 160     -25.516  16.091  38.330  1.00 79.04           C  
ANISOU  682  CG2 THR A 160     7264   9079  13688   -678    745   -490       C  
ATOM    683  N   ALA A 161     -27.637  16.844  35.060  1.00 68.66           N  
ANISOU  683  N   ALA A 161     5755   8072  12260   -780    669    -29       N  
ATOM    684  CA  ALA A 161     -28.997  17.343  34.897  1.00 52.77           C  
ANISOU  684  CA  ALA A 161     3625   6061  10365   -749    675      1       C  
ATOM    685  C   ALA A 161     -29.936  16.218  34.483  1.00 59.32           C  
ANISOU  685  C   ALA A 161     4493   7195  10852   -817    741     -3       C  
ATOM    686  O   ALA A 161     -30.978  15.999  35.114  1.00 68.06           O  
ANISOU  686  O   ALA A 161     5587   8319  11956   -777    794   -105       O  
ATOM    687  CB  ALA A 161     -29.021  18.478  33.875  1.00 53.01           C  
ANISOU  687  CB  ALA A 161     3513   6029  10600   -751    591    217       C  
ATOM    688  N   LYS A 162     -29.557  15.463  33.448  1.00 60.31           N  
ANISOU  688  N   LYS A 162     4642   7518  10757   -919    755     89       N  
ATOM    689  CA  LYS A 162     -30.440  14.429  32.916  1.00 54.73           C  
ANISOU  689  CA  LYS A 162     3933   7074   9788  -1002    823     86       C  
ATOM    690  C   LYS A 162     -30.795  13.404  33.980  1.00 53.34           C  
ANISOU  690  C   LYS A 162     3876   6880   9512   -968    910    -83       C  
ATOM    691  O   LYS A 162     -31.975  13.141  34.240  1.00 58.79           O  
ANISOU  691  O   LYS A 162     4536   7656  10148   -961    953   -129       O  
ATOM    692  CB  LYS A 162     -29.778  13.735  31.729  1.00 65.55           C  
ANISOU  692  CB  LYS A 162     5317   8645  10944  -1127    831    171       C  
ATOM    693  CG  LYS A 162     -29.664  14.576  30.488  1.00 73.61           C  
ANISOU  693  CG  LYS A 162     6202   9759  12007  -1185    764    335       C  
ATOM    694  CD  LYS A 162     -29.296  13.690  29.326  1.00 93.67           C  
ANISOU  694  CD  LYS A 162     8744  12570  14276  -1336    802    361       C  
ATOM    695  CE  LYS A 162     -30.312  12.567  29.152  1.00 79.84           C  
ANISOU  695  CE  LYS A 162     6994  11074  12265  -1428    879    293       C  
ATOM    696  NZ  LYS A 162     -29.969  11.661  28.021  1.00 94.33           N  
ANISOU  696  NZ  LYS A 162     8819  13190  13830  -1594    920    305       N  
ATOM    697  N   ILE A 163     -29.777  12.829  34.624  1.00 60.74           N  
ANISOU  697  N   ILE A 163     4940   7706  10430   -944    941   -170       N  
ATOM    698  CA  ILE A 163     -30.009  11.837  35.661  1.00 57.58           C  
ANISOU  698  CA  ILE A 163     4654   7274   9948   -907   1031   -325       C  
ATOM    699  C   ILE A 163     -30.796  12.433  36.818  1.00 59.29           C  
ANISOU  699  C   ILE A 163     4841   7380  10306   -817   1034   -444       C  
ATOM    700  O   ILE A 163     -31.476  11.701  37.545  1.00 70.43           O  
ANISOU  700  O   ILE A 163     6307   8822  11632   -798   1110   -557       O  
ATOM    701  CB  ILE A 163     -28.658  11.247  36.118  1.00 81.04           C  
ANISOU  701  CB  ILE A 163     7742  10155  12895   -893   1056   -375       C  
ATOM    702  CG1 ILE A 163     -28.865  10.046  37.044  1.00 83.80           C  
ANISOU  702  CG1 ILE A 163     8206  10496  13137   -869   1163   -511       C  
ATOM    703  CG2 ILE A 163     -27.813  12.316  36.781  1.00 79.23           C  
ANISOU  703  CG2 ILE A 163     7488   9749  12866   -827    982   -397       C  
ATOM    704  CD1 ILE A 163     -29.665   8.923  36.424  1.00 84.63           C  
ANISOU  704  CD1 ILE A 163     8346  10743  13067   -937   1244   -507       C  
ATOM    705  N   TRP A 164     -30.742  13.756  36.997  1.00 61.07           N  
ANISOU  705  N   TRP A 164     4976   7473  10756   -761    956   -426       N  
ATOM    706  CA  TRP A 164     -31.589  14.409  37.984  1.00 56.82           C  
ANISOU  706  CA  TRP A 164     4363   6789  10438   -675    978   -568       C  
ATOM    707  C   TRP A 164     -32.895  14.919  37.396  1.00 58.12           C  
ANISOU  707  C   TRP A 164     4394   7044  10646   -672    965   -483       C  
ATOM    708  O   TRP A 164     -33.867  15.084  38.141  1.00 72.47           O  
ANISOU  708  O   TRP A 164     6160   8819  12556   -612   1009   -602       O  
ATOM    709  CB  TRP A 164     -30.842  15.564  38.658  1.00 60.05           C  
ANISOU  709  CB  TRP A 164     4713   6913  11192   -605    929   -656       C  
ATOM    710  CG  TRP A 164     -29.965  15.110  39.786  1.00 74.02           C  
ANISOU  710  CG  TRP A 164     6576   8604  12945   -586    966   -826       C  
ATOM    711  CD1 TRP A 164     -28.601  15.103  39.815  1.00 84.03           C  
ANISOU  711  CD1 TRP A 164     7893   9816  14218   -603    930   -802       C  
ATOM    712  CD2 TRP A 164     -30.396  14.579  41.045  1.00 68.19           C  
ANISOU  712  CD2 TRP A 164     5878   7871  12161   -553   1045  -1034       C  
ATOM    713  NE1 TRP A 164     -28.155  14.608  41.017  1.00 85.63           N  
ANISOU  713  NE1 TRP A 164     8154   9997  14385   -583    981   -976       N  
ATOM    714  CE2 TRP A 164     -29.238  14.279  41.790  1.00 89.14           C  
ANISOU  714  CE2 TRP A 164     8594  10480  14794   -555   1053  -1121       C  
ATOM    715  CE3 TRP A 164     -31.647  14.331  41.616  1.00 59.36           C  
ANISOU  715  CE3 TRP A 164     4738   6813  11004   -526   1109  -1147       C  
ATOM    716  CZ2 TRP A 164     -29.295  13.744  43.075  1.00 88.09           C  
ANISOU  716  CZ2 TRP A 164     8496  10377  14598   -536   1121  -1311       C  
ATOM    717  CZ3 TRP A 164     -31.702  13.801  42.892  1.00 68.36           C  
ANISOU  717  CZ3 TRP A 164     5925   7969  12078   -507   1176  -1342       C  
ATOM    718  CH2 TRP A 164     -30.534  13.513  43.607  1.00 65.46           C  
ANISOU  718  CH2 TRP A 164     5613   7571  11686   -514   1181  -1419       C  
ATOM    719  N   HIS A 165     -32.947  15.176  36.087  1.00 49.76           N  
ANISOU  719  N   HIS A 165     3264   6133   9510   -737    909   -282       N  
ATOM    720  CA  HIS A 165     -34.230  15.466  35.455  1.00 50.42           C  
ANISOU  720  CA  HIS A 165     3211   6381   9566   -751    904   -185       C  
ATOM    721  C   HIS A 165     -35.133  14.242  35.491  1.00 49.13           C  
ANISOU  721  C   HIS A 165     3095   6456   9116   -809    982   -232       C  
ATOM    722  O   HIS A 165     -36.276  14.314  35.960  1.00 57.15           O  
ANISOU  722  O   HIS A 165     4051   7521  10141   -764   1014   -283       O  
ATOM    723  CB  HIS A 165     -34.019  15.940  34.018  1.00 50.27           C  
ANISOU  723  CB  HIS A 165     3092   6497   9512   -827    835     28       C  
ATOM    724  CG  HIS A 165     -33.773  17.410  33.898  1.00 60.82           C  
ANISOU  724  CG  HIS A 165     4299   7574  11234   -743    763    128       C  
ATOM    725  ND1 HIS A 165     -32.844  18.073  34.670  1.00 66.91           N  
ANISOU  725  ND1 HIS A 165     5104   8008  12312   -665    736     55       N  
ATOM    726  CD2 HIS A 165     -34.338  18.346  33.101  1.00 65.60           C  
ANISOU  726  CD2 HIS A 165     4730   8186  12009   -724    713    311       C  
ATOM    727  CE1 HIS A 165     -32.846  19.356  34.353  1.00 68.32           C  
ANISOU  727  CE1 HIS A 165     5138   7971  12848   -604    671    190       C  
ATOM    728  NE2 HIS A 165     -33.744  19.548  33.403  1.00 62.64           N  
ANISOU  728  NE2 HIS A 165     4293   7445  12064   -629    656    366       N  
ATOM    729  N   LEU A 166     -34.620  13.098  35.029  1.00 50.99           N  
ANISOU  729  N   LEU A 166     3433   6807   9133   -903   1022   -221       N  
ATOM    730  CA  LEU A 166     -35.374  11.852  35.101  1.00 43.45           C  
ANISOU  730  CA  LEU A 166     2536   6008   7967   -957   1107   -273       C  
ATOM    731  C   LEU A 166     -35.811  11.570  36.531  1.00 42.29           C  
ANISOU  731  C   LEU A 166     2469   5732   7870   -865   1171   -454       C  
ATOM    732  O   LEU A 166     -36.999  11.358  36.804  1.00 65.05           O  
ANISOU  732  O   LEU A 166     5304   8712  10699   -856   1212   -487       O  
ATOM    733  CB  LEU A 166     -34.525  10.699  34.565  1.00 59.19           C  
ANISOU  733  CB  LEU A 166     4647   8050   9791  -1044   1148   -263       C  
ATOM    734  CG  LEU A 166     -33.972  10.798  33.142  1.00 61.96           C  
ANISOU  734  CG  LEU A 166     4928   8563  10050  -1154   1095   -101       C  
ATOM    735  CD1 LEU A 166     -33.020   9.644  32.872  1.00 60.24           C  
ANISOU  735  CD1 LEU A 166     4845   8331   9714  -1206   1150   -130       C  
ATOM    736  CD2 LEU A 166     -35.095  10.817  32.117  1.00 61.77           C  
ANISOU  736  CD2 LEU A 166     4747   8835   9887  -1254   1079     30       C  
ATOM    737  N   CYS A 167     -34.856  11.605  37.466  1.00 41.33           N  
ANISOU  737  N   CYS A 167     2452   5413   7840   -803   1177   -569       N  
ATOM    738  CA  CYS A 167     -35.171  11.408  38.876  1.00 40.88           C  
ANISOU  738  CA  CYS A 167     2455   5264   7814   -728   1231   -745       C  
ATOM    739  C   CYS A 167     -36.214  12.403  39.361  1.00 47.16           C  
ANISOU  739  C   CYS A 167     3113   6015   8791   -651   1222   -807       C  
ATOM    740  O   CYS A 167     -37.021  12.075  40.239  1.00 56.24           O  
ANISOU  740  O   CYS A 167     4272   7184   9913   -615   1286   -936       O  
ATOM    741  CB  CYS A 167     -33.898  11.522  39.715  1.00 60.25           C  
ANISOU  741  CB  CYS A 167     4990   7535  10366   -684   1226   -846       C  
ATOM    742  SG  CYS A 167     -34.160  11.454  41.499  1.00 68.10           S  
ANISOU  742  SG  CYS A 167     6007   8417  11450   -608   1298  -1099       S  
ATOM    743  N   ALA A 168     -36.217  13.618  38.810  1.00 48.53           N  
ANISOU  743  N   ALA A 168     3149   6112   9179   -622   1151   -721       N  
ATOM    744  CA  ALA A 168     -37.280  14.560  39.140  1.00 57.76           C  
ANISOU  744  CA  ALA A 168     4163   7221  10561   -540   1151   -767       C  
ATOM    745  C   ALA A 168     -38.625  14.053  38.637  1.00 51.99           C  
ANISOU  745  C   ALA A 168     3368   6764   9620   -577   1182   -675       C  
ATOM    746  O   ALA A 168     -39.580  13.924  39.416  1.00 50.20           O  
ANISOU  746  O   ALA A 168     3115   6564   9394   -526   1240   -792       O  
ATOM    747  CB  ALA A 168     -36.967  15.937  38.557  1.00 47.01           C  
ANISOU  747  CB  ALA A 168     2661   5692   9508   -496   1069   -658       C  
ATOM    748  N   ILE A 169     -38.694  13.699  37.347  1.00 55.23           N  
ANISOU  748  N   ILE A 169     3751   7409   9822   -680   1143   -474       N  
ATOM    749  CA  ILE A 169     -39.975  13.392  36.706  1.00 46.45           C  
ANISOU  749  CA  ILE A 169     2529   6585   8535   -732   1157   -364       C  
ATOM    750  C   ILE A 169     -40.726  12.340  37.507  1.00 52.03           C  
ANISOU  750  C   ILE A 169     3322   7348   9100   -733   1250   -487       C  
ATOM    751  O   ILE A 169     -41.827  12.586  38.018  1.00 71.41           O  
ANISOU  751  O   ILE A 169     5691   9863  11580   -668   1277   -525       O  
ATOM    752  CB  ILE A 169     -39.760  12.929  35.255  1.00 49.61           C  
ANISOU  752  CB  ILE A 169     2889   7212   8749   -878   1130   -192       C  
ATOM    753  CG1 ILE A 169     -39.040  14.007  34.444  1.00 55.53           C  
ANISOU  753  CG1 ILE A 169     3548   7914   9638   -882   1041    -75       C  
ATOM    754  CG2 ILE A 169     -41.092  12.581  34.613  1.00 61.61           C  
ANISOU  754  CG2 ILE A 169     4269   9045  10094   -950   1149    -86       C  
ATOM    755  CD1 ILE A 169     -38.773  13.610  33.005  1.00 50.83           C  
ANISOU  755  CD1 ILE A 169     2900   7577   8837  -1040   1016     65       C  
ATOM    756  N   SER A 170     -40.118  11.158  37.645  1.00 44.48           N  
ANISOU  756  N   SER A 170     2536   6359   8006   -799   1305   -556       N  
ATOM    757  CA  SER A 170     -40.684  10.085  38.450  1.00 68.05           C  
ANISOU  757  CA  SER A 170     5627   9357  10873   -805   1401   -690       C  
ATOM    758  C   SER A 170     -41.218  10.616  39.773  1.00 56.56           C  
ANISOU  758  C   SER A 170     4150   7814   9526   -686   1421   -833       C  
ATOM    759  O   SER A 170     -42.409  10.471  40.078  1.00 56.95           O  
ANISOU  759  O   SER A 170     4136   7980   9524   -667   1463   -853       O  
ATOM    760  CB  SER A 170     -39.625   9.005  38.688  1.00 58.99           C  
ANISOU  760  CB  SER A 170     4673   8099   9642   -852   1452   -779       C  
ATOM    761  OG  SER A 170     -38.499   9.542  39.358  1.00 49.59           O  
ANISOU  761  OG  SER A 170     3539   6720   8581   -782   1418   -847       O  
ATOM    762  N   LEU A 171     -40.354  11.294  40.537  1.00 45.83           N  
ANISOU  762  N   LEU A 171     2821   6246   8346   -609   1399   -948       N  
ATOM    763  CA  LEU A 171     -40.769  11.819  41.833  1.00 52.45           C  
ANISOU  763  CA  LEU A 171     3620   6970   9340   -509   1437  -1148       C  
ATOM    764  C   LEU A 171     -42.021  12.669  41.692  1.00 55.67           C  
ANISOU  764  C   LEU A 171     3843   7448   9862   -443   1430  -1119       C  
ATOM    765  O   LEU A 171     -43.033  12.424  42.361  1.00 52.96           O  
ANISOU  765  O   LEU A 171     3472   7194   9456   -407   1487  -1203       O  
ATOM    766  CB  LEU A 171     -39.637  12.630  42.464  1.00 55.22           C  
ANISOU  766  CB  LEU A 171     3982   7072   9927   -453   1404  -1278       C  
ATOM    767  CG  LEU A 171     -38.783  11.919  43.514  1.00 46.83           C  
ANISOU  767  CG  LEU A 171     3062   5944   8785   -464   1446  -1427       C  
ATOM    768  CD1 LEU A 171     -37.769  12.882  44.103  1.00 53.84           C  
ANISOU  768  CD1 LEU A 171     3919   6615   9924   -414   1403  -1558       C  
ATOM    769  CD2 LEU A 171     -39.660  11.328  44.606  1.00 44.13           C  
ANISOU  769  CD2 LEU A 171     2744   5703   8320   -441   1523  -1563       C  
ATOM    770  N   ASP A 172     -41.987  13.642  40.777  1.00 64.50           N  
ANISOU  770  N   ASP A 172     4824   8544  11140   -426   1360   -978       N  
ATOM    771  CA  ASP A 172     -43.171  14.452  40.525  1.00 63.59           C  
ANISOU  771  CA  ASP A 172     4511   8510  11140   -355   1353   -911       C  
ATOM    772  C   ASP A 172     -44.350  13.562  40.158  1.00 69.28           C  
ANISOU  772  C   ASP A 172     5204   9543  11576   -417   1394   -808       C  
ATOM    773  O   ASP A 172     -45.400  13.599  40.810  1.00 77.65           O  
ANISOU  773  O   ASP A 172     6197  10667  12638   -350   1446   -886       O  
ATOM    774  CB  ASP A 172     -42.879  15.467  39.417  1.00 64.75           C  
ANISOU  774  CB  ASP A 172     4518   8617  11468   -349   1268   -723       C  
ATOM    775  CG  ASP A 172     -43.986  16.493  39.248  1.00 90.36           C  
ANISOU  775  CG  ASP A 172     7538  11884  14912   -243   1260   -656       C  
ATOM    776  OD1 ASP A 172     -44.942  16.492  40.052  1.00112.62           O  
ANISOU  776  OD1 ASP A 172    10311  14737  17743   -164   1320   -776       O  
ATOM    777  OD2 ASP A 172     -43.894  17.308  38.306  1.00114.17           O  
ANISOU  777  OD2 ASP A 172    10419  14883  18077   -234   1195   -474       O  
ATOM    778  N   ARG A 173     -44.161  12.691  39.166  1.00 61.52           N  
ANISOU  778  N   ARG A 173     4280   8750  10343   -549   1374   -641       N  
ATOM    779  CA  ARG A 173     -45.255  11.828  38.747  1.00 65.08           C  
ANISOU  779  CA  ARG A 173     4695   9466  10568   -625   1413   -538       C  
ATOM    780  C   ARG A 173     -45.625  10.813  39.816  1.00 53.82           C  
ANISOU  780  C   ARG A 173     3410   7996   9042   -624   1508   -714       C  
ATOM    781  O   ARG A 173     -46.713  10.231  39.750  1.00 49.39           O  
ANISOU  781  O   ARG A 173     2804   7596   8367   -661   1561   -684       O  
ATOM    782  CB  ARG A 173     -44.901  11.125  37.438  1.00 67.50           C  
ANISOU  782  CB  ARG A 173     5013   9912  10721   -779   1394   -380       C  
ATOM    783  CG  ARG A 173     -45.045  12.018  36.216  1.00 74.49           C  
ANISOU  783  CG  ARG A 173     5691  10991  11619   -813   1306   -163       C  
ATOM    784  CD  ARG A 173     -44.628  11.299  34.951  1.00 73.06           C  
ANISOU  784  CD  ARG A 173     5519  10960  11278   -972   1286     -5       C  
ATOM    785  NE  ARG A 173     -45.290  10.008  34.810  1.00 88.04           N  
ANISOU  785  NE  ARG A 173     7482  12908  13060  -1051   1370      2       N  
ATOM    786  CZ  ARG A 173     -46.414   9.809  34.135  1.00 89.60           C  
ANISOU  786  CZ  ARG A 173     7526  13290  13229  -1096   1388    172       C  
ATOM    787  NH1 ARG A 173     -47.032  10.800  33.513  1.00 81.45           N  
ANISOU  787  NH1 ARG A 173     6310  12435  12201  -1060   1299    372       N  
ATOM    788  NH2 ARG A 173     -46.930   8.584  34.082  1.00 81.42           N  
ANISOU  788  NH2 ARG A 173     6599  12212  12125  -1173   1490     58       N  
ATOM    789  N   TYR A 174     -44.755  10.590  40.802  1.00 64.56           N  
ANISOU  789  N   TYR A 174     4930   9159  10441   -588   1531   -888       N  
ATOM    790  CA  TYR A 174     -45.144   9.735  41.914  1.00 53.69           C  
ANISOU  790  CA  TYR A 174     3662   7771   8965   -582   1616  -1048       C  
ATOM    791  C   TYR A 174     -46.021  10.475  42.912  1.00 58.02           C  
ANISOU  791  C   TYR A 174     4101   8317   9625   -461   1643  -1171       C  
ATOM    792  O   TYR A 174     -46.909   9.867  43.519  1.00 74.23           O  
ANISOU  792  O   TYR A 174     6170  10475  11560   -460   1707  -1224       O  
ATOM    793  CB  TYR A 174     -43.910   9.175  42.617  1.00 60.88           C  
ANISOU  793  CB  TYR A 174     4757   8515   9862   -596   1635  -1173       C  
ATOM    794  CG  TYR A 174     -44.245   8.378  43.853  1.00 54.08           C  
ANISOU  794  CG  TYR A 174     3987   7661   8900   -585   1714  -1318       C  
ATOM    795  CD1 TYR A 174     -44.932   7.175  43.759  1.00 54.16           C  
ANISOU  795  CD1 TYR A 174     4055   7778   8746   -675   1789  -1317       C  
ATOM    796  CD2 TYR A 174     -43.883   8.830  45.114  1.00 45.04           C  
ANISOU  796  CD2 TYR A 174     2851   6414   7847   -501   1725  -1487       C  
ATOM    797  CE1 TYR A 174     -45.249   6.446  44.886  1.00 49.85           C  
ANISOU  797  CE1 TYR A 174     3580   7252   8110   -669   1860  -1425       C  
ATOM    798  CE2 TYR A 174     -44.193   8.106  46.248  1.00 45.06           C  
ANISOU  798  CE2 TYR A 174     2920   6468   7734   -494   1792  -1589       C  
ATOM    799  CZ  TYR A 174     -44.876   6.913  46.128  1.00 46.16           C  
ANISOU  799  CZ  TYR A 174     3120   6723   7696   -572   1855  -1534       C  
ATOM    800  OH  TYR A 174     -45.187   6.187  47.255  1.00 57.43           O  
ANISOU  800  OH  TYR A 174     4600   8205   9018   -567   1923  -1615       O  
ATOM    801  N   VAL A 175     -45.798  11.774  43.086  1.00 66.55           N  
ANISOU  801  N   VAL A 175     5066   9264  10954   -359   1602  -1232       N  
ATOM    802  CA  VAL A 175     -46.472  12.542  44.123  1.00 66.63           C  
ANISOU  802  CA  VAL A 175     4979   9223  11115   -232   1633  -1401       C  
ATOM    803  C   VAL A 175     -47.618  13.369  43.558  1.00 70.18           C  
ANISOU  803  C   VAL A 175     5212   9788  11665   -157   1621  -1283       C  
ATOM    804  O   VAL A 175     -48.662  13.498  44.196  1.00 77.55           O  
ANISOU  804  O   VAL A 175     6066  10808  12593    -80   1671  -1355       O  
ATOM    805  CB  VAL A 175     -45.455  13.433  44.870  1.00 68.14           C  
ANISOU  805  CB  VAL A 175     5187   9148  11554   -160   1605  -1589       C  
ATOM    806  CG1 VAL A 175     -46.133  14.185  46.007  1.00 79.42           C  
ANISOU  806  CG1 VAL A 175     6524  10526  13127    -33   1639  -1797       C  
ATOM    807  CG2 VAL A 175     -44.302  12.593  45.396  1.00 69.04           C  
ANISOU  807  CG2 VAL A 175     5491   9192  11548   -234   1616  -1674       C  
ATOM    808  N   ALA A 176     -47.444  13.923  42.357  1.00 72.54           N  
ANISOU  808  N   ALA A 176     5404  10113  12046   -177   1554  -1086       N  
ATOM    809  CA  ALA A 176     -48.493  14.737  41.754  1.00 73.03           C  
ANISOU  809  CA  ALA A 176     5235  10311  12203   -103   1536   -942       C  
ATOM    810  C   ALA A 176     -49.724  13.927  41.374  1.00 80.75           C  
ANISOU  810  C   ALA A 176     6148  11618  12914   -164   1574   -797       C  
ATOM    811  O   ALA A 176     -50.754  14.526  41.047  1.00102.82           O  
ANISOU  811  O   ALA A 176     8735  14573  15758    -91   1573   -687       O  
ATOM    812  CB  ALA A 176     -47.960  15.469  40.521  1.00 79.59           C  
ANISOU  812  CB  ALA A 176     5960  11123  13157   -127   1448   -747       C  
ATOM    813  N   ILE A 177     -49.646  12.594  41.388  1.00 71.56           N  
ANISOU  813  N   ILE A 177     5150  10544  11495   -292   1610   -784       N  
ATOM    814  CA  ILE A 177     -50.808  11.765  41.081  1.00 87.52           C  
ANISOU  814  CA  ILE A 177     7127  12814  13312   -358   1654   -652       C  
ATOM    815  C   ILE A 177     -51.460  11.185  42.326  1.00 90.35           C  
ANISOU  815  C   ILE A 177     7567  13155  13605   -318   1743   -837       C  
ATOM    816  O   ILE A 177     -52.534  10.572  42.220  1.00 93.68           O  
ANISOU  816  O   ILE A 177     7944  13747  13905   -360   1794   -761       O  
ATOM    817  CB  ILE A 177     -50.451  10.620  40.112  1.00 68.39           C  
ANISOU  817  CB  ILE A 177     4810  10458  10718   -542   1653   -539       C  
ATOM    818  CG1 ILE A 177     -49.678   9.523  40.845  1.00 51.14           C  
ANISOU  818  CG1 ILE A 177     2883   8105   8441   -609   1708   -747       C  
ATOM    819  CG2 ILE A 177     -49.672  11.154  38.917  1.00 72.45           C  
ANISOU  819  CG2 ILE A 177     5253  11002  11272   -592   1561   -364       C  
ATOM    820  CD1 ILE A 177     -49.507   8.260  40.039  1.00 50.55           C  
ANISOU  820  CD1 ILE A 177     2922   8072   8214   -782   1741   -720       C  
ATOM    821  N   GLN A 178     -50.853  11.357  43.499  1.00 90.55           N  
ANISOU  821  N   GLN A 178     7703  12987  13715   -249   1767  -1078       N  
ATOM    822  CA  GLN A 178     -51.386  10.767  44.718  1.00 92.96           C  
ANISOU  822  CA  GLN A 178     8087  13311  13924   -225   1845  -1246       C  
ATOM    823  C   GLN A 178     -52.441  11.631  45.395  1.00 87.66           C  
ANISOU  823  C   GLN A 178     7247  12696  13365    -75   1879  -1325       C  
ATOM    824  O   GLN A 178     -53.210  11.113  46.213  1.00 83.81           O  
ANISOU  824  O   GLN A 178     6781  12301  12763    -63   1946  -1407       O  
ATOM    825  CB  GLN A 178     -50.251  10.474  45.702  1.00 89.21           C  
ANISOU  825  CB  GLN A 178     7793  12649  13452   -231   1853  -1447       C  
ATOM    826  CG  GLN A 178     -50.239   9.036  46.190  1.00 92.91           C  
ANISOU  826  CG  GLN A 178     8435  13171  13696   -333   1910  -1474       C  
ATOM    827  CD  GLN A 178     -48.853   8.425  46.175  1.00 70.56           C  
ANISOU  827  CD  GLN A 178     5782  10199  10828   -409   1890  -1497       C  
ATOM    828  OE1 GLN A 178     -48.431   7.837  45.178  1.00 75.21           O  
ANISOU  828  OE1 GLN A 178     6431  10782  11363   -518   1876  -1392       O  
ATOM    829  NE2 GLN A 178     -48.136   8.558  47.283  1.00 82.23           N  
ANISOU  829  NE2 GLN A 178     7327  11569  12347   -361   1900  -1662       N  
ATOM    830  N   ASN A 179     -52.496  12.922  45.084  1.00111.51           N  
ANISOU  830  N   ASN A 179    10097  15656  16615     44   1838  -1302       N  
ATOM    831  CA  ASN A 179     -53.594  13.739  45.571  1.00104.69           C  
ANISOU  831  CA  ASN A 179     9053  14856  15868    200   1876  -1349       C  
ATOM    832  C   ASN A 179     -54.893  13.298  44.900  1.00 95.04           C  
ANISOU  832  C   ASN A 179     7695  13920  14497    165   1906  -1123       C  
ATOM    833  O   ASN A 179     -54.907  13.011  43.699  1.00 97.93           O  
ANISOU  833  O   ASN A 179     8011  14413  14786     63   1864   -884       O  
ATOM    834  CB  ASN A 179     -53.334  15.223  45.306  1.00108.10           C  
ANISOU  834  CB  ASN A 179     9330  15120  16622    341   1825  -1362       C  
ATOM    835  CG  ASN A 179     -53.097  15.522  43.841  1.00116.86           C  
ANISOU  835  CG  ASN A 179    10332  16296  17771    286   1749  -1098       C  
ATOM    836  OD1 ASN A 179     -52.606  14.677  43.096  1.00114.91           O  
ANISOU  836  OD1 ASN A 179    10186  16140  17337    126   1719   -964       O  
ATOM    837  ND2 ASN A 179     -53.444  16.733  43.420  1.00111.06           N  
ANISOU  837  ND2 ASN A 179     9391  15520  17285    420   1718  -1023       N  
ATOM    838  N   PRO A 180     -56.000  13.229  45.646  1.00 70.61           N  
ANISOU  838  N   PRO A 180     4532  10939  11358    242   1979  -1185       N  
ATOM    839  CA  PRO A 180     -57.240  12.668  45.088  1.00 62.92           C  
ANISOU  839  CA  PRO A 180     3444  10217  10246    188   2019   -974       C  
ATOM    840  C   PRO A 180     -57.858  13.487  43.965  1.00 64.79           C  
ANISOU  840  C   PRO A 180     3415  10613  10588    250   1980   -704       C  
ATOM    841  O   PRO A 180     -58.930  13.112  43.480  1.00 65.77           O  
ANISOU  841  O   PRO A 180     3415  10934  10641    210   2017   -504       O  
ATOM    842  CB  PRO A 180     -58.177  12.616  46.306  1.00 76.28           C  
ANISOU  842  CB  PRO A 180     5116  11961  11907    284   2106  -1139       C  
ATOM    843  CG  PRO A 180     -57.266  12.648  47.496  1.00 63.35           C  
ANISOU  843  CG  PRO A 180     3655  10126  10290    316   2110  -1429       C  
ATOM    844  CD  PRO A 180     -56.124  13.519  47.083  1.00 77.02           C  
ANISOU  844  CD  PRO A 180     5388  11654  12222    355   2032  -1459       C  
ATOM    845  N   ILE A 181     -57.243  14.589  43.537  1.00 65.52           N  
ANISOU  845  N   ILE A 181     3408  10619  10866    341   1907   -689       N  
ATOM    846  CA  ILE A 181     -57.779  15.384  42.435  1.00 67.51           C  
ANISOU  846  CA  ILE A 181     3389  11080  11181    397   1853   -432       C  
ATOM    847  C   ILE A 181     -56.742  15.482  41.322  1.00 72.08           C  
ANISOU  847  C   ILE A 181     3991  11650  11745    279   1751   -312       C  
ATOM    848  O   ILE A 181     -56.673  16.489  40.608  1.00 67.99           O  
ANISOU  848  O   ILE A 181     3291  11185  11357    347   1680   -245       O  
ATOM    849  CB  ILE A 181     -58.210  16.783  42.912  1.00 70.33           C  
ANISOU  849  CB  ILE A 181     3562  11351  11810    642   1860   -550       C  
ATOM    850  CG1 ILE A 181     -58.713  16.725  44.354  1.00 77.94           C  
ANISOU  850  CG1 ILE A 181     4599  12200  12815    755   1960   -795       C  
ATOM    851  CG2 ILE A 181     -59.304  17.346  42.007  1.00 72.97           C  
ANISOU  851  CG2 ILE A 181     3579  12030  12116    712   1833   -308       C  
ATOM    852  CD1 ILE A 181     -59.223  18.041  44.875  1.00 98.45           C  
ANISOU  852  CD1 ILE A 181     7026  14682  15697   1004   1985   -911       C  
ATOM    853  N   HIS A 182     -55.926  14.436  41.165  1.00 75.67           N  
ANISOU  853  N   HIS A 182     4675  12022  12054    103   1744   -313       N  
ATOM    854  CA  HIS A 182     -54.839  14.488  40.192  1.00 68.88           C  
ANISOU  854  CA  HIS A 182     3863  11136  11172     -9   1654   -221       C  
ATOM    855  C   HIS A 182     -55.331  14.393  38.753  1.00 71.21           C  
ANISOU  855  C   HIS A 182     4011  11753  11294   -122   1583     97       C  
ATOM    856  O   HIS A 182     -54.645  14.877  37.849  1.00 88.08           O  
ANISOU  856  O   HIS A 182     6117  13943  13405   -183   1487    124       O  
ATOM    857  CB  HIS A 182     -53.824  13.378  40.472  1.00 59.71           C  
ANISOU  857  CB  HIS A 182     3000   9784   9901   -147   1669   -331       C  
ATOM    858  CG  HIS A 182     -54.233  12.031  39.957  1.00 58.73           C  
ANISOU  858  CG  HIS A 182     2964   9773   9580   -314   1707   -183       C  
ATOM    859  ND1 HIS A 182     -54.973  11.138  40.702  1.00 73.50           N  
ANISOU  859  ND1 HIS A 182     4926  11630  11371   -343   1804   -317       N  
ATOM    860  CD2 HIS A 182     -53.985  11.418  38.775  1.00 58.45           C  
ANISOU  860  CD2 HIS A 182     2934   9790   9484   -475   1686    -14       C  
ATOM    861  CE1 HIS A 182     -55.174  10.039  39.996  1.00 65.62           C  
ANISOU  861  CE1 HIS A 182     3996  10669  10266   -519   1839   -277       C  
ATOM    862  NE2 HIS A 182     -54.584  10.183  38.824  1.00 58.28           N  
ANISOU  862  NE2 HIS A 182     3021   9753   9370   -596   1776   -102       N  
ATOM    863  N   HIS A 183     -56.498  13.794  38.519  1.00 64.36           N  
ANISOU  863  N   HIS A 183     3134  10973  10349   -158   1618    294       N  
ATOM    864  CA  HIS A 183     -57.066  13.711  37.180  1.00 65.71           C  
ANISOU  864  CA  HIS A 183     3246  11189  10531   -240   1564    642       C  
ATOM    865  C   HIS A 183     -57.726  15.009  36.740  1.00 68.63           C  
ANISOU  865  C   HIS A 183     3353  12171  10552   -187   1433    435       C  
ATOM    866  O   HIS A 183     -58.419  15.017  35.718  1.00 70.26           O  
ANISOU  866  O   HIS A 183     3507  11751  11438   -518   1596   -898       O  
ATOM    867  CB  HIS A 183     -58.075  12.561  37.101  1.00 66.11           C  
ANISOU  867  CB  HIS A 183     3313  10908  10899   -356   1750    553       C  
ATOM    868  CG  HIS A 183     -57.453  11.231  36.804  1.00 77.44           C  
ANISOU  868  CG  HIS A 183     4914  12326  12184   -570   1802    369       C  
ATOM    869  ND1 HIS A 183     -57.602  10.138  37.630  1.00 86.17           N  
ANISOU  869  ND1 HIS A 183     6128  13521  13090   -649   1898    160       N  
ATOM    870  CD2 HIS A 183     -56.688  10.814  35.766  1.00 86.72           C  
ANISOU  870  CD2 HIS A 183     6158  13435  13358   -719   1778    366       C  
ATOM    871  CE1 HIS A 183     -56.952   9.108  37.120  1.00 91.93           C  
ANISOU  871  CE1 HIS A 183     7059  14234  13637   -831   1893     31       C  
ATOM    872  NE2 HIS A 183     -56.388   9.492  35.988  1.00 96.84           N  
ANISOU  872  NE2 HIS A 183     7602  14804  14390   -876   1843    180       N  
ATOM    873  N   SER A 184     -57.531  16.095  37.478  1.00 69.63           N  
ANISOU  873  N   SER A 184     3317  12164  10975    -13   1471    108       N  
ATOM    874  CA  SER A 184     -58.140  17.372  37.150  1.00 72.77           C  
ANISOU  874  CA  SER A 184     3401  12583  11665    116   1461    -92       C  
ATOM    875  C   SER A 184     -57.281  18.150  36.159  1.00 73.32           C  
ANISOU  875  C   SER A 184     3346  12480  12031     94   1406    -71       C  
ATOM    876  O   SER A 184     -56.090  17.884  35.978  1.00107.75           O  
ANISOU  876  O   SER A 184     7869  16715  16355      4   1375    -28       O  
ATOM    877  CB  SER A 184     -58.350  18.207  38.413  1.00 74.00           C  
ANISOU  877  CB  SER A 184     3422  12532  12161    421   1544    -72       C  
ATOM    878  OG  SER A 184     -57.113  18.527  39.024  1.00 72.52           O  
ANISOU  878  OG  SER A 184     3423  11885  12247    493   1552   -124       O  
ATOM    879  N   ARG A 185     -57.915  19.126  35.513  1.00 85.88           N  
ANISOU  879  N   ARG A 185     4647  14042  13940    201   1390     11       N  
ATOM    880  CA  ARG A 185     -57.218  20.097  34.681  1.00 99.44           C  
ANISOU  880  CA  ARG A 185     6319  15481  15982    267   1313    278       C  
ATOM    881  C   ARG A 185     -56.614  21.181  35.564  1.00103.29           C  
ANISOU  881  C   ARG A 185     6853  15523  16868    530   1315    381       C  
ATOM    882  O   ARG A 185     -56.470  20.987  36.776  1.00102.27           O  
ANISOU  882  O   ARG A 185     6857  15264  16737    615   1377    212       O  
ATOM    883  CB  ARG A 185     -58.164  20.701  33.643  1.00 98.85           C  
ANISOU  883  CB  ARG A 185     5989  15492  16077    300   1282    505       C  
ATOM    884  CG  ARG A 185     -58.669  19.700  32.620  1.00103.75           C  
ANISOU  884  CG  ARG A 185     6596  16356  16470     25   1300    424       C  
ATOM    885  CD  ARG A 185     -59.871  20.247  31.878  1.00106.11           C  
ANISOU  885  CD  ARG A 185     6639  16783  16896     99   1281    715       C  
ATOM    886  NE  ARG A 185     -60.812  20.878  32.796  1.00121.87           N  
ANISOU  886  NE  ARG A 185     8476  18784  19046    337   1320    693       N  
ATOM    887  CZ  ARG A 185     -61.651  20.217  33.582  1.00130.77           C  
ANISOU  887  CZ  ARG A 185     9598  20033  20054    305   1407    392       C  
ATOM    888  NH1 ARG A 185     -61.698  18.895  33.587  1.00119.92           N  
ANISOU  888  NH1 ARG A 185     8378  18695  18490     43   1484    104       N  
ATOM    889  NH2 ARG A 185     -62.461  20.900  34.386  1.00145.27           N  
ANISOU  889  NH2 ARG A 185    11281  21881  22034    549   1438    394       N  
ATOM    890  N   PHE A 186     -56.240  22.310  34.962  1.00 88.20           N  
ANISOU  890  N   PHE A 186     4846  13324  15344    645   1259    646       N  
ATOM    891  CA  PHE A 186     -55.589  23.418  35.662  1.00 86.87           C  
ANISOU  891  CA  PHE A 186     4719  12633  15653    855   1270    689       C  
ATOM    892  C   PHE A 186     -54.234  22.976  36.219  1.00 94.60           C  
ANISOU  892  C   PHE A 186     5972  13371  16602    760   1269    509       C  
ATOM    893  O   PHE A 186     -53.982  23.005  37.424  1.00 80.73           O  
ANISOU  893  O   PHE A 186     4346  11368  14960    847   1330    276       O  
ATOM    894  CB  PHE A 186     -56.479  23.986  36.778  1.00100.43           C  
ANISOU  894  CB  PHE A 186     6351  14221  17588   1093   1355    560       C  
ATOM    895  CG  PHE A 186     -57.927  24.137  36.397  1.00106.48           C  
ANISOU  895  CG  PHE A 186     6863  15307  18287   1170   1370    676       C  
ATOM    896  CD1 PHE A 186     -58.359  25.236  35.674  1.00112.79           C  
ANISOU  896  CD1 PHE A 186     7443  15982  19430   1313   1338    996       C  
ATOM    897  CD2 PHE A 186     -58.861  23.188  36.785  1.00 86.72           C  
ANISOU  897  CD2 PHE A 186     4338  13217  15395   1100   1418    478       C  
ATOM    898  CE1 PHE A 186     -59.691  25.378  35.330  1.00 92.86           C  
ANISOU  898  CE1 PHE A 186     4681  13741  16859   1387   1351   1116       C  
ATOM    899  CE2 PHE A 186     -60.193  23.324  36.443  1.00 88.21           C  
ANISOU  899  CE2 PHE A 186     4286  13684  15545   1158   1431    553       C  
ATOM    900  CZ  PHE A 186     -60.609  24.421  35.716  1.00 91.86           C  
ANISOU  900  CZ  PHE A 186     4533  14016  16352   1306   1396    876       C  
ATOM    901  N   ASN A 187     -53.366  22.547  35.308  1.00106.58           N  
ANISOU  901  N   ASN A 187     7575  14964  17955    573   1200    609       N  
ATOM    902  CA  ASN A 187     -52.009  22.180  35.685  1.00 99.19           C  
ANISOU  902  CA  ASN A 187     6884  13795  17008    481   1189    479       C  
ATOM    903  C   ASN A 187     -51.193  23.422  36.023  1.00102.49           C  
ANISOU  903  C   ASN A 187     7314  13661  17968    631   1171    535       C  
ATOM    904  O   ASN A 187     -51.392  24.500  35.457  1.00115.07           O  
ANISOU  904  O   ASN A 187     8733  15084  19906    744   1138    790       O  
ATOM    905  CB  ASN A 187     -51.330  21.395  34.563  1.00109.78           C  
ANISOU  905  CB  ASN A 187     8306  15387  18019    243   1127    561       C  
ATOM    906  CG  ASN A 187     -51.740  19.936  34.544  1.00113.99           C  
ANISOU  906  CG  ASN A 187     8927  16369  18015     45   1166    375       C  
ATOM    907  OD1 ASN A 187     -52.166  19.387  35.560  1.00115.69           O  
ANISOU  907  OD1 ASN A 187     9216  16645  18097     77   1234    204       O  
ATOM    908  ND2 ASN A 187     -51.607  19.298  33.387  1.00120.95           N  
ANISOU  908  ND2 ASN A 187     9807  17541  18608   -169   1133    400       N  
ATOM    909  N   SER A 188     -50.264  23.259  36.963  1.00 96.90           N  
ANISOU  909  N   SER A 188     6810  12665  17342    621   1197    293       N  
ATOM    910  CA  SER A 188     -49.426  24.360  37.436  1.00113.44           C  
ANISOU  910  CA  SER A 188     8932  14225  19945    728   1188    252       C  
ATOM    911  C   SER A 188     -48.213  24.472  36.517  1.00122.73           C  
ANISOU  911  C   SER A 188    10168  15289  21175    606   1100    444       C  
ATOM    912  O   SER A 188     -47.181  23.832  36.726  1.00123.08           O  
ANISOU  912  O   SER A 188    10409  15294  21062    482   1085    303       O  
ATOM    913  CB  SER A 188     -49.031  24.140  38.891  1.00109.94           C  
ANISOU  913  CB  SER A 188     8665  13558  19548    756   1254   -137       C  
ATOM    914  OG  SER A 188     -48.677  22.788  39.129  1.00 99.84           O  
ANISOU  914  OG  SER A 188     7578  12539  17818    598   1266   -285       O  
ATOM    915  N   ARG A 189     -48.350  25.300  35.478  1.00 99.92           N  
ANISOU  915  N   ARG A 189     7103  12357  18505    646   1043    790       N  
ATOM    916  CA  ARG A 189     -47.281  25.468  34.496  1.00 93.35           C  
ANISOU  916  CA  ARG A 189     6304  11451  17715    535    956   1021       C  
ATOM    917  C   ARG A 189     -46.046  26.105  35.123  1.00 98.73           C  
ANISOU  917  C   ARG A 189     7099  11627  18788    556    946    898       C  
ATOM    918  O   ARG A 189     -44.929  25.582  35.001  1.00102.65           O  
ANISOU  918  O   ARG A 189     7761  12111  19131    425    906    835       O  
ATOM    919  CB  ARG A 189     -47.788  26.321  33.333  1.00 83.76           C  
ANISOU  919  CB  ARG A 189     4857  10280  16689    591    904   1446       C  
ATOM    920  CG  ARG A 189     -47.544  25.746  31.952  1.00 77.89           C  
ANISOU  920  CG  ARG A 189     4103   9914  15577    419    827   1688       C  
ATOM    921  CD  ARG A 189     -48.042  26.713  30.891  1.00 94.44           C  
ANISOU  921  CD  ARG A 189     5959  12015  17907    492    778   2137       C  
ATOM    922  NE  ARG A 189     -47.974  26.159  29.544  1.00103.65           N  
ANISOU  922  NE  ARG A 189     7098  13592  18693    325    709   2353       N  
ATOM    923  CZ  ARG A 189     -48.325  26.819  28.449  1.00107.45           C  
ANISOU  923  CZ  ARG A 189     7385  14166  19276    348    655   2777       C  
ATOM    924  NH1 ARG A 189     -48.765  28.065  28.504  1.00 88.88           N  
ANISOU  924  NH1 ARG A 189     4843  11517  17409    533    663   3064       N  
ATOM    925  NH2 ARG A 189     -48.233  26.213  27.269  1.00116.70           N  
ANISOU  925  NH2 ARG A 189     8552  15729  20060    178    598   2916       N  
ATOM    926  N   THR A 190     -46.232  27.241  35.801  1.00108.93           N  
ANISOU  926  N   THR A 190     8298  12501  20591    715    985    843       N  
ATOM    927  CA  THR A 190     -45.104  27.954  36.391  1.00 98.69           C  
ANISOU  927  CA  THR A 190     7078  10710  19710    718    976    698       C  
ATOM    928  C   THR A 190     -44.434  27.130  37.480  1.00105.65           C  
ANISOU  928  C   THR A 190     8184  11579  20377    639   1008    276       C  
ATOM    929  O   THR A 190     -43.214  27.216  37.662  1.00100.53           O  
ANISOU  929  O   THR A 190     7649  10696  19851    559    971    182       O  
ATOM    930  CB  THR A 190     -45.570  29.302  36.946  1.00 88.68           C  
ANISOU  930  CB  THR A 190     5656   9020  19017    888   1030    669       C  
ATOM    931  OG1 THR A 190     -46.238  30.038  35.913  1.00 94.72           O  
ANISOU  931  OG1 THR A 190     6203   9812  19974    969   1007   1103       O  
ATOM    932  CG2 THR A 190     -44.389  30.118  37.449  1.00 84.45           C  
ANISOU  932  CG2 THR A 190     5171   7975  18942    858   1018    520       C  
ATOM    933  N   LYS A 191     -45.209  26.323  38.208  1.00121.76           N  
ANISOU  933  N   LYS A 191    10286  13882  22095    658   1076     37       N  
ATOM    934  CA  LYS A 191     -44.626  25.451  39.222  1.00117.25           C  
ANISOU  934  CA  LYS A 191     9926  13343  21282    578   1109   -324       C  
ATOM    935  C   LYS A 191     -43.647  24.467  38.593  1.00115.16           C  
ANISOU  935  C   LYS A 191     9819  13276  20660    406   1052   -241       C  
ATOM    936  O   LYS A 191     -42.527  24.290  39.084  1.00127.75           O  
ANISOU  936  O   LYS A 191    11560  14697  22282    338   1038   -418       O  
ATOM    937  CB  LYS A 191     -45.736  24.710  39.970  1.00135.64           C  
ANISOU  937  CB  LYS A 191    12276  15963  23299    623   1190   -522       C  
ATOM    938  CG  LYS A 191     -45.572  24.664  41.482  1.00132.17           C  
ANISOU  938  CG  LYS A 191    11948  15357  22912    657   1254   -944       C  
ATOM    939  CD  LYS A 191     -46.767  23.982  42.136  1.00111.69           C  
ANISOU  939  CD  LYS A 191     9356  13068  20012    709   1333  -1083       C  
ATOM    940  CE  LYS A 191     -46.662  24.004  43.652  1.00117.08           C  
ANISOU  940  CE  LYS A 191    10136  13618  20732    744   1395  -1495       C  
ATOM    941  NZ  LYS A 191     -46.680  25.392  44.188  1.00128.26           N  
ANISOU  941  NZ  LYS A 191    11442  14649  22643    869   1412  -1643       N  
ATOM    942  N   ALA A 192     -44.046  23.833  37.487  1.00101.15           N  
ANISOU  942  N   ALA A 192     8009  11883  18541    330   1021     18       N  
ATOM    943  CA  ALA A 192     -43.153  22.900  36.803  1.00104.65           C  
ANISOU  943  CA  ALA A 192     8599  12538  18627    162    975     92       C  
ATOM    944  C   ALA A 192     -41.953  23.621  36.200  1.00 98.95           C  
ANISOU  944  C   ALA A 192     7879  11541  18178    131    894    260       C  
ATOM    945  O   ALA A 192     -40.835  23.088  36.200  1.00110.26           O  
ANISOU  945  O   ALA A 192     9474  12959  19461     30    868    190       O  
ATOM    946  CB  ALA A 192     -43.919  22.138  35.723  1.00103.03           C  
ANISOU  946  CB  ALA A 192     8330  12819  17996     69    963    291       C  
ATOM    947  N   PHE A 193     -42.166  24.829  35.675  1.00102.06           N  
ANISOU  947  N   PHE A 193     8088  11715  18975    221    856    502       N  
ATOM    948  CA  PHE A 193     -41.057  25.610  35.136  1.00103.20           C  
ANISOU  948  CA  PHE A 193     8218  11565  19428    195    781    686       C  
ATOM    949  C   PHE A 193     -40.020  25.902  36.218  1.00 98.98           C  
ANISOU  949  C   PHE A 193     7801  10639  19166    199    791    390       C  
ATOM    950  O   PHE A 193     -38.809  25.738  36.007  1.00 96.09           O  
ANISOU  950  O   PHE A 193     7546  10200  18763    110    739    401       O  
ATOM    951  CB  PHE A 193     -41.602  26.901  34.521  1.00110.54           C  
ANISOU  951  CB  PHE A 193     8913  12290  20797    304    755   1007       C  
ATOM    952  CG  PHE A 193     -40.556  27.769  33.886  1.00133.70           C  
ANISOU  952  CG  PHE A 193    11805  14919  24077    276    678   1255       C  
ATOM    953  CD1 PHE A 193     -40.017  27.442  32.653  1.00149.32           C  
ANISOU  953  CD1 PHE A 193    13800  17145  25791    167    599   1546       C  
ATOM    954  CD2 PHE A 193     -40.130  28.929  34.511  1.00143.77           C  
ANISOU  954  CD2 PHE A 193    13015  15668  25944    348    688   1186       C  
ATOM    955  CE1 PHE A 193     -39.059  28.247  32.064  1.00152.91           C  
ANISOU  955  CE1 PHE A 193    14212  17331  26555    144    526   1796       C  
ATOM    956  CE2 PHE A 193     -39.176  29.739  33.927  1.00144.40           C  
ANISOU  956  CE2 PHE A 193    13045  15457  26366    311    619   1428       C  
ATOM    957  CZ  PHE A 193     -38.638  29.397  32.702  1.00147.47           C  
ANISOU  957  CZ  PHE A 193    13455  16100  26476    217    534   1752       C  
ATOM    958  N   LEU A 194     -40.484  26.307  37.402  1.00 89.88           N  
ANISOU  958  N   LEU A 194     6622   9266  18260    294    860     99       N  
ATOM    959  CA  LEU A 194     -39.570  26.569  38.507  1.00 81.12           C  
ANISOU  959  CA  LEU A 194     5609   7832  17383    280    874   -239       C  
ATOM    960  C   LEU A 194     -38.929  25.287  39.025  1.00 80.11           C  
ANISOU  960  C   LEU A 194     5699   7935  16802    178    888   -468       C  
ATOM    961  O   LEU A 194     -37.781  25.316  39.475  1.00 77.03           O  
ANISOU  961  O   LEU A 194     5406   7365  16498    122    862   -627       O  
ATOM    962  CB  LEU A 194     -40.299  27.301  39.633  1.00 78.12           C  
ANISOU  962  CB  LEU A 194     5139   7215  17329    393    948   -523       C  
ATOM    963  CG  LEU A 194     -40.749  28.722  39.284  1.00 82.85           C  
ANISOU  963  CG  LEU A 194     5522   7483  18474    497    948   -332       C  
ATOM    964  CD1 LEU A 194     -41.360  29.412  40.493  1.00 98.18           C  
ANISOU  964  CD1 LEU A 194     7396   9197  20709    599   1031   -677       C  
ATOM    965  CD2 LEU A 194     -39.586  29.532  38.729  1.00 82.95           C  
ANISOU  965  CD2 LEU A 194     5492   7154  18871    432    873   -154       C  
ATOM    966  N   LYS A 195     -39.643  24.160  38.972  1.00 84.24           N  
ANISOU  966  N   LYS A 195     6295   8857  16854    150    930   -480       N  
ATOM    967  CA  LYS A 195     -39.027  22.883  39.326  1.00 81.61           C  
ANISOU  967  CA  LYS A 195     6169   8746  16094     47    949   -634       C  
ATOM    968  C   LYS A 195     -37.866  22.560  38.393  1.00 73.82           C  
ANISOU  968  C   LYS A 195     5270   7815  14961    -59    877   -435       C  
ATOM    969  O   LYS A 195     -36.799  22.122  38.842  1.00 66.21           O  
ANISOU  969  O   LYS A 195     4451   6799  13906   -116    870   -579       O  
ATOM    970  CB  LYS A 195     -40.066  21.760  39.283  1.00 81.02           C  
ANISOU  970  CB  LYS A 195     6136   9076  15572     22   1008   -635       C  
ATOM    971  CG  LYS A 195     -41.139  21.835  40.354  1.00 79.32           C  
ANISOU  971  CG  LYS A 195     5873   8863  15402    119   1087   -867       C  
ATOM    972  CD  LYS A 195     -42.289  20.893  40.028  1.00 91.74           C  
ANISOU  972  CD  LYS A 195     7437  10841  16578     96   1132   -780       C  
ATOM    973  CE  LYS A 195     -43.479  21.121  40.946  1.00107.11           C  
ANISOU  973  CE  LYS A 195     9302  12804  18590    212   1205   -956       C  
ATOM    974  NZ  LYS A 195     -44.650  20.289  40.550  1.00 91.04           N  
ANISOU  974  NZ  LYS A 195     7228  11168  16194    188   1243   -841       N  
ATOM    975  N   ILE A 196     -38.061  22.768  37.089  1.00 75.49           N  
ANISOU  975  N   ILE A 196     5389   8163  15130    -85    823   -103       N  
ATOM    976  CA  ILE A 196     -36.991  22.524  36.123  1.00 77.20           C  
ANISOU  976  CA  ILE A 196     5677   8461  15192   -186    752     91       C  
ATOM    977  C   ILE A 196     -35.811  23.451  36.389  1.00 78.59           C  
ANISOU  977  C   ILE A 196     5852   8238  15770   -163    697     71       C  
ATOM    978  O   ILE A 196     -34.644  23.031  36.344  1.00 70.48           O  
ANISOU  978  O   ILE A 196     4958   7222  14600   -234    667     39       O  
ATOM    979  CB  ILE A 196     -37.523  22.683  34.687  1.00 70.77           C  
ANISOU  979  CB  ILE A 196     4735   7890  14265   -220    705    436       C  
ATOM    980  CG1 ILE A 196     -38.531  21.579  34.366  1.00 74.99           C  
ANISOU  980  CG1 ILE A 196     5286   8878  14329   -286    756    418       C  
ATOM    981  CG2 ILE A 196     -36.379  22.679  33.685  1.00 72.01           C  
ANISOU  981  CG2 ILE A 196     4941   8090  14330   -314    627    635       C  
ATOM    982  CD1 ILE A 196     -39.128  21.690  32.985  1.00 75.80           C  
ANISOU  982  CD1 ILE A 196     5245   9272  14283   -337    714    706       C  
ATOM    983  N   ILE A 197     -36.095  24.726  36.665  1.00 78.67           N  
ANISOU  983  N   ILE A 197     5703   7890  16298    -67    687     87       N  
ATOM    984  CA  ILE A 197     -35.021  25.673  36.958  1.00 72.65           C  
ANISOU  984  CA  ILE A 197     4917   6719  15967    -56    638     45       C  
ATOM    985  C   ILE A 197     -34.267  25.259  38.219  1.00 71.63           C  
ANISOU  985  C   ILE A 197     4927   6496  15792    -79    672   -344       C  
ATOM    986  O   ILE A 197     -33.038  25.369  38.289  1.00 61.37           O  
ANISOU  986  O   ILE A 197     3694   5069  14555   -122    624   -377       O  
ATOM    987  CB  ILE A 197     -35.581  27.104  37.066  1.00 67.76           C  
ANISOU  987  CB  ILE A 197     4087   5713  15947     41    640    112       C  
ATOM    988  CG1 ILE A 197     -35.946  27.633  35.678  1.00 68.91           C  
ANISOU  988  CG1 ILE A 197     4088   5918  16176     53    584    576       C  
ATOM    989  CG2 ILE A 197     -34.581  28.029  37.744  1.00 77.24           C  
ANISOU  989  CG2 ILE A 197     5260   6457  17631     39    615    -71       C  
ATOM    990  CD1 ILE A 197     -36.217  29.119  35.642  1.00 76.18           C  
ANISOU  990  CD1 ILE A 197     4798   6401  17744    135    579    719       C  
ATOM    991  N   ALA A 198     -34.988  24.766  39.230  1.00 80.62           N  
ANISOU  991  N   ALA A 198     6105   7728  16800    -50    754   -633       N  
ATOM    992  CA  ALA A 198     -34.344  24.321  40.463  1.00 70.28           C  
ANISOU  992  CA  ALA A 198     4915   6383  15406    -77    789   -997       C  
ATOM    993  C   ALA A 198     -33.468  23.097  40.228  1.00 71.61           C  
ANISOU  993  C   ALA A 198     5273   6831  15106   -165    779   -951       C  
ATOM    994  O   ALA A 198     -32.385  22.980  40.815  1.00 75.42           O  
ANISOU  994  O   ALA A 198     5835   7235  15586   -197    764  -1112       O  
ATOM    995  CB  ALA A 198     -35.400  24.026  41.528  1.00 70.55           C  
ANISOU  995  CB  ALA A 198     4942   6508  15357    -30    878  -1281       C  
ATOM    996  N   VAL A 199     -33.926  22.163  39.391  1.00 67.56           N  
ANISOU  996  N   VAL A 199     4823   6657  14189   -208    790   -745       N  
ATOM    997  CA  VAL A 199     -33.102  21.000  39.065  1.00 66.42           C  
ANISOU  997  CA  VAL A 199     4850   6764  13621   -299    788   -689       C  
ATOM    998  C   VAL A 199     -31.835  21.437  38.339  1.00 71.52           C  
ANISOU  998  C   VAL A 199     5507   7304  14362   -338    701   -514       C  
ATOM    999  O   VAL A 199     -30.733  20.946  38.623  1.00 69.34           O  
ANISOU  999  O   VAL A 199     5351   7058  13939   -382    693   -585       O  
ATOM   1000  CB  VAL A 199     -33.906  19.977  38.241  1.00 67.83           C  
ANISOU 1000  CB  VAL A 199     5070   7318  13382   -355    820   -527       C  
ATOM   1001  CG1 VAL A 199     -33.019  18.813  37.835  1.00 48.82           C  
ANISOU 1001  CG1 VAL A 199     2832   5139  10580   -454    821   -475       C  
ATOM   1002  CG2 VAL A 199     -35.096  19.473  39.041  1.00 80.36           C  
ANISOU 1002  CG2 VAL A 199     6657   9022  14855   -318    905   -705       C  
ATOM   1003  N   TRP A 200     -31.965  22.374  37.396  1.00 75.28           N  
ANISOU 1003  N   TRP A 200     5851   7667  15086   -321    636   -264       N  
ATOM   1004  CA  TRP A 200     -30.777  22.907  36.735  1.00 67.69           C  
ANISOU 1004  CA  TRP A 200     4885   6586  14248   -353    550    -88       C  
ATOM   1005  C   TRP A 200     -29.847  23.584  37.735  1.00 60.47           C  
ANISOU 1005  C   TRP A 200     3966   5345  13666   -318    530   -307       C  
ATOM   1006  O   TRP A 200     -28.621  23.467  37.633  1.00 61.26           O  
ANISOU 1006  O   TRP A 200     4140   5450  13684   -361    484   -281       O  
ATOM   1007  CB  TRP A 200     -31.173  23.882  35.625  1.00 76.75           C  
ANISOU 1007  CB  TRP A 200     5868   7644  15651   -331    487    234       C  
ATOM   1008  CG  TRP A 200     -31.257  23.248  34.269  1.00 64.48           C  
ANISOU 1008  CG  TRP A 200     4337   6458  13704   -416    461    503       C  
ATOM   1009  CD1 TRP A 200     -32.372  23.112  33.495  1.00 82.95           C  
ANISOU 1009  CD1 TRP A 200     6585   9031  15903   -425    475    670       C  
ATOM   1010  CD2 TRP A 200     -30.181  22.657  33.529  1.00 59.33           C  
ANISOU 1010  CD2 TRP A 200     3796   6008  12738   -512    422    604       C  
ATOM   1011  NE1 TRP A 200     -32.057  22.478  32.317  1.00 82.38           N  
ANISOU 1011  NE1 TRP A 200     6557   9295  15449   -532    448    843       N  
ATOM   1012  CE2 TRP A 200     -30.718  22.187  32.314  1.00 66.34           C  
ANISOU 1012  CE2 TRP A 200     4652   7243  13311   -586    419    802       C  
ATOM   1013  CE3 TRP A 200     -28.816  22.480  33.775  1.00 77.71           C  
ANISOU 1013  CE3 TRP A 200     6236   8275  15014   -547    394    534       C  
ATOM   1014  CZ2 TRP A 200     -29.939  21.553  31.347  1.00 79.81           C  
ANISOU 1014  CZ2 TRP A 200     6438   9217  14670   -697    396    900       C  
ATOM   1015  CZ3 TRP A 200     -28.043  21.850  32.814  1.00 84.66           C  
ANISOU 1015  CZ3 TRP A 200     7199   9420  15550   -645    369    665       C  
ATOM   1016  CH2 TRP A 200     -28.607  21.394  31.616  1.00 85.34           C  
ANISOU 1016  CH2 TRP A 200     7254   9831  15342   -721    373    832       C  
ATOM   1017  N   THR A 201     -30.414  24.299  38.709  1.00 68.27           N  
ANISOU 1017  N   THR A 201     4854   6065  15019   -246    566   -541       N  
ATOM   1018  CA  THR A 201     -29.599  24.979  39.711  1.00 65.56           C  
ANISOU 1018  CA  THR A 201     4480   5428  15001   -223    554   -808       C  
ATOM   1019  C   THR A 201     -28.827  23.985  40.571  1.00 56.56           C  
ANISOU 1019  C   THR A 201     3495   4483  13510   -268    587  -1041       C  
ATOM   1020  O   THR A 201     -27.640  24.188  40.856  1.00 61.77           O  
ANISOU 1020  O   THR A 201     4179   5071  14220   -290    543  -1107       O  
ATOM   1021  CB  THR A 201     -30.482  25.869  40.588  1.00 85.64           C  
ANISOU 1021  CB  THR A 201     6878   7679  17983   -154    603  -1063       C  
ATOM   1022  OG1 THR A 201     -31.200  26.796  39.763  1.00 80.88           O  
ANISOU 1022  OG1 THR A 201     6117   6885  17728   -110    578   -803       O  
ATOM   1023  CG2 THR A 201     -29.638  26.640  41.593  1.00 89.94           C  
ANISOU 1023  CG2 THR A 201     7363   7924  18886   -140    592  -1383       C  
ATOM   1024  N   ILE A 202     -29.482  22.903  40.999  1.00 55.71           N  
ANISOU 1024  N   ILE A 202     3486   4638  13045   -283    664  -1150       N  
ATOM   1025  CA  ILE A 202     -28.769  21.919  41.808  1.00 67.00           C  
ANISOU 1025  CA  ILE A 202     5052   6252  14154   -325    701  -1329       C  
ATOM   1026  C   ILE A 202     -27.717  21.204  40.968  1.00 70.28           C  
ANISOU 1026  C   ILE A 202     5588   6859  14257   -393    659  -1089       C  
ATOM   1027  O   ILE A 202     -26.645  20.855  41.476  1.00 71.68           O  
ANISOU 1027  O   ILE A 202     5834   7083  14317   -425    650  -1175       O  
ATOM   1028  CB  ILE A 202     -29.735  20.926  42.489  1.00 71.65           C  
ANISOU 1028  CB  ILE A 202     5709   7060  14455   -323    797  -1484       C  
ATOM   1029  CG1 ILE A 202     -30.349  19.951  41.483  1.00 65.47           C  
ANISOU 1029  CG1 ILE A 202     5008   6552  13315   -357    821  -1229       C  
ATOM   1030  CG2 ILE A 202     -30.817  21.672  43.261  1.00 66.10           C  
ANISOU 1030  CG2 ILE A 202     4879   6193  14042   -262    837  -1720       C  
ATOM   1031  CD1 ILE A 202     -31.119  18.819  42.124  1.00 55.50           C  
ANISOU 1031  CD1 ILE A 202     3832   5520  11737   -366    914  -1354       C  
ATOM   1032  N   SER A 203     -27.984  20.989  39.675  1.00 72.78           N  
ANISOU 1032  N   SER A 203     5919   7307  14427   -422    632   -792       N  
ATOM   1033  CA  SER A 203     -26.961  20.410  38.809  1.00 69.58           C  
ANISOU 1033  CA  SER A 203     5612   7079  13748   -494    591   -586       C  
ATOM   1034  C   SER A 203     -25.760  21.340  38.676  1.00 69.23           C  
ANISOU 1034  C   SER A 203     5516   6837  13951   -497    502   -528       C  
ATOM   1035  O   SER A 203     -24.610  20.887  38.687  1.00 76.36           O  
ANISOU 1035  O   SER A 203     6506   7839  14670   -546    482   -507       O  
ATOM   1036  CB  SER A 203     -27.549  20.089  37.436  1.00 59.65           C  
ANISOU 1036  CB  SER A 203     4350   6026  12287   -537    580   -320       C  
ATOM   1037  OG  SER A 203     -28.480  19.027  37.524  1.00 51.64           O  
ANISOU 1037  OG  SER A 203     3403   5247  10972   -555    662   -375       O  
ATOM   1038  N   VAL A 204     -26.010  22.644  38.546  1.00 67.58           N  
ANISOU 1038  N   VAL A 204     5157   6343  14177   -446    450   -490       N  
ATOM   1039  CA  VAL A 204     -24.920  23.616  38.491  1.00 67.10           C  
ANISOU 1039  CA  VAL A 204     5030   6066  14399   -446    366   -448       C  
ATOM   1040  C   VAL A 204     -24.117  23.586  39.785  1.00 68.89           C  
ANISOU 1040  C   VAL A 204     5283   6234  14657   -448    380   -748       C  
ATOM   1041  O   VAL A 204     -22.880  23.643  39.770  1.00 77.33           O  
ANISOU 1041  O   VAL A 204     6386   7329  15666   -496    326   -712       O  
ATOM   1042  CB  VAL A 204     -25.473  25.025  38.198  1.00 70.90           C  
ANISOU 1042  CB  VAL A 204     5325   6211  15404   -378    323   -363       C  
ATOM   1043  CG1 VAL A 204     -24.393  26.078  38.400  1.00 71.88           C  
ANISOU 1043  CG1 VAL A 204     5362   6076  15874   -369    247   -387       C  
ATOM   1044  CG2 VAL A 204     -26.025  25.099  36.784  1.00 65.10           C  
ANISOU 1044  CG2 VAL A 204     4549   5577  14610   -393    290      1       C  
ATOM   1045  N   GLY A 205     -24.807  23.508  40.923  1.00 71.63           N  
ANISOU 1045  N   GLY A 205     5605   6529  15081   -406    452  -1052       N  
ATOM   1046  CA  GLY A 205     -24.108  23.428  42.196  1.00 80.13           C  
ANISOU 1046  CA  GLY A 205     6691   7610  16144   -420    470  -1356       C  
ATOM   1047  C   GLY A 205     -23.259  22.176  42.319  1.00 78.19           C  
ANISOU 1047  C   GLY A 205     6600   7666  15443   -490    486  -1308       C  
ATOM   1048  O   GLY A 205     -22.148  22.216  42.854  1.00 71.00           O  
ANISOU 1048  O   GLY A 205     5698   6785  14494   -534    453  -1392       O  
ATOM   1049  N   ILE A 206     -23.773  21.047  41.827  1.00 79.35           N  
ANISOU 1049  N   ILE A 206     6860   8041  15249   -506    541  -1171       N  
ATOM   1050  CA  ILE A 206     -23.008  19.803  41.862  1.00 84.62           C  
ANISOU 1050  CA  ILE A 206     7662   8968  15521   -562    570  -1105       C  
ATOM   1051  C   ILE A 206     -21.800  19.889  40.935  1.00 78.93           C  
ANISOU 1051  C   ILE A 206     6975   8290  14725   -617    492   -868       C  
ATOM   1052  O   ILE A 206     -20.721  19.375  41.251  1.00 72.74           O  
ANISOU 1052  O   ILE A 206     6246   7622  13768   -662    485   -870       O  
ATOM   1053  CB  ILE A 206     -23.914  18.610  41.505  1.00 86.55           C  
ANISOU 1053  CB  ILE A 206     8007   9424  15456   -564    653  -1028       C  
ATOM   1054  CG1 ILE A 206     -24.982  18.410  42.582  1.00 78.90           C  
ANISOU 1054  CG1 ILE A 206     7013   8450  14514   -521    734  -1278       C  
ATOM   1055  CG2 ILE A 206     -23.098  17.337  41.335  1.00 84.30           C  
ANISOU 1055  CG2 ILE A 206     7850   9370  14811   -616    686   -925       C  
ATOM   1056  CD1 ILE A 206     -25.954  17.293  42.273  1.00 86.30           C  
ANISOU 1056  CD1 ILE A 206     8040   9586  15166   -527    815  -1208       C  
ATOM   1057  N   SER A 207     -21.956  20.538  39.780  1.00 82.98           N  
ANISOU 1057  N   SER A 207     7443   8722  15362   -617    434   -653       N  
ATOM   1058  CA  SER A 207     -20.893  20.569  38.783  1.00 86.23           C  
ANISOU 1058  CA  SER A 207     7886   9210  15668   -676    366   -420       C  
ATOM   1059  C   SER A 207     -19.863  21.668  39.022  1.00 90.24           C  
ANISOU 1059  C   SER A 207     8310   9527  16450   -690    276   -436       C  
ATOM   1060  O   SER A 207     -18.797  21.629  38.403  1.00 86.01           O  
ANISOU 1060  O   SER A 207     7806   9073  15802   -748    224   -276       O  
ATOM   1061  CB  SER A 207     -21.498  20.728  37.387  1.00 81.99           C  
ANISOU 1061  CB  SER A 207     7326   8721  15104   -686    343   -171       C  
ATOM   1062  OG  SER A 207     -22.448  19.709  37.126  1.00 75.85           O  
ANISOU 1062  OG  SER A 207     6619   8148  14053   -692    423   -167       O  
ATOM   1063  N   MET A 208     -20.156  22.642  39.884  1.00 91.90           N  
ANISOU 1063  N   MET A 208     8409   9493  17017   -644    262   -639       N  
ATOM   1064  CA  MET A 208     -19.195  23.711  40.160  1.00 86.60           C  
ANISOU 1064  CA  MET A 208     7649   8638  16617   -668    180   -684       C  
ATOM   1065  C   MET A 208     -17.835  23.222  40.664  1.00 98.84           C  
ANISOU 1065  C   MET A 208     9266  10353  17938   -750    158   -732       C  
ATOM   1066  O   MET A 208     -16.811  23.802  40.249  1.00106.27           O  
ANISOU 1066  O   MET A 208    10179  11247  18951   -804     77   -611       O  
ATOM   1067  CB  MET A 208     -19.813  24.701  41.155  1.00 74.62           C  
ANISOU 1067  CB  MET A 208     5995   6853  15502   -607    193   -970       C  
ATOM   1068  CG  MET A 208     -19.131  26.056  41.200  1.00 72.48           C  
ANISOU 1068  CG  MET A 208     5596   6328  15614   -619    110   -994       C  
ATOM   1069  SD  MET A 208     -19.568  27.090  39.791  1.00105.26           S  
ANISOU 1069  SD  MET A 208     9632  10242  20119   -567     47   -656       S  
ATOM   1070  CE  MET A 208     -21.328  27.292  40.059  1.00116.31           C  
ANISOU 1070  CE  MET A 208    10936  11475  21780   -448    132   -783       C  
ATOM   1071  N   PRO A 209     -17.740  22.224  41.554  1.00103.23           N  
ANISOU 1071  N   PRO A 209     9892  11096  18233   -765    223   -891       N  
ATOM   1072  CA  PRO A 209     -16.411  21.815  42.040  1.00105.75           C  
ANISOU 1072  CA  PRO A 209    10245  11572  18363   -845    196   -911       C  
ATOM   1073  C   PRO A 209     -15.441  21.398  40.948  1.00102.08           C  
ANISOU 1073  C   PRO A 209     9850  11249  17687   -900    158   -625       C  
ATOM   1074  O   PRO A 209     -14.233  21.600  41.120  1.00 96.79           O  
ANISOU 1074  O   PRO A 209     9162  10623  16991   -972    100   -604       O  
ATOM   1075  CB  PRO A 209     -16.732  20.646  42.980  1.00107.01           C  
ANISOU 1075  CB  PRO A 209    10461  11926  18271   -832    290  -1064       C  
ATOM   1076  CG  PRO A 209     -18.076  20.964  43.499  1.00108.38           C  
ANISOU 1076  CG  PRO A 209    10585  11971  18625   -759    344  -1267       C  
ATOM   1077  CD  PRO A 209     -18.812  21.594  42.350  1.00 98.13           C  
ANISOU 1077  CD  PRO A 209     9265  10505  17514   -712    319  -1090       C  
ATOM   1078  N   ILE A 210     -15.913  20.838  39.836  1.00121.55           N  
ANISOU 1078  N   ILE A 210    12385  13805  19995   -878    189   -423       N  
ATOM   1079  CA  ILE A 210     -15.003  20.379  38.785  1.00123.20           C  
ANISOU 1079  CA  ILE A 210    12654  14175  19982   -933    167   -192       C  
ATOM   1080  C   ILE A 210     -14.172  21.559  38.283  1.00124.85           C  
ANISOU 1080  C   ILE A 210    12785  14246  20408   -977     60    -80       C  
ATOM   1081  O   ILE A 210     -12.943  21.525  38.441  1.00122.21           O  
ANISOU 1081  O   ILE A 210    12451  13990  19993  -1044     22    -57       O  
ATOM   1082  CB  ILE A 210     -15.750  19.667  37.642  1.00117.96           C  
ANISOU 1082  CB  ILE A 210    12059  13642  19117   -916    218    -35       C  
ATOM   1083  CG1 ILE A 210     -16.419  18.386  38.141  1.00117.89           C  
ANISOU 1083  CG1 ILE A 210    12137  13784  18873   -887    327   -138       C  
ATOM   1084  CG2 ILE A 210     -14.802  19.366  36.488  1.00121.72           C  
ANISOU 1084  CG2 ILE A 210    12574  14275  19401   -978    193    169       C  
ATOM   1085  CD1 ILE A 210     -17.914  18.512  38.299  1.00124.85           C  
ANISOU 1085  CD1 ILE A 210    13000  14581  19858   -828    370   -222       C  
ATOM   1086  N   PRO A 211     -14.752  22.617  37.696  1.00107.67           N  
ANISOU 1086  N   PRO A 211    10526  11865  18518   -945     10      3       N  
ATOM   1087  CA  PRO A 211     -13.906  23.760  37.318  1.00 99.57           C  
ANISOU 1087  CA  PRO A 211     9415  10689  17729   -989    -90    109       C  
ATOM   1088  C   PRO A 211     -13.260  24.452  38.503  1.00 94.79           C  
ANISOU 1088  C   PRO A 211     8744   9949  17324  -1027   -131   -106       C  
ATOM   1089  O   PRO A 211     -12.113  24.907  38.380  1.00 93.51           O  
ANISOU 1089  O   PRO A 211     8554   9785  17189  -1105   -200    -41       O  
ATOM   1090  CB  PRO A 211     -14.877  24.690  36.579  1.00108.65           C  
ANISOU 1090  CB  PRO A 211    10469  11627  19187   -926   -120    237       C  
ATOM   1091  CG  PRO A 211     -16.192  24.373  37.148  1.00112.34           C  
ANISOU 1091  CG  PRO A 211    10940  12051  19692   -850    -45     77       C  
ATOM   1092  CD  PRO A 211     -16.168  22.894  37.386  1.00110.16           C  
ANISOU 1092  CD  PRO A 211    10802  12063  18990   -870     39     15       C  
ATOM   1093  N   VAL A 212     -13.942  24.519  39.655  1.00105.90           N  
ANISOU 1093  N   VAL A 212    10120  11265  18851   -986    -89   -377       N  
ATOM   1094  CA  VAL A 212     -13.404  25.272  40.788  1.00104.27           C  
ANISOU 1094  CA  VAL A 212     9835  10938  18845  -1036   -127   -624       C  
ATOM   1095  C   VAL A 212     -12.057  24.701  41.223  1.00104.37           C  
ANISOU 1095  C   VAL A 212     9894  11178  18585  -1143   -151   -634       C  
ATOM   1096  O   VAL A 212     -11.096  25.442  41.462  1.00 97.38           O  
ANISOU 1096  O   VAL A 212     8950  10234  17816  -1234   -224   -669       O  
ATOM   1097  CB  VAL A 212     -14.414  25.294  41.950  1.00108.25           C  
ANISOU 1097  CB  VAL A 212    10298  11360  19472   -975    -60   -942       C  
ATOM   1098  CG1 VAL A 212     -13.714  25.612  43.263  1.00107.72           C  
ANISOU 1098  CG1 VAL A 212    10179  11310  19439  -1056    -80  -1237       C  
ATOM   1099  CG2 VAL A 212     -15.503  26.318  41.676  1.00 91.30           C  
ANISOU 1099  CG2 VAL A 212     8044   8913  17731   -883    -57   -971       C  
ATOM   1100  N   PHE A 213     -11.963  23.376  41.324  1.00129.21           N  
ANISOU 1100  N   PHE A 213    13133  14585  21376  -1139    -87   -596       N  
ATOM   1101  CA  PHE A 213     -10.720  22.729  41.718  1.00124.09           C  
ANISOU 1101  CA  PHE A 213    12506  14167  20474  -1227   -100   -577       C  
ATOM   1102  C   PHE A 213      -9.851  22.313  40.537  1.00112.12           C  
ANISOU 1102  C   PHE A 213    11045  12792  18765  -1261   -118   -294       C  
ATOM   1103  O   PHE A 213      -8.719  21.868  40.754  1.00100.76           O  
ANISOU 1103  O   PHE A 213     9604  11536  17145  -1334   -132   -254       O  
ATOM   1104  CB  PHE A 213     -11.015  21.507  42.595  1.00121.43           C  
ANISOU 1104  CB  PHE A 213    12211  14036  19892  -1198    -12   -696       C  
ATOM   1105  CG  PHE A 213     -11.365  21.852  44.016  1.00117.46           C  
ANISOU 1105  CG  PHE A 213    11630  13490  19510  -1208     -6  -1014       C  
ATOM   1106  CD1 PHE A 213     -12.668  22.157  44.371  1.00116.63           C  
ANISOU 1106  CD1 PHE A 213    11506  13227  19579  -1126     43  -1196       C  
ATOM   1107  CD2 PHE A 213     -10.387  21.874  44.996  1.00123.14           C  
ANISOU 1107  CD2 PHE A 213    12279  14352  20155  -1307    -47  -1143       C  
ATOM   1108  CE1 PHE A 213     -12.989  22.477  45.678  1.00115.31           C  
ANISOU 1108  CE1 PHE A 213    11259  13043  19510  -1137     58  -1526       C  
ATOM   1109  CE2 PHE A 213     -10.701  22.192  46.304  1.00121.85           C  
ANISOU 1109  CE2 PHE A 213    12034  14189  20073  -1329    -41  -1465       C  
ATOM   1110  CZ  PHE A 213     -12.004  22.494  46.645  1.00105.82           C  
ANISOU 1110  CZ  PHE A 213     9993  11999  18214  -1242     16  -1670       C  
ATOM   1111  N   GLY A 214     -10.337  22.445  39.303  1.00102.36           N  
ANISOU 1111  N   GLY A 214     9840  11493  17558  -1215   -116   -104       N  
ATOM   1112  CA  GLY A 214      -9.499  22.161  38.157  1.00 96.87           C  
ANISOU 1112  CA  GLY A 214     9180  10932  16692  -1254   -133    131       C  
ATOM   1113  C   GLY A 214      -8.701  23.361  37.699  1.00 92.90           C  
ANISOU 1113  C   GLY A 214     8599  10295  16405  -1320   -235    231       C  
ATOM   1114  O   GLY A 214      -7.613  23.209  37.136  1.00 94.49           O  
ANISOU 1114  O   GLY A 214     8806  10627  16469  -1383   -260    368       O  
ATOM   1115  N   LEU A 215      -9.232  24.564  37.926  1.00 92.62           N  
ANISOU 1115  N   LEU A 215     8478   9987  16725  -1304   -287    162       N  
ATOM   1116  CA  LEU A 215      -8.483  25.763  37.569  1.00 91.85           C  
ANISOU 1116  CA  LEU A 215     8293   9731  16874  -1371   -383    251       C  
ATOM   1117  C   LEU A 215      -7.297  25.972  38.503  1.00103.38           C  
ANISOU 1117  C   LEU A 215     9719  11249  18310  -1489   -426    109       C  
ATOM   1118  O   LEU A 215      -6.232  26.426  38.070  1.00 90.93           O  
ANISOU 1118  O   LEU A 215     8107   9694  16748  -1577   -489    230       O  
ATOM   1119  CB  LEU A 215      -9.403  26.982  37.574  1.00 78.25           C  
ANISOU 1119  CB  LEU A 215     6471   7678  15581  -1313   -416    212       C  
ATOM   1120  CG  LEU A 215     -10.434  27.022  36.444  1.00 59.63           C  
ANISOU 1120  CG  LEU A 215     4105   5258  13293  -1216   -400    423       C  
ATOM   1121  CD1 LEU A 215     -11.174  28.349  36.438  1.00 62.46           C  
ANISOU 1121  CD1 LEU A 215     4326   5270  14136  -1158   -441    418       C  
ATOM   1122  CD2 LEU A 215      -9.769  26.766  35.098  1.00 58.90           C  
ANISOU 1122  CD2 LEU A 215     4040   5331  13008  -1252   -428    719       C  
ATOM   1123  N   GLN A 216      -7.459  25.644  39.787  1.00135.98           N  
ANISOU 1123  N   GLN A 216    13848  15425  22392  -1502   -396   -146       N  
ATOM   1124  CA  GLN A 216      -6.354  25.776  40.731  1.00137.78           C  
ANISOU 1124  CA  GLN A 216    14029  15759  22562  -1631   -440   -287       C  
ATOM   1125  C   GLN A 216      -5.267  24.747  40.446  1.00144.40           C  
ANISOU 1125  C   GLN A 216    14909  16911  23045  -1681   -425   -135       C  
ATOM   1126  O   GLN A 216      -4.110  25.099  40.188  1.00168.83           O  
ANISOU 1126  O   GLN A 216    17962  20070  26117  -1785   -484    -45       O  
ATOM   1127  CB  GLN A 216      -6.864  25.637  42.167  1.00140.96           C  
ANISOU 1127  CB  GLN A 216    14405  16169  22985  -1630   -409   -601       C  
ATOM   1128  CG  GLN A 216      -7.827  26.728  42.602  1.00154.11           C  
ANISOU 1128  CG  GLN A 216    16008  17521  25027  -1587   -415   -815       C  
ATOM   1129  CD  GLN A 216      -8.075  26.719  44.099  1.00163.48           C  
ANISOU 1129  CD  GLN A 216    17148  18745  26223  -1620   -392  -1175       C  
ATOM   1130  OE1 GLN A 216      -7.142  26.820  44.895  1.00161.50           O  
ANISOU 1130  OE1 GLN A 216    16849  18630  25884  -1752   -438  -1308       O  
ATOM   1131  NE2 GLN A 216      -9.338  26.593  44.489  1.00158.37           N  
ANISOU 1131  NE2 GLN A 216    16503  18000  25669  -1506   -320  -1339       N  
ATOM   1132  N   ASP A 217      -5.621  23.466  40.490  1.00108.83           N  
ANISOU 1132  N   ASP A 217     8524  17160  15665  -1226   1947   3239       N  
ATOM   1133  CA  ASP A 217      -4.681  22.380  40.245  1.00106.40           C  
ANISOU 1133  CA  ASP A 217     8094  17075  15257  -1082   2013   3171       C  
ATOM   1134  C   ASP A 217      -4.892  21.853  38.831  1.00103.50           C  
ANISOU 1134  C   ASP A 217     7707  16863  14756   -964   2107   3162       C  
ATOM   1135  O   ASP A 217      -5.978  21.359  38.505  1.00101.19           O  
ANISOU 1135  O   ASP A 217     7522  16472  14453   -853   2141   3070       O  
ATOM   1136  CB  ASP A 217      -4.860  21.264  41.274  1.00104.48           C  
ANISOU 1136  CB  ASP A 217     7893  16750  15057   -928   2014   2996       C  
ATOM   1137  CG  ASP A 217      -3.762  20.218  41.202  1.00101.48           C  
ANISOU 1137  CG  ASP A 217     7380  16581  14595   -794   2063   2931       C  
ATOM   1138  OD1 ASP A 217      -2.792  20.417  40.441  1.00107.94           O  
ANISOU 1138  OD1 ASP A 217     8067  17616  15328   -831   2094   3025       O  
ATOM   1139  OD2 ASP A 217      -3.870  19.194  41.910  1.00 91.01           O  
ANISOU 1139  OD2 ASP A 217     6082  15206  13293   -649   2068   2788       O  
ATOM   1140  N   ASP A 218      -3.854  21.951  38.000  1.00111.13           N  
ANISOU 1140  N   ASP A 218     8531  18077  15618   -986   2147   3259       N  
ATOM   1141  CA  ASP A 218      -3.927  21.481  36.622  1.00109.90           C  
ANISOU 1141  CA  ASP A 218     8337  18102  15320   -877   2236   3261       C  
ATOM   1142  C   ASP A 218      -3.736  19.976  36.496  1.00 92.72           C  
ANISOU 1142  C   ASP A 218     6128  16031  13071   -643   2306   3085       C  
ATOM   1143  O   ASP A 218      -3.913  19.436  35.398  1.00 85.88           O  
ANISOU 1143  O   ASP A 218     5243  15298  12088   -525   2380   3052       O  
ATOM   1144  CB  ASP A 218      -2.886  22.203  35.761  1.00108.06           C  
ANISOU 1144  CB  ASP A 218     7958  18103  14997   -993   2251   3443       C  
ATOM   1145  CG  ASP A 218      -3.178  23.685  35.605  1.00115.70           C  
ANISOU 1145  CG  ASP A 218     8965  18971  16025  -1216   2185   3626       C  
ATOM   1146  OD1 ASP A 218      -4.184  24.160  36.175  1.00121.40           O  
ANISOU 1146  OD1 ASP A 218     9826  19440  16860  -1277   2128   3605       O  
ATOM   1147  OD2 ASP A 218      -2.403  24.375  34.910  1.00 91.54           O  
ANISOU 1147  OD2 ASP A 218     5795  16084  12902  -1328   2189   3793       O  
ATOM   1148  N   SER A 219      -3.383  19.289  37.581  1.00111.90           N  
ANISOU 1148  N   SER A 219     8549  18403  15565   -573   2281   2972       N  
ATOM   1149  CA  SER A 219      -3.202  17.844  37.563  1.00115.03           C  
ANISOU 1149  CA  SER A 219     8923  18872  15912   -351   2334   2801       C  
ATOM   1150  C   SER A 219      -4.475  17.082  37.909  1.00103.76           C  
ANISOU 1150  C   SER A 219     7649  17234  14541   -219   2334   2638       C  
ATOM   1151  O   SER A 219      -4.462  15.847  37.900  1.00121.27           O  
ANISOU 1151  O   SER A 219     9865  19479  16732    -31   2370   2485       O  
ATOM   1152  CB  SER A 219      -2.082  17.440  38.529  1.00116.08           C  
ANISOU 1152  CB  SER A 219     8955  19066  16082   -335   2305   2770       C  
ATOM   1153  OG  SER A 219      -2.409  17.786  39.864  1.00124.12           O  
ANISOU 1153  OG  SER A 219    10051  19876  17235   -417   2225   2755       O  
ATOM   1154  N   LYS A 220      -5.567  17.781  38.216  1.00100.19           N  
ANISOU 1154  N   LYS A 220     7328  16569  14172   -312   2292   2667       N  
ATOM   1155  CA  LYS A 220      -6.832  17.120  38.510  1.00 89.98           C  
ANISOU 1155  CA  LYS A 220     6180  15076  12932   -194   2292   2526       C  
ATOM   1156  C   LYS A 220      -7.659  16.852  37.261  1.00 83.88           C  
ANISOU 1156  C   LYS A 220     5455  14335  12079   -106   2352   2495       C  
ATOM   1157  O   LYS A 220      -8.440  15.893  37.239  1.00 97.52           O  
ANISOU 1157  O   LYS A 220     7264  15973  13816     51   2372   2345       O  
ATOM   1158  CB  LYS A 220      -7.652  17.957  39.496  1.00 93.01           C  
ANISOU 1158  CB  LYS A 220     6682  15210  13448   -325   2217   2564       C  
ATOM   1159  CG  LYS A 220      -7.002  18.110  40.861  1.00 92.37           C  
ANISOU 1159  CG  LYS A 220     6570  15070  13454   -392   2151   2569       C  
ATOM   1160  CD  LYS A 220      -7.899  18.872  41.823  1.00 77.44           C  
ANISOU 1160  CD  LYS A 220     4803  12928  11690   -502   2079   2592       C  
ATOM   1161  CE  LYS A 220      -7.238  19.023  43.183  1.00 74.43           C  
ANISOU 1161  CE  LYS A 220     4387  12504  11391   -567   2012   2595       C  
ATOM   1162  NZ  LYS A 220      -8.096  19.777  44.135  1.00 82.96           N  
ANISOU 1162  NZ  LYS A 220     5584  13344  12593   -671   1941   2614       N  
ATOM   1163  N   VAL A 221      -7.507  17.675  36.220  1.00 78.99           N  
ANISOU 1163  N   VAL A 221     4788  13845  11381   -205   2376   2637       N  
ATOM   1164  CA  VAL A 221      -8.227  17.471  34.966  1.00 79.06           C  
ANISOU 1164  CA  VAL A 221     4828  13913  11299   -125   2433   2622       C  
ATOM   1165  C   VAL A 221      -7.340  16.902  33.867  1.00 82.33           C  
ANISOU 1165  C   VAL A 221     5110  14614  11558    -24   2507   2620       C  
ATOM   1166  O   VAL A 221      -7.859  16.526  32.803  1.00 81.43           O  
ANISOU 1166  O   VAL A 221     5011  14577  11351     76   2560   2581       O  
ATOM   1167  CB  VAL A 221      -8.884  18.780  34.478  1.00 88.43           C  
ANISOU 1167  CB  VAL A 221     6068  15031  12499   -294   2409   2785       C  
ATOM   1168  CG1 VAL A 221      -9.951  19.236  35.460  1.00106.37           C  
ANISOU 1168  CG1 VAL A 221     8487  17008  14922   -365   2342   2765       C  
ATOM   1169  CG2 VAL A 221      -7.833  19.862  34.280  1.00 81.29           C  
ANISOU 1169  CG2 VAL A 221     5052  14270  11564   -475   2388   2979       C  
ATOM   1170  N   PHE A 222      -6.028  16.826  34.084  1.00104.55           N  
ANISOU 1170  N   PHE A 222     7793  17594  14339    -42   2512   2659       N  
ATOM   1171  CA  PHE A 222      -5.093  16.240  33.131  1.00 91.07           C  
ANISOU 1171  CA  PHE A 222     5950  16166  12485     63   2581   2652       C  
ATOM   1172  C   PHE A 222      -4.453  15.013  33.763  1.00 90.33           C  
ANISOU 1172  C   PHE A 222     5811  16097  12412    222   2589   2492       C  
ATOM   1173  O   PHE A 222      -3.774  15.124  34.789  1.00 85.07           O  
ANISOU 1173  O   PHE A 222     5105  15395  11824    162   2544   2508       O  
ATOM   1174  CB  PHE A 222      -4.016  17.245  32.717  1.00 87.55           C  
ANISOU 1174  CB  PHE A 222     5370  15923  11974    -98   2582   2856       C  
ATOM   1175  CG  PHE A 222      -4.447  18.188  31.632  1.00 88.43           C  
ANISOU 1175  CG  PHE A 222     5488  16104  12008   -203   2600   3011       C  
ATOM   1176  CD1 PHE A 222      -4.509  17.763  30.315  1.00 89.66           C  
ANISOU 1176  CD1 PHE A 222     5600  16460  12008    -89   2674   3000       C  
ATOM   1177  CD2 PHE A 222      -4.775  19.501  31.924  1.00 88.16           C  
ANISOU 1177  CD2 PHE A 222     5503  15938  12056   -414   2537   3169       C  
ATOM   1178  CE1 PHE A 222      -4.900  18.627  29.310  1.00 90.57           C  
ANISOU 1178  CE1 PHE A 222     5717  16651  12045   -184   2688   3152       C  
ATOM   1179  CE2 PHE A 222      -5.166  20.371  30.924  1.00 89.07           C  
ANISOU 1179  CE2 PHE A 222     5625  16113  12105   -511   2546   3320       C  
ATOM   1180  CZ  PHE A 222      -5.228  19.933  29.614  1.00 90.27           C  
ANISOU 1180  CZ  PHE A 222     5729  16474  12095   -397   2623   3316       C  
ATOM   1181  N   LYS A 223      -4.670  13.848  33.152  1.00109.97           N  
ANISOU 1181  N   LYS A 223     8306  18646  14834    426   2640   2338       N  
ATOM   1182  CA  LYS A 223      -4.043  12.605  33.600  1.00108.69           C  
ANISOU 1182  CA  LYS A 223     8096  18517  14685    593   2649   2183       C  
ATOM   1183  C   LYS A 223      -2.908  12.275  32.634  1.00114.27           C  
ANISOU 1183  C   LYS A 223     8644  19530  15243    668   2714   2212       C  
ATOM   1184  O   LYS A 223      -3.059  11.503  31.685  1.00129.87           O  
ANISOU 1184  O   LYS A 223    10608  21615  17120    826   2768   2116       O  
ATOM   1185  CB  LYS A 223      -5.071  11.478  33.689  1.00125.55           C  
ANISOU 1185  CB  LYS A 223    10353  20480  16871    772   2649   1980       C  
ATOM   1186  CG  LYS A 223      -4.508  10.166  34.224  1.00121.75           C  
ANISOU 1186  CG  LYS A 223     9836  19997  16425    944   2646   1817       C  
ATOM   1187  CD  LYS A 223      -5.588   9.102  34.361  1.00136.18           C  
ANISOU 1187  CD  LYS A 223    11793  21627  18322   1104   2632   1624       C  
ATOM   1188  CE  LYS A 223      -6.563   9.435  35.481  1.00144.59           C  
ANISOU 1188  CE  LYS A 223    12995  22415  19527   1022   2566   1616       C  
ATOM   1189  NZ  LYS A 223      -7.666   8.437  35.578  1.00146.24           N  
ANISOU 1189  NZ  LYS A 223    13329  22433  19802   1169   2549   1438       N  
ATOM   1190  N   GLU A 224      -1.751  12.889  32.891  1.00132.21           N  
ANISOU 1190  N   GLU A 224    10790  21947  17499    551   2705   2347       N  
ATOM   1191  CA  GLU A 224      -0.529  12.687  32.108  1.00105.05           C  
ANISOU 1191  CA  GLU A 224     7181  18810  13922    601   2761   2397       C  
ATOM   1192  C   GLU A 224      -0.753  13.008  30.628  1.00 93.95           C  
ANISOU 1192  C   GLU A 224     5746  17594  12358    610   2825   2472       C  
ATOM   1193  O   GLU A 224      -0.565  12.171  29.742  1.00 95.18           O  
ANISOU 1193  O   GLU A 224     5853  17917  12395    780   2885   2381       O  
ATOM   1194  CB  GLU A 224       0.009  11.263  32.291  1.00 92.97           C  
ANISOU 1194  CB  GLU A 224     5605  17332  12387    816   2783   2216       C  
ATOM   1195  CG  GLU A 224       0.486  10.963  33.702  1.00106.97           C  
ANISOU 1195  CG  GLU A 224     7372  18976  14296    806   2723   2167       C  
ATOM   1196  CD  GLU A 224       0.980   9.539  33.858  1.00119.37           C  
ANISOU 1196  CD  GLU A 224     8901  20586  15870   1023   2739   1992       C  
ATOM   1197  OE1 GLU A 224       0.687   8.708  32.973  1.00115.87           O  
ANISOU 1197  OE1 GLU A 224     8470  20204  15350   1191   2788   1876       O  
ATOM   1198  OE2 GLU A 224       1.665   9.252  34.863  1.00128.31           O  
ANISOU 1198  OE2 GLU A 224     9984  21684  17083   1026   2700   1971       O  
ATOM   1199  N   GLY A 225      -1.161  14.252  30.375  1.00 93.86           N  
ANISOU 1199  N   GLY A 225     5765  17554  12345    424   2806   2643       N  
ATOM   1200  CA  GLY A 225      -1.333  14.752  29.031  1.00 95.35           C  
ANISOU 1200  CA  GLY A 225     5918  17925  12384    398   2856   2754       C  
ATOM   1201  C   GLY A 225      -2.728  14.603  28.457  1.00125.17           C  
ANISOU 1201  C   GLY A 225     9834  21577  16149    463   2868   2681       C  
ATOM   1202  O   GLY A 225      -3.057  15.291  27.484  1.00140.86           O  
ANISOU 1202  O   GLY A 225    11814  23668  18037    396   2892   2804       O  
ATOM   1203  N   SER A 226      -3.556  13.735  29.029  1.00118.88           N  
ANISOU 1203  N   SER A 226     9158  20561  15449    588   2848   2490       N  
ATOM   1204  CA  SER A 226      -4.914  13.515  28.551  1.00104.31           C  
ANISOU 1204  CA  SER A 226     7445  18583  13605    657   2855   2406       C  
ATOM   1205  C   SER A 226      -5.905  14.242  29.449  1.00119.81           C  
ANISOU 1205  C   SER A 226     9545  20250  15726    519   2787   2444       C  
ATOM   1206  O   SER A 226      -5.802  14.186  30.677  1.00122.85           O  
ANISOU 1206  O   SER A 226     9967  20463  16249    478   2734   2404       O  
ATOM   1207  CB  SER A 226      -5.242  12.021  28.504  1.00107.99           C  
ANISOU 1207  CB  SER A 226     7955  19001  14076    897   2875   2164       C  
ATOM   1208  OG  SER A 226      -5.012  11.406  29.759  1.00102.21           O  
ANISOU 1208  OG  SER A 226     7250  18100  13484    937   2831   2053       O  
ATOM   1209  N   CYS A 227      -6.864  14.926  28.828  1.00121.97           N  
ANISOU 1209  N   CYS A 227     9893  20472  15977    449   2787   2523       N  
ATOM   1210  CA  CYS A 227      -7.834  15.748  29.550  1.00100.03           C  
ANISOU 1210  CA  CYS A 227     7241  17426  13339    308   2724   2580       C  
ATOM   1211  C   CYS A 227      -8.987  14.865  30.013  1.00 98.33           C  
ANISOU 1211  C   CYS A 227     7163  16979  13219    443   2708   2384       C  
ATOM   1212  O   CYS A 227      -9.916  14.585  29.252  1.00123.90           O  
ANISOU 1212  O   CYS A 227    10465  20199  16412    529   2734   2327       O  
ATOM   1213  CB  CYS A 227      -8.325  16.892  28.670  1.00100.69           C  
ANISOU 1213  CB  CYS A 227     7337  17557  13362    172   2727   2762       C  
ATOM   1214  SG  CYS A 227      -9.720  17.818  29.350  1.00105.19           S  
ANISOU 1214  SG  CYS A 227     8076  17795  14096     29   2655   2815       S  
ATOM   1215  N   LEU A 228      -8.924  14.423  31.267  1.00 80.95           N  
ANISOU 1215  N   LEU A 228     5006  14604  11148    463   2663   2286       N  
ATOM   1216  CA  LEU A 228      -9.998  13.650  31.875  1.00 99.76           C  
ANISOU 1216  CA  LEU A 228     7520  16747  13638    572   2636   2116       C  
ATOM   1217  C   LEU A 228      -9.846  13.723  33.387  1.00 90.69           C  
ANISOU 1217  C   LEU A 228     6412  15413  12634    507   2572   2096       C  
ATOM   1218  O   LEU A 228      -8.785  14.085  33.903  1.00 88.26           O  
ANISOU 1218  O   LEU A 228     6015  15188  12332    421   2555   2176       O  
ATOM   1219  CB  LEU A 228      -9.996  12.196  31.382  1.00114.06           C  
ANISOU 1219  CB  LEU A 228     9318  18624  15393    804   2677   1918       C  
ATOM   1220  CG  LEU A 228      -8.675  11.422  31.436  1.00 95.01           C  
ANISOU 1220  CG  LEU A 228     6781  16390  12927    901   2702   1860       C  
ATOM   1221  CD1 LEU A 228      -8.550  10.645  32.736  1.00 79.31           C  
ANISOU 1221  CD1 LEU A 228     4832  14231  11072    963   2653   1733       C  
ATOM   1222  CD2 LEU A 228      -8.537  10.494  30.235  1.00 87.60           C  
ANISOU 1222  CD2 LEU A 228     5791  15635  11858   1085   2763   1753       C  
ATOM   1223  N   LEU A 229     -10.922  13.376  34.092  1.00 83.89           N  
ANISOU 1223  N   LEU A 229     5684  14307  11885    550   2533   1993       N  
ATOM   1224  CA  LEU A 229     -10.915  13.433  35.549  1.00 81.23           C  
ANISOU 1224  CA  LEU A 229     5397  13788  11678    496   2470   1973       C  
ATOM   1225  C   LEU A 229      -9.872  12.478  36.116  1.00 91.27           C  
ANISOU 1225  C   LEU A 229     6588  15140  12950    600   2470   1877       C  
ATOM   1226  O   LEU A 229      -9.899  11.275  35.836  1.00 99.52           O  
ANISOU 1226  O   LEU A 229     7631  16210  13971    779   2494   1723       O  
ATOM   1227  CB  LEU A 229     -12.299  13.096  36.100  1.00 96.17           C  
ANISOU 1227  CB  LEU A 229     7446  15422  13674    550   2435   1872       C  
ATOM   1228  CG  LEU A 229     -13.234  14.277  36.356  1.00 89.32           C  
ANISOU 1228  CG  LEU A 229     6674  14385  12880    395   2398   1989       C  
ATOM   1229  CD1 LEU A 229     -14.565  13.793  36.907  1.00 67.88           C  
ANISOU 1229  CD1 LEU A 229     4105  11424  10263    472   2368   1878       C  
ATOM   1230  CD2 LEU A 229     -12.586  15.271  37.308  1.00 79.08           C  
ANISOU 1230  CD2 LEU A 229     5347  13054  11646    219   2348   2118       C  
ATOM   1231  N   ALA A 230      -8.954  13.021  36.918  1.00 90.84           N  
ANISOU 1231  N   ALA A 230     6465  15120  12929    485   2437   1969       N  
ATOM   1232  CA  ALA A 230      -7.890  12.236  37.525  1.00 92.52           C  
ANISOU 1232  CA  ALA A 230     6591  15415  13148    566   2432   1900       C  
ATOM   1233  C   ALA A 230      -7.993  12.129  39.038  1.00 94.37           C  
ANISOU 1233  C   ALA A 230     6883  15468  13505    540   2364   1865       C  
ATOM   1234  O   ALA A 230      -7.352  11.249  39.620  1.00108.59           O  
ANISOU 1234  O   ALA A 230     8638  17295  15325    642   2353   1776       O  
ATOM   1235  CB  ALA A 230      -6.519  12.825  37.163  1.00111.99           C  
ANISOU 1235  CB  ALA A 230     8899  18119  15534    473   2453   2034       C  
ATOM   1236  N   ASP A 231      -8.771  12.993  39.684  1.00 99.14           N  
ANISOU 1236  N   ASP A 231     7585  15892  14191    412   2317   1933       N  
ATOM   1237  CA  ASP A 231      -8.930  12.945  41.132  1.00101.40           C  
ANISOU 1237  CA  ASP A 231     7932  16010  14588    387   2253   1907       C  
ATOM   1238  C   ASP A 231      -9.846  11.783  41.500  1.00 93.62           C  
ANISOU 1238  C   ASP A 231     7056  14865  13650    555   2245   1743       C  
ATOM   1239  O   ASP A 231     -11.017  11.758  41.107  1.00 97.02           O  
ANISOU 1239  O   ASP A 231     7596  15172  14096    585   2253   1705       O  
ATOM   1240  CB  ASP A 231      -9.494  14.267  41.649  1.00 86.64           C  
ANISOU 1240  CB  ASP A 231     6131  13998  12790    200   2206   2032       C  
ATOM   1241  CG  ASP A 231      -9.399  14.394  43.158  1.00 88.48           C  
ANISOU 1241  CG  ASP A 231     6395  14099  13124    150   2139   2032       C  
ATOM   1242  OD1 ASP A 231      -8.863  13.470  43.806  1.00 94.52           O  
ANISOU 1242  OD1 ASP A 231     7123  14892  13898    257   2130   1946       O  
ATOM   1243  OD2 ASP A 231      -9.859  15.422  43.698  1.00 89.32           O  
ANISOU 1243  OD2 ASP A 231     6561  14074  13302      6   2094   2119       O  
ATOM   1244  N   ASP A 232      -9.310  10.820  42.255  1.00101.29           N  
ANISOU 1244  N   ASP A 232     7999  15839  14649    662   2225   1650       N  
ATOM   1245  CA  ASP A 232     -10.093   9.646  42.630  1.00109.99           C  
ANISOU 1245  CA  ASP A 232     9200  16793  15798    822   2209   1498       C  
ATOM   1246  C   ASP A 232     -11.256  10.020  43.540  1.00114.93           C  
ANISOU 1246  C   ASP A 232     9970  17182  16517    768   2162   1512       C  
ATOM   1247  O   ASP A 232     -12.344   9.438  43.435  1.00125.04           O  
ANISOU 1247  O   ASP A 232    11364  18320  17827    861   2158   1423       O  
ATOM   1248  CB  ASP A 232      -9.192   8.609  43.300  1.00126.54           C  
ANISOU 1248  CB  ASP A 232    11227  18943  17909    936   2190   1415       C  
ATOM   1249  CG  ASP A 232      -8.102   8.102  42.376  1.00141.76           C  
ANISOU 1249  CG  ASP A 232    13016  21093  19752   1016   2240   1384       C  
ATOM   1250  OD1 ASP A 232      -8.336   8.057  41.149  1.00141.13           O  
ANISOU 1250  OD1 ASP A 232    12926  21092  19603   1055   2291   1363       O  
ATOM   1251  OD2 ASP A 232      -7.013   7.750  42.875  1.00154.72           O  
ANISOU 1251  OD2 ASP A 232    14557  22834  21396   1043   2228   1384       O  
ATOM   1252  N   ASN A 233     -11.046  10.981  44.444  1.00 92.71           N  
ANISOU 1252  N   ASN A 233     7153  14320  13754    621   2123   1624       N  
ATOM   1253  CA  ASN A 233     -12.136  11.437  45.300  1.00 81.62           C  
ANISOU 1253  CA  ASN A 233     5881  12691  12440    564   2082   1647       C  
ATOM   1254  C   ASN A 233     -13.275  12.015  44.472  1.00 77.60           C  
ANISOU 1254  C   ASN A 233     5462  12090  11931    523   2104   1674       C  
ATOM   1255  O   ASN A 233     -14.451  11.740  44.741  1.00 73.47           O  
ANISOU 1255  O   ASN A 233     5069  11381  11466    575   2091   1621       O  
ATOM   1256  CB  ASN A 233     -11.624  12.473  46.302  1.00 71.60           C  
ANISOU 1256  CB  ASN A 233     4577  11405  11224    403   2037   1763       C  
ATOM   1257  CG  ASN A 233     -10.708  11.871  47.348  1.00 90.92           C  
ANISOU 1257  CG  ASN A 233     6956  13902  13689    450   2005   1734       C  
ATOM   1258  OD1 ASN A 233     -10.249  10.738  47.211  1.00102.96           O  
ANISOU 1258  OD1 ASN A 233     8438  15506  15178    595   2020   1640       O  
ATOM   1259  ND2 ASN A 233     -10.436  12.632  48.403  1.00 92.61           N  
ANISOU 1259  ND2 ASN A 233     7157  14069  13962    330   1955   1815       N  
ATOM   1260  N   PHE A 234     -12.942  12.817  43.456  1.00 76.62           N  
ANISOU 1260  N   PHE A 234     5272  12096  11745    429   2136   1762       N  
ATOM   1261  CA  PHE A 234     -13.969  13.366  42.576  1.00 64.32           C  
ANISOU 1261  CA  PHE A 234     3788  10469  10180    393   2158   1796       C  
ATOM   1262  C   PHE A 234     -14.732  12.253  41.872  1.00 65.93           C  
ANISOU 1262  C   PHE A 234     4051  10645  10356    566   2189   1660       C  
ATOM   1263  O   PHE A 234     -15.966  12.270  41.822  1.00 76.72           O  
ANISOU 1263  O   PHE A 234     5536  11842  11772    588   2181   1633       O  
ATOM   1264  CB  PHE A 234     -13.340  14.312  41.551  1.00 72.84           C  
ANISOU 1264  CB  PHE A 234     4770  11721  11183    273   2188   1921       C  
ATOM   1265  CG  PHE A 234     -13.098  15.701  42.069  1.00 73.02           C  
ANISOU 1265  CG  PHE A 234     4782  11702  11259     69   2144   2072       C  
ATOM   1266  CD1 PHE A 234     -13.389  16.029  43.383  1.00 67.06           C  
ANISOU 1266  CD1 PHE A 234     4093  10774  10612     10   2085   2080       C  
ATOM   1267  CD2 PHE A 234     -12.594  16.684  41.234  1.00 84.32           C  
ANISOU 1267  CD2 PHE A 234     6138  13263  12636    -63   2157   2207       C  
ATOM   1268  CE1 PHE A 234     -13.170  17.309  43.858  1.00 80.27           C  
ANISOU 1268  CE1 PHE A 234     5756  12399  12343   -177   2036   2208       C  
ATOM   1269  CE2 PHE A 234     -12.374  17.966  41.702  1.00 97.26           C  
ANISOU 1269  CE2 PHE A 234     7771  14849  14335   -256   2104   2342       C  
ATOM   1270  CZ  PHE A 234     -12.662  18.279  43.016  1.00 92.35           C  
ANISOU 1270  CZ  PHE A 234     7214  14047  13826   -313   2041   2336       C  
ATOM   1271  N   VAL A 235     -14.011  11.264  41.340  1.00 73.30           N  
ANISOU 1271  N   VAL A 235     4901  11733  11216    693   2220   1568       N  
ATOM   1272  CA  VAL A 235     -14.662  10.164  40.632  1.00 76.91           C  
ANISOU 1272  CA  VAL A 235     5405  12168  11649    861   2242   1425       C  
ATOM   1273  C   VAL A 235     -15.631   9.439  41.556  1.00 71.65           C  
ANISOU 1273  C   VAL A 235     4870  11276  11075    945   2195   1330       C  
ATOM   1274  O   VAL A 235     -16.807   9.246  41.221  1.00 69.38           O  
ANISOU 1274  O   VAL A 235     4688  10857  10816    992   2192   1282       O  
ATOM   1275  CB  VAL A 235     -13.609   9.204  40.049  1.00 77.71           C  
ANISOU 1275  CB  VAL A 235     5390  12465  11674    984   2275   1336       C  
ATOM   1276  CG1 VAL A 235     -14.280   7.986  39.431  1.00 84.29           C  
ANISOU 1276  CG1 VAL A 235     6274  13252  12499   1163   2283   1168       C  
ATOM   1277  CG2 VAL A 235     -12.752   9.922  39.018  1.00 72.17           C  
ANISOU 1277  CG2 VAL A 235     4564  11989  10868    906   2328   1440       C  
ATOM   1278  N   LEU A 236     -15.163   9.060  42.749  1.00 72.32           N  
ANISOU 1278  N   LEU A 236     4953  11314  11211    960   2156   1314       N  
ATOM   1279  CA  LEU A 236     -16.006   8.310  43.676  1.00 65.88           C  
ANISOU 1279  CA  LEU A 236     4258  10295  10477   1042   2112   1236       C  
ATOM   1280  C   LEU A 236     -17.233   9.116  44.089  1.00 73.55           C  
ANISOU 1280  C   LEU A 236     5359  11062  11525    953   2094   1303       C  
ATOM   1281  O   LEU A 236     -18.371   8.642  43.970  1.00 91.59           O  
ANISOU 1281  O   LEU A 236     7757  13194  13848   1025   2084   1237       O  
ATOM   1282  CB  LEU A 236     -15.197   7.905  44.909  1.00 69.78           C  
ANISOU 1282  CB  LEU A 236     4715  10794  11006   1057   2076   1234       C  
ATOM   1283  CG  LEU A 236     -14.032   6.937  44.700  1.00 83.14           C  
ANISOU 1283  CG  LEU A 236     6289  12653  12647   1167   2084   1152       C  
ATOM   1284  CD1 LEU A 236     -13.218   6.795  45.978  1.00 88.56           C  
ANISOU 1284  CD1 LEU A 236     6931  13347  13373   1153   2046   1184       C  
ATOM   1285  CD2 LEU A 236     -14.540   5.584  44.233  1.00 82.52           C  
ANISOU 1285  CD2 LEU A 236     6260  12525  12570   1344   2077    995       C  
ATOM   1286  N   ILE A 237     -17.022  10.346  44.567  1.00 69.80           N  
ANISOU 1286  N   ILE A 237     4867  10574  11079    794   2086   1433       N  
ATOM   1287  CA  ILE A 237     -18.135  11.131  45.093  1.00 62.98           C  
ANISOU 1287  CA  ILE A 237     4122   9502  10305    711   2065   1492       C  
ATOM   1288  C   ILE A 237     -19.133  11.457  43.990  1.00 60.30           C  
ANISOU 1288  C   ILE A 237     3842   9114   9957    708   2092   1495       C  
ATOM   1289  O   ILE A 237     -20.348  11.319  44.177  1.00 83.87           O  
ANISOU 1289  O   ILE A 237     6951  11906  13010    742   2080   1461       O  
ATOM   1290  CB  ILE A 237     -17.615  12.402  45.787  1.00 58.23           C  
ANISOU 1290  CB  ILE A 237     3478   8905   9742    539   2043   1622       C  
ATOM   1291  CG1 ILE A 237     -16.716  12.030  46.968  1.00 66.38           C  
ANISOU 1291  CG1 ILE A 237     4457   9974  10791    550   2011   1614       C  
ATOM   1292  CG2 ILE A 237     -18.776  13.255  46.268  1.00 56.94           C  
ANISOU 1292  CG2 ILE A 237     3433   8522   9678    455   2022   1674       C  
ATOM   1293  CD1 ILE A 237     -16.192  13.223  47.735  1.00 58.99           C  
ANISOU 1293  CD1 ILE A 237     3477   9039   9899    384   1979   1730       C  
ATOM   1294  N   GLY A 238     -18.646  11.879  42.822  1.00 58.69           N  
ANISOU 1294  N   GLY A 238     3547   9084   9667    669   2130   1539       N  
ATOM   1295  CA  GLY A 238     -19.550  12.200  41.734  1.00 61.26           C  
ANISOU 1295  CA  GLY A 238     3917   9381   9977    669   2157   1550       C  
ATOM   1296  C   GLY A 238     -20.310  10.993  41.220  1.00 71.42           C  
ANISOU 1296  C   GLY A 238     5267  10618  11253    836   2164   1407       C  
ATOM   1297  O   GLY A 238     -21.487  11.101  40.867  1.00 86.80           O  
ANISOU 1297  O   GLY A 238     7308  12429  13243    851   2164   1394       O  
ATOM   1298  N   SER A 239     -19.655   9.829  41.164  1.00 70.57           N  
ANISOU 1298  N   SER A 239     5105  10613  11096    964   2166   1294       N  
ATOM   1299  CA  SER A 239     -20.370   8.613  40.796  1.00 78.71           C  
ANISOU 1299  CA  SER A 239     6200  11576  12130   1123   2156   1146       C  
ATOM   1300  C   SER A 239     -21.473   8.312  41.799  1.00 73.55           C  
ANISOU 1300  C   SER A 239     5694  10664  11586   1144   2109   1118       C  
ATOM   1301  O   SER A 239     -22.588   7.938  41.415  1.00 79.06           O  
ANISOU 1301  O   SER A 239     6486  11238  12317   1204   2099   1058       O  
ATOM   1302  CB  SER A 239     -19.396   7.438  40.696  1.00 91.47           C  
ANISOU 1302  CB  SER A 239     7730  13332  13692   1250   2155   1030       C  
ATOM   1303  OG  SER A 239     -18.386   7.689  39.734  1.00 76.69           O  
ANISOU 1303  OG  SER A 239     5721  11698  11720   1236   2205   1054       O  
ATOM   1304  N   PHE A 240     -21.181   8.470  43.091  1.00 85.88           N  
ANISOU 1304  N   PHE A 240     7277  12147  13207   1093   2080   1164       N  
ATOM   1305  CA  PHE A 240     -22.222   8.312  44.101  1.00 89.64           C  
ANISOU 1305  CA  PHE A 240     7892  12380  13788   1097   2043   1156       C  
ATOM   1306  C   PHE A 240     -23.265   9.420  44.000  1.00 94.10           C  
ANISOU 1306  C   PHE A 240     8537  12800  14416    993   2051   1238       C  
ATOM   1307  O   PHE A 240     -24.470   9.147  43.946  1.00 95.87           O  
ANISOU 1307  O   PHE A 240     8874  12853  14698   1033   2039   1195       O  
ATOM   1308  CB  PHE A 240     -21.597   8.285  45.497  1.00 86.36           C  
ANISOU 1308  CB  PHE A 240     7466  11934  13412   1065   2016   1192       C  
ATOM   1309  CG  PHE A 240     -20.793   7.049  45.777  1.00100.29           C  
ANISOU 1309  CG  PHE A 240     9177  13787  15140   1184   1998   1103       C  
ATOM   1310  CD1 PHE A 240     -21.269   5.801  45.416  1.00102.48           C  
ANISOU 1310  CD1 PHE A 240     9505  14018  15415   1323   1978    981       C  
ATOM   1311  CD2 PHE A 240     -19.557   7.137  46.395  1.00114.91           C  
ANISOU 1311  CD2 PHE A 240    10926  15766  16968   1155   1993   1141       C  
ATOM   1312  CE1 PHE A 240     -20.530   4.661  45.669  1.00123.04           C  
ANISOU 1312  CE1 PHE A 240    12059  16695  17997   1435   1955    898       C  
ATOM   1313  CE2 PHE A 240     -18.812   6.001  46.651  1.00128.87           C  
ANISOU 1313  CE2 PHE A 240    12641  17611  18711   1269   1974   1060       C  
ATOM   1314  CZ  PHE A 240     -19.300   4.762  46.287  1.00139.61           C  
ANISOU 1314  CZ  PHE A 240    14054  18918  20073   1410   1955    938       C  
ATOM   1315  N   VAL A 241     -22.820  10.678  43.965  1.00 78.75           N  
ANISOU 1315  N   VAL A 241     6534  10918  12468    856   2067   1357       N  
ATOM   1316  CA  VAL A 241     -23.750  11.803  44.045  1.00 83.42           C  
ANISOU 1316  CA  VAL A 241     7200  11356  13139    749   2066   1441       C  
ATOM   1317  C   VAL A 241     -24.582  11.915  42.772  1.00 87.66           C  
ANISOU 1317  C   VAL A 241     7764  11887  13657    774   2091   1428       C  
ATOM   1318  O   VAL A 241     -25.809  12.062  42.826  1.00 99.11           O  
ANISOU 1318  O   VAL A 241     9323  13148  15187    778   2082   1417       O  
ATOM   1319  CB  VAL A 241     -22.990  13.109  44.338  1.00 70.80           C  
ANISOU 1319  CB  VAL A 241     5527   9827  11546    589   2063   1571       C  
ATOM   1320  CG1 VAL A 241     -23.867  14.316  44.042  1.00 68.99           C  
ANISOU 1320  CG1 VAL A 241     5354   9474  11385    480   2063   1657       C  
ATOM   1321  CG2 VAL A 241     -22.524  13.134  45.785  1.00 57.92           C  
ANISOU 1321  CG2 VAL A 241     3900   8140   9969    557   2030   1584       C  
ATOM   1322  N   SER A 242     -23.934  11.844  41.610  1.00 68.43           N  
ANISOU 1322  N   SER A 242     5225   9660  11113    794   2124   1429       N  
ATOM   1323  CA  SER A 242     -24.632  12.142  40.365  1.00 80.83           C  
ANISOU 1323  CA  SER A 242     6804  11250  12657    799   2152   1441       C  
ATOM   1324  C   SER A 242     -25.348  10.934  39.774  1.00 90.82           C  
ANISOU 1324  C   SER A 242     8120  12482  13906    956   2150   1299       C  
ATOM   1325  O   SER A 242     -26.455  11.075  39.248  1.00106.72           O  
ANISOU 1325  O   SER A 242    10205  14385  15960    971   2152   1290       O  
ATOM   1326  CB  SER A 242     -23.655  12.713  39.333  1.00 71.72           C  
ANISOU 1326  CB  SER A 242     5515  10346  11389    740   2192   1521       C  
ATOM   1327  OG  SER A 242     -23.095  13.935  39.781  1.00 69.47           O  
ANISOU 1327  OG  SER A 242     5190  10079  11128    576   2183   1663       O  
ATOM   1328  N   PHE A 243     -24.751   9.745  39.845  1.00 80.53           N  
ANISOU 1328  N   PHE A 243     6782  11265  12551   1074   2141   1186       N  
ATOM   1329  CA  PHE A 243     -25.265   8.591  39.114  1.00 83.13           C  
ANISOU 1329  CA  PHE A 243     7137  11596  12851   1222   2132   1043       C  
ATOM   1330  C   PHE A 243     -26.067   7.637  39.996  1.00 81.12           C  
ANISOU 1330  C   PHE A 243     7007  11130  12684   1299   2078    951       C  
ATOM   1331  O   PHE A 243     -27.229   7.343  39.701  1.00 71.33           O  
ANISOU 1331  O   PHE A 243     5861   9748  11491   1341   2058    899       O  
ATOM   1332  CB  PHE A 243     -24.100   7.851  38.441  1.00 63.85           C  
ANISOU 1332  CB  PHE A 243     4569   9396  10297   1313   2154    963       C  
ATOM   1333  CG  PHE A 243     -24.534   6.800  37.462  1.00 56.48           C  
ANISOU 1333  CG  PHE A 243     3640   8498   9323   1462   2148    813       C  
ATOM   1334  CD1 PHE A 243     -25.217   7.150  36.309  1.00 56.70           C  
ANISOU 1334  CD1 PHE A 243     3668   8557   9319   1471   2175    818       C  
ATOM   1335  CD2 PHE A 243     -24.247   5.464  37.686  1.00 56.78           C  
ANISOU 1335  CD2 PHE A 243     3676   8539   9358   1597   2109    667       C  
ATOM   1336  CE1 PHE A 243     -25.615   6.185  35.403  1.00 62.17           C  
ANISOU 1336  CE1 PHE A 243     4360   9285   9976   1613   2165    669       C  
ATOM   1337  CE2 PHE A 243     -24.641   4.494  36.784  1.00 57.30           C  
ANISOU 1337  CE2 PHE A 243     3744   8631   9395   1737   2092    517       C  
ATOM   1338  CZ  PHE A 243     -25.326   4.854  35.640  1.00 58.17           C  
ANISOU 1338  CZ  PHE A 243     3854   8774   9473   1746   2120    513       C  
ATOM   1339  N   PHE A 244     -25.464   7.146  41.081  1.00 72.91           N  
ANISOU 1339  N   PHE A 244     5968  10069  11665   1312   2051    936       N  
ATOM   1340  CA  PHE A 244     -26.068   6.044  41.825  1.00 58.84           C  
ANISOU 1340  CA  PHE A 244     4289   8123   9946   1398   1999    846       C  
ATOM   1341  C   PHE A 244     -27.290   6.493  42.620  1.00 77.09           C  
ANISOU 1341  C   PHE A 244     6737  10185  12370   1327   1980    898       C  
ATOM   1342  O   PHE A 244     -28.306   5.787  42.652  1.00 83.23           O  
ANISOU 1342  O   PHE A 244     7615  10812  13196   1384   1946    828       O  
ATOM   1343  CB  PHE A 244     -25.025   5.411  42.744  1.00 70.42           C  
ANISOU 1343  CB  PHE A 244     5706   9649  11400   1433   1980    827       C  
ATOM   1344  CG  PHE A 244     -23.866   4.802  42.007  1.00 95.20           C  
ANISOU 1344  CG  PHE A 244     8712  13018  14440   1519   1993    753       C  
ATOM   1345  CD1 PHE A 244     -24.074   4.048  40.865  1.00 88.75           C  
ANISOU 1345  CD1 PHE A 244     7875  12273  13573   1634   1991    633       C  
ATOM   1346  CD2 PHE A 244     -22.569   4.996  42.448  1.00 90.61           C  
ANISOU 1346  CD2 PHE A 244     8024  12584  13820   1487   2008    796       C  
ATOM   1347  CE1 PHE A 244     -23.009   3.489  40.183  1.00 83.82           C  
ANISOU 1347  CE1 PHE A 244     7124  11857  12866   1718   2007    552       C  
ATOM   1348  CE2 PHE A 244     -21.501   4.442  41.770  1.00 79.09           C  
ANISOU 1348  CE2 PHE A 244     6440  11333  12279   1565   2025    723       C  
ATOM   1349  CZ  PHE A 244     -21.721   3.688  40.636  1.00 86.20           C  
ANISOU 1349  CZ  PHE A 244     7320  12298  13134   1682   2027    598       C  
ATOM   1350  N   ILE A 245     -27.207   7.650  43.282  1.00 81.00           N  
ANISOU 1350  N   ILE A 245     7234  10634  12909   1203   1998   1015       N  
ATOM   1351  CA  ILE A 245     -28.336   8.123  44.087  1.00 76.31           C  
ANISOU 1351  CA  ILE A 245     6762   9808  12424   1140   1983   1056       C  
ATOM   1352  C   ILE A 245     -29.586   8.345  43.242  1.00 68.54           C  
ANISOU 1352  C   ILE A 245     5848   8717  11475   1142   1986   1038       C  
ATOM   1353  O   ILE A 245     -30.652   7.819  43.606  1.00 75.47           O  
ANISOU 1353  O   ILE A 245     6837   9417  12419   1171   1956    989       O  
ATOM   1354  CB  ILE A 245     -27.929   9.372  44.887  1.00 70.94           C  
ANISOU 1354  CB  ILE A 245     6056   9113  11784   1012   1997   1174       C  
ATOM   1355  CG1 ILE A 245     -26.922   9.009  45.979  1.00 67.00           C  
ANISOU 1355  CG1 ILE A 245     5512   8672  11272   1018   1982   1182       C  
ATOM   1356  CG2 ILE A 245     -29.158  10.054  45.475  1.00 73.84           C  
ANISOU 1356  CG2 ILE A 245     6537   9255  12263    947   1990   1213       C  
ATOM   1357  CD1 ILE A 245     -26.378  10.207  46.725  1.00 57.38           C  
ANISOU 1357  CD1 ILE A 245     4251   7467  10085    894   1989   1289       C  
ATOM   1358  N   PRO A 246     -29.545   9.099  42.136  1.00 74.69           N  
ANISOU 1358  N   PRO A 246     6568   9597  12215   1108   2020   1081       N  
ATOM   1359  CA  PRO A 246     -30.759   9.222  41.317  1.00 77.04           C  
ANISOU 1359  CA  PRO A 246     6930   9795  12548   1123   2019   1057       C  
ATOM   1360  C   PRO A 246     -31.220   7.903  40.733  1.00 79.73           C  
ANISOU 1360  C   PRO A 246     7304  10131  12860   1252   1989    922       C  
ATOM   1361  O   PRO A 246     -32.426   7.713  40.562  1.00 80.98           O  
ANISOU 1361  O   PRO A 246     7555  10136  13077   1267   1966    884       O  
ATOM   1362  CB  PRO A 246     -30.349  10.217  40.223  1.00 92.91           C  
ANISOU 1362  CB  PRO A 246     8840  11962  14499   1067   2065   1140       C  
ATOM   1363  CG  PRO A 246     -29.198  10.956  40.796  1.00 84.55           C  
ANISOU 1363  CG  PRO A 246     7700  11010  13416    975   2081   1237       C  
ATOM   1364  CD  PRO A 246     -28.458   9.935  41.595  1.00 76.42           C  
ANISOU 1364  CD  PRO A 246     6659  10020  12359   1043   2058   1165       C  
ATOM   1365  N   LEU A 247     -30.304   6.980  40.426  1.00 75.54           N  
ANISOU 1365  N   LEU A 247     6699   9762  12242   1345   1983    845       N  
ATOM   1366  CA  LEU A 247     -30.715   5.675  39.916  1.00 72.23           C  
ANISOU 1366  CA  LEU A 247     6310   9331  11801   1474   1942    706       C  
ATOM   1367  C   LEU A 247     -31.531   4.912  40.952  1.00 72.41           C  
ANISOU 1367  C   LEU A 247     6459   9141  11914   1486   1888    667       C  
ATOM   1368  O   LEU A 247     -32.601   4.368  40.646  1.00 82.55           O  
ANISOU 1368  O   LEU A 247     7823  10304  13237   1525   1851    601       O  
ATOM   1369  CB  LEU A 247     -29.487   4.867  39.494  1.00 87.89           C  
ANISOU 1369  CB  LEU A 247     8183  11529  13684   1575   1944    627       C  
ATOM   1370  CG  LEU A 247     -29.669   3.353  39.357  1.00 97.67           C  
ANISOU 1370  CG  LEU A 247     9452  12742  14915   1716   1886    477       C  
ATOM   1371  CD1 LEU A 247     -30.727   3.002  38.314  1.00 94.81           C  
ANISOU 1371  CD1 LEU A 247     9136  12330  14555   1782   1862    392       C  
ATOM   1372  CD2 LEU A 247     -28.340   2.692  39.023  1.00 92.69           C  
ANISOU 1372  CD2 LEU A 247     8698  12328  14193   1810   1891    403       C  
ATOM   1373  N   THR A 248     -31.033   4.856  42.189  1.00 86.98           N  
ANISOU 1373  N   THR A 248     8316  10945  13789   1448   1882    711       N  
ATOM   1374  CA  THR A 248     -31.773   4.176  43.247  1.00 92.35           C  
ANISOU 1374  CA  THR A 248     9106  11436  14549   1447   1839    693       C  
ATOM   1375  C   THR A 248     -33.110   4.858  43.503  1.00 84.85           C  
ANISOU 1375  C   THR A 248     8259  10293  13687   1362   1839    741       C  
ATOM   1376  O   THR A 248     -34.135   4.186  43.691  1.00 84.30           O  
ANISOU 1376  O   THR A 248     8280  10079  13669   1378   1801    694       O  
ATOM   1377  CB  THR A 248     -30.938   4.131  44.527  1.00 94.26           C  
ANISOU 1377  CB  THR A 248     9327  11686  14801   1420   1840    746       C  
ATOM   1378  OG1 THR A 248     -30.583   5.465  44.913  1.00107.94           O  
ANISOU 1378  OG1 THR A 248    11027  13440  16546   1313   1882    855       O  
ATOM   1379  CG2 THR A 248     -29.671   3.320  44.304  1.00 90.16           C  
ANISOU 1379  CG2 THR A 248     8707  11348  14202   1514   1832    687       C  
ATOM   1380  N   ILE A 249     -33.123   6.194  43.502  1.00 70.26           N  
ANISOU 1380  N   ILE A 249     6394   8442  11861   1268   1881    835       N  
ATOM   1381  CA  ILE A 249     -34.376   6.912  43.709  1.00 47.31           C  
ANISOU 1381  CA  ILE A 249     3577   5355   9042   1193   1882    876       C  
ATOM   1382  C   ILE A 249     -35.362   6.594  42.592  1.00 52.03           C  
ANISOU 1382  C   ILE A 249     4211   5917   9643   1236   1864    810       C  
ATOM   1383  O   ILE A 249     -36.550   6.371  42.844  1.00 78.40           O  
ANISOU 1383  O   ILE A 249     7645   9096  13049   1217   1836    788       O  
ATOM   1384  CB  ILE A 249     -34.121   8.426  43.830  1.00 51.29           C  
ANISOU 1384  CB  ILE A 249     4045   5871   9573   1093   1925    987       C  
ATOM   1385  CG1 ILE A 249     -33.298   8.730  45.082  1.00 45.18           C  
ANISOU 1385  CG1 ILE A 249     3248   5108   8811   1047   1933   1046       C  
ATOM   1386  CG2 ILE A 249     -35.436   9.182  43.884  1.00 58.98           C  
ANISOU 1386  CG2 ILE A 249     5103   6665  10641   1030   1926   1019       C  
ATOM   1387  CD1 ILE A 249     -33.008  10.202  45.278  1.00 45.25           C  
ANISOU 1387  CD1 ILE A 249     3216   5123   8854    945   1964   1151       C  
ATOM   1388  N   MET A 250     -34.886   6.559  41.344  1.00 46.15           N  
ANISOU 1388  N   MET A 250     3384   5330   8820   1295   1878    777       N  
ATOM   1389  CA  MET A 250     -35.765   6.253  40.220  1.00 58.66           C  
ANISOU 1389  CA  MET A 250     4991   6897  10401   1348   1859    707       C  
ATOM   1390  C   MET A 250     -36.339   4.849  40.332  1.00 67.00           C  
ANISOU 1390  C   MET A 250     6113   7876  11469   1427   1796    595       C  
ATOM   1391  O   MET A 250     -37.531   4.642  40.088  1.00 81.56           O  
ANISOU 1391  O   MET A 250     8031   9594  13364   1423   1763    559       O  
ATOM   1392  CB  MET A 250     -35.016   6.412  38.897  1.00 65.36           C  
ANISOU 1392  CB  MET A 250     5723   7961  11150   1408   1892    689       C  
ATOM   1393  CG  MET A 250     -34.771   7.849  38.476  1.00 64.07           C  
ANISOU 1393  CG  MET A 250     5496   7865  10982   1320   1952    811       C  
ATOM   1394  SD  MET A 250     -34.028   7.963  36.837  1.00 76.86           S  
ANISOU 1394  SD  MET A 250     6975   9754  12472   1387   1996    796       S  
ATOM   1395  CE  MET A 250     -32.674   6.806  37.002  1.00 64.39           C  
ANISOU 1395  CE  MET A 250     5318   8354  10791   1486   1985    702       C  
ATOM   1396  N   VAL A 251     -35.510   3.870  40.700  1.00 58.85           N  
ANISOU 1396  N   VAL A 251     5051   6917  10394   1497   1774    542       N  
ATOM   1397  CA  VAL A 251     -36.001   2.496  40.813  1.00 59.78           C  
ANISOU 1397  CA  VAL A 251     5224   6959  10528   1573   1709    442       C  
ATOM   1398  C   VAL A 251     -37.058   2.397  41.909  1.00 62.85           C  
ANISOU 1398  C   VAL A 251     5723   7141  11016   1491   1685    482       C  
ATOM   1399  O   VAL A 251     -38.135   1.810  41.714  1.00 72.05           O  
ANISOU 1399  O   VAL A 251     6954   8196  12225   1500   1640    431       O  
ATOM   1400  CB  VAL A 251     -34.834   1.525  41.061  1.00 67.29           C  
ANISOU 1400  CB  VAL A 251     6115   8028  11423   1665   1692    388       C  
ATOM   1401  CG1 VAL A 251     -35.360   0.125  41.337  1.00 52.95           C  
ANISOU 1401  CG1 VAL A 251     4363   6111   9644   1735   1622    304       C  
ATOM   1402  CG2 VAL A 251     -33.892   1.515  39.868  1.00 78.02           C  
ANISOU 1402  CG2 VAL A 251     7359   9609  12677   1758   1715    329       C  
ATOM   1403  N   ILE A 252     -36.770   2.981  43.076  1.00 72.77           N  
ANISOU 1403  N   ILE A 252     6992   8352  12307   1407   1715    574       N  
ATOM   1404  CA  ILE A 252     -37.705   2.896  44.197  1.00 69.46           C  
ANISOU 1404  CA  ILE A 252     6662   7759  11970   1332   1701    614       C  
ATOM   1405  C   ILE A 252     -39.010   3.611  43.862  1.00 74.12           C  
ANISOU 1405  C   ILE A 252     7312   8234  12616   1262   1704    633       C  
ATOM   1406  O   ILE A 252     -40.104   3.100  44.139  1.00 90.24           O  
ANISOU 1406  O   ILE A 252     9421  10156  14711   1239   1670    611       O  
ATOM   1407  CB  ILE A 252     -37.056   3.452  45.480  1.00 71.87           C  
ANISOU 1407  CB  ILE A 252     6958   8056  12292   1270   1736    703       C  
ATOM   1408  CG1 ILE A 252     -36.355   2.334  46.262  1.00 75.76           C  
ANISOU 1408  CG1 ILE A 252     7436   8577  12771   1326   1712    682       C  
ATOM   1409  CG2 ILE A 252     -38.090   4.141  46.363  1.00 68.27           C  
ANISOU 1409  CG2 ILE A 252     6578   7447  11914   1168   1750    768       C  
ATOM   1410  CD1 ILE A 252     -35.164   1.717  45.554  1.00 89.23           C  
ANISOU 1410  CD1 ILE A 252     9055  10451  14397   1432   1701    619       C  
ATOM   1411  N   THR A 253     -38.920   4.796  43.251  1.00 58.32           N  
ANISOU 1411  N   THR A 253     5279   6273  10606   1228   1743    678       N  
ATOM   1412  CA  THR A 253     -40.124   5.536  42.899  1.00 48.52           C  
ANISOU 1412  CA  THR A 253     4088   4925   9422   1167   1746    698       C  
ATOM   1413  C   THR A 253     -40.909   4.844  41.796  1.00 59.53           C  
ANISOU 1413  C   THR A 253     5498   6314  10807   1228   1701    608       C  
ATOM   1414  O   THR A 253     -42.136   4.926  41.783  1.00 73.98           O  
ANISOU 1414  O   THR A 253     7387   8028  12693   1184   1679    602       O  
ATOM   1415  CB  THR A 253     -39.773   6.964  42.482  1.00 45.64           C  
ANISOU 1415  CB  THR A 253     3676   4605   9059   1121   1798    777       C  
ATOM   1416  OG1 THR A 253     -38.756   6.935  41.473  1.00 58.96           O  
ANISOU 1416  OG1 THR A 253     5268   6470  10663   1190   1816    758       O  
ATOM   1417  CG2 THR A 253     -39.283   7.764  43.681  1.00 42.54           C  
ANISOU 1417  CG2 THR A 253     3284   4179   8701   1047   1832    866       C  
ATOM   1418  N   TYR A 254     -40.235   4.154  40.873  1.00 53.89           N  
ANISOU 1418  N   TYR A 254     4725   5730  10020   1333   1685    533       N  
ATOM   1419  CA  TYR A 254     -40.949   3.393  39.851  1.00 49.32           C  
ANISOU 1419  CA  TYR A 254     4161   5147   9432   1407   1635    434       C  
ATOM   1420  C   TYR A 254     -41.722   2.234  40.467  1.00 59.23           C  
ANISOU 1420  C   TYR A 254     5486   6284  10736   1410   1575    384       C  
ATOM   1421  O   TYR A 254     -42.886   1.994  40.111  1.00 71.01           O  
ANISOU 1421  O   TYR A 254     7025   7685  12271   1398   1535    348       O  
ATOM   1422  CB  TYR A 254     -39.957   2.890  38.802  1.00 55.73           C  
ANISOU 1422  CB  TYR A 254     4886   6140  10148   1531   1634    358       C  
ATOM   1423  CG  TYR A 254     -40.581   2.178  37.623  1.00 57.97           C  
ANISOU 1423  CG  TYR A 254     5174   6441  10412   1627   1584    246       C  
ATOM   1424  CD1 TYR A 254     -41.058   2.890  36.529  1.00 54.62           C  
ANISOU 1424  CD1 TYR A 254     4725   6051   9976   1636   1600    245       C  
ATOM   1425  CD2 TYR A 254     -40.670   0.791  37.591  1.00 49.18           C  
ANISOU 1425  CD2 TYR A 254     4084   5310   9294   1717   1518    144       C  
ATOM   1426  CE1 TYR A 254     -41.620   2.242  35.443  1.00 58.76           C  
ANISOU 1426  CE1 TYR A 254     5250   6596  10480   1733   1551    138       C  
ATOM   1427  CE2 TYR A 254     -41.230   0.134  36.509  1.00 47.63           C  
ANISOU 1427  CE2 TYR A 254     3892   5126   9081   1813   1467     37       C  
ATOM   1428  CZ  TYR A 254     -41.703   0.864  35.439  1.00 57.94           C  
ANISOU 1428  CZ  TYR A 254     5173   6470  10369   1822   1483     31       C  
ATOM   1429  OH  TYR A 254     -42.261   0.215  34.361  1.00 58.95           O  
ANISOU 1429  OH  TYR A 254     5304   6614  10479   1926   1430    -79       O  
ATOM   1430  N   PHE A 255     -41.095   1.505  41.395  1.00 86.95           N  
ANISOU 1430  N   PHE A 255     8995   9796  14244   1423   1567    388       N  
ATOM   1431  CA  PHE A 255     -41.803   0.425  42.078  1.00 93.92           C  
ANISOU 1431  CA  PHE A 255     9934  10566  15184   1416   1517    361       C  
ATOM   1432  C   PHE A 255     -42.996   0.961  42.865  1.00 85.79           C  
ANISOU 1432  C   PHE A 255     8966   9397  14232   1294   1528    430       C  
ATOM   1433  O   PHE A 255     -44.108   0.418  42.789  1.00 98.12           O  
ANISOU 1433  O   PHE A 255    10568  10869  15844   1277   1486    399       O  
ATOM   1434  CB  PHE A 255     -40.846  -0.333  42.998  1.00101.38           C  
ANISOU 1434  CB  PHE A 255    10860  11542  16117   1450   1515    371       C  
ATOM   1435  CG  PHE A 255     -40.043  -1.391  42.299  1.00103.45           C  
ANISOU 1435  CG  PHE A 255    11077  11906  16323   1586   1476    273       C  
ATOM   1436  CD1 PHE A 255     -40.516  -1.987  41.141  1.00103.80           C  
ANISOU 1436  CD1 PHE A 255    11124  11962  16353   1671   1428    173       C  
ATOM   1437  CD2 PHE A 255     -38.816  -1.793  42.800  1.00117.37           C  
ANISOU 1437  CD2 PHE A 255    12792  13755  18048   1639   1486    278       C  
ATOM   1438  CE1 PHE A 255     -39.780  -2.964  40.496  1.00118.69           C  
ANISOU 1438  CE1 PHE A 255    12969  13945  18184   1811   1391     74       C  
ATOM   1439  CE2 PHE A 255     -38.074  -2.768  42.160  1.00122.77           C  
ANISOU 1439  CE2 PHE A 255    13431  14539  18679   1774   1449    181       C  
ATOM   1440  CZ  PHE A 255     -38.556  -3.354  41.007  1.00125.44           C  
ANISOU 1440  CZ  PHE A 255    13774  14887  19000   1864   1402     77       C  
ATOM   1441  N   LEU A 256     -42.788   2.043  43.618  1.00 50.80           N  
ANISOU 1441  N   LEU A 256     4536   4952   9812   1212   1583    522       N  
ATOM   1442  CA  LEU A 256     -43.889   2.610  44.385  1.00 51.13           C  
ANISOU 1442  CA  LEU A 256     4629   4877   9921   1106   1597    581       C  
ATOM   1443  C   LEU A 256     -44.962   3.198  43.476  1.00 56.71           C  
ANISOU 1443  C   LEU A 256     5355   5542  10651   1079   1585    562       C  
ATOM   1444  O   LEU A 256     -46.142   3.194  43.835  1.00 69.36           O  
ANISOU 1444  O   LEU A 256     6995   7053  12307   1017   1572    572       O  
ATOM   1445  CB  LEU A 256     -43.361   3.661  45.359  1.00 44.60           C  
ANISOU 1445  CB  LEU A 256     3798   4048   9099   1039   1656    673       C  
ATOM   1446  CG  LEU A 256     -42.473   3.120  46.481  1.00 42.08           C  
ANISOU 1446  CG  LEU A 256     3465   3754   8770   1053   1667    703       C  
ATOM   1447  CD1 LEU A 256     -42.167   4.210  47.494  1.00 59.88           C  
ANISOU 1447  CD1 LEU A 256     5723   5990  11040    984   1719    790       C  
ATOM   1448  CD2 LEU A 256     -43.123   1.918  47.155  1.00 58.28           C  
ANISOU 1448  CD2 LEU A 256     5545   5736  10862   1053   1633    686       C  
ATOM   1449  N   THR A 257     -44.581   3.668  42.287  1.00 50.87           N  
ANISOU 1449  N   THR A 257     4581   4879   9869   1130   1591    535       N  
ATOM   1450  CA  THR A 257     -45.553   4.212  41.347  1.00 45.38           C  
ANISOU 1450  CA  THR A 257     3898   4150   9196   1117   1577    517       C  
ATOM   1451  C   THR A 257     -46.432   3.116  40.765  1.00 53.60           C  
ANISOU 1451  C   THR A 257     4960   5155  10252   1164   1509    428       C  
ATOM   1452  O   THR A 257     -47.650   3.289  40.654  1.00 78.01           O  
ANISOU 1452  O   THR A 257     8082   8165  13392   1115   1487    426       O  
ATOM   1453  CB  THR A 257     -44.833   4.971  40.230  1.00 53.36           C  
ANISOU 1453  CB  THR A 257     4851   5265  10158   1167   1607    521       C  
ATOM   1454  OG1 THR A 257     -44.225   6.152  40.767  1.00 69.32           O  
ANISOU 1454  OG1 THR A 257     6854   7297  12189   1106   1669    618       O  
ATOM   1455  CG2 THR A 257     -45.805   5.361  39.125  1.00 42.46           C  
ANISOU 1455  CG2 THR A 257     3477   3859   8798   1176   1586    493       C  
ATOM   1456  N   ILE A 258     -45.841   1.982  40.381  1.00 56.75           N  
ANISOU 1456  N   ILE A 258     5338   5613  10611   1262   1472    351       N  
ATOM   1457  CA  ILE A 258     -46.676   0.891  39.884  1.00 58.18           C  
ANISOU 1457  CA  ILE A 258     5541   5746  10818   1309   1402    266       C  
ATOM   1458  C   ILE A 258     -47.567   0.359  41.003  1.00 57.99           C  
ANISOU 1458  C   ILE A 258     5557   5606  10870   1229   1385    300       C  
ATOM   1459  O   ILE A 258     -48.743   0.040  40.778  1.00 67.30           O  
ANISOU 1459  O   ILE A 258     6758   6712  12102   1204   1344    273       O  
ATOM   1460  CB  ILE A 258     -45.827  -0.222  39.234  1.00 75.71           C  
ANISOU 1460  CB  ILE A 258     7731   8053  12984   1444   1364    170       C  
ATOM   1461  CG1 ILE A 258     -44.997  -0.986  40.266  1.00 69.67           C  
ANISOU 1461  CG1 ILE A 258     6961   7295  12217   1456   1368    188       C  
ATOM   1462  CG2 ILE A 258     -44.937   0.355  38.138  1.00 57.23           C  
ANISOU 1462  CG2 ILE A 258     5331   5854  10559   1526   1393    142       C  
ATOM   1463  CD1 ILE A 258     -44.225  -2.153  39.691  1.00 78.96           C  
ANISOU 1463  CD1 ILE A 258     8108   8546  13347   1595   1324     89       C  
ATOM   1464  N   LYS A 259     -47.041   0.298  42.233  1.00 65.49           N  
ANISOU 1464  N   LYS A 259     6508   6546  11829   1185   1419    363       N  
ATOM   1465  CA  LYS A 259     -47.866  -0.133  43.359  1.00 69.31           C  
ANISOU 1465  CA  LYS A 259     7016   6936  12384   1108   1417    408       C  
ATOM   1466  C   LYS A 259     -49.031   0.824  43.597  1.00 60.77           C  
ANISOU 1466  C   LYS A 259     5953   5792  11344   1008   1440    458       C  
ATOM   1467  O   LYS A 259     -50.160   0.387  43.850  1.00 62.15           O  
ANISOU 1467  O   LYS A 259     6137   5898  11580    967   1415    456       O  
ATOM   1468  CB  LYS A 259     -47.009  -0.262  44.619  1.00 72.81           C  
ANISOU 1468  CB  LYS A 259     7450   7391  12822   1089   1456    471       C  
ATOM   1469  CG  LYS A 259     -46.181  -1.536  44.678  1.00 80.65           C  
ANISOU 1469  CG  LYS A 259     8426   8415  13803   1178   1422    425       C  
ATOM   1470  CD  LYS A 259     -47.066  -2.756  44.889  1.00 97.82           C  
ANISOU 1470  CD  LYS A 259    10611  10503  16053   1180   1371    398       C  
ATOM   1471  CE  LYS A 259     -46.267  -4.045  44.785  1.00 90.85           C  
ANISOU 1471  CE  LYS A 259     9712   9641  15165   1283   1326    341       C  
ATOM   1472  NZ  LYS A 259     -45.128  -4.075  45.743  1.00 99.64           N  
ANISOU 1472  NZ  LYS A 259    10807  10799  16252   1293   1364    395       N  
ATOM   1473  N   SER A 260     -48.777   2.132  43.518  1.00 63.03           N  
ANISOU 1473  N   SER A 260     6239   6104  11604    972   1487    505       N  
ATOM   1474  CA  SER A 260     -49.832   3.115  43.745  1.00 71.68           C  
ANISOU 1474  CA  SER A 260     7351   7146  12738    886   1508    549       C  
ATOM   1475  C   SER A 260     -50.861   3.103  42.621  1.00 70.08           C  
ANISOU 1475  C   SER A 260     7152   6919  12555    900   1461    494       C  
ATOM   1476  O   SER A 260     -52.065   3.233  42.873  1.00 92.97           O  
ANISOU 1476  O   SER A 260    10060   9761  15505    842   1452    506       O  
ATOM   1477  CB  SER A 260     -49.220   4.509  43.896  1.00 69.65           C  
ANISOU 1477  CB  SER A 260     7091   6915  12460    852   1566    611       C  
ATOM   1478  OG  SER A 260     -50.225   5.497  44.036  1.00101.77           O  
ANISOU 1478  OG  SER A 260    11171  10931  16565    779   1582    646       O  
ATOM   1479  N   LEU A 261     -50.411   2.950  41.374  1.00 51.72           N  
ANISOU 1479  N   LEU A 261     4815   4647  10191    984   1432    432       N  
ATOM   1480  CA  LEU A 261     -51.337   2.963  40.248  1.00 57.84           C  
ANISOU 1480  CA  LEU A 261     5592   5402  10982   1010   1385    376       C  
ATOM   1481  C   LEU A 261     -52.170   1.692  40.185  1.00 52.03           C  
ANISOU 1481  C   LEU A 261     4864   4615  10291   1029   1321    315       C  
ATOM   1482  O   LEU A 261     -53.284   1.713  39.648  1.00 51.83           O  
ANISOU 1482  O   LEU A 261     4842   4545  10305   1016   1283    288       O  
ATOM   1483  CB  LEU A 261     -50.576   3.166  38.938  1.00 68.27           C  
ANISOU 1483  CB  LEU A 261     6889   6808  12245   1106   1379    328       C  
ATOM   1484  CG  LEU A 261     -50.229   4.617  38.601  1.00 51.66           C  
ANISOU 1484  CG  LEU A 261     4768   4736  10125   1081   1434    391       C  
ATOM   1485  CD1 LEU A 261     -49.544   4.705  37.248  1.00 50.72           C  
ANISOU 1485  CD1 LEU A 261     4606   4715   9950   1185   1432    345       C  
ATOM   1486  CD2 LEU A 261     -51.482   5.477  38.626  1.00 73.78           C  
ANISOU 1486  CD2 LEU A 261     7590   7460  12984   1002   1432    429       C  
ATOM   1487  N   GLN A 262     -51.655   0.578  40.712  1.00 72.70           N  
ANISOU 1487  N   GLN A 262     7478   7233  12912   1062   1306    296       N  
ATOM   1488  CA  GLN A 262     -52.479  -0.625  40.790  1.00 72.85           C  
ANISOU 1488  CA  GLN A 262     7499   7186  12996   1069   1249    253       C  
ATOM   1489  C   GLN A 262     -53.689  -0.414  41.691  1.00 82.07           C  
ANISOU 1489  C   GLN A 262     8664   8281  14238    962   1265    316       C  
ATOM   1490  O   GLN A 262     -54.730  -1.051  41.492  1.00 93.85           O  
ANISOU 1490  O   GLN A 262    10148   9714  15797    953   1219    286       O  
ATOM   1491  CB  GLN A 262     -51.642  -1.807  41.278  1.00 74.28           C  
ANISOU 1491  CB  GLN A 262     7673   7374  13176   1123   1234    233       C  
ATOM   1492  CG  GLN A 262     -50.704  -2.371  40.223  1.00 83.17           C  
ANISOU 1492  CG  GLN A 262     8791   8569  14239   1253   1197    141       C  
ATOM   1493  CD  GLN A 262     -49.715  -3.370  40.791  1.00 96.36           C  
ANISOU 1493  CD  GLN A 262    10454  10259  15901   1310   1190    130       C  
ATOM   1494  OE1 GLN A 262     -49.780  -3.725  41.967  1.00 97.40           O  
ANISOU 1494  OE1 GLN A 262    10585  10342  16082   1250   1209    192       O  
ATOM   1495  NE2 GLN A 262     -48.789  -3.825  39.956  1.00113.30           N  
ANISOU 1495  NE2 GLN A 262    12585  12480  17982   1432   1165     50       N  
ATOM   1496  N   LYS A 263     -53.576   0.474  42.683  1.00 79.77           N  
ANISOU 1496  N   LYS A 263     8375   7996  13940    887   1331    401       N  
ATOM   1497  CA  LYS A 263     -54.706   0.774  43.555  1.00 64.80           C  
ANISOU 1497  CA  LYS A 263     6468   6047  12104    796   1356    458       C  
ATOM   1498  C   LYS A 263     -55.731   1.681  42.881  1.00 60.43           C  
ANISOU 1498  C   LYS A 263     5918   5481  11564    766   1346    450       C  
ATOM   1499  O   LYS A 263     -56.929   1.567  43.163  1.00 80.31           O  
ANISOU 1499  O   LYS A 263     8414   7949  14152    717   1338    464       O  
ATOM   1500  CB  LYS A 263     -54.211   1.410  44.857  1.00 60.24           C  
ANISOU 1500  CB  LYS A 263     5893   5485  11510    741   1430    543       C  
ATOM   1501  CG  LYS A 263     -55.321   1.801  45.821  1.00 88.84           C  
ANISOU 1501  CG  LYS A 263     9499   9069  15186    660   1466    601       C  
ATOM   1502  CD  LYS A 263     -54.778   2.176  47.190  1.00 98.32           C  
ANISOU 1502  CD  LYS A 263    10701  10283  16374    623   1534    676       C  
ATOM   1503  CE  LYS A 263     -55.871   2.774  48.063  1.00100.95           C  
ANISOU 1503  CE  LYS A 263    11018  10590  16749    556   1576    728       C  
ATOM   1504  NZ  LYS A 263     -57.083   1.909  48.121  1.00 88.52           N  
ANISOU 1504  NZ  LYS A 263     9394   8956  15283    535   1563    729       N  
ATOM   1505  N   GLU A 264     -55.287   2.576  41.992  1.00 60.53           N  
ANISOU 1505  N   GLU A 264     5944   5532  11523    795   1348    435       N  
ATOM   1506  CA  GLU A 264     -56.221   3.467  41.308  1.00 60.95           C  
ANISOU 1506  CA  GLU A 264     5998   5569  11591    773   1336    431       C  
ATOM   1507  C   GLU A 264     -57.239   2.682  40.490  1.00 60.75           C  
ANISOU 1507  C   GLU A 264     5963   5504  11613    802   1264    364       C  
ATOM   1508  O   GLU A 264     -58.436   2.987  40.515  1.00 78.92           O  
ANISOU 1508  O   GLU A 264     8252   7768  13965    756   1252    375       O  
ATOM   1509  CB  GLU A 264     -55.467   4.443  40.403  1.00 68.18           C  
ANISOU 1509  CB  GLU A 264     6922   6531  12452    812   1350    428       C  
ATOM   1510  CG  GLU A 264     -54.901   5.665  41.106  1.00 66.38           C  
ANISOU 1510  CG  GLU A 264     6698   6319  12204    760   1420    506       C  
ATOM   1511  CD  GLU A 264     -54.499   6.763  40.133  1.00 55.65           C  
ANISOU 1511  CD  GLU A 264     5336   4987  10824    786   1433    518       C  
ATOM   1512  OE1 GLU A 264     -55.112   6.863  39.048  1.00 43.29           O  
ANISOU 1512  OE1 GLU A 264     3767   3414   9268    820   1391    479       O  
ATOM   1513  OE2 GLU A 264     -53.566   7.528  40.453  1.00 59.90           O  
ANISOU 1513  OE2 GLU A 264     5870   5550  11341    773   1486    571       O  
ATOM   1514  N   ALA A 265     -56.783   1.663  39.760  1.00 54.36           N  
ANISOU 1514  N   ALA A 265     5156   4705  10793    884   1213    292       N  
ATOM   1515  CA  ALA A 265     -57.682   0.874  38.930  1.00 65.13           C  
ANISOU 1515  CA  ALA A 265     6511   6027  12209    921   1139    220       C  
ATOM   1516  C   ALA A 265     -58.574  -0.053  39.743  1.00 86.05           C  
ANISOU 1516  C   ALA A 265     9134   8607  14953    869   1123    235       C  
ATOM   1517  O   ALA A 265     -59.506  -0.636  39.180  1.00 91.68           O  
ANISOU 1517  O   ALA A 265     9827   9268  15740    880   1065    188       O  
ATOM   1518  CB  ALA A 265     -56.882   0.059  37.912  1.00 58.85           C  
ANISOU 1518  CB  ALA A 265     5724   5264  11374   1036   1090    130       C  
ATOM   1519  N   ALA A1001     -58.312  -0.208  41.040  1.00 98.00           N  
ANISOU 1519  N   ALA A1001    10628  10108  16501    812   1181    305       N  
ATOM   1520  CA  ALA A1001     -59.156  -1.030  41.898  1.00 97.69           C  
ANISOU 1520  CA  ALA A1001    10534   9994  16589    755   1188    340       C  
ATOM   1521  C   ALA A1001     -60.276  -0.222  42.540  1.00 97.44           C  
ANISOU 1521  C   ALA A1001    10471   9941  16612    669   1233    406       C  
ATOM   1522  O   ALA A1001     -61.405  -0.712  42.657  1.00100.34           O  
ANISOU 1522  O   ALA A1001    10786  10248  17088    636   1214    410       O  
ATOM   1523  CB  ALA A1001     -58.310  -1.704  42.981  1.00 96.09           C  
ANISOU 1523  CB  ALA A1001    10323   9792  16396    750   1227    384       C  
ATOM   1524  N   ASP A1002     -59.982   1.010  42.959  1.00 69.61           N  
ANISOU 1524  N   ASP A1002     6971   6463  13016    637   1290    455       N  
ATOM   1525  CA  ASP A1002     -61.020   1.874  43.510  1.00 69.87           C  
ANISOU 1525  CA  ASP A1002     6978   6482  13090    570   1331    507       C  
ATOM   1526  C   ASP A1002     -62.030   2.267  42.440  1.00 65.53           C  
ANISOU 1526  C   ASP A1002     6423   5913  12563    578   1277    463       C  
ATOM   1527  O   ASP A1002     -63.228   2.395  42.722  1.00 78.52           O  
ANISOU 1527  O   ASP A1002     8023   7521  14291    534   1284    486       O  
ATOM   1528  CB  ASP A1002     -60.385   3.113  44.136  1.00 58.99           C  
ANISOU 1528  CB  ASP A1002     5633   5154  11625    546   1394    558       C  
ATOM   1529  CG  ASP A1002     -59.341   2.765  45.179  1.00 60.41           C  
ANISOU 1529  CG  ASP A1002     5823   5355  11776    544   1442    601       C  
ATOM   1530  OD1 ASP A1002     -59.174   1.562  45.474  1.00 56.37           O  
ANISOU 1530  OD1 ASP A1002     5288   4817  11315    558   1431    597       O  
ATOM   1531  OD2 ASP A1002     -58.686   3.691  45.701  1.00 61.55           O  
ANISOU 1531  OD2 ASP A1002     5997   5540  11850    531   1487    636       O  
ATOM   1532  N   LEU A1003     -61.562   2.465  41.205  1.00 55.49           N  
ANISOU 1532  N   LEU A1003     5195   4671  11219    642   1225    401       N  
ATOM   1533  CA  LEU A1003     -62.467   2.788  40.108  1.00 55.00           C  
ANISOU 1533  CA  LEU A1003     5133   4593  11172    662   1166    356       C  
ATOM   1534  C   LEU A1003     -63.444   1.648  39.846  1.00 65.97           C  
ANISOU 1534  C   LEU A1003     6475   5915  12677    664   1110    316       C  
ATOM   1535  O   LEU A1003     -64.634   1.883  39.599  1.00 79.57           O  
ANISOU 1535  O   LEU A1003     8165   7602  14466    638   1086    315       O  
ATOM   1536  CB  LEU A1003     -61.658   3.112  38.853  1.00 55.69           C  
ANISOU 1536  CB  LEU A1003     5271   4726  11161    743   1127    300       C  
ATOM   1537  CG  LEU A1003     -62.424   3.529  37.599  1.00 62.79           C  
ANISOU 1537  CG  LEU A1003     6170   5610  12075    778   1070    255       C  
ATOM   1538  CD1 LEU A1003     -61.701   4.677  36.926  1.00 63.99           C  
ANISOU 1538  CD1 LEU A1003     6348   5808  12156    810   1092    267       C  
ATOM   1539  CD2 LEU A1003     -62.566   2.356  36.641  1.00 84.87           C  
ANISOU 1539  CD2 LEU A1003     8963   8382  14903    850    990    165       C  
ATOM   1540  N   GLU A1004     -62.961   0.404  39.893  1.00 59.05           N  
ANISOU 1540  N   GLU A1004     5590   5016  11830    696   1083    283       N  
ATOM   1541  CA  GLU A1004     -63.859  -0.731  39.718  1.00 65.97           C  
ANISOU 1541  CA  GLU A1004     6416   5819  12832    694   1026    248       C  
ATOM   1542  C   GLU A1004     -64.863  -0.817  40.861  1.00 69.04           C  
ANISOU 1542  C   GLU A1004     6732   6163  13338    608   1073    325       C  
ATOM   1543  O   GLU A1004     -66.024  -1.183  40.646  1.00 71.16           O  
ANISOU 1543  O   GLU A1004     6948   6377  13714    586   1034    314       O  
ATOM   1544  CB  GLU A1004     -63.065  -2.031  39.608  1.00 61.60           C  
ANISOU 1544  CB  GLU A1004     5870   5247  12290    750    988    200       C  
ATOM   1545  CG  GLU A1004     -63.854  -3.163  38.966  1.00 58.98           C  
ANISOU 1545  CG  GLU A1004     5503   4839  12068    776    899    132       C  
ATOM   1546  CD  GLU A1004     -63.539  -4.516  39.570  1.00 62.61           C  
ANISOU 1546  CD  GLU A1004     5930   5245  12615    781    886    132       C  
ATOM   1547  OE1 GLU A1004     -62.958  -4.555  40.675  1.00 66.47           O  
ANISOU 1547  OE1 GLU A1004     6409   5750  13098    746    955    204       O  
ATOM   1548  OE2 GLU A1004     -63.877  -5.542  38.942  1.00 75.48           O  
ANISOU 1548  OE2 GLU A1004     7545   6813  14321    822    802     61       O  
ATOM   1549  N   ASP A1005     -64.434  -0.491  42.083  1.00 65.82           N  
ANISOU 1549  N   ASP A1005     6317   5780  12912    563   1159    404       N  
ATOM   1550  CA  ASP A1005     -65.366  -0.461  43.205  1.00 61.97           C  
ANISOU 1550  CA  ASP A1005     5763   5263  12521    492   1215    481       C  
ATOM   1551  C   ASP A1005     -66.444   0.593  42.999  1.00 60.58           C  
ANISOU 1551  C   ASP A1005     5571   5090  12357    462   1223    494       C  
ATOM   1552  O   ASP A1005     -67.621   0.355  43.295  1.00 66.82           O  
ANISOU 1552  O   ASP A1005     6294   5836  13259    425   1223    519       O  
ATOM   1553  CB  ASP A1005     -64.614  -0.208  44.511  1.00 60.80           C  
ANISOU 1553  CB  ASP A1005     5622   5149  12328    464   1304    558       C  
ATOM   1554  CG  ASP A1005     -64.349  -1.483  45.283  1.00 88.29           C  
ANISOU 1554  CG  ASP A1005     9066   8596  15886    461   1314    588       C  
ATOM   1555  OD1 ASP A1005     -64.674  -2.572  44.764  1.00 92.17           O  
ANISOU 1555  OD1 ASP A1005     9524   9032  16464    482   1247    545       O  
ATOM   1556  OD2 ASP A1005     -63.824  -1.397  46.412  1.00104.37           O  
ANISOU 1556  OD2 ASP A1005    11103  10655  17898    441   1384    656       O  
ATOM   1557  N   ASN A1006     -66.062   1.769  42.497  1.00 42.58           N  
ANISOU 1557  N   ASN A1006     3350   2861   9970    479   1228    480       N  
ATOM   1558  CA  ASN A1006     -67.056   2.799  42.211  1.00 42.45           C  
ANISOU 1558  CA  ASN A1006     3323   2843   9962    460   1226    487       C  
ATOM   1559  C   ASN A1006     -68.022   2.344  41.123  1.00 44.99           C  
ANISOU 1559  C   ASN A1006     3617   3119  10357    481   1139    428       C  
ATOM   1560  O   ASN A1006     -69.232   2.579  41.221  1.00 69.49           O  
ANISOU 1560  O   ASN A1006     6670   6191  13542    450   1136    445       O  
ATOM   1561  CB  ASN A1006     -66.365   4.103  41.813  1.00 49.27           C  
ANISOU 1561  CB  ASN A1006     4255   3764  10701    481   1240    484       C  
ATOM   1562  CG  ASN A1006     -65.554   4.700  42.947  1.00 52.94           C  
ANISOU 1562  CG  ASN A1006     4742   4269  11105    454   1323    544       C  
ATOM   1563  OD1 ASN A1006     -65.739   4.345  44.110  1.00 59.42           O  
ANISOU 1563  OD1 ASN A1006     5526   5077  11975    417   1379    595       O  
ATOM   1564  ND2 ASN A1006     -64.654   5.615  42.614  1.00 54.78           N  
ANISOU 1564  ND2 ASN A1006     5034   4549  11229    477   1330    539       N  
ATOM   1565  N   TRP A1007     -67.506   1.686  40.081  1.00 43.52           N  
ANISOU 1565  N   TRP A1007     3467   2929  10142    541   1067    354       N  
ATOM   1566  CA  TRP A1007     -68.379   1.167  39.030  1.00 49.89           C  
ANISOU 1566  CA  TRP A1007     4251   3688  11015    570    975    288       C  
ATOM   1567  C   TRP A1007     -69.355   0.134  39.581  1.00 56.42           C  
ANISOU 1567  C   TRP A1007     4990   4444  12002    527    963    306       C  
ATOM   1568  O   TRP A1007     -70.544   0.143  39.238  1.00 67.78           O  
ANISOU 1568  O   TRP A1007     6382   5842  13530    511    922    296       O  
ATOM   1569  CB  TRP A1007     -67.541   0.565  37.900  1.00 50.38           C  
ANISOU 1569  CB  TRP A1007     4371   3762  11010    655    904    201       C  
ATOM   1570  CG  TRP A1007     -68.354  -0.134  36.846  1.00 52.60           C  
ANISOU 1570  CG  TRP A1007     4634   3990  11362    694    803    123       C  
ATOM   1571  CD1 TRP A1007     -69.100   0.449  35.863  1.00 53.94           C  
ANISOU 1571  CD1 TRP A1007     4815   4157  11521    721    748     87       C  
ATOM   1572  CD2 TRP A1007     -68.493  -1.549  36.666  1.00 60.47           C  
ANISOU 1572  CD2 TRP A1007     5599   4924  12453    715    740     70       C  
ATOM   1573  NE1 TRP A1007     -69.698  -0.512  35.086  1.00 63.73           N  
ANISOU 1573  NE1 TRP A1007     6031   5337  12846    756    655     12       N  
ATOM   1574  CE2 TRP A1007     -69.341  -1.748  35.558  1.00 68.26           C  
ANISOU 1574  CE2 TRP A1007     6579   5872  13482    753    646     -1       C  
ATOM   1575  CE3 TRP A1007     -67.985  -2.666  37.335  1.00 65.31           C  
ANISOU 1575  CE3 TRP A1007     6188   5506  13123    708    749     77       C  
ATOM   1576  CZ2 TRP A1007     -69.691  -3.018  35.104  1.00 75.45           C  
ANISOU 1576  CZ2 TRP A1007     7461   6713  14495    781    560    -71       C  
ATOM   1577  CZ3 TRP A1007     -68.334  -3.927  36.883  1.00 68.95           C  
ANISOU 1577  CZ3 TRP A1007     6619   5894  13686    737    663     11       C  
ATOM   1578  CH2 TRP A1007     -69.180  -4.092  35.778  1.00 79.51           C  
ANISOU 1578  CH2 TRP A1007     7951   7193  15067    772    569    -64       C  
ATOM   1579  N   GLU A1008     -68.867  -0.764  40.439  1.00 52.02           N  
ANISOU 1579  N   GLU A1008     4408   3871  11488    509    995    336       N  
ATOM   1580  CA  GLU A1008     -69.736  -1.774  41.033  1.00 51.19           C  
ANISOU 1580  CA  GLU A1008     4212   3697  11541    468    988    366       C  
ATOM   1581  C   GLU A1008     -70.795  -1.140  41.926  1.00 56.68           C  
ANISOU 1581  C   GLU A1008     4843   4389  12304    403   1055    448       C  
ATOM   1582  O   GLU A1008     -71.956  -1.564  41.919  1.00 67.21           O  
ANISOU 1582  O   GLU A1008     6101   5668  13769    377   1025    456       O  
ATOM   1583  CB  GLU A1008     -68.899  -2.785  41.816  1.00 63.87           C  
ANISOU 1583  CB  GLU A1008     5809   5291  13170    469   1014    392       C  
ATOM   1584  CG  GLU A1008     -68.085  -3.723  40.939  1.00 71.10           C  
ANISOU 1584  CG  GLU A1008     6768   6186  14060    538    932    304       C  
ATOM   1585  CD  GLU A1008     -67.332  -4.767  41.741  1.00 83.24           C  
ANISOU 1585  CD  GLU A1008     8291   7703  15635    541    953    332       C  
ATOM   1586  OE1 GLU A1008     -67.183  -4.586  42.967  1.00 91.01           O  
ANISOU 1586  OE1 GLU A1008     9248   8705  16625    494   1041    424       O  
ATOM   1587  OE2 GLU A1008     -66.893  -5.772  41.143  1.00 93.63           O  
ANISOU 1587  OE2 GLU A1008     9623   8980  16973    595    878    261       O  
ATOM   1588  N   THR A1009     -70.413  -0.125  42.706  1.00 49.62           N  
ANISOU 1588  N   THR A1009     3979   3551  11324    382   1143    506       N  
ATOM   1589  CA  THR A1009     -71.382   0.576  43.543  1.00 51.98           C  
ANISOU 1589  CA  THR A1009     4228   3849  11671    333   1209    576       C  
ATOM   1590  C   THR A1009     -72.450   1.255  42.694  1.00 45.06           C  
ANISOU 1590  C   THR A1009     3340   2959  10822    337   1159    542       C  
ATOM   1591  O   THR A1009     -73.645   1.200  43.018  1.00 65.49           O  
ANISOU 1591  O   THR A1009     5854   5509  13521    305   1167    575       O  
ATOM   1592  CB  THR A1009     -70.666   1.601  44.424  1.00 51.22           C  
ANISOU 1592  CB  THR A1009     4183   3816  11464    323   1300    627       C  
ATOM   1593  OG1 THR A1009     -69.802   0.922  45.345  1.00 55.17           O  
ANISOU 1593  OG1 THR A1009     4684   4325  11954    317   1350    669       O  
ATOM   1594  CG2 THR A1009     -71.666   2.444  45.200  1.00 43.90           C  
ANISOU 1594  CG2 THR A1009     3219   2889  10573    288   1363    686       C  
ATOM   1595  N   LEU A1010     -72.036   1.899  41.600  1.00 44.75           N  
ANISOU 1595  N   LEU A1010     3371   2948  10683    381   1107    480       N  
ATOM   1596  CA  LEU A1010     -72.998   2.531  40.705  1.00 44.99           C  
ANISOU 1596  CA  LEU A1010     3396   2964  10734    393   1051    446       C  
ATOM   1597  C   LEU A1010     -73.956   1.503  40.118  1.00 56.98           C  
ANISOU 1597  C   LEU A1010     4849   4414  12387    394    969    407       C  
ATOM   1598  O   LEU A1010     -75.171   1.734  40.071  1.00 74.67           O  
ANISOU 1598  O   LEU A1010     7032   6621  14717    372    953    421       O  
ATOM   1599  CB  LEU A1010     -72.265   3.286  39.596  1.00 44.55           C  
ANISOU 1599  CB  LEU A1010     3431   2952  10545    449   1007    391       C  
ATOM   1600  CG  LEU A1010     -71.468   4.514  40.046  1.00 43.65           C  
ANISOU 1600  CG  LEU A1010     3376   2900  10308    447   1077    430       C  
ATOM   1601  CD1 LEU A1010     -70.549   4.993  38.949  1.00 62.07           C  
ANISOU 1601  CD1 LEU A1010     5792   5273  12517    507   1033    380       C  
ATOM   1602  CD2 LEU A1010     -72.394   5.630  40.457  1.00 43.53           C  
ANISOU 1602  CD2 LEU A1010     3339   2887  10315    420   1112    472       C  
ATOM   1603  N   ASN A1011     -73.432   0.353  39.683  1.00 48.79           N  
ANISOU 1603  N   ASN A1011     3817   3349  11372    421    912    357       N  
ATOM   1604  CA  ASN A1011     -74.299  -0.688  39.139  1.00 54.00           C  
ANISOU 1604  CA  ASN A1011     4414   3935  12169    423    825    314       C  
ATOM   1605  C   ASN A1011     -75.278  -1.203  40.190  1.00 60.00           C  
ANISOU 1605  C   ASN A1011     5063   4647  13086    359    867    390       C  
ATOM   1606  O   ASN A1011     -76.466  -1.394  39.900  1.00 68.54           O  
ANISOU 1606  O   ASN A1011     6076   5678  14287    341    819    384       O  
ATOM   1607  CB  ASN A1011     -73.460  -1.837  38.577  1.00 59.20           C  
ANISOU 1607  CB  ASN A1011     5103   4570  12819    471    758    245       C  
ATOM   1608  CG  ASN A1011     -72.872  -1.519  37.215  1.00 69.97           C  
ANISOU 1608  CG  ASN A1011     6560   5964  14063    550    687    152       C  
ATOM   1609  OD1 ASN A1011     -72.658  -0.356  36.873  1.00 67.46           O  
ANISOU 1609  OD1 ASN A1011     6298   5702  13630    568    710    157       O  
ATOM   1610  ND2 ASN A1011     -72.614  -2.556  36.425  1.00 81.04           N  
ANISOU 1610  ND2 ASN A1011     7977   7325  15488    603    598     68       N  
ATOM   1611  N   ASP A1012     -74.800  -1.425  41.418  1.00 61.47           N  
ANISOU 1611  N   ASP A1012     5230   4850  13276    326    957    464       N  
ATOM   1612  CA  ASP A1012     -75.670  -1.937  42.474  1.00 68.64           C  
ANISOU 1612  CA  ASP A1012     6033   5717  14328    272   1006    546       C  
ATOM   1613  C   ASP A1012     -76.796  -0.960  42.781  1.00 50.88           C  
ANISOU 1613  C   ASP A1012     3746   3474  12111    242   1049    592       C  
ATOM   1614  O   ASP A1012     -77.964  -1.352  42.892  1.00 57.45           O  
ANISOU 1614  O   ASP A1012     4486   4253  13089    214   1030    619       O  
ATOM   1615  CB  ASP A1012     -74.858  -2.221  43.738  1.00 67.31           C  
ANISOU 1615  CB  ASP A1012     5867   5577  14133    254   1101    621       C  
ATOM   1616  CG  ASP A1012     -73.848  -3.328  43.545  1.00 66.08           C  
ANISOU 1616  CG  ASP A1012     5734   5402  13971    283   1057    583       C  
ATOM   1617  OD1 ASP A1012     -73.819  -3.929  42.449  1.00 65.10           O  
ANISOU 1617  OD1 ASP A1012     5625   5239  13872    318    952    496       O  
ATOM   1618  OD2 ASP A1012     -73.073  -3.598  44.488  1.00 57.03           O  
ANISOU 1618  OD2 ASP A1012     4596   4277  12794    275   1124    638       O  
ATOM   1619  N   ASN A1013     -76.468   0.325  42.912  1.00 47.26           N  
ANISOU 1619  N   ASN A1013     3356   3077  11524    251   1103    602       N  
ATOM   1620  CA  ASN A1013     -77.505   1.288  43.265  1.00 49.66           C  
ANISOU 1620  CA  ASN A1013     3631   3383  11855    230   1145    644       C  
ATOM   1621  C   ASN A1013     -78.443   1.564  42.094  1.00 54.87           C  
ANISOU 1621  C   ASN A1013     4276   4011  12560    248   1052    585       C  
ATOM   1622  O   ASN A1013     -79.619   1.882  42.310  1.00 48.41           O  
ANISOU 1622  O   ASN A1013     3397   3165  11831    226   1063    618       O  
ATOM   1623  CB  ASN A1013     -76.870   2.574  43.786  1.00 49.23           C  
ANISOU 1623  CB  ASN A1013     3654   3395  11655    239   1223    669       C  
ATOM   1624  CG  ASN A1013     -76.224   2.386  45.148  1.00 51.01           C  
ANISOU 1624  CG  ASN A1013     3882   3645  11855    218   1324    741       C  
ATOM   1625  OD1 ASN A1013     -76.877   2.521  46.183  1.00 61.94           O  
ANISOU 1625  OD1 ASN A1013     5221   5018  13296    191   1398    813       O  
ATOM   1626  ND2 ASN A1013     -74.938   2.061  45.151  1.00 63.09           N  
ANISOU 1626  ND2 ASN A1013     5467   5206  13297    235   1327    724       N  
ATOM   1627  N   LEU A1014     -77.960   1.431  40.855  1.00 63.84           N  
ANISOU 1627  N   LEU A1014     5468   5150  13637    291    960    500       N  
ATOM   1628  CA  LEU A1014     -78.857   1.530  39.707  1.00 64.93           C  
ANISOU 1628  CA  LEU A1014     5591   5253  13827    313    862    442       C  
ATOM   1629  C   LEU A1014     -79.809   0.342  39.648  1.00 63.75           C  
ANISOU 1629  C   LEU A1014     5329   5018  13875    284    806    441       C  
ATOM   1630  O   LEU A1014     -80.973   0.492  39.258  1.00 63.17           O  
ANISOU 1630  O   LEU A1014     5187   4896  13919    272    763    437       O  
ATOM   1631  CB  LEU A1014     -78.046   1.647  38.418  1.00 69.28           C  
ANISOU 1631  CB  LEU A1014     6234   5827  14260    376    781    353       C  
ATOM   1632  CG  LEU A1014     -77.466   3.040  38.169  1.00 68.21           C  
ANISOU 1632  CG  LEU A1014     6189   5759  13969    406    814    354       C  
ATOM   1633  CD1 LEU A1014     -76.381   3.004  37.107  1.00 77.41           C  
ANISOU 1633  CD1 LEU A1014     7447   6956  15009    470    757    283       C  
ATOM   1634  CD2 LEU A1014     -78.575   4.004  37.773  1.00 86.04           C  
ANISOU 1634  CD2 LEU A1014     8429   8008  16253    410    790    359       C  
ATOM   1635  N   LYS A1015     -79.330  -0.847  40.020  1.00 63.19           N  
ANISOU 1635  N   LYS A1015     5226   4919  13865    272    803    446       N  
ATOM   1636  CA  LYS A1015     -80.228  -1.989  40.167  1.00 61.02           C  
ANISOU 1636  CA  LYS A1015     4818   4551  13814    234    762    464       C  
ATOM   1637  C   LYS A1015     -81.251  -1.735  41.265  1.00 61.91           C  
ANISOU 1637  C   LYS A1015     4825   4642  14056    176    851    570       C  
ATOM   1638  O   LYS A1015     -82.423  -2.110  41.136  1.00 72.94           O  
ANISOU 1638  O   LYS A1015     6106   5964  15643    144    812    586       O  
ATOM   1639  CB  LYS A1015     -79.427  -3.257  40.465  1.00 66.15           C  
ANISOU 1639  CB  LYS A1015     5458   5175  14499    236    749    459       C  
ATOM   1640  CG  LYS A1015     -78.573  -3.747  39.307  1.00104.64           C  
ANISOU 1640  CG  LYS A1015    10420  10048  19290    299    647    347       C  
ATOM   1641  CD  LYS A1015     -77.507  -4.728  39.781  1.00 96.54           C  
ANISOU 1641  CD  LYS A1015     9417   9019  18243    310    660    350       C  
ATOM   1642  CE  LYS A1015     -78.116  -5.910  40.518  1.00 86.75           C  
ANISOU 1642  CE  LYS A1015     8043   7696  17222    262    657    410       C  
ATOM   1643  NZ  LYS A1015     -77.069  -6.839  41.030  1.00 82.11           N  
ANISOU 1643  NZ  LYS A1015     7480   7104  16614    277    670    419       N  
ATOM   1644  N   VAL A1016     -80.819  -1.106  42.360  1.00 55.21           N  
ANISOU 1644  N   VAL A1016     4012   3851  13112    162    970    642       N  
ATOM   1645  CA  VAL A1016     -81.733  -0.794  43.456  1.00 54.02           C  
ANISOU 1645  CA  VAL A1016     3774   3680  13070    116   1066    745       C  
ATOM   1646  C   VAL A1016     -82.823   0.170  42.995  1.00 53.80           C  
ANISOU 1646  C   VAL A1016     3732   3638  13071    117   1047    734       C  
ATOM   1647  O   VAL A1016     -84.007  -0.020  43.298  1.00 54.10           O  
ANISOU 1647  O   VAL A1016     3662   3612  13280     84   1057    787       O  
ATOM   1648  CB  VAL A1016     -80.950  -0.237  44.660  1.00 55.25           C  
ANISOU 1648  CB  VAL A1016     3993   3903  13098    113   1191    812       C  
ATOM   1649  CG1 VAL A1016     -81.894   0.418  45.656  1.00 59.47           C  
ANISOU 1649  CG1 VAL A1016     4521   4441  13636    114   1271    892       C  
ATOM   1650  CG2 VAL A1016     -80.159  -1.348  45.334  1.00 54.86           C  
ANISOU 1650  CG2 VAL A1016     3929   3850  13063    109   1216    848       C  
ATOM   1651  N   ILE A1017     -82.443   1.212  42.249  1.00 57.44           N  
ANISOU 1651  N   ILE A1017     4305   4158  13362    162   1014    670       N  
ATOM   1652  CA  ILE A1017     -83.415   2.214  41.814  1.00 50.56           C  
ANISOU 1652  CA  ILE A1017     3429   3278  12504    172    994    660       C  
ATOM   1653  C   ILE A1017     -84.450   1.597  40.881  1.00 51.76           C  
ANISOU 1653  C   ILE A1017     3487   3347  12831    163    886    620       C  
ATOM   1654  O   ILE A1017     -85.646   1.906  40.965  1.00 64.28           O  
ANISOU 1654  O   ILE A1017     4994   4885  14543    143    888    653       O  
ATOM   1655  CB  ILE A1017     -82.697   3.406  41.152  1.00 58.61           C  
ANISOU 1655  CB  ILE A1017     4583   4375  13312    227    974    603       C  
ATOM   1656  CG1 ILE A1017     -81.874   4.175  42.186  1.00 68.69           C  
ANISOU 1656  CG1 ILE A1017     5936   5722  14441    230   1081    649       C  
ATOM   1657  CG2 ILE A1017     -83.699   4.330  40.470  1.00 49.89           C  
ANISOU 1657  CG2 ILE A1017     3471   3253  12232    247    927    581       C  
ATOM   1658  CD1 ILE A1017     -81.092   5.335  41.608  1.00 52.63           C  
ANISOU 1658  CD1 ILE A1017     4010   3749  12240    273   1069    606       C  
ATOM   1659  N   GLU A1018     -84.009   0.713  39.981  1.00 52.05           N  
ANISOU 1659  N   GLU A1018     3531   3362  12885    182    787    547       N  
ATOM   1660  CA  GLU A1018     -84.910   0.156  38.976  1.00 56.28           C  
ANISOU 1660  CA  GLU A1018     3989   3818  13578    182    667    493       C  
ATOM   1661  C   GLU A1018     -86.070  -0.596  39.618  1.00 68.71           C  
ANISOU 1661  C   GLU A1018     5398   5302  15408    118    681    564       C  
ATOM   1662  O   GLU A1018     -87.194  -0.577  39.102  1.00 73.99           O  
ANISOU 1662  O   GLU A1018     5984   5905  16224    105    615    553       O  
ATOM   1663  CB  GLU A1018     -84.133  -0.763  38.032  1.00 57.53           C  
ANISOU 1663  CB  GLU A1018     4189   3961  13709    217    564    400       C  
ATOM   1664  CG  GLU A1018     -84.908  -1.189  36.794  1.00 78.55           C  
ANISOU 1664  CG  GLU A1018     6799   6547  16498    234    421    320       C  
ATOM   1665  CD  GLU A1018     -84.152  -2.200  35.952  1.00 88.72           C  
ANISOU 1665  CD  GLU A1018     8127   7809  17774    274    320    225       C  
ATOM   1666  OE1 GLU A1018     -83.344  -2.965  36.521  1.00 73.97           O  
ANISOU 1666  OE1 GLU A1018     6269   5947  15888    267    354    240       O  
ATOM   1667  OE2 GLU A1018     -84.363  -2.228  34.722  1.00110.36           O  
ANISOU 1667  OE2 GLU A1018    10889  10520  20523    318    204    133       O  
ATOM   1668  N   LYS A1019     -85.822  -1.260  40.740  1.00 72.41           N  
ANISOU 1668  N   LYS A1019     6972   6830  13712    225    -89   1293       N  
ATOM   1669  CA  LYS A1019     -86.844  -2.019  41.457  1.00 76.50           C  
ANISOU 1669  CA  LYS A1019     7435   7279  14353    213    -25   1353       C  
ATOM   1670  C   LYS A1019     -87.054  -1.344  42.811  1.00 81.16           C  
ANISOU 1670  C   LYS A1019     8102   7823  14911    257    171   1395       C  
ATOM   1671  O   LYS A1019     -86.363  -1.648  43.786  1.00102.92           O  
ANISOU 1671  O   LYS A1019    11016  10547  17543    296    193   1357       O  
ATOM   1672  CB  LYS A1019     -86.425  -3.476  41.618  1.00 74.32           C  
ANISOU 1672  CB  LYS A1019     7207   6978  14055    203   -154   1306       C  
ATOM   1673  CG  LYS A1019     -85.941  -4.131  40.340  1.00 85.20           C  
ANISOU 1673  CG  LYS A1019     8554   8403  15416    174   -368   1232       C  
ATOM   1674  CD  LYS A1019     -85.126  -5.377  40.641  1.00 99.43           C  
ANISOU 1674  CD  LYS A1019    10450  10190  17138    183   -501   1158       C  
ATOM   1675  CE  LYS A1019     -83.907  -5.037  41.488  1.00 99.78           C  
ANISOU 1675  CE  LYS A1019    10667  10248  16998    237   -471   1096       C  
ATOM   1676  NZ  LYS A1019     -83.057  -6.226  41.779  1.00100.07           N  
ANISOU 1676  NZ  LYS A1019    10819  10265  16940    259   -613   1012       N  
ATOM   1677  N   ALA A1020     -88.012  -0.424  42.869  1.00 64.92           N  
ANISOU 1677  N   ALA A1020     5956   5753  12956    260    308   1467       N  
ATOM   1678  CA  ALA A1020     -88.265   0.308  44.100  1.00 67.96           C  
ANISOU 1678  CA  ALA A1020     6420   6092  13310    310    496   1502       C  
ATOM   1679  C   ALA A1020     -89.704   0.800  44.131  1.00 92.83           C  
ANISOU 1679  C   ALA A1020     9418   9207  16644    305    637   1597       C  
ATOM   1680  O   ALA A1020     -90.269   1.164  43.097  1.00 82.96           O  
ANISOU 1680  O   ALA A1020     8034   7982  15503    270    586   1618       O  
ATOM   1681  CB  ALA A1020     -87.302   1.492  44.254  1.00 49.22           C  
ANISOU 1681  CB  ALA A1020     4155   3748  10797    344    511   1438       C  
ATOM   1682  N   ASP A1021     -90.287   0.801  45.332  1.00 91.20           N  
ANISOU 1682  N   ASP A1021     9253   8931  16469    345    816   1655       N  
ATOM   1683  CA  ASP A1021     -91.595   1.386  45.579  1.00 80.84           C  
ANISOU 1683  CA  ASP A1021     7807   7575  15333    355    984   1743       C  
ATOM   1684  C   ASP A1021     -91.563   2.489  46.625  1.00 88.43           C  
ANISOU 1684  C   ASP A1021     8888   8507  16204    425   1152   1752       C  
ATOM   1685  O   ASP A1021     -92.595   3.131  46.854  1.00119.12           O  
ANISOU 1685  O   ASP A1021    12675  12359  20227    442   1299   1818       O  
ATOM   1686  CB  ASP A1021     -92.599   0.305  46.017  1.00101.24           C  
ANISOU 1686  CB  ASP A1021    10284  10078  18105    344   1081   1824       C  
ATOM   1687  CG  ASP A1021     -92.313  -0.235  47.410  1.00 97.84           C  
ANISOU 1687  CG  ASP A1021    10046   9575  17553    398   1216   1855       C  
ATOM   1688  OD1 ASP A1021     -92.793   0.365  48.397  1.00108.07           O  
ANISOU 1688  OD1 ASP A1021    11396  10818  18848    457   1425   1914       O  
ATOM   1689  OD2 ASP A1021     -91.613  -1.264  47.520  1.00 97.65           O  
ANISOU 1689  OD2 ASP A1021    10136   9539  17427    385   1115   1823       O  
ATOM   1690  N   ASN A1022     -90.419   2.727  47.259  1.00 62.12           N  
ANISOU 1690  N   ASN A1022     5762   5179  12663    469   1126   1679       N  
ATOM   1691  CA  ASN A1022     -90.275   3.728  48.303  1.00 64.41           C  
ANISOU 1691  CA  ASN A1022     6184   5426  12861    546   1258   1665       C  
ATOM   1692  C   ASN A1022     -89.756   5.040  47.714  1.00 60.24           C  
ANISOU 1692  C   ASN A1022     5649   4948  12293    542   1193   1599       C  
ATOM   1693  O   ASN A1022     -89.389   5.125  46.541  1.00 62.24           O  
ANISOU 1693  O   ASN A1022     5822   5267  12560    486   1058   1570       O  
ATOM   1694  CB  ASN A1022     -89.338   3.213  49.399  1.00 60.96           C  
ANISOU 1694  CB  ASN A1022     5986   4938  12236    612   1254   1612       C  
ATOM   1695  CG  ASN A1022     -89.362   4.074  50.649  1.00 87.72           C  
ANISOU 1695  CG  ASN A1022     9525   8261  15546    720   1402   1605       C  
ATOM   1696  OD1 ASN A1022     -88.665   5.086  50.732  1.00 83.77           O  
ANISOU 1696  OD1 ASN A1022     9093   7771  14966    755   1352   1511       O  
ATOM   1697  ND2 ASN A1022     -90.166   3.676  51.628  1.00108.10           N  
ANISOU 1697  ND2 ASN A1022    12154  10762  18155    780   1593   1704       N  
ATOM   1698  N   ALA A1023     -89.736   6.076  48.549  1.00 68.18           N  
ANISOU 1698  N   ALA A1023     6745   5909  13250    611   1299   1578       N  
ATOM   1699  CA  ALA A1023     -89.232   7.388  48.162  1.00 69.90           C  
ANISOU 1699  CA  ALA A1023     6970   6148  13441    614   1258   1515       C  
ATOM   1700  C   ALA A1023     -87.814   7.652  48.649  1.00 62.58           C  
ANISOU 1700  C   ALA A1023     6210   5204  12365    651   1174   1387       C  
ATOM   1701  O   ALA A1023     -87.024   8.268  47.927  1.00 53.00           O  
ANISOU 1701  O   ALA A1023     4974   4021  11142    614   1081   1324       O  
ATOM   1702  CB  ALA A1023     -90.163   8.486  48.686  1.00 93.15           C  
ANISOU 1702  CB  ALA A1023     9887   9046  16459    667   1411   1559       C  
ATOM   1703  N   ALA A1024     -87.468   7.201  49.858  1.00 89.70           N  
ANISOU 1703  N   ALA A1024     9811   8577  15692    732   1208   1346       N  
ATOM   1704  CA  ALA A1024     -86.131   7.425  50.396  1.00 88.26           C  
ANISOU 1704  CA  ALA A1024     9789   8365  15381    787   1110   1201       C  
ATOM   1705  C   ALA A1024     -85.109   6.418  49.886  1.00 86.87           C  
ANISOU 1705  C   ALA A1024     9642   8227  15138    742    949   1137       C  
ATOM   1706  O   ALA A1024     -83.901   6.663  50.008  1.00 97.20           O  
ANISOU 1706  O   ALA A1024    11029   9523  16378    766    843   1002       O  
ATOM   1707  CB  ALA A1024     -86.168   7.390  51.925  1.00 94.21           C  
ANISOU 1707  CB  ALA A1024    10735   9032  16028    931   1197   1169       C  
ATOM   1708  N   GLN A1025     -85.563   5.295  49.323  1.00 65.38           N  
ANISOU 1708  N   GLN A1025     6847   5546  12451    681    923   1221       N  
ATOM   1709  CA  GLN A1025     -84.637   4.342  48.722  1.00 53.87           C  
ANISOU 1709  CA  GLN A1025     5403   4129  10938    638    759   1160       C  
ATOM   1710  C   GLN A1025     -83.874   4.987  47.575  1.00 55.31           C  
ANISOU 1710  C   GLN A1025     5480   4374  11163    572    659   1100       C  
ATOM   1711  O   GLN A1025     -82.662   4.778  47.422  1.00 69.82           O  
ANISOU 1711  O   GLN A1025     7369   6219  12940    572    538    988       O  
ATOM   1712  CB  GLN A1025     -85.401   3.110  48.234  1.00 48.41           C  
ANISOU 1712  CB  GLN A1025     4625   3463  10306    583    747   1260       C  
ATOM   1713  CG  GLN A1025     -84.528   1.912  47.901  1.00 45.10           C  
ANISOU 1713  CG  GLN A1025     4260   3063   9811    563    582   1198       C  
ATOM   1714  CD  GLN A1025     -84.081   1.152  49.135  1.00 68.35           C  
ANISOU 1714  CD  GLN A1025     7426   5925  12619    654    582   1159       C  
ATOM   1715  OE1 GLN A1025     -84.408   1.525  50.262  1.00 78.39           O  
ANISOU 1715  OE1 GLN A1025     8818   7123  13842    741    711   1181       O  
ATOM   1716  NE2 GLN A1025     -83.333   0.075  48.927  1.00 75.59           N  
ANISOU 1716  NE2 GLN A1025     8409   6849  13464    649    434   1101       N  
ATOM   1717  N   VAL A1026     -84.574   5.780  46.761  1.00 50.21           N  
ANISOU 1717  N   VAL A1026     4687   3764  10625    524    717   1176       N  
ATOM   1718  CA  VAL A1026     -83.919   6.535  45.701  1.00 55.19           C  
ANISOU 1718  CA  VAL A1026     5235   4435  11300    476    660   1146       C  
ATOM   1719  C   VAL A1026     -82.876   7.475  46.289  1.00 54.07           C  
ANISOU 1719  C   VAL A1026     5176   4237  11131    510    661   1027       C  
ATOM   1720  O   VAL A1026     -81.779   7.622  45.743  1.00 62.98           O  
ANISOU 1720  O   VAL A1026     6283   5376  12270    479    582    949       O  
ATOM   1721  CB  VAL A1026     -84.963   7.295  44.862  1.00 53.17           C  
ANISOU 1721  CB  VAL A1026     4844   4207  11151    447    733   1256       C  
ATOM   1722  CG1 VAL A1026     -84.294   8.027  43.709  1.00 42.20           C  
ANISOU 1722  CG1 VAL A1026     3390   2847   9798    411    690   1250       C  
ATOM   1723  CG2 VAL A1026     -86.022   6.335  44.345  1.00 47.82           C  
ANISOU 1723  CG2 VAL A1026     4073   3568  10529    419    717   1350       C  
ATOM   1724  N   LYS A1027     -83.195   8.118  47.415  1.00 55.11           N  
ANISOU 1724  N   LYS A1027     5395   4301  11244    578    751   1002       N  
ATOM   1725  CA  LYS A1027     -82.245   9.035  48.038  1.00 55.57           C  
ANISOU 1725  CA  LYS A1027     5528   4293  11294    621    737    866       C  
ATOM   1726  C   LYS A1027     -80.981   8.306  48.482  1.00 70.23           C  
ANISOU 1726  C   LYS A1027     7488   6133  13063    655    609    718       C  
ATOM   1727  O   LYS A1027     -79.863   8.775  48.237  1.00 79.49           O  
ANISOU 1727  O   LYS A1027     8634   7289  14281    633    541    599       O  
ATOM   1728  CB  LYS A1027     -82.904   9.748  49.219  1.00 60.09           C  
ANISOU 1728  CB  LYS A1027     6189   4794  11847    714    842    860       C  
ATOM   1729  CG  LYS A1027     -81.989  10.705  49.967  1.00 57.46           C  
ANISOU 1729  CG  LYS A1027     5938   4385  11511    778    810    698       C  
ATOM   1730  CD  LYS A1027     -82.788  11.838  50.590  1.00 74.37           C  
ANISOU 1730  CD  LYS A1027     8096   6470  13691    840    921    719       C  
ATOM   1731  CE  LYS A1027     -81.946  12.652  51.557  1.00 72.84           C  
ANISOU 1731  CE  LYS A1027     8007   6192  13477    935    871    533       C  
ATOM   1732  NZ  LYS A1027     -80.704  13.167  50.919  1.00 70.23           N  
ANISOU 1732  NZ  LYS A1027     7594   5845  13244    855    781    419       N  
ATOM   1733  N   ASP A1028     -81.138   7.148  49.129  1.00 61.20           N  
ANISOU 1733  N   ASP A1028     6459   4987  11807    712    577    722       N  
ATOM   1734  CA  ASP A1028     -79.971   6.387  49.574  1.00 58.01           C  
ANISOU 1734  CA  ASP A1028     6172   4566  11302    766    441    575       C  
ATOM   1735  C   ASP A1028     -79.125   5.933  48.388  1.00 58.83           C  
ANISOU 1735  C   ASP A1028     6161   4734  11456    672    325    541       C  
ATOM   1736  O   ASP A1028     -77.892   6.085  48.387  1.00 69.37           O  
ANISOU 1736  O   ASP A1028     7501   6056  12800    679    227    384       O  
ATOM   1737  CB  ASP A1028     -80.419   5.184  50.406  1.00 43.74           C  
ANISOU 1737  CB  ASP A1028     4519   2734   9366    849    444    619       C  
ATOM   1738  CG  ASP A1028     -79.490   4.902  51.572  1.00 44.47           C  
ANISOU 1738  CG  ASP A1028     4819   2762   9315    996    357    451       C  
ATOM   1739  OD1 ASP A1028     -78.876   5.858  52.090  1.00 47.51           O  
ANISOU 1739  OD1 ASP A1028     5241   3109   9702   1061    337    310       O  
ATOM   1740  OD2 ASP A1028     -79.372   3.723  51.969  1.00 52.58           O  
ANISOU 1740  OD2 ASP A1028     5976   3773  10229   1057    300    453       O  
ATOM   1741  N   ALA A1029     -79.776   5.377  47.362  1.00 65.38           N  
ANISOU 1741  N   ALA A1029     6880   5634  12329    591    331    676       N  
ATOM   1742  CA  ALA A1029     -79.042   4.890  46.199  1.00 51.53           C  
ANISOU 1742  CA  ALA A1029     5025   3943  10613    522    221    652       C  
ATOM   1743  C   ALA A1029     -78.326   6.027  45.483  1.00 55.33           C  
ANISOU 1743  C   ALA A1029     5392   4418  11212    472    242    609       C  
ATOM   1744  O   ALA A1029     -77.175   5.876  45.058  1.00 71.74           O  
ANISOU 1744  O   ALA A1029     7434   6503  13322    451    151    501       O  
ATOM   1745  CB  ALA A1029     -79.988   4.165  45.245  1.00 51.03           C  
ANISOU 1745  CB  ALA A1029     4866   3948  10575    465    218    798       C  
ATOM   1746  N   LEU A1030     -78.986   7.178  45.349  1.00 41.33           N  
ANISOU 1746  N   LEU A1030     3561   2625   9519    454    368    691       N  
ATOM   1747  CA  LEU A1030     -78.363   8.301  44.663  1.00 51.39           C  
ANISOU 1747  CA  LEU A1030     4731   3873  10921    408    411    672       C  
ATOM   1748  C   LEU A1030     -77.232   8.905  45.482  1.00 60.61           C  
ANISOU 1748  C   LEU A1030     5942   4961  12128    434    382    487       C  
ATOM   1749  O   LEU A1030     -76.253   9.380  44.906  1.00 66.60           O  
ANISOU 1749  O   LEU A1030     6606   5694  13005    387    373    418       O  
ATOM   1750  CB  LEU A1030     -79.411   9.357  44.324  1.00 55.20           C  
ANISOU 1750  CB  LEU A1030     5154   4348  11470    395    544    808       C  
ATOM   1751  CG  LEU A1030     -80.362   8.950  43.198  1.00 41.70           C  
ANISOU 1751  CG  LEU A1030     3364   2718   9760    367    557    969       C  
ATOM   1752  CD1 LEU A1030     -81.370  10.048  42.964  1.00 48.12           C  
ANISOU 1752  CD1 LEU A1030     4132   3517  10634    374    676   1079       C  
ATOM   1753  CD2 LEU A1030     -79.603   8.638  41.916  1.00 41.29           C  
ANISOU 1753  CD2 LEU A1030     3234   2709   9746    327    496    985       C  
ATOM   1754  N   THR A1031     -77.334   8.892  46.813  1.00 50.59           N  
ANISOU 1754  N   THR A1031     4808   3642  10770    518    369    396       N  
ATOM   1755  CA  THR A1031     -76.209   9.331  47.633  1.00 64.78           C  
ANISOU 1755  CA  THR A1031     6654   5371  12588    564    302    183       C  
ATOM   1756  C   THR A1031     -75.000   8.425  47.425  1.00 56.73           C  
ANISOU 1756  C   THR A1031     5626   4380  11547    559    156     39       C  
ATOM   1757  O   THR A1031     -73.872   8.899  47.216  1.00 62.41           O  
ANISOU 1757  O   THR A1031     6256   5069  12390    523    113   -108       O  
ATOM   1758  CB  THR A1031     -76.614   9.353  49.107  1.00 60.65           C  
ANISOU 1758  CB  THR A1031     6311   4799  11935    693    304    116       C  
ATOM   1759  OG1 THR A1031     -77.815  10.119  49.263  1.00 49.29           O  
ANISOU 1759  OG1 THR A1031     4869   3339  10519    701    441    254       O  
ATOM   1760  CG2 THR A1031     -75.509   9.973  49.953  1.00 93.03           C  
ANISOU 1760  CG2 THR A1031    10455   8832  16059    759    223   -123       C  
ATOM   1761  N   LYS A1032     -75.225   7.109  47.463  1.00 48.61           N  
ANISOU 1761  N   LYS A1032     4681   3409  10381    592     79     76       N  
ATOM   1762  CA  LYS A1032     -74.127   6.171  47.255  1.00 46.02           C  
ANISOU 1762  CA  LYS A1032     4351   3116  10019    598    -75    -63       C  
ATOM   1763  C   LYS A1032     -73.527   6.324  45.862  1.00 50.99           C  
ANISOU 1763  C   LYS A1032     4793   3779  10803    491    -77    -41       C  
ATOM   1764  O   LYS A1032     -72.307   6.217  45.686  1.00 53.04           O  
ANISOU 1764  O   LYS A1032     4989   4037  11127    479   -171   -212       O  
ATOM   1765  CB  LYS A1032     -74.611   4.742  47.491  1.00 43.44           C  
ANISOU 1765  CB  LYS A1032     4149   2833   9524    650   -147     -1       C  
ATOM   1766  CG  LYS A1032     -74.856   4.436  48.956  1.00 43.07           C  
ANISOU 1766  CG  LYS A1032     4316   2733   9314    789   -158    -59       C  
ATOM   1767  CD  LYS A1032     -75.594   3.125  49.149  1.00 51.50           C  
ANISOU 1767  CD  LYS A1032     5500   3817  10250    828   -174     59       C  
ATOM   1768  CE  LYS A1032     -75.626   2.742  50.618  1.00 51.72           C  
ANISOU 1768  CE  LYS A1032     5768   3776  10106    993   -186     -8       C  
ATOM   1769  NZ  LYS A1032     -75.883   3.924  51.489  1.00 43.94           N  
ANISOU 1769  NZ  LYS A1032     4839   2729   9127   1068    -86    -45       N  
ATOM   1770  N   MET A1033     -74.370   6.576  44.860  1.00 50.21           N  
ANISOU 1770  N   MET A1033     4604   3712  10763    425     27    161       N  
ATOM   1771  CA  MET A1033     -73.867   6.825  43.514  1.00 53.67           C  
ANISOU 1771  CA  MET A1033     4884   4169  11340    349     53    208       C  
ATOM   1772  C   MET A1033     -73.111   8.146  43.424  1.00 55.48           C  
ANISOU 1772  C   MET A1033     5006   4313  11760    307    144    133       C  
ATOM   1773  O   MET A1033     -72.154   8.262  42.650  1.00 60.91           O  
ANISOU 1773  O   MET A1033     5573   4986  12583    262    144     77       O  
ATOM   1774  CB  MET A1033     -75.022   6.800  42.517  1.00 41.60           C  
ANISOU 1774  CB  MET A1033     3309   2696   9800    319    133    439       C  
ATOM   1775  CG  MET A1033     -75.505   5.401  42.199  1.00 39.79           C  
ANISOU 1775  CG  MET A1033     3126   2551   9443    335     23    495       C  
ATOM   1776  SD  MET A1033     -76.852   5.365  41.011  1.00 39.50           S  
ANISOU 1776  SD  MET A1033     3025   2582   9402    309     87    725       S  
ATOM   1777  CE  MET A1033     -76.405   6.742  39.959  1.00 40.26           C  
ANISOU 1777  CE  MET A1033     3004   2640   9654    276    218    796       C  
ATOM   1778  N   ARG A1034     -73.536   9.150  44.190  1.00 56.32           N  
ANISOU 1778  N   ARG A1034     5149   4356  11892    323    230    131       N  
ATOM   1779  CA  ARG A1034     -72.839  10.428  44.221  1.00 57.58           C  
ANISOU 1779  CA  ARG A1034     5209   4422  12247    283    310     45       C  
ATOM   1780  C   ARG A1034     -71.428  10.265  44.767  1.00 59.34           C  
ANISOU 1780  C   ARG A1034     5402   4611  12535    291    191   -225       C  
ATOM   1781  O   ARG A1034     -70.471  10.835  44.229  1.00 73.34           O  
ANISOU 1781  O   ARG A1034     7020   6330  14514    227    233   -306       O  
ATOM   1782  CB  ARG A1034     -73.636  11.424  45.059  1.00 58.26           C  
ANISOU 1782  CB  ARG A1034     5363   4451  12324    317    393     76       C  
ATOM   1783  CG  ARG A1034     -72.923  12.730  45.343  1.00 67.85           C  
ANISOU 1783  CG  ARG A1034     6491   5556  13733    288    448    -47       C  
ATOM   1784  CD  ARG A1034     -73.715  13.555  46.342  1.00 76.15           C  
ANISOU 1784  CD  ARG A1034     7639   6553  14741    346    490    -46       C  
ATOM   1785  NE  ARG A1034     -73.122  14.866  46.574  1.00 73.69           N  
ANISOU 1785  NE  ARG A1034     7239   6129  14630    316    538   -157       N  
ATOM   1786  CZ  ARG A1034     -72.179  15.113  47.473  1.00 94.28           C  
ANISOU 1786  CZ  ARG A1034     9848   8680  17296    347    436   -407       C  
ATOM   1787  NH1 ARG A1034     -71.668  14.151  48.223  1.00116.19           N  
ANISOU 1787  NH1 ARG A1034    12722  11504  19923    420    278   -575       N  
ATOM   1788  NH2 ARG A1034     -71.740  16.358  47.624  1.00 92.36           N  
ANISOU 1788  NH2 ARG A1034     9506   8328  17258    312    485   -496       N  
ATOM   1789  N   ALA A1035     -71.278   9.486  45.841  1.00 53.07           N  
ANISOU 1789  N   ALA A1035     4750   3845  11568    378     46   -371       N  
ATOM   1790  CA  ALA A1035     -69.941   9.261  46.388  1.00 47.30           C  
ANISOU 1790  CA  ALA A1035     3998   3106  10868    405    -98   -651       C  
ATOM   1791  C   ALA A1035     -69.042   8.548  45.384  1.00 50.22           C  
ANISOU 1791  C   ALA A1035     4241   3524  11315    350   -160   -704       C  
ATOM   1792  O   ALA A1035     -67.857   8.877  45.257  1.00 75.01           O  
ANISOU 1792  O   ALA A1035     7241   6634  14623    311   -194   -897       O  
ATOM   1793  CB  ALA A1035     -70.028   8.464  47.689  1.00 70.22           C  
ANISOU 1793  CB  ALA A1035     7112   6043  13526    541   -243   -772       C  
ATOM   1794  N   ALA A1036     -69.586   7.563  44.666  1.00 46.36           N  
ANISOU 1794  N   ALA A1036     3789   3110  10716    350   -179   -547       N  
ATOM   1795  CA  ALA A1036     -68.784   6.802  43.712  1.00 43.73           C  
ANISOU 1795  CA  ALA A1036     3354   2829  10434    318   -252   -600       C  
ATOM   1796  C   ALA A1036     -68.313   7.667  42.550  1.00 51.41           C  
ANISOU 1796  C   ALA A1036     4126   3742  11667    223    -97   -537       C  
ATOM   1797  O   ALA A1036     -67.170   7.539  42.097  1.00 75.62           O  
ANISOU 1797  O   ALA A1036     7061   6801  14869    192   -131   -693       O  
ATOM   1798  CB  ALA A1036     -69.581   5.606  43.197  1.00 52.87           C  
ANISOU 1798  CB  ALA A1036     4598   4075  11413    346   -311   -436       C  
ATOM   1799  N   ALA A1037     -69.181   8.546  42.047  1.00 47.33           N  
ANISOU 1799  N   ALA A1037     3583   3180  11221    185     84   -309       N  
ATOM   1800  CA  ALA A1037     -68.840   9.332  40.866  1.00 57.57           C  
ANISOU 1800  CA  ALA A1037     4717   4414  12744    116    260   -198       C  
ATOM   1801  C   ALA A1037     -67.783  10.390  41.156  1.00 67.82           C  
ANISOU 1801  C   ALA A1037     5868   5602  14297     64    340   -376       C  
ATOM   1802  O   ALA A1037     -67.100  10.840  40.228  1.00 86.47           O  
ANISOU 1802  O   ALA A1037     8071   7904  16880     14    477   -351       O  
ATOM   1803  CB  ALA A1037     -70.093   9.983  40.293  1.00 69.06           C  
ANISOU 1803  CB  ALA A1037     6204   5867  14169    115    418     91       C  
ATOM   1804  N   LEU A1038     -67.637  10.802  42.420  1.00 61.12           N  
ANISOU 1804  N   LEU A1038     5070   4725  13429     87    265   -554       N  
ATOM   1805  CA  LEU A1038     -66.705  11.873  42.767  1.00 73.32           C  
ANISOU 1805  CA  LEU A1038     6467   6169  15221     43    325   -735       C  
ATOM   1806  C   LEU A1038     -65.296  11.575  42.261  1.00 90.55           C  
ANISOU 1806  C   LEU A1038     8464   8345  17595      2    301   -933       C  
ATOM   1807  O   LEU A1038     -64.707  12.371  41.521  1.00 96.56           O  
ANISOU 1807  O   LEU A1038     9048   9021  18620    -45    484   -910       O  
ATOM   1808  CB  LEU A1038     -66.703  12.083  44.282  1.00 73.08           C  
ANISOU 1808  CB  LEU A1038     6545   6133  15088    103    182   -933       C  
ATOM   1809  CG  LEU A1038     -67.636  13.167  44.821  1.00 62.52           C  
ANISOU 1809  CG  LEU A1038     5280   4726  13748    117    281   -819       C  
ATOM   1810  CD1 LEU A1038     -67.887  12.954  46.301  1.00 83.52           C  
ANISOU 1810  CD1 LEU A1038     8121   7409  16204    221    119   -971       C  
ATOM   1811  CD2 LEU A1038     -67.031  14.540  44.575  1.00 63.33           C  
ANISOU 1811  CD2 LEU A1038     5196   4705  14162     47    426   -867       C  
ATOM   1812  N   ASP A1039     -64.751  10.417  42.639  1.00 69.83           N  
ANISOU 1812  N   ASP A1039     5890   5815  14826     44     85  -1126       N  
ATOM   1813  CA  ASP A1039     -63.479   9.925  42.116  1.00 74.01           C  
ANISOU 1813  CA  ASP A1039     6253   6369  15498     13     35  -1326       C  
ATOM   1814  C   ASP A1039     -62.353  10.954  42.177  1.00 95.77           C  
ANISOU 1814  C   ASP A1039     8798   9040  18550    -22    137  -1518       C  
ATOM   1815  O   ASP A1039     -62.212  11.677  43.169  1.00113.43           O  
ANISOU 1815  O   ASP A1039    11002  11238  20856    -12     91  -1659       O  
ATOM   1816  CB  ASP A1039     -63.656   9.439  40.677  1.00 73.63           C  
ANISOU 1816  CB  ASP A1039     6186   6322  15466    -20    150  -1117       C  
ATOM   1817  CG  ASP A1039     -63.944   7.958  40.601  1.00 68.61           C  
ANISOU 1817  CG  ASP A1039     5705   5816  14548     46    -54  -1116       C  
ATOM   1818  OD1 ASP A1039     -63.501   7.225  41.509  1.00 82.77           O  
ANISOU 1818  OD1 ASP A1039     7567   7698  16186    108   -280  -1349       O  
ATOM   1819  OD2 ASP A1039     -64.610   7.525  39.638  1.00 70.24           O  
ANISOU 1819  OD2 ASP A1039     5971   6069  14649     69      6   -874       O  
ATOM   1820  N   ALA A1040     -61.557  11.029  41.108  1.00 78.35           N  
ANISOU 1820  N   ALA A1040     6534   6783  16455    -32    282  -1513       N  
ATOM   1821  CA  ALA A1040     -60.335  11.818  41.081  1.00 69.36           C  
ANISOU 1821  CA  ALA A1040     5252   5535  15565    -47    380  -1719       C  
ATOM   1822  C   ALA A1040     -60.557  13.259  40.629  1.00 57.74           C  
ANISOU 1822  C   ALA A1040     3701   3886  14350    -88    666  -1543       C  
ATOM   1823  O   ALA A1040     -59.602  13.916  40.197  1.00 61.88           O  
ANISOU 1823  O   ALA A1040     4101   4283  15129   -121    823  -1640       O  
ATOM   1824  CB  ALA A1040     -59.292  11.141  40.190  1.00 59.59           C  
ANISOU 1824  CB  ALA A1040     3983   4286  14374    -64    399  -1841       C  
ATOM   1825  N   GLY A1041     -61.786  13.762  40.718  1.00 72.12           N  
ANISOU 1825  N   GLY A1041     5587   5698  16119    -86    740  -1292       N  
ATOM   1826  CA  GLY A1041     -62.054  15.167  40.474  1.00 77.86           C  
ANISOU 1826  CA  GLY A1041     6259   6279  17046   -113    973  -1141       C  
ATOM   1827  C   GLY A1041     -61.695  15.657  39.086  1.00 59.96           C  
ANISOU 1827  C   GLY A1041     3998   3916  14869   -180   1237   -942       C  
ATOM   1828  O   GLY A1041     -61.064  16.706  38.937  1.00 62.41           O  
ANISOU 1828  O   GLY A1041     4213   4098  15404   -231   1399   -981       O  
ATOM   1829  N   SER A1042     -62.096  14.905  38.060  1.00 65.55           N  
ANISOU 1829  N   SER A1042     4805   4711  15391   -193   1278   -719       N  
ATOM   1830  CA  SER A1042     -61.789  15.298  36.688  1.00 78.44           C  
ANISOU 1830  CA  SER A1042     6428   6325  17049   -268   1527   -497       C  
ATOM   1831  C   SER A1042     -62.442  16.622  36.311  1.00 82.24           C  
ANISOU 1831  C   SER A1042     6940   6694  17613   -272   1754   -241       C  
ATOM   1832  O   SER A1042     -61.931  17.339  35.443  1.00 83.23           O  
ANISOU 1832  O   SER A1042     7023   6748  17852   -333   1987   -122       O  
ATOM   1833  CB  SER A1042     -62.230  14.201  35.718  1.00 85.22           C  
ANISOU 1833  CB  SER A1042     7364   7353  17663   -261   1501   -299       C  
ATOM   1834  OG  SER A1042     -63.623  13.961  35.815  1.00 82.98           O  
ANISOU 1834  OG  SER A1042     7201   7108  17218   -187   1435    -91       O  
ATOM   1835  N   GLY A1043     -63.563  16.961  36.944  1.00 86.01           N  
ANISOU 1835  N   GLY A1043     7491   7168  18023   -209   1692   -154       N  
ATOM   1836  CA  GLY A1043     -64.330  18.131  36.566  1.00 98.44           C  
ANISOU 1836  CA  GLY A1043     9117   8666  19621   -202   1876     95       C  
ATOM   1837  C   GLY A1043     -65.561  17.713  35.792  1.00105.91           C  
ANISOU 1837  C   GLY A1043    10199   9719  20321   -143   1897    407       C  
ATOM   1838  O   GLY A1043     -66.659  18.227  36.019  1.00109.55           O  
ANISOU 1838  O   GLY A1043    10739  10188  20698    -98   1900    548       O  
ATOM   1839  N   SER A1044     -65.380  16.758  34.875  1.00124.71           N  
ANISOU 1839  N   SER A1044    12602  12197  22585   -145   1902    505       N  
ATOM   1840  CA  SER A1044     -66.504  16.031  34.303  1.00118.06           C  
ANISOU 1840  CA  SER A1044    11865  11480  21514    -74   1848    738       C  
ATOM   1841  C   SER A1044     -66.943  14.883  35.196  1.00120.06           C  
ANISOU 1841  C   SER A1044    12141  11830  21645    -38   1578    591       C  
ATOM   1842  O   SER A1044     -67.939  14.221  34.890  1.00123.63           O  
ANISOU 1842  O   SER A1044    12669  12383  21922     18   1501    754       O  
ATOM   1843  CB  SER A1044     -66.153  15.499  32.911  1.00122.14           C  
ANISOU 1843  CB  SER A1044    12375  12075  21958    -86   1969    918       C  
ATOM   1844  OG  SER A1044     -67.235  15.675  32.013  1.00122.00           O  
ANISOU 1844  OG  SER A1044    12452  12099  21802     -7   2067   1243       O  
ATOM   1845  N   GLY A1045     -66.202  14.614  36.271  1.00135.50           N  
ANISOU 1845  N   GLY A1045    14031  13761  23691    -65   1431    281       N  
ATOM   1846  CA  GLY A1045     -66.763  13.840  37.362  1.00144.50           C  
ANISOU 1846  CA  GLY A1045    15207  14986  24710    -28   1197    152       C  
ATOM   1847  C   GLY A1045     -67.912  14.568  38.025  1.00157.50           C  
ANISOU 1847  C   GLY A1045    16934  16639  26270    -11   1202    253       C  
ATOM   1848  O   GLY A1045     -68.930  13.963  38.362  1.00143.47           O  
ANISOU 1848  O   GLY A1045    15266  14961  24284     17   1082    328       O  
ATOM   1849  N   ASP A1046     -67.775  15.885  38.186  1.00174.01           N  
ANISOU 1849  N   ASP A1046    18988  18615  28511    -31   1344    255       N  
ATOM   1850  CA  ASP A1046     -68.836  16.698  38.762  1.00160.70           C  
ANISOU 1850  CA  ASP A1046    17383  16919  26757    -14   1359    344       C  
ATOM   1851  C   ASP A1046     -70.003  16.911  37.806  1.00151.11           C  
ANISOU 1851  C   ASP A1046    16267  15753  25395     32   1464    655       C  
ATOM   1852  O   ASP A1046     -71.114  17.189  38.269  1.00152.17           O  
ANISOU 1852  O   ASP A1046    16493  15924  25402     60   1427    729       O  
ATOM   1853  CB  ASP A1046     -68.280  18.053  39.205  1.00175.20           C  
ANISOU 1853  CB  ASP A1046    19137  18607  28824    -50   1463    236       C  
ATOM   1854  CG  ASP A1046     -69.241  18.810  40.109  1.00167.72           C  
ANISOU 1854  CG  ASP A1046    18267  17640  27820    -34   1427    248       C  
ATOM   1855  OD1 ASP A1046     -69.440  18.371  41.261  1.00151.94           O  
ANISOU 1855  OD1 ASP A1046    16318  15687  25726    -25   1251     88       O  
ATOM   1856  OD2 ASP A1046     -69.789  19.843  39.673  1.00181.37           O  
ANISOU 1856  OD2 ASP A1046    20024  19303  29587    -25   1571    416       O  
ATOM   1857  N   ILE A1047     -69.785  16.802  36.490  1.00125.49           N  
ANISOU 1857  N   ILE A1047    13012  12510  22157     45   1593    831       N  
ATOM   1858  CA  ILE A1047     -70.919  16.843  35.567  1.00115.33           C  
ANISOU 1858  CA  ILE A1047    11823  11294  20705    105   1656   1111       C  
ATOM   1859  C   ILE A1047     -71.781  15.605  35.751  1.00100.23           C  
ANISOU 1859  C   ILE A1047     9978   9531  18575    141   1467   1133       C  
ATOM   1860  O   ILE A1047     -73.009  15.663  35.615  1.00104.31           O  
ANISOU 1860  O   ILE A1047    10583  10115  18933    188   1444   1276       O  
ATOM   1861  CB  ILE A1047     -70.460  17.003  34.101  1.00107.40           C  
ANISOU 1861  CB  ILE A1047    10806  10258  19741    120   1841   1307       C  
ATOM   1862  CG1 ILE A1047     -71.521  17.738  33.277  1.00107.53           C  
ANISOU 1862  CG1 ILE A1047    10923  10286  19649    188   1962   1578       C  
ATOM   1863  CG2 ILE A1047     -70.204  15.657  33.434  1.00102.65           C  
ANISOU 1863  CG2 ILE A1047    10191   9754  19056    137   1761   1342       C  
ATOM   1864  CD1 ILE A1047     -71.274  17.647  31.762  1.00114.51           C  
ANISOU 1864  CD1 ILE A1047    11831  11180  20500    232   2126   1814       C  
ATOM   1865  N   LEU A1048     -71.152  14.461  36.034  1.00 86.44           N  
ANISOU 1865  N   LEU A1048     8192   7831  16819    117   1325    982       N  
ATOM   1866  CA  LEU A1048     -71.914  13.272  36.389  1.00 78.19           C  
ANISOU 1866  CA  LEU A1048     7228   6913  15567    139   1130    970       C  
ATOM   1867  C   LEU A1048     -72.499  13.408  37.788  1.00 79.56           C  
ANISOU 1867  C   LEU A1048     7473   7097  15660    132   1029    844       C  
ATOM   1868  O   LEU A1048     -73.645  13.013  38.026  1.00 84.67           O  
ANISOU 1868  O   LEU A1048     8217   7827  16126    166    955    922       O  
ATOM   1869  CB  LEU A1048     -71.033  12.029  36.282  1.00 76.79           C  
ANISOU 1869  CB  LEU A1048     7007   6771  15397    121    998    837       C  
ATOM   1870  CG  LEU A1048     -71.727  10.683  36.496  1.00 70.58           C  
ANISOU 1870  CG  LEU A1048     6326   6115  14375    153    788    827       C  
ATOM   1871  CD1 LEU A1048     -72.824  10.467  35.460  1.00 74.56           C  
ANISOU 1871  CD1 LEU A1048     6894   6708  14727    216    805   1069       C  
ATOM   1872  CD2 LEU A1048     -70.721   9.539  36.471  1.00 59.59           C  
ANISOU 1872  CD2 LEU A1048     4904   4755  12981    150    639    653       C  
ATOM   1873  N   VAL A1049     -71.734  13.980  38.722  1.00 77.84           N  
ANISOU 1873  N   VAL A1049     7208   6789  15579     95   1029    647       N  
ATOM   1874  CA  VAL A1049     -72.271  14.259  40.053  1.00 73.27           C  
ANISOU 1874  CA  VAL A1049     6710   6200  14928    104    953    540       C  
ATOM   1875  C   VAL A1049     -73.426  15.250  39.964  1.00 79.46           C  
ANISOU 1875  C   VAL A1049     7547   6970  15676    133   1062    710       C  
ATOM   1876  O   VAL A1049     -74.447  15.099  40.647  1.00 77.01           O  
ANISOU 1876  O   VAL A1049     7337   6707  15217    166   1003    732       O  
ATOM   1877  CB  VAL A1049     -71.156  14.767  40.987  1.00 75.64           C  
ANISOU 1877  CB  VAL A1049     6941   6400  15399     68    922    285       C  
ATOM   1878  CG1 VAL A1049     -71.746  15.279  42.286  1.00 82.22           C  
ANISOU 1878  CG1 VAL A1049     7871   7204  16166     95    867    199       C  
ATOM   1879  CG2 VAL A1049     -70.154  13.662  41.267  1.00 73.86           C  
ANISOU 1879  CG2 VAL A1049     6688   6211  15164     56    767     80       C  
ATOM   1880  N   GLY A1050     -73.283  16.279  39.126  1.00 77.11           N  
ANISOU 1880  N   GLY A1050     7189   6599  15511    128   1228    829       N  
ATOM   1881  CA  GLY A1050     -74.364  17.235  38.955  1.00 69.30           C  
ANISOU 1881  CA  GLY A1050     6255   5591  14483    163   1321    985       C  
ATOM   1882  C   GLY A1050     -75.639  16.594  38.439  1.00 62.36           C  
ANISOU 1882  C   GLY A1050     5458   4836  13398    216   1276   1155       C  
ATOM   1883  O   GLY A1050     -76.737  16.913  38.902  1.00 70.77           O  
ANISOU 1883  O   GLY A1050     6591   5922  14377    247   1263   1198       O  
ATOM   1884  N   GLN A1051     -75.512  15.686  37.469  1.00 58.43           N  
ANISOU 1884  N   GLN A1051     4949   4417  12834    229   1248   1243       N  
ATOM   1885  CA  GLN A1051     -76.685  14.970  36.977  1.00 59.15           C  
ANISOU 1885  CA  GLN A1051     5106   4626  12743    277   1178   1375       C  
ATOM   1886  C   GLN A1051     -77.278  14.072  38.057  1.00 59.99           C  
ANISOU 1886  C   GLN A1051     5269   4802  12721    272   1031   1268       C  
ATOM   1887  O   GLN A1051     -78.504  13.967  38.177  1.00 69.96           O  
ANISOU 1887  O   GLN A1051     6584   6120  13876    306   1005   1340       O  
ATOM   1888  CB  GLN A1051     -76.324  14.162  35.732  1.00 51.44           C  
ANISOU 1888  CB  GLN A1051     4107   3708  11729    298   1162   1475       C  
ATOM   1889  CG  GLN A1051     -76.144  15.008  34.482  1.00 62.23           C  
ANISOU 1889  CG  GLN A1051     5462   5022  13162    339   1329   1655       C  
ATOM   1890  CD  GLN A1051     -75.989  14.170  33.228  1.00 67.39           C  
ANISOU 1890  CD  GLN A1051     6121   5746  13738    391   1305   1779       C  
ATOM   1891  OE1 GLN A1051     -75.480  13.050  33.274  1.00 61.38           O  
ANISOU 1891  OE1 GLN A1051     5335   5038  12948    373   1184   1691       O  
ATOM   1892  NE2 GLN A1051     -76.438  14.708  32.098  1.00 54.02           N  
ANISOU 1892  NE2 GLN A1051     4477   4053  11995    473   1409   1981       N  
ATOM   1893  N   ILE A1052     -76.427  13.413  38.848  1.00 49.97           N  
ANISOU 1893  N   ILE A1052     3994   3524  11466    237    939   1094       N  
ATOM   1894  CA  ILE A1052     -76.920  12.607  39.962  1.00 44.49           C  
ANISOU 1894  CA  ILE A1052     3382   2878  10644    248    819    998       C  
ATOM   1895  C   ILE A1052     -77.625  13.491  40.983  1.00 47.93           C  
ANISOU 1895  C   ILE A1052     3870   3261  11080    268    871    974       C  
ATOM   1896  O   ILE A1052     -78.684  13.130  41.514  1.00 62.60           O  
ANISOU 1896  O   ILE A1052     5795   5166  12824    300    843   1009       O  
ATOM   1897  CB  ILE A1052     -75.768  11.808  40.600  1.00 61.85           C  
ANISOU 1897  CB  ILE A1052     5585   5063  12850    225    705    806       C  
ATOM   1898  CG1 ILE A1052     -75.237  10.760  39.619  1.00 69.54           C  
ANISOU 1898  CG1 ILE A1052     6520   6101  13801    216    629    829       C  
ATOM   1899  CG2 ILE A1052     -76.223  11.143  41.890  1.00 46.48           C  
ANISOU 1899  CG2 ILE A1052     3754   3142  10765    259    605    709       C  
ATOM   1900  CD1 ILE A1052     -74.058   9.970  40.149  1.00 61.24           C  
ANISOU 1900  CD1 ILE A1052     5468   5038  12764    202    504    625       C  
ATOM   1901  N   ASP A1053     -77.053  14.663  41.273  1.00 57.26           N  
ANISOU 1901  N   ASP A1053     5015   4336  12405    251    952    912       N  
ATOM   1902  CA  ASP A1053     -77.695  15.589  42.200  1.00 59.90           C  
ANISOU 1902  CA  ASP A1053     5400   4608  12750    277    996    886       C  
ATOM   1903  C   ASP A1053     -79.022  16.106  41.653  1.00 54.91           C  
ANISOU 1903  C   ASP A1053     4782   4007  12074    312   1073   1064       C  
ATOM   1904  O   ASP A1053     -79.932  16.410  42.433  1.00 65.32           O  
ANISOU 1904  O   ASP A1053     6158   5315  13343    348   1081   1064       O  
ATOM   1905  CB  ASP A1053     -76.755  16.754  42.519  1.00 68.94           C  
ANISOU 1905  CB  ASP A1053     6490   5622  14083    247   1055    773       C  
ATOM   1906  CG  ASP A1053     -75.525  16.320  43.303  1.00 65.89           C  
ANISOU 1906  CG  ASP A1053     6092   5196  13748    225    954    549       C  
ATOM   1907  OD1 ASP A1053     -75.242  15.104  43.354  1.00 65.28           O  
ANISOU 1907  OD1 ASP A1053     6045   5194  13566    229    850    499       O  
ATOM   1908  OD2 ASP A1053     -74.845  17.197  43.876  1.00 67.78           O  
ANISOU 1908  OD2 ASP A1053     6292   5327  14136    208    968    409       O  
ATOM   1909  N   ASP A1054     -79.151  16.221  40.327  1.00 61.60           N  
ANISOU 1909  N   ASP A1054     5581   4886  12938    314   1128   1213       N  
ATOM   1910  CA  ASP A1054     -80.440  16.584  39.743  1.00 57.52           C  
ANISOU 1910  CA  ASP A1054     5086   4405  12364    360   1172   1369       C  
ATOM   1911  C   ASP A1054     -81.489  15.516  40.021  1.00 53.89           C  
ANISOU 1911  C   ASP A1054     4662   4047  11767    382   1085   1390       C  
ATOM   1912  O   ASP A1054     -82.629  15.834  40.378  1.00 62.50           O  
ANISOU 1912  O   ASP A1054     5778   5141  12828    417   1107   1433       O  
ATOM   1913  CB  ASP A1054     -80.297  16.812  38.237  1.00 61.56           C  
ANISOU 1913  CB  ASP A1054     5566   4927  12897    378   1234   1519       C  
ATOM   1914  CG  ASP A1054     -79.569  18.099  37.909  1.00 83.44           C  
ANISOU 1914  CG  ASP A1054     8309   7576  15817    368   1364   1541       C  
ATOM   1915  OD1 ASP A1054     -79.089  18.766  38.850  1.00 94.44           O  
ANISOU 1915  OD1 ASP A1054     9690   8878  17315    336   1388   1418       O  
ATOM   1916  OD2 ASP A1054     -79.482  18.446  36.712  1.00 86.71           O  
ANISOU 1916  OD2 ASP A1054     8721   7978  16247    398   1446   1684       O  
ATOM   1917  N   ALA A1055     -81.124  14.242  39.857  1.00 45.32           N  
ANISOU 1917  N   ALA A1055     3572   3035  10612    362    989   1358       N  
ATOM   1918  CA  ALA A1055     -82.042  13.164  40.206  1.00 44.41           C  
ANISOU 1918  CA  ALA A1055     3485   2999  10391    375    910   1366       C  
ATOM   1919  C   ALA A1055     -82.315  13.141  41.704  1.00 44.37           C  
ANISOU 1919  C   ALA A1055     3541   2958  10359    386    913   1269       C  
ATOM   1920  O   ALA A1055     -83.448  12.889  42.131  1.00 73.97           O  
ANISOU 1920  O   ALA A1055     7307   6731  14068    413    925   1311       O  
ATOM   1921  CB  ALA A1055     -81.481  11.822  39.739  1.00 43.43           C  
ANISOU 1921  CB  ALA A1055     3352   2944  10206    351    798   1341       C  
ATOM   1922  N   LEU A1056     -81.286  13.396  42.518  1.00 44.56           N  
ANISOU 1922  N   LEU A1056     3600   2916  10413    375    904   1135       N  
ATOM   1923  CA  LEU A1056     -81.489  13.493  43.960  1.00 44.82           C  
ANISOU 1923  CA  LEU A1056     3720   2899  10408    413    907   1039       C  
ATOM   1924  C   LEU A1056     -82.446  14.624  44.309  1.00 48.86           C  
ANISOU 1924  C   LEU A1056     4239   3361  10964    450   1004   1091       C  
ATOM   1925  O   LEU A1056     -83.203  14.521  45.281  1.00 64.34           O  
ANISOU 1925  O   LEU A1056     6264   5310  12873    499   1026   1079       O  
ATOM   1926  CB  LEU A1056     -80.146  13.686  44.666  1.00 63.72           C  
ANISOU 1926  CB  LEU A1056     6150   5220  12841    407    861    865       C  
ATOM   1927  CG  LEU A1056     -80.164  13.787  46.192  1.00 78.71           C  
ANISOU 1927  CG  LEU A1056     8167   7057  14682    475    841    738       C  
ATOM   1928  CD1 LEU A1056     -80.708  12.510  46.814  1.00 76.12           C  
ANISOU 1928  CD1 LEU A1056     7932   6786  14204    523    796    751       C  
ATOM   1929  CD2 LEU A1056     -78.773  14.098  46.725  1.00 73.06           C  
ANISOU 1929  CD2 LEU A1056     7466   6265  14028    474    775    543       C  
ATOM   1930  N   LYS A1057     -82.429  15.707  43.530  1.00 66.97           N  
ANISOU 1930  N   LYS A1057     6475   5616  13355    436   1069   1155       N  
ATOM   1931  CA  LYS A1057     -83.407  16.771  43.722  1.00 73.60           C  
ANISOU 1931  CA  LYS A1057     7321   6409  14236    476   1149   1213       C  
ATOM   1932  C   LYS A1057     -84.819  16.275  43.432  1.00 75.82           C  
ANISOU 1932  C   LYS A1057     7584   6764  14460    504   1160   1330       C  
ATOM   1933  O   LYS A1057     -85.759  16.591  44.168  1.00 84.56           O  
ANISOU 1933  O   LYS A1057     8718   7846  15565    550   1206   1338       O  
ATOM   1934  CB  LYS A1057     -83.060  17.966  42.837  1.00 78.16           C  
ANISOU 1934  CB  LYS A1057     7849   6923  14926    461   1214   1269       C  
ATOM   1935  CG  LYS A1057     -83.312  19.321  43.475  1.00 83.08           C  
ANISOU 1935  CG  LYS A1057     8499   7435  15634    492   1277   1234       C  
ATOM   1936  CD  LYS A1057     -83.072  20.447  42.479  1.00102.11           C  
ANISOU 1936  CD  LYS A1057    10867   9776  18153    482   1351   1318       C  
ATOM   1937  CE  LYS A1057     -81.691  20.346  41.850  1.00102.52           C  
ANISOU 1937  CE  LYS A1057    10866   9805  18283    424   1359   1289       C  
ATOM   1938  NZ  LYS A1057     -81.466  21.401  40.825  1.00 95.34           N  
ANISOU 1938  NZ  LYS A1057     9926   8820  17479    424   1459   1395       N  
ATOM   1939  N   LEU A1058     -84.987  15.494  42.359  1.00 59.10           N  
ANISOU 1939  N   LEU A1058     5416   4729  12309    483   1116   1413       N  
ATOM   1940  CA  LEU A1058     -86.301  14.935  42.048  1.00 46.38           C  
ANISOU 1940  CA  LEU A1058     3771   3179  10673    504   1108   1504       C  
ATOM   1941  C   LEU A1058     -86.785  14.015  43.160  1.00 51.07           C  
ANISOU 1941  C   LEU A1058     4392   3790  11224    512   1102   1461       C  
ATOM   1942  O   LEU A1058     -87.969  14.029  43.518  1.00 82.70           O  
ANISOU 1942  O   LEU A1058     8375   7791  15255    543   1153   1509       O  
ATOM   1943  CB  LEU A1058     -86.258  14.175  40.723  1.00 45.85           C  
ANISOU 1943  CB  LEU A1058     3655   3187  10577    486   1035   1576       C  
ATOM   1944  CG  LEU A1058     -85.971  14.963  39.445  1.00 60.32           C  
ANISOU 1944  CG  LEU A1058     5475   5007  12436    505   1054   1658       C  
ATOM   1945  CD1 LEU A1058     -85.768  14.016  38.270  1.00 75.19           C  
ANISOU 1945  CD1 LEU A1058     7337   6966  14267    502    966   1709       C  
ATOM   1946  CD2 LEU A1058     -87.093  15.943  39.154  1.00 70.07           C  
ANISOU 1946  CD2 LEU A1058     6709   6206  13708    563   1110   1740       C  
ATOM   1947  N   ALA A1059     -85.883  13.204  43.713  1.00 45.30           N  
ANISOU 1947  N   ALA A1059     3711   3067  10432    492   1047   1373       N  
ATOM   1948  CA  ALA A1059     -86.261  12.277  44.774  1.00 46.10           C  
ANISOU 1948  CA  ALA A1059     3863   3172  10479    515   1050   1343       C  
ATOM   1949  C   ALA A1059     -86.658  13.018  46.045  1.00 53.94           C  
ANISOU 1949  C   ALA A1059     4930   4089  11476    579   1142   1304       C  
ATOM   1950  O   ALA A1059     -87.698  12.725  46.645  1.00 73.74           O  
ANISOU 1950  O   ALA A1059     7436   6590  13991    616   1213   1355       O  
ATOM   1951  CB  ALA A1059     -85.116  11.307  45.055  1.00 44.33           C  
ANISOU 1951  CB  ALA A1059     3702   2963  10176    496    957   1251       C  
ATOM   1952  N   ASN A1060     -85.835  13.979  46.476  1.00 48.75           N  
ANISOU 1952  N   ASN A1060     4331   3363  10828    597   1143   1211       N  
ATOM   1953  CA  ASN A1060     -86.140  14.713  47.701  1.00 62.20           C  
ANISOU 1953  CA  ASN A1060     6117   4987  12528    676   1210   1154       C  
ATOM   1954  C   ASN A1060     -87.436  15.504  47.576  1.00 75.08           C  
ANISOU 1954  C   ASN A1060     7692   6604  14231    706   1305   1249       C  
ATOM   1955  O   ASN A1060     -88.114  15.746  48.582  1.00 76.10           O  
ANISOU 1955  O   ASN A1060     7875   6690  14351    783   1379   1239       O  
ATOM   1956  CB  ASN A1060     -84.980  15.638  48.073  1.00 69.07           C  
ANISOU 1956  CB  ASN A1060     7042   5778  13425    687   1171   1018       C  
ATOM   1957  CG  ASN A1060     -83.968  14.965  48.985  1.00 65.48           C  
ANISOU 1957  CG  ASN A1060     6699   5300  12880    726   1092    875       C  
ATOM   1958  OD1 ASN A1060     -84.224  14.765  50.172  1.00 72.43           O  
ANISOU 1958  OD1 ASN A1060     7695   6147  13678    826   1110    821       O  
ATOM   1959  ND2 ASN A1060     -82.810  14.619  48.436  1.00 58.36           N  
ANISOU 1959  ND2 ASN A1060     5769   4413  11991    663   1005    811       N  
ATOM   1960  N   GLU A1061     -87.792  15.925  46.361  1.00103.31           N  
ANISOU 1960  N   GLU A1061    11169  10210  17875    662   1303   1337       N  
ATOM   1961  CA  GLU A1061     -89.097  16.542  46.149  1.00105.34           C  
ANISOU 1961  CA  GLU A1061    11369  10456  18198    696   1374   1426       C  
ATOM   1962  C   GLU A1061     -90.221  15.538  46.383  1.00104.87           C  
ANISOU 1962  C   GLU A1061    11259  10440  18145    707   1415   1497       C  
ATOM   1963  O   GLU A1061     -91.210  15.845  47.059  1.00110.13           O  
ANISOU 1963  O   GLU A1061    11920  11071  18854    765   1507   1523       O  
ATOM   1964  CB  GLU A1061     -89.178  17.134  44.743  1.00104.96           C  
ANISOU 1964  CB  GLU A1061    11251  10425  18202    667   1347   1503       C  
ATOM   1965  CG  GLU A1061     -88.331  18.383  44.554  1.00109.54           C  
ANISOU 1965  CG  GLU A1061    11866  10930  18824    667   1353   1460       C  
ATOM   1966  CD  GLU A1061     -88.323  18.869  43.120  1.00126.49           C  
ANISOU 1966  CD  GLU A1061    13966  13088  21006    653   1342   1555       C  
ATOM   1967  OE1 GLU A1061     -88.931  18.196  42.262  1.00127.66           O  
ANISOU 1967  OE1 GLU A1061    14064  13309  21130    651   1307   1638       O  
ATOM   1968  OE2 GLU A1061     -87.708  19.922  42.849  1.00134.48           O  
ANISOU 1968  OE2 GLU A1061    14996  14026  22074    652   1367   1546       O  
ATOM   1969  N   GLY A1062     -90.085  14.329  45.843  1.00 79.82           N  
ANISOU 1969  N   GLY A1062     8042   7336  14949    654   1354   1527       N  
ATOM   1970  CA  GLY A1062     -91.043  13.288  46.153  1.00 73.64           C  
ANISOU 1970  CA  GLY A1062     7204   6575  14201    654   1399   1586       C  
ATOM   1971  C   GLY A1062     -91.447  12.364  45.022  1.00 78.34           C  
ANISOU 1971  C   GLY A1062     7688   7233  14843    596   1322   1652       C  
ATOM   1972  O   GLY A1062     -91.831  11.219  45.281  1.00 83.28           O  
ANISOU 1972  O   GLY A1062     8274   7872  15496    576   1330   1678       O  
ATOM   1973  N   LYS A1063     -91.380  12.825  43.775  1.00 78.21           N  
ANISOU 1973  N   LYS A1063     7629   7245  14840    578   1247   1679       N  
ATOM   1974  CA  LYS A1063     -91.879  12.023  42.656  1.00 97.50           C  
ANISOU 1974  CA  LYS A1063     9981   9736  17326    544   1158   1732       C  
ATOM   1975  C   LYS A1063     -90.900  10.892  42.361  1.00 74.11           C  
ANISOU 1975  C   LYS A1063     7041   6828  14290    494   1055   1694       C  
ATOM   1976  O   LYS A1063     -89.868  11.090  41.716  1.00 72.63           O  
ANISOU 1976  O   LYS A1063     6898   6670  14029    482    987   1666       O  
ATOM   1977  CB  LYS A1063     -92.119  12.891  41.425  1.00 96.60           C  
ANISOU 1977  CB  LYS A1063     9851   9628  17223    573   1109   1776       C  
ATOM   1978  CG  LYS A1063     -91.119  14.009  41.192  1.00 80.58           C  
ANISOU 1978  CG  LYS A1063     7902   7582  15132    591   1122   1755       C  
ATOM   1979  CD  LYS A1063     -91.506  14.792  39.944  1.00101.89           C  
ANISOU 1979  CD  LYS A1063    10595  10278  17840    641   1088   1822       C  
ATOM   1980  CE  LYS A1063     -90.697  16.068  39.793  1.00107.41           C  
ANISOU 1980  CE  LYS A1063    11362  10929  18520    664   1138   1823       C  
ATOM   1981  NZ  LYS A1063     -91.123  16.851  38.599  1.00106.81           N  
ANISOU 1981  NZ  LYS A1063    11301  10838  18443    735   1119   1904       N  
ATOM   1982  N   VAL A1064     -91.232   9.691  42.842  1.00 86.17           N  
ANISOU 1982  N   VAL A1064     9966   8056  14720   -662   1874   2073       N  
ATOM   1983  CA  VAL A1064     -90.383   8.526  42.620  1.00 64.70           C  
ANISOU 1983  CA  VAL A1064     7479   5413  11692   -811   1691   1924       C  
ATOM   1984  C   VAL A1064     -90.444   8.082  41.164  1.00 62.00           C  
ANISOU 1984  C   VAL A1064     7074   5231  11254   -920   1524   2083       C  
ATOM   1985  O   VAL A1064     -89.423   7.721  40.568  1.00 68.08           O  
ANISOU 1985  O   VAL A1064     7944   6062  11861   -983   1426   2036       O  
ATOM   1986  CB  VAL A1064     -90.788   7.387  43.572  1.00 66.14           C  
ANISOU 1986  CB  VAL A1064     7809   5546  11773   -922   1670   1742       C  
ATOM   1987  CG1 VAL A1064     -89.794   6.240  43.484  1.00 61.31           C  
ANISOU 1987  CG1 VAL A1064     7409   4970  10916  -1038   1514   1590       C  
ATOM   1988  CG2 VAL A1064     -90.903   7.903  44.995  1.00 76.31           C  
ANISOU 1988  CG2 VAL A1064     9123   6717  13155   -852   1862   1625       C  
ATOM   1989  N   LYS A1065     -91.641   8.093  40.570  1.00 76.49           N  
ANISOU 1989  N   LYS A1065     8629   7107  13327   -926   1553   2331       N  
ATOM   1990  CA  LYS A1065     -91.809   7.597  39.208  1.00 75.94           C  
ANISOU 1990  CA  LYS A1065     8343   7208  13300  -1053   1451   2563       C  
ATOM   1991  C   LYS A1065     -91.007   8.399  38.192  1.00 79.73           C  
ANISOU 1991  C   LYS A1065     8676   7822  13796   -981   1420   2812       C  
ATOM   1992  O   LYS A1065     -90.727   7.891  37.101  1.00 86.66           O  
ANISOU 1992  O   LYS A1065     9422   8906  14598  -1141   1316   2951       O  
ATOM   1993  CB  LYS A1065     -93.291   7.607  38.826  1.00 94.68           C  
ANISOU 1993  CB  LYS A1065    10382   9670  15923  -1076   1471   2848       C  
ATOM   1994  CG  LYS A1065     -94.179   6.764  39.732  1.00 89.49           C  
ANISOU 1994  CG  LYS A1065     9838   8897  15267  -1167   1503   2627       C  
ATOM   1995  CD  LYS A1065     -93.843   5.286  39.621  1.00 87.13           C  
ANISOU 1995  CD  LYS A1065     9712   8618  14774  -1412   1398   2362       C  
ATOM   1996  CE  LYS A1065     -94.073   4.770  38.210  1.00 89.23           C  
ANISOU 1996  CE  LYS A1065     9665   9149  15090  -1640   1303   2547       C  
ATOM   1997  NZ  LYS A1065     -93.743   3.323  38.087  1.00103.03           N  
ANISOU 1997  NZ  LYS A1065    11534  10887  16726  -1902   1234   2217       N  
ATOM   1998  N   GLU A1066     -90.631   9.634  38.523  1.00113.90           N  
ANISOU 1998  N   GLU A1066    12989  12063  18223   -771   1519   2868       N  
ATOM   1999  CA  GLU A1066     -89.868  10.472  37.607  1.00120.28           C  
ANISOU 1999  CA  GLU A1066    13646  12990  19066   -682   1500   3122       C  
ATOM   2000  C   GLU A1066     -88.362  10.296  37.757  1.00112.06           C  
ANISOU 2000  C   GLU A1066    12915  11909  17756   -726   1459   2837       C  
ATOM   2001  O   GLU A1066     -87.629  10.427  36.770  1.00112.56           O  
ANISOU 2001  O   GLU A1066    12893  12124  17752   -756   1391   3009       O  
ATOM   2002  CB  GLU A1066     -90.238  11.944  37.816  1.00121.34           C  
ANISOU 2002  CB  GLU A1066    13547  13033  19524   -433   1653   3342       C  
ATOM   2003  CG  GLU A1066     -89.621  12.888  36.801  1.00139.95           C  
ANISOU 2003  CG  GLU A1066    15667  15529  21977   -318   1635   3693       C  
ATOM   2004  CD  GLU A1066     -90.036  12.562  35.381  1.00173.15           C  
ANISOU 2004  CD  GLU A1066    19537  20100  26152   -407   1467   4178       C  
ATOM   2005  OE1 GLU A1066     -91.231  12.273  35.159  1.00153.51           O  
ANISOU 2005  OE1 GLU A1066    16806  17738  23781   -443   1426   4420       O  
ATOM   2006  OE2 GLU A1066     -89.164  12.587  34.487  1.00204.89           O  
ANISOU 2006  OE2 GLU A1066    23514  24339  29994   -465   1367   4329       O  
ATOM   2007  N   ALA A1067     -87.884   9.990  38.966  1.00 88.08           N  
ANISOU 2007  N   ALA A1067    10205   8716  14545   -742   1483   2443       N  
ATOM   2008  CA  ALA A1067     -86.447   9.877  39.190  1.00 82.89           C  
ANISOU 2008  CA  ALA A1067     9811   8044  13637   -772   1427   2208       C  
ATOM   2009  C   ALA A1067     -85.858   8.636  38.529  1.00 75.18           C  
ANISOU 2009  C   ALA A1067     8947   7144  12475   -949   1294   2121       C  
ATOM   2010  O   ALA A1067     -84.680   8.637  38.155  1.00 77.35           O  
ANISOU 2010  O   ALA A1067     9323   7451  12614   -969   1246   2060       O  
ATOM   2011  CB  ALA A1067     -86.151   9.867  40.690  1.00 52.35           C  
ANISOU 2011  CB  ALA A1067     6082   4009   9799   -709   1538   1954       C  
ATOM   2012  N   GLN A1068     -86.653   7.575  38.378  1.00 65.89           N  
ANISOU 2012  N   GLN A1068     7729   5983  11323  -1090   1250   2101       N  
ATOM   2013  CA  GLN A1068     -86.120   6.312  37.876  1.00 56.68           C  
ANISOU 2013  CA  GLN A1068     6646   4845  10046  -1286   1159   1949       C  
ATOM   2014  C   GLN A1068     -85.752   6.403  36.399  1.00 65.61           C  
ANISOU 2014  C   GLN A1068     7528   6176  11225  -1404   1133   2183       C  
ATOM   2015  O   GLN A1068     -84.735   5.841  35.974  1.00 82.07           O  
ANISOU 2015  O   GLN A1068     9698   8278  13208  -1520   1089   2036       O  
ATOM   2016  CB  GLN A1068     -87.131   5.193  38.118  1.00 70.72           C  
ANISOU 2016  CB  GLN A1068     8398   6584  11887  -1430   1140   1845       C  
ATOM   2017  CG  GLN A1068     -87.622   5.136  39.556  1.00 65.43           C  
ANISOU 2017  CG  GLN A1068     7916   5786  11158  -1332   1165   1692       C  
ATOM   2018  CD  GLN A1068     -88.635   4.034  39.799  1.00 59.60           C  
ANISOU 2018  CD  GLN A1068     7148   5007  10491  -1466   1151   1609       C  
ATOM   2019  OE1 GLN A1068     -89.175   3.448  38.860  1.00 80.77           O  
ANISOU 2019  OE1 GLN A1068     9617   7761  13310  -1639   1138   1670       O  
ATOM   2020  NE2 GLN A1068     -88.897   3.744  41.068  1.00 48.83           N  
ANISOU 2020  NE2 GLN A1068     5960   3559   9033  -1419   1151   1474       N  
ATOM   2021  N   ALA A1069     -86.569   7.093  35.600  1.00 53.73           N  
ANISOU 2021  N   ALA A1069     5670   4883   9861  -1391   1147   2580       N  
ATOM   2022  CA  ALA A1069     -86.231   7.282  34.193  1.00 72.89           C  
ANISOU 2022  CA  ALA A1069     7780   7676  12239  -1524   1087   2897       C  
ATOM   2023  C   ALA A1069     -84.972   8.124  34.040  1.00 76.25           C  
ANISOU 2023  C   ALA A1069     8326   8070  12577  -1374   1105   2936       C  
ATOM   2024  O   ALA A1069     -84.153   7.878  33.147  1.00 71.33           O  
ANISOU 2024  O   ALA A1069     7606   7677  11818  -1530   1056   2988       O  
ATOM   2025  CB  ALA A1069     -87.402   7.925  33.451  1.00 68.23           C  
ANISOU 2025  CB  ALA A1069     6743   7435  11745  -1504   1053   3398       C  
ATOM   2026  N   ALA A1070     -84.805   9.130  34.902  1.00 73.07           N  
ANISOU 2026  N   ALA A1070     8087   7431  12243  -1108   1181   2883       N  
ATOM   2027  CA  ALA A1070     -83.595   9.944  34.871  1.00 76.06           C  
ANISOU 2027  CA  ALA A1070     8578   7769  12554   -984   1207   2857       C  
ATOM   2028  C   ALA A1070     -82.361   9.106  35.177  1.00 64.73           C  
ANISOU 2028  C   ALA A1070     7462   6223  10909  -1094   1165   2478       C  
ATOM   2029  O   ALA A1070     -81.334   9.230  34.500  1.00 82.28           O  
ANISOU 2029  O   ALA A1070     9678   8544  13041  -1135   1145   2526       O  
ATOM   2030  CB  ALA A1070     -83.720  11.104  35.855  1.00 71.40           C  
ANISOU 2030  CB  ALA A1070     8050   6981  12098   -754   1315   2793       C  
ATOM   2031  N   ALA A1071     -82.446   8.236  36.187  1.00 53.36           N  
ANISOU 2031  N   ALA A1071     6277   4607   9391  -1137   1141   2133       N  
ATOM   2032  CA  ALA A1071     -81.305   7.397  36.539  1.00 55.90           C  
ANISOU 2032  CA  ALA A1071     6862   4842   9536  -1209   1075   1819       C  
ATOM   2033  C   ALA A1071     -80.953   6.428  35.420  1.00 68.10           C  
ANISOU 2033  C   ALA A1071     8286   6481  11107  -1435   1044   1813       C  
ATOM   2034  O   ALA A1071     -79.788   6.040  35.280  1.00 92.52           O  
ANISOU 2034  O   ALA A1071    11504   9535  14114  -1481   1012   1641       O  
ATOM   2035  CB  ALA A1071     -81.588   6.633  37.832  1.00 57.92           C  
ANISOU 2035  CB  ALA A1071     7339   4969   9701  -1201   1025   1553       C  
ATOM   2036  N   GLU A1072     -81.943   6.017  34.624  1.00 67.42           N  
ANISOU 2036  N   GLU A1072     7908   6561  11149  -1617   1050   1979       N  
ATOM   2037  CA  GLU A1072     -81.657   5.170  33.471  1.00 81.28           C  
ANISOU 2037  CA  GLU A1072     9409   8543  12929  -1935   1023   1937       C  
ATOM   2038  C   GLU A1072     -80.791   5.904  32.455  1.00 86.33           C  
ANISOU 2038  C   GLU A1072     9857   9487  13458  -1972   1022   2197       C  
ATOM   2039  O   GLU A1072     -79.844   5.330  31.905  1.00 84.92           O  
ANISOU 2039  O   GLU A1072     9629   9396  13240  -2162   1010   2002       O  
ATOM   2040  CB  GLU A1072     -82.962   4.705  32.825  1.00 89.45           C  
ANISOU 2040  CB  GLU A1072    10051   9888  14048  -2178    991   2068       C  
ATOM   2041  CG  GLU A1072     -82.797   3.577  31.819  1.00108.87           C  
ANISOU 2041  CG  GLU A1072    12272  12756  16340  -2493    891   1690       C  
ATOM   2042  CD  GLU A1072     -83.047   2.210  32.429  1.00128.53           C  
ANISOU 2042  CD  GLU A1072    14909  14886  19039  -2626    917   1196       C  
ATOM   2043  OE1 GLU A1072     -83.642   2.147  33.526  1.00131.46           O  
ANISOU 2043  OE1 GLU A1072    15510  14851  19588  -2485    969   1249       O  
ATOM   2044  OE2 GLU A1072     -82.653   1.199  31.811  1.00128.25           O  
ANISOU 2044  OE2 GLU A1072    14798  15046  18884  -2814    868    704       O  
ATOM   2045  N   GLN A1073     -81.106   7.174  32.189  1.00 86.06           N  
ANISOU 2045  N   GLN A1073     9686   9632  13382  -1782   1030   2622       N  
ATOM   2046  CA  GLN A1073     -80.267   7.972  31.301  1.00 81.93           C  
ANISOU 2046  CA  GLN A1073     9005   9414  12712  -1760   1019   2903       C  
ATOM   2047  C   GLN A1073     -78.885   8.193  31.901  1.00 87.02           C  
ANISOU 2047  C   GLN A1073    10023   9703  13338  -1613   1068   2626       C  
ATOM   2048  O   GLN A1073     -77.875   8.136  31.190  1.00104.05           O  
ANISOU 2048  O   GLN A1073    12108  12048  15376  -1730   1064   2641       O  
ATOM   2049  CB  GLN A1073     -80.943   9.310  31.000  1.00 80.76           C  
ANISOU 2049  CB  GLN A1073     8637   9451  12597  -1528   1012   3390       C  
ATOM   2050  CG  GLN A1073     -82.211   9.196  30.171  1.00100.25           C  
ANISOU 2050  CG  GLN A1073    10651  12448  14991  -1672    920   3762       C  
ATOM   2051  CD  GLN A1073     -82.880  10.538  29.954  1.00126.95           C  
ANISOU 2051  CD  GLN A1073    13807  15932  18497  -1391    907   4262       C  
ATOM   2052  OE1 GLN A1073     -82.677  11.476  30.725  1.00141.30           O  
ANISOU 2052  OE1 GLN A1073    15822  17305  20560  -1095   1005   4214       O  
ATOM   2053  NE2 GLN A1073     -83.679  10.639  28.898  1.00136.36           N  
ANISOU 2053  NE2 GLN A1073    14528  17775  19507  -1501    779   4709       N  
ATOM   2054  N   LEU A1074     -78.818   8.449  33.211  1.00 79.79           N  
ANISOU 2054  N   LEU A1074     9454   8389  12473  -1388   1094   2367       N  
ATOM   2055  CA  LEU A1074     -77.522   8.630  33.855  1.00 79.32           C  
ANISOU 2055  CA  LEU A1074     9694   8133  12311  -1283   1091   2099       C  
ATOM   2056  C   LEU A1074     -76.714   7.340  33.855  1.00 79.20           C  
ANISOU 2056  C   LEU A1074     9819   8026  12247  -1449   1048   1779       C  
ATOM   2057  O   LEU A1074     -75.481   7.384  33.911  1.00 92.09           O  
ANISOU 2057  O   LEU A1074    11589   9604  13796  -1420   1033   1646       O  
ATOM   2058  CB  LEU A1074     -77.703   9.141  35.285  1.00 76.89           C  
ANISOU 2058  CB  LEU A1074     9608   7629  11978  -1092   1089   1911       C  
ATOM   2059  CG  LEU A1074     -78.565  10.393  35.471  1.00 85.01           C  
ANISOU 2059  CG  LEU A1074    10477   8671  13152   -932   1166   2136       C  
ATOM   2060  CD1 LEU A1074     -78.399  10.954  36.875  1.00 71.42           C  
ANISOU 2060  CD1 LEU A1074     8903   6791  11443   -802   1211   1923       C  
ATOM   2061  CD2 LEU A1074     -78.255  11.448  34.418  1.00 82.76           C  
ANISOU 2061  CD2 LEU A1074     9951   8541  12952   -864   1213   2483       C  
ATOM   2062  N   LYS A1075     -77.388   6.189  33.793  1.00 77.40           N  
ANISOU 2062  N   LYS A1075     9530   7769  12108  -1620   1027   1633       N  
ATOM   2063  CA  LYS A1075     -76.681   4.915  33.697  1.00 86.45           C  
ANISOU 2063  CA  LYS A1075    10744   8808  13297  -1777    995   1279       C  
ATOM   2064  C   LYS A1075     -75.869   4.834  32.410  1.00 77.84           C  
ANISOU 2064  C   LYS A1075     9397   7933  12243  -2012   1052   1284       C  
ATOM   2065  O   LYS A1075     -74.721   4.372  32.417  1.00 73.24           O  
ANISOU 2065  O   LYS A1075     8940   7229  11659  -2022   1052   1005       O  
ATOM   2066  CB  LYS A1075     -77.676   3.758  33.778  1.00 98.32           C  
ANISOU 2066  CB  LYS A1075    12164  10259  14935  -1933    975   1082       C  
ATOM   2067  CG  LYS A1075     -77.049   2.384  33.598  1.00 83.79           C  
ANISOU 2067  CG  LYS A1075    10339   8307  13189  -2075    951    640       C  
ATOM   2068  CD  LYS A1075     -78.082   1.280  33.745  1.00 72.06           C  
ANISOU 2068  CD  LYS A1075     8776   6770  11833  -2195    931    419       C  
ATOM   2069  CE  LYS A1075     -77.438  -0.092  33.641  1.00 73.30           C  
ANISOU 2069  CE  LYS A1075     8956   6808  12086  -2253    911    -41       C  
ATOM   2070  NZ  LYS A1075     -78.438  -1.183  33.798  1.00 88.30           N  
ANISOU 2070  NZ  LYS A1075    10779   8654  14116  -2342    901   -254       N  
ATOM   2071  N   THR A1076     -76.452   5.272  31.291  1.00 90.18           N  
ANISOU 2071  N   THR A1076    10602  10032  13630  -2128   1017   1533       N  
ATOM   2072  CA  THR A1076     -75.706   5.319  30.038  1.00 83.00           C  
ANISOU 2072  CA  THR A1076     9489   9693  12354  -2226    945   1432       C  
ATOM   2073  C   THR A1076     -74.527   6.277  30.144  1.00 88.32           C  
ANISOU 2073  C   THR A1076    10301  10218  13038  -2077   1013   1660       C  
ATOM   2074  O   THR A1076     -73.428   5.982  29.658  1.00 99.20           O  
ANISOU 2074  O   THR A1076    11699  11737  14254  -2129    998   1387       O  
ATOM   2075  CB  THR A1076     -76.625   5.733  28.890  1.00 91.91           C  
ANISOU 2075  CB  THR A1076    10202  11565  13155  -2333    845   1726       C  
ATOM   2076  OG1 THR A1076     -76.714   7.162  28.840  1.00 96.60           O  
ANISOU 2076  OG1 THR A1076    10706  12206  13789  -2163    890   2377       O  
ATOM   2077  CG2 THR A1076     -78.018   5.156  29.093  1.00108.90           C  
ANISOU 2077  CG2 THR A1076    12236  13749  15393  -2424    805   1672       C  
ATOM   2078  N   THR A1077     -74.743   7.435  30.769  1.00 79.56           N  
ANISOU 2078  N   THR A1077     9266   8816  12146  -1903   1111   2136       N  
ATOM   2079  CA  THR A1077     -73.652   8.374  31.004  1.00 75.84           C  
ANISOU 2079  CA  THR A1077     8996   8212  11607  -1693   1144   2184       C  
ATOM   2080  C   THR A1077     -72.602   7.774  31.930  1.00 69.84           C  
ANISOU 2080  C   THR A1077     8596   7064  10875  -1622   1125   1738       C  
ATOM   2081  O   THR A1077     -71.398   7.974  31.729  1.00 84.09           O  
ANISOU 2081  O   THR A1077    10462   8863  12626  -1613   1147   1677       O  
ATOM   2082  CB  THR A1077     -74.207   9.676  31.583  1.00 75.10           C  
ANISOU 2082  CB  THR A1077     8978   8020  11537  -1398   1146   2390       C  
ATOM   2083  OG1 THR A1077     -75.194  10.213  30.693  1.00 72.29           O  
ANISOU 2083  OG1 THR A1077     8258   8040  11169  -1418   1133   2840       O  
ATOM   2084  CG2 THR A1077     -73.101  10.698  31.770  1.00 86.71           C  
ANISOU 2084  CG2 THR A1077    10576   9407  12964  -1233   1173   2386       C  
ATOM   2085  N   ILE A1078     -73.040   7.029  32.948  1.00 68.24           N  
ANISOU 2085  N   ILE A1078     8599   6617  10712  -1559   1055   1464       N  
ATOM   2086  CA  ILE A1078     -72.109   6.436  33.905  1.00 62.26           C  
ANISOU 2086  CA  ILE A1078     8107   5655   9894  -1453    962   1145       C  
ATOM   2087  C   ILE A1078     -71.194   5.433  33.214  1.00 63.06           C  
ANISOU 2087  C   ILE A1078     8145   5721  10096  -1618    991    893       C  
ATOM   2088  O   ILE A1078     -69.976   5.432  33.426  1.00 77.86           O  
ANISOU 2088  O   ILE A1078    10131   7533  11917  -1537    961    774       O  
ATOM   2089  CB  ILE A1078     -72.883   5.791  35.068  1.00 76.64           C  
ANISOU 2089  CB  ILE A1078    10067   7362  11689  -1368    865   1005       C  
ATOM   2090  CG1 ILE A1078     -73.253   6.849  36.109  1.00 78.65           C  
ANISOU 2090  CG1 ILE A1078    10423   7642  11818  -1200    836   1107       C  
ATOM   2091  CG2 ILE A1078     -72.081   4.661  35.696  1.00 66.20           C  
ANISOU 2091  CG2 ILE A1078     8877   5927  10348  -1337    765    743       C  
ATOM   2092  CD1 ILE A1078     -74.188   6.345  37.175  1.00 70.85           C  
ANISOU 2092  CD1 ILE A1078     9499   6595  10827  -1160    790   1034       C  
ATOM   2093  N   ASN A1079     -71.765   4.563  32.375  1.00 70.22           N  
ANISOU 2093  N   ASN A1079     8824   6698  11157  -1882   1061    737       N  
ATOM   2094  CA  ASN A1079     -70.947   3.587  31.660  1.00 75.93           C  
ANISOU 2094  CA  ASN A1079     9442   7470  11937  -2071   1104    301       C  
ATOM   2095  C   ASN A1079     -69.951   4.273  30.734  1.00 74.08           C  
ANISOU 2095  C   ASN A1079     9103   7627  11416  -2069   1099    352       C  
ATOM   2096  O   ASN A1079     -68.796   3.844  30.622  1.00 73.47           O  
ANISOU 2096  O   ASN A1079     9083   7472  11361  -2073   1118     62       O  
ATOM   2097  CB  ASN A1079     -71.838   2.625  30.874  1.00 81.31           C  
ANISOU 2097  CB  ASN A1079     9877   8499  12519  -2267   1051    -23       C  
ATOM   2098  CG  ASN A1079     -72.365   1.488  31.726  1.00 91.03           C  
ANISOU 2098  CG  ASN A1079    11221   9279  14089  -2282   1066   -266       C  
ATOM   2099  OD1 ASN A1079     -71.672   0.987  32.611  1.00 96.31           O  
ANISOU 2099  OD1 ASN A1079    12127   9696  14770  -2018    977   -316       O  
ATOM   2100  ND2 ASN A1079     -73.598   1.070  31.460  1.00 90.71           N  
ANISOU 2100  ND2 ASN A1079    11008   9410  14048  -2424   1047   -336       N  
ATOM   2101  N   ALA A1080     -70.383   5.337  30.054  1.00 75.20           N  
ANISOU 2101  N   ALA A1080     9064   8196  11313  -2062   1080    750       N  
ATOM   2102  CA  ALA A1080     -69.482   6.066  29.168  1.00 80.70           C  
ANISOU 2102  CA  ALA A1080     9637   9289  11736  -2065   1082    878       C  
ATOM   2103  C   ALA A1080     -68.349   6.725  29.945  1.00 74.68           C  
ANISOU 2103  C   ALA A1080     9132   8080  11163  -1905   1168   1006       C  
ATOM   2104  O   ALA A1080     -67.192   6.697  29.512  1.00 90.24           O  
ANISOU 2104  O   ALA A1080    11101  10171  13016  -1921   1178    833       O  
ATOM   2105  CB  ALA A1080     -70.262   7.108  28.369  1.00 94.19           C  
ANISOU 2105  CB  ALA A1080    11067  11516  13204  -2075   1050   1393       C  
ATOM   2106  N   TYR A1081     -68.658   7.327  31.095  1.00 60.62           N  
ANISOU 2106  N   TYR A1081     7559   5823   9652  -1763   1231   1271       N  
ATOM   2107  CA  TYR A1081     -67.636   8.067  31.829  1.00 56.43           C  
ANISOU 2107  CA  TYR A1081     7264   5155   9020  -1533   1165   1260       C  
ATOM   2108  C   TYR A1081     -66.639   7.143  32.517  1.00 61.19           C  
ANISOU 2108  C   TYR A1081     8048   5547   9654  -1473   1081    885       C  
ATOM   2109  O   TYR A1081     -65.455   7.481  32.615  1.00 82.21           O  
ANISOU 2109  O   TYR A1081    10775   8192  12267  -1407   1078    840       O  
ATOM   2110  CB  TYR A1081     -68.292   9.004  32.841  1.00 59.96           C  
ANISOU 2110  CB  TYR A1081     7844   5549   9387  -1311   1080   1380       C  
ATOM   2111  CG  TYR A1081     -68.635  10.355  32.258  1.00 64.78           C  
ANISOU 2111  CG  TYR A1081     8303   6334   9977  -1254   1157   1731       C  
ATOM   2112  CD1 TYR A1081     -69.610  10.483  31.280  1.00 70.11           C  
ANISOU 2112  CD1 TYR A1081     8706   7257  10674  -1346   1213   2053       C  
ATOM   2113  CD2 TYR A1081     -67.978  11.500  32.679  1.00 74.33           C  
ANISOU 2113  CD2 TYR A1081     9581   7506  11156  -1109   1161   1753       C  
ATOM   2114  CE1 TYR A1081     -69.923  11.717  30.740  1.00 81.16           C  
ANISOU 2114  CE1 TYR A1081     9921   8852  12066  -1240   1247   2417       C  
ATOM   2115  CE2 TYR A1081     -68.284  12.737  32.148  1.00 91.05           C  
ANISOU 2115  CE2 TYR A1081    11529   9742  13324  -1028   1235   2055       C  
ATOM   2116  CZ  TYR A1081     -69.258  12.840  31.180  1.00 95.33           C  
ANISOU 2116  CZ  TYR A1081    11812  10514  13896  -1069   1269   2400       C  
ATOM   2117  OH  TYR A1081     -69.566  14.071  30.647  1.00 99.32           O  
ANISOU 2117  OH  TYR A1081    12101  11156  14480   -950   1312   2747       O  
ATOM   2118  N   ILE A1082     -67.087   5.984  33.000  1.00 55.98           N  
ANISOU 2118  N   ILE A1082     7439   4761   9070  -1476   1005    647       N  
ATOM   2119  CA  ILE A1082     -66.164   5.060  33.651  1.00 54.71           C  
ANISOU 2119  CA  ILE A1082     7389   4471   8926  -1380    910    382       C  
ATOM   2120  C   ILE A1082     -65.215   4.444  32.632  1.00 77.41           C  
ANISOU 2120  C   ILE A1082    10145   7336  11931  -1537   1028    100       C  
ATOM   2121  O   ILE A1082     -64.018   4.280  32.900  1.00 84.25           O  
ANISOU 2121  O   ILE A1082    11074   8150  12788  -1441    994     -5       O  
ATOM   2122  CB  ILE A1082     -66.944   3.990  34.430  1.00 65.62           C  
ANISOU 2122  CB  ILE A1082     8825   5764  10344  -1330    806    271       C  
ATOM   2123  CG1 ILE A1082     -67.684   4.647  35.590  1.00 68.35           C  
ANISOU 2123  CG1 ILE A1082     9291   6158  10519  -1206    701    475       C  
ATOM   2124  CG2 ILE A1082     -66.010   2.909  34.949  1.00 66.19           C  
ANISOU 2124  CG2 ILE A1082     8946   5738  10463  -1250    735     76       C  
ATOM   2125  CD1 ILE A1082     -68.554   3.705  36.342  1.00 65.66           C  
ANISOU 2125  CD1 ILE A1082     8995   5759  10194  -1188    626    419       C  
ATOM   2126  N   GLN A1083     -65.725   4.095  31.448  1.00 96.15           N  
ANISOU 2126  N   GLN A1083    12299   9838  14397  -1836   1176    -83       N  
ATOM   2127  CA  GLN A1083     -64.843   3.640  30.381  1.00 98.66           C  
ANISOU 2127  CA  GLN A1083    12445  10449  14593  -1963   1210   -448       C  
ATOM   2128  C   GLN A1083     -63.904   4.745  29.917  1.00 85.00           C  
ANISOU 2128  C   GLN A1083    10698   8965  12631  -1914   1234   -225       C  
ATOM   2129  O   GLN A1083     -62.900   4.453  29.260  1.00 94.81           O  
ANISOU 2129  O   GLN A1083    11848  10404  13773  -1964   1257   -507       O  
ATOM   2130  CB  GLN A1083     -65.661   3.099  29.203  1.00 96.59           C  
ANISOU 2130  CB  GLN A1083    11893  10721  14085  -2160   1181   -707       C  
ATOM   2131  CG  GLN A1083     -66.054   4.134  28.155  1.00 98.06           C  
ANISOU 2131  CG  GLN A1083    11863  11565  13830  -2230   1143   -390       C  
ATOM   2132  CD  GLN A1083     -65.047   4.245  27.023  1.00109.09           C  
ANISOU 2132  CD  GLN A1083    13073  13471  14907  -2332   1163   -588       C  
ATOM   2133  OE1 GLN A1083     -64.325   3.294  26.722  1.00124.90           O  
ANISOU 2133  OE1 GLN A1083    15022  15459  16975  -2419   1210  -1116       O  
ATOM   2134  NE2 GLN A1083     -64.991   5.414  26.393  1.00115.61           N  
ANISOU 2134  NE2 GLN A1083    13773  14735  15418  -2323   1145   -153       N  
ATOM   2135  N   LYS A1084     -64.208   6.003  30.243  1.00 65.54           N  
ANISOU 2135  N   LYS A1084     8304   6475  10122  -1823   1253    262       N  
ATOM   2136  CA  LYS A1084     -63.293   7.108  29.992  1.00 73.71           C  
ANISOU 2136  CA  LYS A1084     9344   7626  11037  -1764   1305    510       C  
ATOM   2137  C   LYS A1084     -62.350   7.357  31.160  1.00 70.86           C  
ANISOU 2137  C   LYS A1084     9236   6811  10876  -1609   1313    523       C  
ATOM   2138  O   LYS A1084     -61.210   7.784  30.943  1.00 90.97           O  
ANISOU 2138  O   LYS A1084    11791   9388  13388  -1603   1370    516       O  
ATOM   2139  CB  LYS A1084     -64.078   8.388  29.684  1.00 72.01           C  
ANISOU 2139  CB  LYS A1084     9017   7628  10715  -1734   1334   1039       C  
ATOM   2140  CG  LYS A1084     -64.815   8.364  28.352  1.00 86.86           C  
ANISOU 2140  CG  LYS A1084    10572  10182  12248  -1866   1267   1121       C  
ATOM   2141  CD  LYS A1084     -65.696   9.593  28.183  1.00111.19           C  
ANISOU 2141  CD  LYS A1084    13516  13409  15322  -1805   1297   1734       C  
ATOM   2142  CE  LYS A1084     -66.480   9.538  26.880  1.00122.53           C  
ANISOU 2142  CE  LYS A1084    14583  15597  16375  -1950   1204   1875       C  
ATOM   2143  NZ  LYS A1084     -67.328  10.748  26.683  1.00114.42           N  
ANISOU 2143  NZ  LYS A1084    13368  14715  15392  -1871   1233   2557       N  
ATOM   2144  N   TYR A1085     -62.798   7.111  32.395  1.00 67.91           N  
ANISOU 2144  N   TYR A1085     9022   6298  10483  -1400   1121    513       N  
ATOM   2145  CA  TYR A1085     -61.926   7.282  33.554  1.00 67.67           C  
ANISOU 2145  CA  TYR A1085     9137   6211  10365  -1209    976    480       C  
ATOM   2146  C   TYR A1085     -60.922   6.142  33.660  1.00 69.58           C  
ANISOU 2146  C   TYR A1085     9386   6353  10699  -1198    948    207       C  
ATOM   2147  O   TYR A1085     -59.722   6.376  33.843  1.00 79.87           O  
ANISOU 2147  O   TYR A1085    10714   7654  11979  -1148    942    175       O  
ATOM   2148  CB  TYR A1085     -62.752   7.368  34.839  1.00 82.05           C  
ANISOU 2148  CB  TYR A1085    11057   8034  12082  -1092    818    551       C  
ATOM   2149  CG  TYR A1085     -63.695   8.544  34.913  1.00 85.63           C  
ANISOU 2149  CG  TYR A1085    11497   8571  12466  -1072    843    763       C  
ATOM   2150  CD1 TYR A1085     -63.568   9.624  34.050  1.00 85.94           C  
ANISOU 2150  CD1 TYR A1085    11450   8691  12510  -1105    967    949       C  
ATOM   2151  CD2 TYR A1085     -64.711   8.574  35.858  1.00 65.45           C  
ANISOU 2151  CD2 TYR A1085     8989   6013   9867  -1017    771    785       C  
ATOM   2152  CE1 TYR A1085     -64.430  10.696  34.122  1.00 85.92           C  
ANISOU 2152  CE1 TYR A1085    11409   8751  12486  -1059   1000   1139       C  
ATOM   2153  CE2 TYR A1085     -65.577   9.641  35.939  1.00 66.97           C  
ANISOU 2153  CE2 TYR A1085     9131   6238  10077   -978    856    937       C  
ATOM   2154  CZ  TYR A1085     -65.432  10.699  35.069  1.00 78.45           C  
ANISOU 2154  CZ  TYR A1085    10516   7774  11517  -1000    927   1106       C  
ATOM   2155  OH  TYR A1085     -66.293  11.764  35.146  1.00 84.96           O  
ANISOU 2155  OH  TYR A1085    11256   8608  12418   -931   1025   1266       O  
ATOM   2156  N   GLY A1086     -61.397   4.900  33.544  1.00 69.39           N  
ANISOU 2156  N   GLY A1086     9318   6248  10799  -1240    936      5       N  
ATOM   2157  CA  GLY A1086     -60.508   3.756  33.566  1.00 80.80           C  
ANISOU 2157  CA  GLY A1086    10723   7600  12376  -1212    924   -255       C  
ATOM   2158  C   GLY A1086     -59.553   3.704  32.394  1.00 86.50           C  
ANISOU 2158  C   GLY A1086    11316   8350  13201  -1351   1086   -517       C  
ATOM   2159  O   GLY A1086     -58.500   3.064  32.497  1.00 81.72           O  
ANISOU 2159  O   GLY A1086    10676   7681  12693  -1284   1076   -688       O  
ATOM   2160  N   GLN A 313     -59.904   4.353  31.278  1.00 81.33           N  
ANISOU 2160  N   GLN A 313    10558   7834  12510  -1586   1250   -548       N  
ATOM   2161  CA  GLN A 313     -58.971   4.526  30.169  1.00 71.25           C  
ANISOU 2161  CA  GLN A 313     9127   6813  11130  -1735   1361   -767       C  
ATOM   2162  C   GLN A 313     -57.899   5.557  30.494  1.00 68.96           C  
ANISOU 2162  C   GLN A 313     8944   6461  10795  -1646   1391   -523       C  
ATOM   2163  O   GLN A 313     -56.761   5.433  30.027  1.00 85.02           O  
ANISOU 2163  O   GLN A 313    10901   8614  12790  -1655   1425   -727       O  
ATOM   2164  CB  GLN A 313     -59.719   4.956  28.903  1.00 71.01           C  
ANISOU 2164  CB  GLN A 313     8878   7392  10710  -1870   1355   -717       C  
ATOM   2165  CG  GLN A 313     -58.926   4.839  27.599  1.00 95.82           C  
ANISOU 2165  CG  GLN A 313    11783  11060  13564  -1997   1396  -1009       C  
ATOM   2166  CD  GLN A 313     -59.247   3.562  26.843  1.00128.50           C  
ANISOU 2166  CD  GLN A 313    15707  15431  17688  -2168   1419  -1569       C  
ATOM   2167  OE1 GLN A 313     -59.875   2.656  27.386  1.00124.39           O  
ANISOU 2167  OE1 GLN A 313    15233  14567  17462  -2167   1411  -1760       O  
ATOM   2168  NE2 GLN A 313     -58.828   3.489  25.583  1.00142.45           N  
ANISOU 2168  NE2 GLN A 313    17214  17796  19115  -2337   1466  -1850       N  
ATOM   2169  N   SER A 314     -58.248   6.580  31.278  1.00 67.01           N  
ANISOU 2169  N   SER A 314     8843   6129  10487  -1514   1339   -112       N  
ATOM   2170  CA  SER A 314     -57.276   7.602  31.651  1.00 70.77           C  
ANISOU 2170  CA  SER A 314     9391   6627  10871  -1402   1326     82       C  
ATOM   2171  C   SER A 314     -56.178   7.024  32.534  1.00 74.51           C  
ANISOU 2171  C   SER A 314     9932   6992  11386  -1248   1198    -70       C  
ATOM   2172  O   SER A 314     -55.009   7.404  32.407  1.00 79.35           O  
ANISOU 2172  O   SER A 314    10534   7618  11999  -1250   1252   -102       O  
ATOM   2173  CB  SER A 314     -57.977   8.764  32.354  1.00 74.72           C  
ANISOU 2173  CB  SER A 314     9968   7185  11238  -1269   1230    425       C  
ATOM   2174  OG  SER A 314     -58.938   9.372  31.506  1.00 79.13           O  
ANISOU 2174  OG  SER A 314    10422   7880  11764  -1380   1342    665       O  
ATOM   2175  N   ILE A 315     -56.535   6.115  33.445  1.00100.23           N  
ANISOU 2175  N   ILE A 315    13238  10172  14672  -1134   1038   -116       N  
ATOM   2176  CA  ILE A 315     -55.526   5.465  34.275  1.00103.45           C  
ANISOU 2176  CA  ILE A 315    13669  10512  15124  -1029    934   -180       C  
ATOM   2177  C   ILE A 315     -54.625   4.575  33.424  1.00100.30           C  
ANISOU 2177  C   ILE A 315    13135  10044  14931  -1077   1044   -483       C  
ATOM   2178  O   ILE A 315     -53.437   4.399  33.731  1.00 94.74           O  
ANISOU 2178  O   ILE A 315    12407   9298  14290  -1019   1028   -523       O  
ATOM   2179  CB  ILE A 315     -56.202   4.678  35.414  1.00 94.90           C  
ANISOU 2179  CB  ILE A 315    12656   9384  14020   -947    773   -105       C  
ATOM   2180  CG1 ILE A 315     -57.182   5.577  36.171  1.00102.96           C  
ANISOU 2180  CG1 ILE A 315    13775  10499  14846   -933    686    107       C  
ATOM   2181  CG2 ILE A 315     -55.162   4.117  36.372  1.00 76.07           C  
ANISOU 2181  CG2 ILE A 315    10291   6936  11678   -875    691    -87       C  
ATOM   2182  CD1 ILE A 315     -57.854   4.902  37.350  1.00 88.08           C  
ANISOU 2182  CD1 ILE A 315    11948   8573  12944   -891    585    168       C  
ATOM   2183  N   SER A 316     -55.164   4.007  32.342  1.00 89.39           N  
ANISOU 2183  N   SER A 316    11631   8671  13663  -1211   1166   -748       N  
ATOM   2184  CA  SER A 316     -54.340   3.211  31.438  1.00 77.19           C  
ANISOU 2184  CA  SER A 316     9906   7127  12296  -1294   1287  -1154       C  
ATOM   2185  C   SER A 316     -53.247   4.060  30.797  1.00 72.84           C  
ANISOU 2185  C   SER A 316     9319   6674  11683  -1399   1412  -1224       C  
ATOM   2186  O   SER A 316     -52.093   3.629  30.701  1.00 79.54           O  
ANISOU 2186  O   SER A 316    10076   7489  12656  -1350   1440  -1415       O  
ATOM   2187  CB  SER A 316     -55.217   2.557  30.370  1.00 84.31           C  
ANISOU 2187  CB  SER A 316    10649   8136  13251  -1495   1396  -1524       C  
ATOM   2188  OG  SER A 316     -54.469   1.650  29.580  1.00 87.23           O  
ANISOU 2188  OG  SER A 316    10804   8573  13767  -1560   1499  -1999       O  
ATOM   2189  N   ASN A 317     -53.584   5.275  30.360  1.00 70.55           N  
ANISOU 2189  N   ASN A 317     9074   6541  11191  -1535   1492  -1019       N  
ATOM   2190  CA  ASN A 317     -52.556   6.187  29.864  1.00 65.64           C  
ANISOU 2190  CA  ASN A 317     8407   6168  10366  -1546   1544   -935       C  
ATOM   2191  C   ASN A 317     -51.629   6.627  30.990  1.00 74.57           C  
ANISOU 2191  C   ASN A 317     9689   6998  11646  -1422   1513   -751       C  
ATOM   2192  O   ASN A 317     -50.422   6.811  30.781  1.00 84.88           O  
ANISOU 2192  O   ASN A 317    10939   8339  12973  -1434   1570   -851       O  
ATOM   2193  CB  ASN A 317     -53.207   7.400  29.203  1.00 57.04           C  
ANISOU 2193  CB  ASN A 317     7283   5446   8945  -1610   1572   -601       C  
ATOM   2194  CG  ASN A 317     -54.294   7.013  28.223  1.00 64.98           C  
ANISOU 2194  CG  ASN A 317     8118   6841   9731  -1726   1555   -700       C  
ATOM   2195  OD1 ASN A 317     -54.295   5.906  27.686  1.00 72.77           O  
ANISOU 2195  OD1 ASN A 317     8964   7950  10737  -1802   1559  -1131       O  
ATOM   2196  ND2 ASN A 317     -55.229   7.925  27.986  1.00 72.22           N  
ANISOU 2196  ND2 ASN A 317     9018   7961  10462  -1749   1548   -309       N  
ATOM   2197  N   GLU A 318     -52.188   6.804  32.190  1.00 81.64           N  
ANISOU 2197  N   GLU A 318    10723   7833  12464  -1240   1330   -470       N  
ATOM   2198  CA  GLU A 318     -51.403   7.198  33.355  1.00 77.93           C  
ANISOU 2198  CA  GLU A 318    10335   7343  11932  -1105   1201   -307       C  
ATOM   2199  C   GLU A 318     -50.291   6.194  33.636  1.00 80.84           C  
ANISOU 2199  C   GLU A 318    10627   7613  12475  -1043   1163   -483       C  
ATOM   2200  O   GLU A 318     -49.187   6.574  34.041  1.00 87.91           O  
ANISOU 2200  O   GLU A 318    11522   8507  13372  -1021   1157   -444       O  
ATOM   2201  CB  GLU A 318     -52.338   7.336  34.560  1.00 78.04           C  
ANISOU 2201  CB  GLU A 318    10461   7373  11816  -1013   1024    -98       C  
ATOM   2202  CG  GLU A 318     -51.878   8.267  35.670  1.00 80.62           C  
ANISOU 2202  CG  GLU A 318    10862   7759  12010   -977    941     60       C  
ATOM   2203  CD  GLU A 318     -53.039   8.732  36.540  1.00 68.59           C  
ANISOU 2203  CD  GLU A 318     9412   6295  10353   -953    837    204       C  
ATOM   2204  OE1 GLU A 318     -54.054   9.193  35.979  1.00 63.49           O  
ANISOU 2204  OE1 GLU A 318     8759   5691   9674   -968    885    270       O  
ATOM   2205  OE2 GLU A 318     -52.948   8.630  37.782  1.00 54.85           O  
ANISOU 2205  OE2 GLU A 318     7724   4556   8559   -940    724    250       O  
ATOM   2206  N   GLN A 319     -50.567   4.906  33.429  1.00 75.85           N  
ANISOU 2206  N   GLN A 319     9905   6895  12020  -1015   1148   -673       N  
ATOM   2207  CA  GLN A 319     -49.546   3.878  33.620  1.00 74.72           C  
ANISOU 2207  CA  GLN A 319     9635   6638  12117   -939   1137   -823       C  
ATOM   2208  C   GLN A 319     -48.710   3.626  32.369  1.00 76.36           C  
ANISOU 2208  C   GLN A 319     9659   6869  12484  -1024   1312  -1191       C  
ATOM   2209  O   GLN A 319     -47.551   3.210  32.484  1.00 80.84           O  
ANISOU 2209  O   GLN A 319    10112   7365  13238   -963   1328  -1285       O  
ATOM   2210  CB  GLN A 319     -50.186   2.566  34.089  1.00 80.98           C  
ANISOU 2210  CB  GLN A 319    10381   7313  13075   -857   1058   -838       C  
ATOM   2211  CG  GLN A 319     -51.223   1.990  33.145  1.00 93.35           C  
ANISOU 2211  CG  GLN A 319    11868   8898  14702   -934   1141  -1079       C  
ATOM   2212  CD  GLN A 319     -51.874   0.734  33.688  1.00106.57           C  
ANISOU 2212  CD  GLN A 319    13494  10442  16554   -856   1077  -1067       C  
ATOM   2213  OE1 GLN A 319     -53.077   0.525  33.527  1.00121.65           O  
ANISOU 2213  OE1 GLN A 319    15436  12375  18411   -900   1069  -1086       O  
ATOM   2214  NE2 GLN A 319     -51.080  -0.114  34.332  1.00111.79           N  
ANISOU 2214  NE2 GLN A 319    14057  10957  17462   -750   1049  -1022       N  
ATOM   2215  N   LYS A 320     -49.260   3.870  31.176  1.00 79.62           N  
ANISOU 2215  N   LYS A 320    10018   7411  12822  -1197   1454  -1430       N  
ATOM   2216  CA  LYS A 320     -48.472   3.737  29.952  1.00 75.28           C  
ANISOU 2216  CA  LYS A 320     9279   6994  12332  -1351   1632  -1861       C  
ATOM   2217  C   LYS A 320     -47.344   4.761  29.905  1.00 73.42           C  
ANISOU 2217  C   LYS A 320     9066   6866  11964  -1369   1673  -1736       C  
ATOM   2218  O   LYS A 320     -46.214   4.437  29.510  1.00 85.49           O  
ANISOU 2218  O   LYS A 320    10440   8451  13591  -1356   1736  -1980       O  
ATOM   2219  CB  LYS A 320     -49.381   3.881  28.732  1.00 73.13           C  
ANISOU 2219  CB  LYS A 320     8908   7118  11761  -1536   1704  -2050       C  
ATOM   2220  CG  LYS A 320     -48.656   3.858  27.397  1.00 83.27           C  
ANISOU 2220  CG  LYS A 320     9953   8871  12814  -1656   1820  -2400       C  
ATOM   2221  CD  LYS A 320     -48.032   2.498  27.124  1.00107.78           C  
ANISOU 2221  CD  LYS A 320    12849  11805  16296  -1655   1922  -2944       C  
ATOM   2222  CE  LYS A 320     -47.361   2.464  25.758  1.00108.27           C  
ANISOU 2222  CE  LYS A 320    12651  12391  16097  -1811   2065  -3359       C  
ATOM   2223  NZ  LYS A 320     -46.793   1.123  25.444  1.00 92.49           N  
ANISOU 2223  NZ  LYS A 320    10412  10202  14528  -1827   2214  -3960       N  
ATOM   2224  N   ALA A 321     -47.632   6.004  30.299  1.00 69.65           N  
ANISOU 2224  N   ALA A 321     8758   6449  11257  -1381   1641  -1347       N  
ATOM   2225  CA  ALA A 321     -46.576   7.008  30.381  1.00 78.29           C  
ANISOU 2225  CA  ALA A 321     9872   7640  12234  -1381   1675  -1191       C  
ATOM   2226  C   ALA A 321     -45.517   6.599  31.397  1.00 84.87           C  
ANISOU 2226  C   ALA A 321    10715   8180  13350  -1276   1617  -1197       C  
ATOM   2227  O   ALA A 321     -44.317   6.808  31.177  1.00 82.21           O  
ANISOU 2227  O   ALA A 321    10282   7929  13026  -1279   1664  -1286       O  
ATOM   2228  CB  ALA A 321     -47.170   8.371  30.736  1.00 77.37           C  
ANISOU 2228  CB  ALA A 321     9916   7551  11929  -1416   1686   -791       C  
ATOM   2229  N   CYS A 322     -45.948   6.008  32.514  1.00102.30           N  
ANISOU 2229  N   CYS A 322    12995  10273  15603  -1110   1433  -1011       N  
ATOM   2230  CA  CYS A 322     -45.005   5.498  33.505  1.00108.58           C  
ANISOU 2230  CA  CYS A 322    13744  10951  16562   -990   1324   -931       C  
ATOM   2231  C   CYS A 322     -44.111   4.417  32.911  1.00 98.57           C  
ANISOU 2231  C   CYS A 322    12242   9592  15619   -949   1400  -1245       C  
ATOM   2232  O   CYS A 322     -42.901   4.394  33.164  1.00 95.41           O  
ANISOU 2232  O   CYS A 322    11740   9134  15378   -916   1409  -1263       O  
ATOM   2233  CB  CYS A 322     -45.769   4.961  34.716  1.00 97.15           C  
ANISOU 2233  CB  CYS A 322    12389   9430  15094   -888   1146   -693       C  
ATOM   2234  SG  CYS A 322     -44.843   3.796  35.739  1.00 88.03           S  
ANISOU 2234  SG  CYS A 322    11091   8087  14269   -767   1049   -615       S  
ATOM   2235  N   LYS A 323     -44.691   3.511  32.121  1.00 79.03           N  
ANISOU 2235  N   LYS A 323     9653   7112  13265   -957   1466  -1519       N  
ATOM   2236  CA  LYS A 323     -43.897   2.467  31.477  1.00 78.06           C  
ANISOU 2236  CA  LYS A 323     9267   6930  13464   -923   1571  -1881       C  
ATOM   2237  C   LYS A 323     -42.872   3.061  30.516  1.00 82.16           C  
ANISOU 2237  C   LYS A 323     9679   7599  13938  -1045   1732  -2177       C  
ATOM   2238  O   LYS A 323     -41.708   2.639  30.497  1.00 88.39           O  
ANISOU 2238  O   LYS A 323    10287   8314  14982   -978   1778  -2317       O  
ATOM   2239  CB  LYS A 323     -44.814   1.490  30.739  1.00 94.14           C  
ANISOU 2239  CB  LYS A 323    11187   8993  15589   -957   1643  -2177       C  
ATOM   2240  CG  LYS A 323     -45.094   0.192  31.485  1.00103.75           C  
ANISOU 2240  CG  LYS A 323    12309   9984  17128   -805   1563  -2068       C  
ATOM   2241  CD  LYS A 323     -45.838   0.433  32.788  1.00109.20           C  
ANISOU 2241  CD  LYS A 323    13223  10594  17673   -727   1368  -1598       C  
ATOM   2242  CE  LYS A 323     -46.146  -0.879  33.492  1.00117.18           C  
ANISOU 2242  CE  LYS A 323    14121  11400  19003   -610   1314  -1494       C  
ATOM   2243  NZ  LYS A 323     -46.865  -0.666  34.778  1.00 98.92           N  
ANISOU 2243  NZ  LYS A 323    12012   9064  16510   -564   1137  -1079       N  
ATOM   2244  N   VAL A 324     -43.284   4.043  29.712  1.00 82.02           N  
ANISOU 2244  N   VAL A 324     9745   7866  13555  -1219   1810  -2225       N  
ATOM   2245  CA  VAL A 324     -42.359   4.651  28.754  1.00 78.01           C  
ANISOU 2245  CA  VAL A 324     9109   7742  12790  -1298   1914  -2373       C  
ATOM   2246  C   VAL A 324     -41.219   5.360  29.481  1.00 69.21           C  
ANISOU 2246  C   VAL A 324     8043   6546  11708  -1234   1869  -2127       C  
ATOM   2247  O   VAL A 324     -40.043   5.248  29.097  1.00 56.05           O  
ANISOU 2247  O   VAL A 324     6202   4975  10120  -1222   1942  -2317       O  
ATOM   2248  CB  VAL A 324     -43.115   5.605  27.811  1.00 74.59           C  
ANISOU 2248  CB  VAL A 324     8719   7771  11850  -1450   1955  -2277       C  
ATOM   2249  CG1 VAL A 324     -42.138   6.371  26.933  1.00 71.63           C  
ANISOU 2249  CG1 VAL A 324     8218   7804  11193  -1536   2056  -2322       C  
ATOM   2250  CG2 VAL A 324     -44.103   4.827  26.955  1.00 73.32           C  
ANISOU 2250  CG2 VAL A 324     8442   7802  11615  -1550   2007  -2593       C  
ATOM   2251  N   LEU A 325     -41.545   6.098  30.542  1.00 79.26           N  
ANISOU 2251  N   LEU A 325     9532   7663  12922  -1211   1762  -1732       N  
ATOM   2252  CA  LEU A 325     -40.501   6.780  31.299  1.00 68.00           C  
ANISOU 2252  CA  LEU A 325     8135   6193  11510  -1189   1723  -1534       C  
ATOM   2253  C   LEU A 325     -39.583   5.792  32.006  1.00 67.84           C  
ANISOU 2253  C   LEU A 325     7964   5918  11893  -1063   1657  -1595       C  
ATOM   2254  O   LEU A 325     -38.380   6.043  32.115  1.00 78.22           O  
ANISOU 2254  O   LEU A 325     9168   7302  13249  -1048   1667  -1599       O  
ATOM   2255  CB  LEU A 325     -41.128   7.753  32.292  1.00 75.80           C  
ANISOU 2255  CB  LEU A 325     9359   7089  12352  -1230   1654  -1170       C  
ATOM   2256  CG  LEU A 325     -41.898   8.888  31.614  1.00 76.96           C  
ANISOU 2256  CG  LEU A 325     9610   7457  12174  -1339   1742  -1036       C  
ATOM   2257  CD1 LEU A 325     -42.445   9.854  32.641  1.00 85.66           C  
ANISOU 2257  CD1 LEU A 325    10911   8417  13217  -1378   1717   -728       C  
ATOM   2258  CD2 LEU A 325     -41.021   9.618  30.606  1.00 63.68           C  
ANISOU 2258  CD2 LEU A 325     7802   6095  10297  -1412   1863  -1102       C  
ATOM   2259  N   GLY A 326     -40.115   4.664  32.479  1.00 71.78           N  
ANISOU 2259  N   GLY A 326     8429   6132  12713   -965   1594  -1609       N  
ATOM   2260  CA  GLY A 326     -39.249   3.628  33.015  1.00 75.77           C  
ANISOU 2260  CA  GLY A 326     8723   6434  13634   -814   1541  -1610       C  
ATOM   2261  C   GLY A 326     -38.310   3.070  31.964  1.00 80.98           C  
ANISOU 2261  C   GLY A 326     9114   7107  14548   -804   1707  -2036       C  
ATOM   2262  O   GLY A 326     -37.145   2.776  32.248  1.00 84.51           O  
ANISOU 2262  O   GLY A 326     9368   7479  15261   -715   1699  -2024       O  
ATOM   2263  N   ILE A 327     -38.802   2.929  30.731  1.00 79.08           N  
ANISOU 2263  N   ILE A 327     8830   7054  14164   -896   1850  -2403       N  
ATOM   2264  CA  ILE A 327     -37.951   2.473  29.634  1.00 85.78           C  
ANISOU 2264  CA  ILE A 327     9407   8052  15132   -917   2028  -2856       C  
ATOM   2265  C   ILE A 327     -36.800   3.448  29.414  1.00 83.99           C  
ANISOU 2265  C   ILE A 327     9150   8118  14645   -960   2050  -2789       C  
ATOM   2266  O   ILE A 327     -35.638   3.044  29.264  1.00 85.22           O  
ANISOU 2266  O   ILE A 327     9071   8235  15075   -893   2122  -2965       O  
ATOM   2267  CB  ILE A 327     -38.781   2.284  28.350  1.00 79.74           C  
ANISOU 2267  CB  ILE A 327     8598   7571  14129  -1069   2172  -3257       C  
ATOM   2268  CG1 ILE A 327     -39.546   0.959  28.394  1.00 80.77           C  
ANISOU 2268  CG1 ILE A 327     8613   7491  14586   -999   2182  -3399       C  
ATOM   2269  CG2 ILE A 327     -37.896   2.358  27.114  1.00 69.78           C  
ANISOU 2269  CG2 ILE A 327     7103   6688  12721  -1173   2359  -3676       C  
ATOM   2270  CD1 ILE A 327     -40.292   0.644  27.114  1.00 88.95           C  
ANISOU 2270  CD1 ILE A 327     9542   8841  15413  -1181   2338  -3866       C  
ATOM   2271  N   VAL A 328     -37.102   4.750  29.391  1.00 87.51           N  
ANISOU 2271  N   VAL A 328     9811   8836  14604  -1070   2005  -2530       N  
ATOM   2272  CA  VAL A 328     -36.034   5.720  29.141  1.00 71.16           C  
ANISOU 2272  CA  VAL A 328     7701   7031  12306  -1130   2049  -2470       C  
ATOM   2273  C   VAL A 328     -35.058   5.763  30.317  1.00 76.47           C  
ANISOU 2273  C   VAL A 328     8342   7489  13225  -1027   1933  -2232       C  
ATOM   2274  O   VAL A 328     -33.841   5.897  30.121  1.00 80.84           O  
ANISOU 2274  O   VAL A 328     8722   8153  13840  -1018   1986  -2324       O  
ATOM   2275  CB  VAL A 328     -36.604   7.113  28.798  1.00 63.62           C  
ANISOU 2275  CB  VAL A 328     6944   6376  10853  -1274   2064  -2231       C  
ATOM   2276  CG1 VAL A 328     -37.699   6.998  27.744  1.00 79.77           C  
ANISOU 2276  CG1 VAL A 328     8992   8670  12646  -1374   2139  -2383       C  
ATOM   2277  CG2 VAL A 328     -37.097   7.858  30.028  1.00 75.99           C  
ANISOU 2277  CG2 VAL A 328     8759   7740  12373  -1265   1932  -1817       C  
ATOM   2278  N   PHE A 329     -35.563   5.626  31.551  1.00 96.48           N  
ANISOU 2278  N   PHE A 329    11013   9759  15884   -963   1773  -1922       N  
ATOM   2279  CA  PHE A 329     -34.678   5.535  32.711  1.00 96.71           C  
ANISOU 2279  CA  PHE A 329    10961   9657  16125   -885   1644  -1679       C  
ATOM   2280  C   PHE A 329     -33.718   4.363  32.563  1.00101.99           C  
ANISOU 2280  C   PHE A 329    11304  10163  17285   -735   1679  -1859       C  
ATOM   2281  O   PHE A 329     -32.502   4.503  32.754  1.00107.84           O  
ANISOU 2281  O   PHE A 329    11869  10985  18121   -705   1668  -1825       O  
ATOM   2282  CB  PHE A 329     -35.482   5.362  34.004  1.00 97.41           C  
ANISOU 2282  CB  PHE A 329    11204   9535  16271   -854   1474  -1337       C  
ATOM   2283  CG  PHE A 329     -36.460   6.467  34.291  1.00 98.10           C  
ANISOU 2283  CG  PHE A 329    11590   9726  15958   -992   1457  -1164       C  
ATOM   2284  CD1 PHE A 329     -36.329   7.718  33.712  1.00 93.71           C  
ANISOU 2284  CD1 PHE A 329    11133   9416  15056  -1127   1562  -1199       C  
ATOM   2285  CD2 PHE A 329     -37.516   6.246  35.162  1.00 88.88           C  
ANISOU 2285  CD2 PHE A 329    10579   8384  14807   -984   1354   -948       C  
ATOM   2286  CE1 PHE A 329     -37.243   8.720  33.991  1.00 88.76           C  
ANISOU 2286  CE1 PHE A 329    10742   8821  14160  -1240   1577  -1027       C  
ATOM   2287  CE2 PHE A 329     -38.425   7.243  35.446  1.00 83.86           C  
ANISOU 2287  CE2 PHE A 329    10192   7812  13860  -1106   1364   -810       C  
ATOM   2288  CZ  PHE A 329     -38.288   8.482  34.861  1.00 83.37           C  
ANISOU 2288  CZ  PHE A 329    10212   7956  13509  -1228   1482   -851       C  
ATOM   2289  N   PHE A 330     -34.262   3.190  32.229  1.00 83.36           N  
ANISOU 2289  N   PHE A 330     8837   7551  15284   -643   1740  -2060       N  
ATOM   2290  CA  PHE A 330     -33.449   1.988  32.103  1.00 81.66           C  
ANISOU 2290  CA  PHE A 330     8278   7087  15663   -488   1814  -2242       C  
ATOM   2291  C   PHE A 330     -32.391   2.160  31.024  1.00 82.01           C  
ANISOU 2291  C   PHE A 330     8117   7366  15676   -530   1995  -2623       C  
ATOM   2292  O   PHE A 330     -31.223   1.812  31.225  1.00 81.07           O  
ANISOU 2292  O   PHE A 330     7734   7173  15896   -424   2008  -2614       O  
ATOM   2293  CB  PHE A 330     -34.348   0.787  31.796  1.00 85.30           C  
ANISOU 2293  CB  PHE A 330     8665   7224  16522   -424   1904  -2470       C  
ATOM   2294  CG  PHE A 330     -33.597  -0.483  31.505  1.00 74.94           C  
ANISOU 2294  CG  PHE A 330     6961   5665  15846   -281   2035  -2701       C  
ATOM   2295  CD1 PHE A 330     -33.181  -1.309  32.535  1.00 69.29           C  
ANISOU 2295  CD1 PHE A 330     6042   4637  15649   -101   1920  -2325       C  
ATOM   2296  CD2 PHE A 330     -33.320  -0.858  30.198  1.00 80.60           C  
ANISOU 2296  CD2 PHE A 330     7486   6555  16585   -361   2263  -3238       C  
ATOM   2297  CE1 PHE A 330     -32.497  -2.481  32.271  1.00 75.51           C  
ANISOU 2297  CE1 PHE A 330     6446   5238  17007     -0   2037  -2463       C  
ATOM   2298  CE2 PHE A 330     -32.635  -2.027  29.928  1.00 92.58           C  
ANISOU 2298  CE2 PHE A 330     8631   7897  18647   -286   2382  -3420       C  
ATOM   2299  CZ  PHE A 330     -32.224  -2.840  30.965  1.00 99.20           C  
ANISOU 2299  CZ  PHE A 330     9277   8372  20042   -104   2273  -3026       C  
ATOM   2300  N   LEU A 331     -32.781   2.707  29.872  1.00 85.95           N  
ANISOU 2300  N   LEU A 331     8711   8186  15760   -690   2136  -2935       N  
ATOM   2301  CA  LEU A 331     -31.828   2.858  28.777  1.00 97.02           C  
ANISOU 2301  CA  LEU A 331     9904   9871  17087   -758   2326  -3314       C  
ATOM   2302  C   LEU A 331     -30.706   3.818  29.153  1.00 91.69           C  
ANISOU 2302  C   LEU A 331     9222   9392  16222   -776   2259  -3072       C  
ATOM   2303  O   LEU A 331     -29.522   3.510  28.960  1.00 85.62           O  
ANISOU 2303  O   LEU A 331     8182   8629  15723   -713   2340  -3230       O  
ATOM   2304  CB  LEU A 331     -32.551   3.322  27.514  1.00 97.06           C  
ANISOU 2304  CB  LEU A 331    10000  10274  16604   -955   2466  -3610       C  
ATOM   2305  CG  LEU A 331     -33.515   2.282  26.940  1.00 84.27           C  
ANISOU 2305  CG  LEU A 331     8306   8538  15174   -979   2576  -3985       C  
ATOM   2306  CD1 LEU A 331     -34.090   2.751  25.623  1.00 84.42           C  
ANISOU 2306  CD1 LEU A 331     8346   9081  14651  -1205   2711  -4278       C  
ATOM   2307  CD2 LEU A 331     -32.821   0.937  26.777  1.00 87.52           C  
ANISOU 2307  CD2 LEU A 331     8362   8625  16268   -858   2738  -4389       C  
ATOM   2308  N   PHE A 332     -31.057   4.979  29.715  1.00 84.85           N  
ANISOU 2308  N   PHE A 332     8634   8671  14933   -869   2127  -2707       N  
ATOM   2309  CA  PHE A 332     -30.037   5.946  30.114  1.00 70.18           C  
ANISOU 2309  CA  PHE A 332     6769   6996  12901   -921   2079  -2506       C  
ATOM   2310  C   PHE A 332     -29.070   5.336  31.122  1.00 69.71           C  
ANISOU 2310  C   PHE A 332     6492   6727  13268   -770   1956  -2331       C  
ATOM   2311  O   PHE A 332     -27.843   5.413  30.955  1.00 74.09           O  
ANISOU 2311  O   PHE A 332     6822   7398  13933   -752   2007  -2414       O  
ATOM   2312  CB  PHE A 332     -30.710   7.195  30.688  1.00 72.00           C  
ANISOU 2312  CB  PHE A 332     7317   7330  12711  -1050   1983  -2171       C  
ATOM   2313  CG  PHE A 332     -29.748   8.222  31.225  1.00 74.61           C  
ANISOU 2313  CG  PHE A 332     7643   7818  12888  -1136   1945  -1985       C  
ATOM   2314  CD1 PHE A 332     -29.207   9.186  30.392  1.00 79.32           C  
ANISOU 2314  CD1 PHE A 332     8221   8705  13210  -1270   2091  -2080       C  
ATOM   2315  CD2 PHE A 332     -29.405   8.238  32.569  1.00 76.77           C  
ANISOU 2315  CD2 PHE A 332     7909   7983  13276  -1106   1770  -1710       C  
ATOM   2316  CE1 PHE A 332     -28.331  10.137  30.885  1.00 84.12           C  
ANISOU 2316  CE1 PHE A 332     8814   9437  13712  -1367   2077  -1939       C  
ATOM   2317  CE2 PHE A 332     -28.529   9.185  33.067  1.00 67.28           C  
ANISOU 2317  CE2 PHE A 332     6680   6964  11919  -1221   1747  -1593       C  
ATOM   2318  CZ  PHE A 332     -27.992  10.135  32.224  1.00 68.84           C  
ANISOU 2318  CZ  PHE A 332     6870   7394  11892  -1350   1908  -1724       C  
ATOM   2319  N   VAL A 333     -29.607   4.700  32.168  1.00 72.21           N  
ANISOU 2319  N   VAL A 333     6845   6758  13834   -661   1794  -2059       N  
ATOM   2320  CA  VAL A 333     -28.754   4.161  33.224  1.00 77.20           C  
ANISOU 2320  CA  VAL A 333     7244   7251  14836   -527   1646  -1776       C  
ATOM   2321  C   VAL A 333     -27.863   3.052  32.680  1.00 80.98           C  
ANISOU 2321  C   VAL A 333     7334   7549  15888   -360   1774  -2025       C  
ATOM   2322  O   VAL A 333     -26.659   3.010  32.960  1.00 81.93           O  
ANISOU 2322  O   VAL A 333     7192   7732  16204   -296   1744  -1934       O  
ATOM   2323  CB  VAL A 333     -29.606   3.673  34.407  1.00 81.49           C  
ANISOU 2323  CB  VAL A 333     7886   7566  15512   -459   1454  -1396       C  
ATOM   2324  CG1 VAL A 333     -28.769   2.805  35.331  1.00 76.95           C  
ANISOU 2324  CG1 VAL A 333     6977   6838  15424   -288   1319  -1082       C  
ATOM   2325  CG2 VAL A 333     -30.178   4.858  35.163  1.00 79.62           C  
ANISOU 2325  CG2 VAL A 333     7966   7542  14744   -637   1330  -1140       C  
ATOM   2326  N   VAL A 334     -28.436   2.138  31.894  1.00 80.97           N  
ANISOU 2326  N   VAL A 334     7260   7319  16184   -297   1938  -2368       N  
ATOM   2327  CA  VAL A 334     -27.662   1.011  31.382  1.00 86.04           C  
ANISOU 2327  CA  VAL A 334     7503   7722  17466   -143   2110  -2666       C  
ATOM   2328  C   VAL A 334     -26.550   1.497  30.464  1.00 95.41           C  
ANISOU 2328  C   VAL A 334     8526   9213  18511   -218   2278  -3002       C  
ATOM   2329  O   VAL A 334     -25.411   1.019  30.541  1.00 85.37           O  
ANISOU 2329  O   VAL A 334     6907   7846  17682    -91   2327  -3024       O  
ATOM   2330  CB  VAL A 334     -28.589   0.004  30.676  1.00 89.83           C  
ANISOU 2330  CB  VAL A 334     7945   7919  18266   -116   2291  -3057       C  
ATOM   2331  CG1 VAL A 334     -27.779  -0.966  29.830  1.00103.98           C  
ANISOU 2331  CG1 VAL A 334     9322   9530  20654    -26   2564  -3548       C  
ATOM   2332  CG2 VAL A 334     -29.412  -0.754  31.703  1.00 77.37           C  
ANISOU 2332  CG2 VAL A 334     6407   5941  17049     14   2139  -2682       C  
ATOM   2333  N   MET A 335     -26.851   2.459  29.588  1.00104.37           N  
ANISOU 2333  N   MET A 335     9883  10730  19042   -425   2371  -3231       N  
ATOM   2334  CA  MET A 335     -25.824   2.924  28.665  1.00109.05           C  
ANISOU 2334  CA  MET A 335    10311  11646  19477   -515   2546  -3540       C  
ATOM   2335  C   MET A 335     -24.746   3.737  29.369  1.00109.52           C  
ANISOU 2335  C   MET A 335    10331  11874  19409   -521   2408  -3205       C  
ATOM   2336  O   MET A 335     -23.598   3.758  28.911  1.00118.50           O  
ANISOU 2336  O   MET A 335    11206  13146  20671   -513   2528  -3398       O  
ATOM   2337  CB  MET A 335     -26.458   3.723  27.530  1.00100.99           C  
ANISOU 2337  CB  MET A 335     9500  11026  17845   -741   2680  -3801       C  
ATOM   2338  CG  MET A 335     -26.760   2.873  26.310  1.00101.80           C  
ANISOU 2338  CG  MET A 335     9419  11169  18090   -789   2939  -4389       C  
ATOM   2339  SD  MET A 335     -27.671   3.757  25.039  1.00114.11           S  
ANISOU 2339  SD  MET A 335    11192  13292  18874  -1072   3053  -4593       S  
ATOM   2340  CE  MET A 335     -29.225   4.030  25.883  1.00101.10           C  
ANISOU 2340  CE  MET A 335     9936  11447  17029  -1060   2821  -4158       C  
ATOM   2341  N   TRP A 336     -25.073   4.407  30.476  1.00 92.01           N  
ANISOU 2341  N   TRP A 336     8343   9672  16944   -554   2172  -2740       N  
ATOM   2342  CA  TRP A 336     -24.024   5.086  31.227  1.00 89.22           C  
ANISOU 2342  CA  TRP A 336     7903   9494  16504   -582   2043  -2459       C  
ATOM   2343  C   TRP A 336     -23.317   4.183  32.233  1.00 84.47           C  
ANISOU 2343  C   TRP A 336     6985   8669  16441   -382   1892  -2173       C  
ATOM   2344  O   TRP A 336     -22.306   4.600  32.807  1.00 79.65           O  
ANISOU 2344  O   TRP A 336     6216   8244  15804   -401   1788  -1966       O  
ATOM   2345  CB  TRP A 336     -24.585   6.313  31.954  1.00 85.41           C  
ANISOU 2345  CB  TRP A 336     7765   9191  15497   -758   1894  -2148       C  
ATOM   2346  CG  TRP A 336     -24.456   7.582  31.162  1.00 87.48           C  
ANISOU 2346  CG  TRP A 336     8185   9772  15280   -966   2034  -2294       C  
ATOM   2347  CD1 TRP A 336     -25.469   8.389  30.739  1.00 88.65           C  
ANISOU 2347  CD1 TRP A 336     8641  10015  15025  -1110   2094  -2292       C  
ATOM   2348  CD2 TRP A 336     -23.241   8.182  30.691  1.00 99.44           C  
ANISOU 2348  CD2 TRP A 336     9526  11547  16711  -1049   2141  -2420       C  
ATOM   2349  NE1 TRP A 336     -24.963   9.459  30.039  1.00 98.23           N  
ANISOU 2349  NE1 TRP A 336     9874  11519  15929  -1273   2234  -2373       N  
ATOM   2350  CE2 TRP A 336     -23.598   9.354  29.994  1.00108.33           C  
ANISOU 2350  CE2 TRP A 336    10870  12907  17384  -1247   2267  -2468       C  
ATOM   2351  CE3 TRP A 336     -21.887   7.844  30.791  1.00 96.06           C  
ANISOU 2351  CE3 TRP A 336     8755  11173  16569   -972   2146  -2470       C  
ATOM   2352  CZ2 TRP A 336     -22.651  10.189  29.402  1.00100.12           C  
ANISOU 2352  CZ2 TRP A 336     9728  12145  16167  -1378   2403  -2566       C  
ATOM   2353  CZ3 TRP A 336     -20.949   8.674  30.202  1.00 89.33           C  
ANISOU 2353  CZ3 TRP A 336     7813  10611  15517  -1106   2276  -2605       C  
ATOM   2354  CH2 TRP A 336     -21.336   9.832  29.516  1.00 84.78           C  
ANISOU 2354  CH2 TRP A 336     7471  10258  14484  -1311   2406  -2652       C  
ATOM   2355  N   CYS A 337     -23.820   2.968  32.459  1.00100.43           N  
ANISOU 2355  N   CYS A 337     8884  10310  18964   -199   1880  -2130       N  
ATOM   2356  CA  CYS A 337     -23.219   2.087  33.461  1.00103.00           C  
ANISOU 2356  CA  CYS A 337     8875  10414  19846      6   1728  -1748       C  
ATOM   2357  C   CYS A 337     -21.764   1.718  33.186  1.00104.51           C  
ANISOU 2357  C   CYS A 337     8624  10622  20463    122   1821  -1845       C  
ATOM   2358  O   CYS A 337     -20.942   1.849  34.110  1.00105.86           O  
ANISOU 2358  O   CYS A 337     8591  10934  20698    163   1628  -1436       O  
ATOM   2359  CB  CYS A 337     -24.080   0.829  33.617  1.00103.60           C  
ANISOU 2359  CB  CYS A 337     8883  10024  20459    181   1750  -1701       C  
ATOM   2360  SG  CYS A 337     -25.360   0.949  34.888  1.00118.38           S  
ANISOU 2360  SG  CYS A 337    11072  11842  22066    141   1476  -1181       S  
ATOM   2361  N   PRO A 338     -21.373   1.241  31.992  1.00105.46           N  
ANISOU 2361  N   PRO A 338     8549  10637  20884    168   2109  -2366       N  
ATOM   2362  CA  PRO A 338     -19.991   0.742  31.837  1.00 94.77           C  
ANISOU 2362  CA  PRO A 338     6719   9232  20056    313   2206  -2431       C  
ATOM   2363  C   PRO A 338     -18.921   1.777  32.141  1.00 89.02           C  
ANISOU 2363  C   PRO A 338     5947   8939  18938    197   2090  -2257       C  
ATOM   2364  O   PRO A 338     -17.879   1.438  32.722  1.00 93.13           O  
ANISOU 2364  O   PRO A 338     6089   9452  19846    332   1997  -1978       O  
ATOM   2365  CB  PRO A 338     -19.944   0.297  30.368  1.00 89.71           C  
ANISOU 2365  CB  PRO A 338     5963   8504  19617    293   2574  -3139       C  
ATOM   2366  CG  PRO A 338     -21.361   0.048  29.999  1.00105.83           C  
ANISOU 2366  CG  PRO A 338     8305  10396  21509    225   2637  -3344       C  
ATOM   2367  CD  PRO A 338     -22.146   1.077  30.748  1.00112.20           C  
ANISOU 2367  CD  PRO A 338     9556  11442  21632     80   2368  -2930       C  
ATOM   2368  N   PHE A 339     -19.154   3.037  31.766  1.00 92.47           N  
ANISOU 2368  N   PHE A 339     6737   9751  18647    -55   2101  -2396       N  
ATOM   2369  CA  PHE A 339     -18.179   4.086  32.041  1.00 87.96           C  
ANISOU 2369  CA  PHE A 339     6133   9577  17710   -198   2018  -2266       C  
ATOM   2370  C   PHE A 339     -17.953   4.237  33.540  1.00 89.35           C  
ANISOU 2370  C   PHE A 339     6245   9851  17852   -185   1696  -1686       C  
ATOM   2371  O   PHE A 339     -16.808   4.279  34.008  1.00102.16           O  
ANISOU 2371  O   PHE A 339     7543  11649  19623   -153   1604  -1493       O  
ATOM   2372  CB  PHE A 339     -18.651   5.404  31.422  1.00 84.30           C  
ANISOU 2372  CB  PHE A 339     6069   9427  16535   -471   2103  -2466       C  
ATOM   2373  CG  PHE A 339     -17.725   6.560  31.667  1.00 86.90           C  
ANISOU 2373  CG  PHE A 339     6382  10131  16504   -650   2054  -2368       C  
ATOM   2374  CD1 PHE A 339     -16.667   6.812  30.809  1.00108.11           C  
ANISOU 2374  CD1 PHE A 339     8850  13010  19216   -694   2245  -2661       C  
ATOM   2375  CD2 PHE A 339     -17.917   7.403  32.749  1.00 78.05           C  
ANISOU 2375  CD2 PHE A 339     5451   9180  15024   -798   1839  -2019       C  
ATOM   2376  CE1 PHE A 339     -15.813   7.875  31.032  1.00106.15           C  
ANISOU 2376  CE1 PHE A 339     8576  13092  18665   -871   2213  -2580       C  
ATOM   2377  CE2 PHE A 339     -17.067   8.466  32.977  1.00 83.55           C  
ANISOU 2377  CE2 PHE A 339     6112  10208  15424   -990   1821  -1981       C  
ATOM   2378  CZ  PHE A 339     -16.014   8.703  32.118  1.00 95.32           C  
ANISOU 2378  CZ  PHE A 339     7388  11863  16965  -1022   2004  -2248       C  
ATOM   2379  N   PHE A 340     -19.040   4.298  34.312  1.00 95.98           N  
ANISOU 2379  N   PHE A 340     7365  10620  18483   -224   1524  -1405       N  
ATOM   2380  CA  PHE A 340     -18.915   4.428  35.760  1.00 88.18           C  
ANISOU 2380  CA  PHE A 340     6308   9802  17395   -252   1222   -866       C  
ATOM   2381  C   PHE A 340     -18.299   3.181  36.378  1.00 86.02           C  
ANISOU 2381  C   PHE A 340     5553   9330  17800     17   1105   -497       C  
ATOM   2382  O   PHE A 340     -17.514   3.279  37.327  1.00 88.17           O  
ANISOU 2382  O   PHE A 340     5557   9881  18064      3    890    -90       O  
ATOM   2383  CB  PHE A 340     -20.278   4.720  36.383  1.00 78.35           C  
ANISOU 2383  CB  PHE A 340     5460   8521  15788   -358   1098   -688       C  
ATOM   2384  CG  PHE A 340     -20.723   6.140  36.212  1.00 74.63           C  
ANISOU 2384  CG  PHE A 340     5392   8316  14649   -646   1148   -870       C  
ATOM   2385  CD1 PHE A 340     -21.431   6.527  35.088  1.00 72.16           C  
ANISOU 2385  CD1 PHE A 340     5371   7903  14142   -710   1367  -1250       C  
ATOM   2386  CD2 PHE A 340     -20.422   7.091  37.172  1.00 74.12           C  
ANISOU 2386  CD2 PHE A 340     5376   8615  14172   -865    992   -659       C  
ATOM   2387  CE1 PHE A 340     -21.837   7.834  34.927  1.00 69.24           C  
ANISOU 2387  CE1 PHE A 340     5330   7739  13241   -955   1428  -1351       C  
ATOM   2388  CE2 PHE A 340     -20.826   8.401  37.017  1.00 71.21           C  
ANISOU 2388  CE2 PHE A 340     5344   8420  13292  -1127   1081   -839       C  
ATOM   2389  CZ  PHE A 340     -21.534   8.774  35.894  1.00 68.77           C  
ANISOU 2389  CZ  PHE A 340     5318   7956  12857  -1156   1300  -1153       C  
ATOM   2390  N   ILE A 341     -18.643   2.001  35.857  1.00 87.86           N  
ANISOU 2390  N   ILE A 341     5640   9093  18649    251   1252   -622       N  
ATOM   2391  CA  ILE A 341     -18.076   0.763  36.385  1.00 96.98           C  
ANISOU 2391  CA  ILE A 341     6294   9971  20583    533   1183   -244       C  
ATOM   2392  C   ILE A 341     -16.562   0.766  36.223  1.00111.07           C  
ANISOU 2392  C   ILE A 341     7635  11928  22640    602   1221   -249       C  
ATOM   2393  O   ILE A 341     -15.816   0.478  37.168  1.00107.82           O  
ANISOU 2393  O   ILE A 341     6844  11663  22461    697   1004    286       O  
ATOM   2394  CB  ILE A 341     -18.713  -0.458  35.697  1.00102.57           C  
ANISOU 2394  CB  ILE A 341     6916  10084  21971    748   1414   -500       C  
ATOM   2395  CG1 ILE A 341     -20.192  -0.577  36.072  1.00 91.42           C  
ANISOU 2395  CG1 ILE A 341     5881   8504  20350    700   1329   -377       C  
ATOM   2396  CG2 ILE A 341     -17.964  -1.730  36.063  1.00107.04           C  
ANISOU 2396  CG2 ILE A 341     6958  10296  23416   1040   1409   -158       C  
ATOM   2397  CD1 ILE A 341     -20.905  -1.722  35.384  1.00 92.98           C  
ANISOU 2397  CD1 ILE A 341     6015   8132  21180    866   1570   -683       C  
ATOM   2398  N   THR A 342     -16.082   1.125  35.030  1.00112.35           N  
ANISOU 2398  N   THR A 342     7822  12128  22740    539   1491   -831       N  
ATOM   2399  CA  THR A 342     -14.642   1.119  34.796  1.00 99.17           C  
ANISOU 2399  CA  THR A 342     5724  10609  21348    603   1558   -883       C  
ATOM   2400  C   THR A 342     -13.943   2.243  35.557  1.00 98.20           C  
ANISOU 2400  C   THR A 342     5621  11060  20632    388   1319   -598       C  
ATOM   2401  O   THR A 342     -12.812   2.065  36.028  1.00101.80           O  
ANISOU 2401  O   THR A 342     5635  11688  21357    472   1210   -309       O  
ATOM   2402  CB  THR A 342     -14.356   1.215  33.298  1.00 99.42           C  
ANISOU 2402  CB  THR A 342     5821  10574  21381    556   1915  -1596       C  
ATOM   2403  OG1 THR A 342     -15.151   0.247  32.602  1.00 99.98           O  
ANISOU 2403  OG1 THR A 342     6043  10174  21773    661   2106  -1907       O  
ATOM   2404  CG2 THR A 342     -12.885   0.936  33.019  1.00122.18           C  
ANISOU 2404  CG2 THR A 342     8385  13508  24531    648   1975  -1636       C  
ATOM   2405  N   ASN A 343     -14.594   3.402  35.698  1.00 94.80           N  
ANISOU 2405  N   ASN A 343     5668  10928  19423    103   1248   -681       N  
ATOM   2406  CA  ASN A 343     -14.007   4.479  36.492  1.00 93.15           C  
ANISOU 2406  CA  ASN A 343     5474  11247  18673   -139   1045   -457       C  
ATOM   2407  C   ASN A 343     -13.861   4.072  37.954  1.00104.26           C  
ANISOU 2407  C   ASN A 343     6612  12838  20164    -89    706    205       C  
ATOM   2408  O   ASN A 343     -12.838   4.361  38.586  1.00109.41           O  
ANISOU 2408  O   ASN A 343     6943  13892  20738   -162    543    463       O  
ATOM   2409  CB  ASN A 343     -14.851   5.748  36.370  1.00 92.22           C  
ANISOU 2409  CB  ASN A 343     5904  11325  17812   -447   1079   -685       C  
ATOM   2410  CG  ASN A 343     -14.551   6.525  35.107  1.00 99.49           C  
ANISOU 2410  CG  ASN A 343     6983  12313  18506   -580   1361  -1211       C  
ATOM   2411  OD1 ASN A 343     -13.727   7.440  35.108  1.00108.05           O  
ANISOU 2411  OD1 ASN A 343     8013  13740  19303   -770   1374  -1286       O  
ATOM   2412  ND2 ASN A 343     -15.212   6.159  34.018  1.00100.92           N  
ANISOU 2412  ND2 ASN A 343     7336  12201  18809   -499   1592  -1571       N  
ATOM   2413  N   ILE A 344     -14.876   3.408  38.512  1.00121.10           N  
ANISOU 2413  N   ILE A 344     8853  14726  22434     17    592    504       N  
ATOM   2414  CA  ILE A 344     -14.781   2.919  39.885  1.00114.85           C  
ANISOU 2414  CA  ILE A 344     7765  14135  21737     71    270   1194       C  
ATOM   2415  C   ILE A 344     -13.707   1.843  39.993  1.00122.38           C  
ANISOU 2415  C   ILE A 344     8078  14954  23469    372    236   1544       C  
ATOM   2416  O   ILE A 344     -12.989   1.762  40.997  1.00140.16           O  
ANISOU 2416  O   ILE A 344     9937  17604  25714    361    -29   2093       O  
ATOM   2417  CB  ILE A 344     -16.154   2.415  40.367  1.00126.31           C  
ANISOU 2417  CB  ILE A 344     9476  15321  23194    122    188   1427       C  
ATOM   2418  CG1 ILE A 344     -17.152   3.573  40.443  1.00108.07           C  
ANISOU 2418  CG1 ILE A 344     7750  13212  20099   -194    195   1155       C  
ATOM   2419  CG2 ILE A 344     -16.037   1.737  41.724  1.00124.61           C  
ANISOU 2419  CG2 ILE A 344     8886  15301  23157    208   -129   2204       C  
ATOM   2420  CD1 ILE A 344     -16.731   4.683  41.381  1.00107.87           C  
ANISOU 2420  CD1 ILE A 344     7743  13834  19407   -523     -2   1301       C  
ATOM   2421  N   MET A 345     -13.573   1.003  38.960  1.00115.34           N  
ANISOU 2421  N   MET A 345     7034  13519  23269    633    515   1228       N  
ATOM   2422  CA  MET A 345     -12.497   0.017  38.944  1.00118.61           C  
ANISOU 2422  CA  MET A 345     6987  13740  24341    906    536   1469       C  
ATOM   2423  C   MET A 345     -11.131   0.689  39.002  1.00112.87           C  
ANISOU 2423  C   MET A 345     5993  13505  23385    795    473   1462       C  
ATOM   2424  O   MET A 345     -10.237   0.240  39.729  1.00117.63           O  
ANISOU 2424  O   MET A 345     6238  14293  24163    903    282   1971       O  
ATOM   2425  CB  MET A 345     -12.599  -0.855  37.693  1.00114.32           C  
ANISOU 2425  CB  MET A 345     6545  12550  24341   1104    896    946       C  
ATOM   2426  CG  MET A 345     -13.732  -1.863  37.707  1.00124.24           C  
ANISOU 2426  CG  MET A 345     7969  13245  25991   1251    959   1024       C  
ATOM   2427  SD  MET A 345     -13.957  -2.634  36.092  1.00176.60           S  
ANISOU 2427  SD  MET A 345    14779  19249  33073   1332   1410    217       S  
ATOM   2428  CE  MET A 345     -12.280  -3.142  35.719  1.00146.84           C  
ANISOU 2428  CE  MET A 345    10606  15427  29758   1466   1523    185       C  
ATOM   2429  N   ALA A 346     -10.955   1.766  38.245  1.00109.42           N  
ANISOU 2429  N   ALA A 346     5729  13296  22551    569    639    905       N  
ATOM   2430  CA  ALA A 346      -9.683   2.481  38.154  1.00113.15           C  
ANISOU 2430  CA  ALA A 346     5985  14212  22795    434    627    803       C  
ATOM   2431  C   ALA A 346      -9.310   3.232  39.434  1.00121.57           C  
ANISOU 2431  C   ALA A 346     6896  15951  23345    187    278   1276       C  
ATOM   2432  O   ALA A 346      -8.296   3.944  39.408  1.00146.83           O  
ANISOU 2432  O   ALA A 346     9925  19568  26297     22    262   1165       O  
ATOM   2433  CB  ALA A 346      -9.721   3.456  36.977  1.00111.35           C  
ANISOU 2433  CB  ALA A 346     6089  14025  22193    224    917     82       C  
ATOM   2434  N   VAL A 347     -10.051   3.121  40.535  1.00111.18           N  
ANISOU 2434  N   VAL A 347     5665  14797  21780    124      8   1758       N  
ATOM   2435  CA  VAL A 347      -9.767   3.867  41.760  1.00112.01           C  
ANISOU 2435  CA  VAL A 347     5688  15619  21252   -175   -311   2131       C  
ATOM   2436  C   VAL A 347      -9.207   2.957  42.852  1.00131.23           C  
ANISOU 2436  C   VAL A 347     7600  18281  23979      1   -613   2915       C  
ATOM   2437  O   VAL A 347      -8.104   3.182  43.353  1.00154.63           O  
ANISOU 2437  O   VAL A 347    10255  21743  26756    -83   -771   3124       O  
ATOM   2438  CB  VAL A 347     -11.019   4.627  42.252  1.00107.52           C  
ANISOU 2438  CB  VAL A 347     5684  15196  19973   -465   -380   2028       C  
ATOM   2439  CG1 VAL A 347     -10.753   5.261  43.607  1.00109.31           C  
ANISOU 2439  CG1 VAL A 347     5759  16189  19584   -788   -698   2406       C  
ATOM   2440  CG2 VAL A 347     -11.429   5.682  41.238  1.00104.22           C  
ANISOU 2440  CG2 VAL A 347     5809  14634  19156   -668    -92   1301       C  
ATOM   2441  N   ILE A 348      -9.955   1.922  43.234  1.00119.17           N  
ANISOU 2441  N   ILE A 348     6099  16380  22800    239   -683   3324       N  
ATOM   2442  CA  ILE A 348      -9.576   1.119  44.395  1.00140.04           C  
ANISOU 2442  CA  ILE A 348     8427  19255  25528    360   -973   4104       C  
ATOM   2443  C   ILE A 348      -8.439   0.163  44.052  1.00170.87           C  
ANISOU 2443  C   ILE A 348    11980  22851  30093    687   -885   4272       C  
ATOM   2444  O   ILE A 348      -7.385   0.172  44.699  1.00177.46           O  
ANISOU 2444  O   ILE A 348    12466  24156  30803    654  -1078   4647       O  
ATOM   2445  CB  ILE A 348     -10.797   0.366  44.955  1.00146.12           C  
ANISOU 2445  CB  ILE A 348     9355  19725  26438    471  -1061   4516       C  
ATOM   2446  CG1 ILE A 348     -11.780   1.354  45.589  1.00144.59           C  
ANISOU 2446  CG1 ILE A 348     9440  20009  25488     97  -1215   4469       C  
ATOM   2447  CG2 ILE A 348     -10.360  -0.684  45.966  1.00143.96           C  
ANISOU 2447  CG2 ILE A 348     8745  19532  26423    653  -1284   5345       C  
ATOM   2448  CD1 ILE A 348     -12.951   0.697  46.286  1.00130.51           C  
ANISOU 2448  CD1 ILE A 348     7791  18054  23745    163  -1337   4922       C  
ATOM   2449  N   CYS A 349      -8.628  -0.675  43.033  1.00195.13           N  
ANISOU 2449  N   CYS A 349    14180  32332  27628  -2168  -4462  -1271       N  
ATOM   2450  CA  CYS A 349      -7.608  -1.659  42.665  1.00205.29           C  
ANISOU 2450  CA  CYS A 349    14860  33286  29853  -1915  -4600   -994       C  
ATOM   2451  C   CYS A 349      -6.624  -1.067  41.654  1.00199.04           C  
ANISOU 2451  C   CYS A 349    13984  32148  29497  -1947  -4284  -1415       C  
ATOM   2452  O   CYS A 349      -6.414  -1.576  40.554  1.00200.42           O  
ANISOU 2452  O   CYS A 349    14013  31881  30255  -1767  -3900  -1530       O  
ATOM   2453  CB  CYS A 349      -8.256  -2.937  42.139  1.00208.14           C  
ANISOU 2453  CB  CYS A 349    15020  33310  30752  -1649  -4430   -734       C  
ATOM   2454  SG  CYS A 349      -9.154  -2.815  40.570  1.00228.61           S  
ANISOU 2454  SG  CYS A 349    18009  35361  33489  -1618  -3667  -1329       S  
ATOM   2455  N   LYS A 350      -5.992   0.033  42.062  1.00168.46           N  
ANISOU 2455  N   LYS A 350    10227  28519  25263  -2187  -4433  -1636       N  
ATOM   2456  CA  LYS A 350      -4.997   0.671  41.211  1.00164.46           C  
ANISOU 2456  CA  LYS A 350     9626  27764  25097  -2253  -4165  -1957       C  
ATOM   2457  C   LYS A 350      -3.697  -0.120  41.136  1.00173.73           C  
ANISOU 2457  C   LYS A 350    10138  28839  27031  -2070  -4382  -1596       C  
ATOM   2458  O   LYS A 350      -2.821   0.238  40.340  1.00177.36           O  
ANISOU 2458  O   LYS A 350    10463  29121  27806  -2084  -4106  -1814       O  
ATOM   2459  CB  LYS A 350      -4.723   2.093  41.703  1.00158.03           C  
ANISOU 2459  CB  LYS A 350     9100  27225  23718  -2581  -4273  -2293       C  
ATOM   2460  CG  LYS A 350      -4.848   3.148  40.616  1.00153.42           C  
ANISOU 2460  CG  LYS A 350     8888  26368  23037  -2715  -3710  -2831       C  
ATOM   2461  CD  LYS A 350      -4.823   4.553  41.194  1.00149.71           C  
ANISOU 2461  CD  LYS A 350     8742  26151  21991  -3037  -3812  -3168       C  
ATOM   2462  CE  LYS A 350      -5.033   5.593  40.105  1.00145.14           C  
ANISOU 2462  CE  LYS A 350     8513  25274  21358  -3152  -3257  -3641       C  
ATOM   2463  NZ  LYS A 350      -5.079   6.976  40.654  1.00145.85           N  
ANISOU 2463  NZ  LYS A 350     8908  25552  20956  -3457  -3330  -3988       N  
ATOM   2464  N   GLU A 351      -3.550  -1.173  41.936  1.00180.17           N  
ANISOU 2464  N   GLU A 351    10530  29791  28138  -1887  -4855  -1031       N  
ATOM   2465  CA  GLU A 351      -2.359  -2.013  41.936  1.00177.42           C  
ANISOU 2465  CA  GLU A 351     9503  29511  28396  -1688  -5045   -587       C  
ATOM   2466  C   GLU A 351      -2.633  -3.449  41.517  1.00178.87           C  
ANISOU 2466  C   GLU A 351     9440  29553  28971  -1261  -4824   -465       C  
ATOM   2467  O   GLU A 351      -1.810  -4.050  40.823  1.00184.98           O  
ANISOU 2467  O   GLU A 351     9913  29967  30402   -987  -4595   -541       O  
ATOM   2468  CB  GLU A 351      -1.710  -2.004  43.332  1.00177.61           C  
ANISOU 2468  CB  GLU A 351     9305  29631  28547  -1677  -5821   -371       C  
ATOM   2469  CG  GLU A 351      -0.474  -2.884  43.463  1.00186.49           C  
ANISOU 2469  CG  GLU A 351     9715  31491  29652  -1313  -5838   -493       C  
ATOM   2470  CD  GLU A 351       0.696  -2.384  42.636  1.00186.25           C  
ANISOU 2470  CD  GLU A 351     9416  31456  29897  -1504  -5566   -330       C  
ATOM   2471  OE1 GLU A 351       0.729  -1.178  42.312  1.00191.34           O  
ANISOU 2471  OE1 GLU A 351    10374  31794  30532  -1896  -5491   -432       O  
ATOM   2472  OE2 GLU A 351       1.585  -3.199  42.310  1.00190.86           O  
ANISOU 2472  OE2 GLU A 351     9507  31862  31148  -1154  -5522   -304       O  
ATOM   2473  N   SER A 352      -3.776  -4.015  41.908  1.00196.80           N  
ANISOU 2473  N   SER A 352    11893  31820  31063  -1169  -4912   -324       N  
ATOM   2474  CA  SER A 352      -4.097  -5.410  41.636  1.00204.91           C  
ANISOU 2474  CA  SER A 352    12800  32272  32784   -777  -4822    -54       C  
ATOM   2475  C   SER A 352      -5.053  -5.577  40.458  1.00214.65           C  
ANISOU 2475  C   SER A 352    14396  32954  34205   -742  -4232   -406       C  
ATOM   2476  O   SER A 352      -5.760  -6.588  40.381  1.00215.89           O  
ANISOU 2476  O   SER A 352    14578  32700  34750   -533  -4190   -163       O  
ATOM   2477  CB  SER A 352      -4.679  -6.069  42.887  1.00207.93           C  
ANISOU 2477  CB  SER A 352    13190  32813  32999   -705  -5350    595       C  
ATOM   2478  OG  SER A 352      -5.862  -5.411  43.309  1.00199.90           O  
ANISOU 2478  OG  SER A 352    12632  32102  31221   -984  -5386    532       O  
ATOM   2479  N   CYS A 353      -5.091  -4.612  39.542  1.00206.33           N  
ANISOU 2479  N   CYS A 353    13669  31824  32905   -939  -3781   -963       N  
ATOM   2480  CA  CYS A 353      -5.931  -4.686  38.354  1.00199.52           C  
ANISOU 2480  CA  CYS A 353    13199  30485  32125   -898  -3200  -1415       C  
ATOM   2481  C   CYS A 353      -5.112  -4.281  37.138  1.00206.43           C  
ANISOU 2481  C   CYS A 353    14103  31091  33242   -868  -2723  -1899       C  
ATOM   2482  O   CYS A 353      -4.432  -3.251  37.160  1.00199.07           O  
ANISOU 2482  O   CYS A 353    13201  30415  32023  -1075  -2735  -2052       O  
ATOM   2483  CB  CYS A 353      -7.162  -3.781  38.484  1.00190.65           C  
ANISOU 2483  CB  CYS A 353    12624  29588  30227  -1186  -3099  -1639       C  
ATOM   2484  SG  CYS A 353      -8.496  -4.431  39.524  1.00204.55           S  
ANISOU 2484  SG  CYS A 353    14430  31555  31737  -1185  -3459  -1189       S  
ATOM   2485  N   ASN A 354      -5.176  -5.092  36.085  1.00222.88           N  
ANISOU 2485  N   ASN A 354    16173  32648  35865   -620  -2313  -2143       N  
ATOM   2486  CA  ASN A 354      -4.511  -4.744  34.837  1.00227.00           C  
ANISOU 2486  CA  ASN A 354    16748  32947  36556   -590  -1820  -2634       C  
ATOM   2487  C   ASN A 354      -5.212  -3.557  34.186  1.00223.35           C  
ANISOU 2487  C   ASN A 354    16851  32597  35415   -872  -1466  -3063       C  
ATOM   2488  O   ASN A 354      -6.442  -3.474  34.174  1.00224.51           O  
ANISOU 2488  O   ASN A 354    17385  32734  35187   -965  -1385  -3133       O  
ATOM   2489  CB  ASN A 354      -4.500  -5.942  33.888  1.00231.53           C  
ANISOU 2489  CB  ASN A 354    17193  32943  37834   -266  -1478  -2843       C  
ATOM   2490  CG  ASN A 354      -3.817  -5.636  32.569  1.00233.70           C  
ANISOU 2490  CG  ASN A 354    17506  33045  38246   -232   -961  -3368       C  
ATOM   2491  OD1 ASN A 354      -4.465  -5.245  31.598  1.00233.56           O  
ANISOU 2491  OD1 ASN A 354    17901  32937  37905   -339   -538  -3806       O  
ATOM   2492  ND2 ASN A 354      -2.501  -5.814  32.528  1.00237.81           N  
ANISOU 2492  ND2 ASN A 354    17580  33553  39225    -86  -1000  -3306       N  
ATOM   2493  N   GLU A 355      -4.421  -2.629  33.649  1.00208.81           N  
ANISOU 2493  N   GLU A 355    15043  30859  33438  -1005  -1259  -3321       N  
ATOM   2494  CA  GLU A 355      -4.961  -1.394  33.086  1.00206.77           C  
ANISOU 2494  CA  GLU A 355    15295  30702  32566  -1269   -958  -3668       C  
ATOM   2495  C   GLU A 355      -4.287  -1.060  31.762  1.00175.55           C  
ANISOU 2495  C   GLU A 355    11357  26585  28759  -1245   -472  -4058       C  
ATOM   2496  O   GLU A 355      -4.035   0.108  31.450  1.00159.05           O  
ANISOU 2496  O   GLU A 355     9459  24643  26327  -1467   -325  -4229       O  
ATOM   2497  CB  GLU A 355      -4.821  -0.234  34.071  1.00219.89           C  
ANISOU 2497  CB  GLU A 355    17051  32754  33743  -1561  -1300  -3529       C  
ATOM   2498  CG  GLU A 355      -5.779  -0.304  35.252  1.00222.71           C  
ANISOU 2498  CG  GLU A 355    17556  33345  33719  -1650  -1695  -3253       C  
ATOM   2499  CD  GLU A 355      -5.512   0.770  36.287  1.00207.19           C  
ANISOU 2499  CD  GLU A 355    15648  31768  31305  -1928  -2065  -3174       C  
ATOM   2500  OE1 GLU A 355      -4.328   1.017  36.599  1.00214.10           O  
ANISOU 2500  OE1 GLU A 355    16173  32771  32402  -1980  -2286  -3069       O  
ATOM   2501  OE2 GLU A 355      -6.487   1.371  36.787  1.00182.87           O  
ANISOU 2501  OE2 GLU A 355    12964  28870  27647  -2096  -2128  -3243       O  
ATOM   2502  N   ASP A 356      -3.984  -2.083  30.962  1.00166.23           N  
ANISOU 2502  N   ASP A 356     9964  25092  28104   -979   -212  -4212       N  
ATOM   2503  CA  ASP A 356      -3.427  -1.844  29.634  1.00167.68           C  
ANISOU 2503  CA  ASP A 356    10173  25159  28379   -955    279  -4612       C  
ATOM   2504  C   ASP A 356      -4.530  -1.553  28.621  1.00146.58           C  
ANISOU 2504  C   ASP A 356     8027  22403  25263  -1048    684  -4976       C  
ATOM   2505  O   ASP A 356      -4.581  -0.467  28.034  1.00136.91           O  
ANISOU 2505  O   ASP A 356     7088  21331  23600  -1257    917  -5153       O  
ATOM   2506  CB  ASP A 356      -2.586  -3.046  29.192  1.00178.88           C  
ANISOU 2506  CB  ASP A 356    11132  26288  30546   -631    399  -4684       C  
ATOM   2507  CG  ASP A 356      -1.315  -3.198  30.006  1.00171.29           C  
ANISOU 2507  CG  ASP A 356     9615  25450  30020   -541     49  -4335       C  
ATOM   2508  OD1 ASP A 356      -1.413  -3.408  31.234  1.00181.06           O  
ANISOU 2508  OD1 ASP A 356    10691  26823  31281   -542   -446  -3906       O  
ATOM   2509  OD2 ASP A 356      -0.217  -3.110  29.418  1.00160.13           O  
ANISOU 2509  OD2 ASP A 356     7907  24032  28902   -477    260  -4474       O  
ATOM   2510  N   VAL A 357      -5.429  -2.516  28.410  1.00161.51           N  
ANISOU 2510  N   VAL A 357    10032  24052  27280   -902    752  -5069       N  
ATOM   2511  CA  VAL A 357      -6.548  -2.317  27.496  1.00177.32           C  
ANISOU 2511  CA  VAL A 357    12514  26010  28850   -999   1087  -5391       C  
ATOM   2512  C   VAL A 357      -7.800  -1.829  28.218  1.00175.16           C  
ANISOU 2512  C   VAL A 357    12619  25889  28045  -1171    876  -5195       C  
ATOM   2513  O   VAL A 357      -8.718  -1.311  27.566  1.00177.22           O  
ANISOU 2513  O   VAL A 357    13309  26205  27821  -1307   1114  -5397       O  
ATOM   2514  CB  VAL A 357      -6.847  -3.615  26.723  1.00186.93           C  
ANISOU 2514  CB  VAL A 357    13649  26868  30506   -775   1320  -5688       C  
ATOM   2515  CG1 VAL A 357      -7.651  -3.324  25.461  1.00178.08           C  
ANISOU 2515  CG1 VAL A 357    12955  25771  28939   -897   1732  -6114       C  
ATOM   2516  CG2 VAL A 357      -5.552  -4.336  26.380  1.00171.61           C  
ANISOU 2516  CG2 VAL A 357    11226  24731  29248   -540   1425  -5803       C  
ATOM   2517  N   ILE A 358      -7.859  -1.968  29.545  1.00196.17           N  
ANISOU 2517  N   ILE A 358    15118  28655  30764  -1173    430  -4794       N  
ATOM   2518  CA  ILE A 358      -9.021  -1.499  30.295  1.00206.78           C  
ANISOU 2518  CA  ILE A 358    16796  30183  31586  -1339    233  -4614       C  
ATOM   2519  C   ILE A 358      -9.142   0.017  30.197  1.00185.99           C  
ANISOU 2519  C   ILE A 358    14518  27804  28345  -1598    333  -4721       C  
ATOM   2520  O   ILE A 358     -10.250   0.565  30.142  1.00185.97           O  
ANISOU 2520  O   ILE A 358    14929  27887  27846  -1729    419  -4778       O  
ATOM   2521  CB  ILE A 358      -8.941  -1.981  31.757  1.00214.44           C  
ANISOU 2521  CB  ILE A 358    17469  31278  32732  -1297   -288  -4151       C  
ATOM   2522  CG1 ILE A 358      -9.115  -3.502  31.818  1.00217.25           C  
ANISOU 2522  CG1 ILE A 358    17525  31312  33707  -1039   -371  -4011       C  
ATOM   2523  CG2 ILE A 358      -9.985  -1.288  32.620  1.00210.56           C  
ANISOU 2523  CG2 ILE A 358    17309  31076  31620  -1504   -493  -3991       C  
ATOM   2524  CD1 ILE A 358      -9.407  -4.040  33.204  1.00219.57           C  
ANISOU 2524  CD1 ILE A 358    17587  31740  34098  -1009   -877  -3496       C  
ATOM   2525  N   GLY A 359      -8.007   0.717  30.160  1.00124.11           N  
ANISOU 2525  N   GLY A 359     6503  20069  20583  -1672    329  -4745       N  
ATOM   2526  CA  GLY A 359      -8.048   2.155  29.947  1.00121.66           C  
ANISOU 2526  CA  GLY A 359     6494  19924  19806  -1913    460  -4872       C  
ATOM   2527  C   GLY A 359      -8.670   2.528  28.615  1.00118.55           C  
ANISOU 2527  C   GLY A 359     6462  19446  19134  -1955    916  -5166       C  
ATOM   2528  O   GLY A 359      -9.361   3.544  28.503  1.00115.17           O  
ANISOU 2528  O   GLY A 359     6400  19120  18237  -2130   1011  -5220       O  
ATOM   2529  N   ALA A 360      -8.435   1.711  27.586  1.00126.32           N  
ANISOU 2529  N   ALA A 360     7334  20256  20408  -1796   1195  -5364       N  
ATOM   2530  CA  ALA A 360      -9.053   1.949  26.287  1.00117.87           C  
ANISOU 2530  CA  ALA A 360     6589  19158  19038  -1845   1594  -5640       C  
ATOM   2531  C   ALA A 360     -10.540   1.620  26.284  1.00131.30           C  
ANISOU 2531  C   ALA A 360     8633  20826  20430  -1847   1595  -5654       C  
ATOM   2532  O   ALA A 360     -11.268   2.113  25.416  1.00130.69           O  
ANISOU 2532  O   ALA A 360     8892  20805  19958  -1948   1842  -5805       O  
ATOM   2533  CB  ALA A 360      -8.337   1.139  25.205  1.00122.53           C  
ANISOU 2533  CB  ALA A 360     6942  19611  20004  -1691   1884  -5905       C  
ATOM   2534  N   LEU A 361     -11.003   0.797  27.229  1.00143.54           N  
ANISOU 2534  N   LEU A 361    10077  22302  22158  -1746   1311  -5464       N  
ATOM   2535  CA  LEU A 361     -12.428   0.491  27.313  1.00110.52           C  
ANISOU 2535  CA  LEU A 361     6187  18103  17703  -1765   1296  -5437       C  
ATOM   2536  C   LEU A 361     -13.240   1.739  27.633  1.00116.95           C  
ANISOU 2536  C   LEU A 361     7385  19132  17920  -1961   1274  -5344       C  
ATOM   2537  O   LEU A 361     -14.363   1.906  27.140  1.00138.67           O  
ANISOU 2537  O   LEU A 361    10462  21906  20321  -2019   1423  -5415       O  
ATOM   2538  CB  LEU A 361     -12.673  -0.590  28.366  1.00111.96           C  
ANISOU 2538  CB  LEU A 361     6121  18184  18233  -1637    969  -5179       C  
ATOM   2539  CG  LEU A 361     -12.029  -1.957  28.129  1.00116.35           C  
ANISOU 2539  CG  LEU A 361     6272  18448  19488  -1408    971  -5250       C  
ATOM   2540  CD1 LEU A 361     -12.322  -2.894  29.291  1.00117.98           C  
ANISOU 2540  CD1 LEU A 361     6222  18567  20038  -1304    595  -4888       C  
ATOM   2541  CD2 LEU A 361     -12.511  -2.557  26.819  1.00116.26           C  
ANISOU 2541  CD2 LEU A 361     6392  18236  19544  -1356   1331  -5653       C  
ATOM   2542  N   LEU A 362     -12.691   2.625  28.468  1.00128.91           N  
ANISOU 2542  N   LEU A 362     8846  20800  19333  -2068   1082  -5200       N  
ATOM   2543  CA  LEU A 362     -13.388   3.865  28.791  1.00129.24           C  
ANISOU 2543  CA  LEU A 362     9222  21012  18872  -2248   1081  -5170       C  
ATOM   2544  C   LEU A 362     -13.584   4.739  27.562  1.00131.57           C  
ANISOU 2544  C   LEU A 362     9782  21300  18908  -2348   1433  -5356       C  
ATOM   2545  O   LEU A 362     -14.585   5.458  27.467  1.00134.47           O  
ANISOU 2545  O   LEU A 362    10471  21741  18880  -2445   1513  -5348       O  
ATOM   2546  CB  LEU A 362     -12.625   4.631  29.871  1.00127.62           C  
ANISOU 2546  CB  LEU A 362     8869  20960  18663  -2362    810  -5063       C  
ATOM   2547  CG  LEU A 362     -12.930   4.175  31.295  1.00128.35           C  
ANISOU 2547  CG  LEU A 362     8848  21199  18719  -2347    414  -4831       C  
ATOM   2548  CD1 LEU A 362     -12.177   5.018  32.310  1.00130.63           C  
ANISOU 2548  CD1 LEU A 362     9015  21688  18930  -2496    134  -4787       C  
ATOM   2549  CD2 LEU A 362     -14.425   4.249  31.528  1.00124.79           C  
ANISOU 2549  CD2 LEU A 362     8729  20832  17853  -2380    449  -4791       C  
ATOM   2550  N   ASN A 363     -12.652   4.681  26.607  1.00113.81           N  
ANISOU 2550  N   ASN A 363     7377  18985  16880  -2324   1642  -5500       N  
ATOM   2551  CA  ASN A 363     -12.743   5.517  25.417  1.00123.48           C  
ANISOU 2551  CA  ASN A 363     8810  20252  17857  -2438   1955  -5620       C  
ATOM   2552  C   ASN A 363     -13.956   5.182  24.557  1.00108.68           C  
ANISOU 2552  C   ASN A 363     7224  18378  15690  -2421   2129  -5702       C  
ATOM   2553  O   ASN A 363     -14.388   6.027  23.767  1.00107.72           O  
ANISOU 2553  O   ASN A 363     7336  18340  15251  -2542   2315  -5707       O  
ATOM   2554  CB  ASN A 363     -11.463   5.391  24.594  1.00123.85           C  
ANISOU 2554  CB  ASN A 363     8585  20271  18200  -2414   2144  -5744       C  
ATOM   2555  CG  ASN A 363     -10.239   5.863  25.354  1.00121.58           C  
ANISOU 2555  CG  ASN A 363     7995  20004  18195  -2465   1975  -5647       C  
ATOM   2556  OD1 ASN A 363      -9.273   5.120  25.522  1.00131.38           O  
ANISOU 2556  OD1 ASN A 363     8878  21188  19852  -2343   1902  -5658       O  
ATOM   2557  ND2 ASN A 363     -10.278   7.106  25.823  1.00112.62           N  
ANISOU 2557  ND2 ASN A 363     6982  18944  16866  -2650   1904  -5561       N  
ATOM   2558  N   VAL A 364     -14.510   3.977  24.682  1.00101.03           N  
ANISOU 2558  N   VAL A 364     6219  17322  14847  -2288   2057  -5745       N  
ATOM   2559  CA  VAL A 364     -15.758   3.648  24.003  1.00116.22           C  
ANISOU 2559  CA  VAL A 364     8404  19263  16492  -2298   2169  -5819       C  
ATOM   2560  C   VAL A 364     -16.946   3.611  24.962  1.00102.93           C  
ANISOU 2560  C   VAL A 364     6889  17604  14616  -2302   1969  -5623       C  
ATOM   2561  O   VAL A 364     -18.094   3.787  24.518  1.00 93.58           O  
ANISOU 2561  O   VAL A 364     5968  16483  13103  -2357   2045  -5612       O  
ATOM   2562  CB  VAL A 364     -15.641   2.314  23.239  1.00104.40           C  
ANISOU 2562  CB  VAL A 364     6745  17643  15279  -2180   2287  -6079       C  
ATOM   2563  CG1 VAL A 364     -14.772   2.487  22.009  1.00104.02           C  
ANISOU 2563  CG1 VAL A 364     6615  17653  15254  -2213   2560  -6311       C  
ATOM   2564  CG2 VAL A 364     -15.088   1.230  24.140  1.00103.46           C  
ANISOU 2564  CG2 VAL A 364     6285  17337  15690  -2013   2087  -6036       C  
ATOM   2565  N   PHE A 365     -16.712   3.407  26.259  1.00 96.29           N  
ANISOU 2565  N   PHE A 365     5885  16749  13950  -2255   1706  -5449       N  
ATOM   2566  CA  PHE A 365     -17.803   3.502  27.220  1.00 97.85           C  
ANISOU 2566  CA  PHE A 365     6234  17035  13909  -2284   1530  -5249       C  
ATOM   2567  C   PHE A 365     -18.330   4.929  27.312  1.00104.77           C  
ANISOU 2567  C   PHE A 365     7390  18058  14359  -2424   1595  -5205       C  
ATOM   2568  O   PHE A 365     -19.538   5.142  27.477  1.00121.99           O  
ANISOU 2568  O   PHE A 365     9793  20314  16243  -2456   1599  -5117       O  
ATOM   2569  CB  PHE A 365     -17.340   3.000  28.587  1.00103.15           C  
ANISOU 2569  CB  PHE A 365     6635  17729  14828  -2229   1210  -5056       C  
ATOM   2570  CG  PHE A 365     -17.013   1.531  28.618  1.00104.71           C  
ANISOU 2570  CG  PHE A 365     6524  17744  15516  -2076   1113  -5032       C  
ATOM   2571  CD1 PHE A 365     -17.458   0.684  27.616  1.00 98.98           C  
ANISOU 2571  CD1 PHE A 365     5825  16847  14937  -2010   1305  -5215       C  
ATOM   2572  CD2 PHE A 365     -16.262   0.998  29.654  1.00101.09           C  
ANISOU 2572  CD2 PHE A 365     5723  17288  15398  -2007    814  -4834       C  
ATOM   2573  CE1 PHE A 365     -17.158  -0.667  27.643  1.00101.26           C  
ANISOU 2573  CE1 PHE A 365     5801  16910  15763  -1867   1232  -5239       C  
ATOM   2574  CE2 PHE A 365     -15.961  -0.353  29.685  1.00103.97           C  
ANISOU 2574  CE2 PHE A 365     5762  17441  16302  -1851    719  -4783       C  
ATOM   2575  CZ  PHE A 365     -16.409  -1.184  28.680  1.00104.07           C  
ANISOU 2575  CZ  PHE A 365     5803  17223  16517  -1776    943  -5003       C  
ATOM   2576  N   VAL A 366     -17.441   5.919  27.190  1.00 93.34           N  
ANISOU 2576  N   VAL A 366     5908  16636  12921  -2513   1654  -5266       N  
ATOM   2577  CA  VAL A 366     -17.878   7.311  27.182  1.00106.31           C  
ANISOU 2577  CA  VAL A 366     7776  18361  14257  -2654   1743  -5251       C  
ATOM   2578  C   VAL A 366     -18.777   7.577  25.980  1.00102.22           C  
ANISOU 2578  C   VAL A 366     7508  17839  13491  -2680   1969  -5254       C  
ATOM   2579  O   VAL A 366     -19.767   8.311  26.075  1.00113.78           O  
ANISOU 2579  O   VAL A 366     9186  19360  14683  -2739   2002  -5169       O  
ATOM   2580  CB  VAL A 366     -16.660   8.258  27.215  1.00109.23           C  
ANISOU 2580  CB  VAL A 366     8006  18720  14777  -2765   1767  -5317       C  
ATOM   2581  CG1 VAL A 366     -15.742   8.022  26.021  1.00107.77           C  
ANISOU 2581  CG1 VAL A 366     7692  18460  14797  -2746   1963  -5403       C  
ATOM   2582  CG2 VAL A 366     -17.113   9.705  27.266  1.00107.52           C  
ANISOU 2582  CG2 VAL A 366     7980  18540  14334  -2923   1861  -5316       C  
ATOM   2583  N   TRP A 367     -18.467   6.968  24.834  1.00108.18           N  
ANISOU 2583  N   TRP A 367     8218  18549  14335  -2641   2117  -5355       N  
ATOM   2584  CA  TRP A 367     -19.306   7.173  23.660  1.00107.13           C  
ANISOU 2584  CA  TRP A 367     8299  18475  13931  -2687   2289  -5347       C  
ATOM   2585  C   TRP A 367     -20.595   6.365  23.721  1.00115.13           C  
ANISOU 2585  C   TRP A 367     9436  19507  14801  -2626   2218  -5312       C  
ATOM   2586  O   TRP A 367     -21.595   6.767  23.122  1.00119.74           O  
ANISOU 2586  O   TRP A 367    10220  20174  15102  -2678   2283  -5225       O  
ATOM   2587  CB  TRP A 367     -18.514   6.864  22.393  1.00111.55           C  
ANISOU 2587  CB  TRP A 367     8753  19052  14580  -2699   2478  -5504       C  
ATOM   2588  CG  TRP A 367     -17.626   8.005  22.031  1.00132.65           C  
ANISOU 2588  CG  TRP A 367    11374  21755  17273  -2811   2608  -5448       C  
ATOM   2589  CD1 TRP A 367     -16.315   8.166  22.371  1.00144.48           C  
ANISOU 2589  CD1 TRP A 367    12633  23197  19065  -2819   2605  -5501       C  
ATOM   2590  CD2 TRP A 367     -17.996   9.177  21.295  1.00131.26           C  
ANISOU 2590  CD2 TRP A 367    11354  21666  16853  -2939   2756  -5288       C  
ATOM   2591  NE1 TRP A 367     -15.842   9.357  21.878  1.00146.14           N  
ANISOU 2591  NE1 TRP A 367    12845  23450  19233  -2960   2755  -5403       N  
ATOM   2592  CE2 TRP A 367     -16.854   9.995  21.211  1.00140.29           C  
ANISOU 2592  CE2 TRP A 367    12342  22788  18174  -3031   2857  -5259       C  
ATOM   2593  CE3 TRP A 367     -19.180   9.607  20.690  1.00126.13           C  
ANISOU 2593  CE3 TRP A 367    10927  21112  15885  -2982   2808  -5133       C  
ATOM   2594  CZ2 TRP A 367     -16.860  11.220  20.547  1.00130.38           C  
ANISOU 2594  CZ2 TRP A 367    11145  21586  16807  -3171   3027  -5074       C  
ATOM   2595  CZ3 TRP A 367     -19.184  10.823  20.031  1.00118.05           C  
ANISOU 2595  CZ3 TRP A 367     9958  20151  14745  -3101   2966  -4933       C  
ATOM   2596  CH2 TRP A 367     -18.033  11.614  19.965  1.00114.62           C  
ANISOU 2596  CH2 TRP A 367     9364  19676  14510  -3197   3084  -4901       C  
ATOM   2597  N   ILE A 368     -20.606   5.243  24.442  1.00111.39           N  
ANISOU 2597  N   ILE A 368     8817  18959  14547  -2522   2076  -5341       N  
ATOM   2598  CA  ILE A 368     -21.878   4.588  24.744  1.00103.29           C  
ANISOU 2598  CA  ILE A 368     7886  17949  13412  -2488   1992  -5251       C  
ATOM   2599  C   ILE A 368     -22.755   5.513  25.583  1.00 89.43           C  
ANISOU 2599  C   ILE A 368     6304  16296  11379  -2532   1917  -5038       C  
ATOM   2600  O   ILE A 368     -23.958   5.673  25.323  1.00 98.82           O  
ANISOU 2600  O   ILE A 368     7671  17553  12323  -2555   1946  -4936       O  
ATOM   2601  CB  ILE A 368     -21.636   3.239  25.446  1.00 98.88           C  
ANISOU 2601  CB  ILE A 368     7082  17268  13222  -2380   1842  -5263       C  
ATOM   2602  CG1 ILE A 368     -20.902   2.274  24.512  1.00 91.79           C  
ANISOU 2602  CG1 ILE A 368     5995  16239  12643  -2324   1957  -5539       C  
ATOM   2603  CG2 ILE A 368     -22.950   2.631  25.909  1.00103.64           C  
ANISOU 2603  CG2 ILE A 368     7750  17888  13738  -2371   1744  -5110       C  
ATOM   2604  CD1 ILE A 368     -20.603   0.925  25.131  1.00 92.38           C  
ANISOU 2604  CD1 ILE A 368     5773  16125  13201  -2206   1813  -5546       C  
ATOM   2605  N   GLY A 369     -22.161   6.149  26.595  1.00 84.38           N  
ANISOU 2605  N   GLY A 369     5593  15687  10781  -2552   1822  -4994       N  
ATOM   2606  CA  GLY A 369     -22.900   7.131  27.375  1.00 98.32           C  
ANISOU 2606  CA  GLY A 369     7499  17567  12291  -2609   1790  -4882       C  
ATOM   2607  C   GLY A 369     -23.379   8.302  26.535  1.00104.53           C  
ANISOU 2607  C   GLY A 369     8487  18356  12874  -2684   1963  -4856       C  
ATOM   2608  O   GLY A 369     -24.458   8.850  26.770  1.00120.40           O  
ANISOU 2608  O   GLY A 369    10644  20428  14675  -2693   1983  -4740       O  
ATOM   2609  N   TYR A 370     -22.573   8.711  25.554  1.00109.31           N  
ANISOU 2609  N   TYR A 370     9071  18901  13563  -2736   2093  -4931       N  
ATOM   2610  CA  TYR A 370     -22.999   9.751  24.621  1.00109.08           C  
ANISOU 2610  CA  TYR A 370     9190  18881  13374  -2812   2253  -4831       C  
ATOM   2611  C   TYR A 370     -24.175   9.285  23.765  1.00112.51           C  
ANISOU 2611  C   TYR A 370     9761  19384  13604  -2776   2282  -4721       C  
ATOM   2612  O   TYR A 370     -25.114  10.051  23.521  1.00107.21           O  
ANISOU 2612  O   TYR A 370     9221  18753  12760  -2794   2334  -4543       O  
ATOM   2613  CB  TYR A 370     -21.828  10.174  23.734  1.00114.37           C  
ANISOU 2613  CB  TYR A 370     9764  19517  14175  -2888   2393  -4896       C  
ATOM   2614  CG  TYR A 370     -20.748  10.949  24.457  1.00129.93           C  
ANISOU 2614  CG  TYR A 370    11595  21423  16350  -2967   2382  -4975       C  
ATOM   2615  CD1 TYR A 370     -21.016  11.601  25.654  1.00119.52           C  
ANISOU 2615  CD1 TYR A 370    10287  20103  15021  -3007   2290  -4998       C  
ATOM   2616  CD2 TYR A 370     -19.460  11.032  23.941  1.00131.18           C  
ANISOU 2616  CD2 TYR A 370    11585  21546  16709  -3019   2466  -5053       C  
ATOM   2617  CE1 TYR A 370     -20.031  12.312  26.319  1.00116.30           C  
ANISOU 2617  CE1 TYR A 370     9730  19656  14803  -3115   2257  -5121       C  
ATOM   2618  CE2 TYR A 370     -18.469  11.740  24.598  1.00135.20           C  
ANISOU 2618  CE2 TYR A 370    11939  21998  17431  -3114   2436  -5124       C  
ATOM   2619  CZ  TYR A 370     -18.761  12.379  25.786  1.00134.41           C  
ANISOU 2619  CZ  TYR A 370    11858  21892  17321  -3171   2318  -5168       C  
ATOM   2620  OH  TYR A 370     -17.781  13.084  26.446  1.00124.70           O  
ANISOU 2620  OH  TYR A 370    10458  20617  16304  -3297   2260  -5282       O  
ATOM   2621  N   LEU A 371     -24.131   8.040  23.284  1.00 98.10           N  
ANISOU 2621  N   LEU A 371     7872  17572  11827  -2732   2254  -4839       N  
ATOM   2622  CA  LEU A 371     -25.223   7.511  22.470  1.00100.46           C  
ANISOU 2622  CA  LEU A 371     8262  17969  11941  -2734   2265  -4795       C  
ATOM   2623  C   LEU A 371     -26.508   7.385  23.282  1.00110.99           C  
ANISOU 2623  C   LEU A 371     9681  19326  13166  -2684   2156  -4630       C  
ATOM   2624  O   LEU A 371     -27.613   7.381  22.716  1.00108.01           O  
ANISOU 2624  O   LEU A 371     9392  19049  12599  -2699   2163  -4511       O  
ATOM   2625  CB  LEU A 371     -24.817   6.158  21.876  1.00 83.34           C  
ANISOU 2625  CB  LEU A 371     5963  15793   9909  -2718   2276  -5050       C  
ATOM   2626  CG  LEU A 371     -25.835   5.431  20.997  1.00 83.63           C  
ANISOU 2626  CG  LEU A 371     6038  15957   9780  -2760   2285  -5117       C  
ATOM   2627  CD1 LEU A 371     -26.243   6.297  19.816  1.00 84.23           C  
ANISOU 2627  CD1 LEU A 371     6220  16235   9550  -2857   2382  -5000       C  
ATOM   2628  CD2 LEU A 371     -25.256   4.108  20.525  1.00 85.85           C  
ANISOU 2628  CD2 LEU A 371     6143  16191  10285  -2751   2325  -5468       C  
ATOM   2629  N   SER A 372     -26.378   7.252  24.604  1.00108.40           N  
ANISOU 2629  N   SER A 372     9295  18946  12944  -2633   2055  -4611       N  
ATOM   2630  CA  SER A 372     -27.558   7.310  25.462  1.00 83.52           C  
ANISOU 2630  CA  SER A 372     6214  15859   9662  -2594   1982  -4433       C  
ATOM   2631  C   SER A 372     -28.339   8.601  25.242  1.00 88.97           C  
ANISOU 2631  C   SER A 372     7051  16589  10164  -2608   2067  -4264       C  
ATOM   2632  O   SER A 372     -29.564   8.622  25.407  1.00101.01           O  
ANISOU 2632  O   SER A 372     8644  18181  11556  -2567   2051  -4093       O  
ATOM   2633  CB  SER A 372     -27.155   7.177  26.933  1.00 90.61           C  
ANISOU 2633  CB  SER A 372     7003  16778  10647  -2565   1875  -4442       C  
ATOM   2634  OG  SER A 372     -26.496   8.344  27.397  1.00 83.67           O  
ANISOU 2634  OG  SER A 372     6128  15904   9757  -2612   1913  -4510       O  
ATOM   2635  N   SER A 373     -27.650   9.685  24.871  1.00 94.46           N  
ANISOU 2635  N   SER A 373     7765  17234  10891  -2661   2172  -4289       N  
ATOM   2636  CA  SER A 373     -28.337  10.932  24.544  1.00103.37           C  
ANISOU 2636  CA  SER A 373     8989  18364  11923  -2667   2287  -4106       C  
ATOM   2637  C   SER A 373     -29.215  10.780  23.305  1.00 95.16           C  
ANISOU 2637  C   SER A 373     8004  17425  10728  -2663   2323  -3930       C  
ATOM   2638  O   SER A 373     -30.365  11.236  23.290  1.00 79.83           O  
ANISOU 2638  O   SER A 373     6117  15534   8682  -2610   2348  -3720       O  
ATOM   2639  CB  SER A 373     -27.315  12.051  24.340  1.00111.02           C  
ANISOU 2639  CB  SER A 373     9919  19245  13021  -2753   2415  -4164       C  
ATOM   2640  OG  SER A 373     -26.528  12.243  25.502  1.00113.13           O  
ANISOU 2640  OG  SER A 373    10103  19463  13418  -2787   2368  -4363       O  
ATOM   2641  N   ALA A 374     -28.691  10.138  22.259  1.00101.55           N  
ANISOU 2641  N   ALA A 374     8773  18299  11513  -2722   2334  -4033       N  
ATOM   2642  CA  ALA A 374     -29.428   9.968  21.012  1.00102.82           C  
ANISOU 2642  CA  ALA A 374     8951  18642  11473  -2759   2363  -3924       C  
ATOM   2643  C   ALA A 374     -30.531   8.926  21.106  1.00 84.51           C  
ANISOU 2643  C   ALA A 374     6628  16419   9062  -2735   2242  -3930       C  
ATOM   2644  O   ALA A 374     -31.449   8.940  20.279  1.00 79.79           O  
ANISOU 2644  O   ALA A 374     6032  16013   8271  -2769   2243  -3801       O  
ATOM   2645  CB  ALA A 374     -28.476   9.576  19.882  1.00102.30           C  
ANISOU 2645  CB  ALA A 374     8821  18670  11379  -2851   2434  -4103       C  
ATOM   2646  N   VAL A 375     -30.453   8.020  22.080  1.00 81.36           N  
ANISOU 2646  N   VAL A 375     6191  15921   8801  -2692   2144  -4061       N  
ATOM   2647  CA  VAL A 375     -31.416   6.921  22.139  1.00 97.61           C  
ANISOU 2647  CA  VAL A 375     8206  18056  10825  -2696   2052  -4075       C  
ATOM   2648  C   VAL A 375     -32.819   7.426  22.475  1.00 89.13           C  
ANISOU 2648  C   VAL A 375     7182  17063   9621  -2643   2028  -3780       C  
ATOM   2649  O   VAL A 375     -33.815   6.906  21.956  1.00 80.87           O  
ANISOU 2649  O   VAL A 375     6094  16168   8464  -2685   1984  -3724       O  
ATOM   2650  CB  VAL A 375     -30.934   5.848  23.131  1.00 99.19           C  
ANISOU 2650  CB  VAL A 375     8312  18122  11253  -2659   1977  -4223       C  
ATOM   2651  CG1 VAL A 375     -32.070   4.917  23.518  1.00 91.55           C  
ANISOU 2651  CG1 VAL A 375     7286  17198  10300  -2659   1895  -4133       C  
ATOM   2652  CG2 VAL A 375     -29.799   5.053  22.512  1.00101.34           C  
ANISOU 2652  CG2 VAL A 375     8479  18335  11690  -2702   2014  -4538       C  
ATOM   2653  N   ASN A 376     -32.926   8.442  23.336  1.00 76.45           N  
ANISOU 2653  N   ASN A 376     5637  15372   8038  -2556   2068  -3618       N  
ATOM   2654  CA  ASN A 376     -34.237   8.864  23.835  1.00 76.08           C  
ANISOU 2654  CA  ASN A 376     5609  15382   7916  -2472   2072  -3364       C  
ATOM   2655  C   ASN A 376     -35.220   9.252  22.732  1.00 76.98           C  
ANISOU 2655  C   ASN A 376     5704  15665   7879  -2487   2103  -3163       C  
ATOM   2656  O   ASN A 376     -36.376   8.790  22.779  1.00 98.56           O  
ANISOU 2656  O   ASN A 376     8381  18518  10550  -2473   2045  -3026       O  
ATOM   2657  CB  ASN A 376     -34.060  10.007  24.843  1.00 75.87           C  
ANISOU 2657  CB  ASN A 376     5635  15245   7948  -2384   2159  -3311       C  
ATOM   2658  CG  ASN A 376     -32.986   9.719  25.873  1.00 81.38           C  
ANISOU 2658  CG  ASN A 376     6315  15861   8747  -2403   2116  -3528       C  
ATOM   2659  OD1 ASN A 376     -32.091  10.533  26.094  1.00 99.55           O  
ANISOU 2659  OD1 ASN A 376     8629  18077  11120  -2427   2183  -3646       O  
ATOM   2660  ND2 ASN A 376     -33.070   8.556  26.507  1.00 75.28           N  
ANISOU 2660  ND2 ASN A 376     5475  15134   7993  -2408   2009  -3568       N  
ATOM   2661  N   PRO A 377     -34.863  10.081  21.742  1.00 78.03           N  
ANISOU 2661  N   PRO A 377     5849  15855   7946  -2525   2195  -3102       N  
ATOM   2662  CA  PRO A 377     -35.833  10.381  20.674  1.00 79.47           C  
ANISOU 2662  CA  PRO A 377     5966  16284   7945  -2553   2210  -2875       C  
ATOM   2663  C   PRO A 377     -36.302   9.150  19.919  1.00 82.88           C  
ANISOU 2663  C   PRO A 377     6318  16956   8217  -2680   2085  -3006       C  
ATOM   2664  O   PRO A 377     -37.440   9.130  19.431  1.00 90.12           O  
ANISOU 2664  O   PRO A 377     7144  18112   8986  -2703   2040  -2820       O  
ATOM   2665  CB  PRO A 377     -35.061  11.344  19.762  1.00 92.30           C  
ANISOU 2665  CB  PRO A 377     7599  17946   9525  -2603   2342  -2805       C  
ATOM   2666  CG  PRO A 377     -34.051  11.966  20.651  1.00100.64           C  
ANISOU 2666  CG  PRO A 377     8722  18713  10802  -2554   2429  -2910       C  
ATOM   2667  CD  PRO A 377     -33.634  10.882  21.590  1.00 90.18           C  
ANISOU 2667  CD  PRO A 377     7425  17267   9571  -2550   2303  -3182       C  
ATOM   2668  N   LEU A 378     -35.459   8.121  19.805  1.00 82.65           N  
ANISOU 2668  N   LEU A 378     6286  16883   8233  -2772   2039  -3345       N  
ATOM   2669  CA  LEU A 378     -35.893   6.882  19.167  1.00 91.36           C  
ANISOU 2669  CA  LEU A 378     7287  18193   9234  -2912   1952  -3557       C  
ATOM   2670  C   LEU A 378     -37.045   6.247  19.935  1.00 85.76           C  
ANISOU 2670  C   LEU A 378     6514  17468   8602  -2881   1859  -3439       C  
ATOM   2671  O   LEU A 378     -38.039   5.821  19.339  1.00 85.93           O  
ANISOU 2671  O   LEU A 378     6424  17743   8482  -2982   1791  -3400       O  
ATOM   2672  CB  LEU A 378     -34.722   5.909  19.050  1.00 90.73           C  
ANISOU 2672  CB  LEU A 378     7187  18002   9285  -2984   1966  -3969       C  
ATOM   2673  CG  LEU A 378     -35.020   4.588  18.337  1.00 83.76           C  
ANISOU 2673  CG  LEU A 378     6170  17302   8352  -3146   1924  -4304       C  
ATOM   2674  CD1 LEU A 378     -35.332   4.825  16.866  1.00 86.38           C  
ANISOU 2674  CD1 LEU A 378     6439  18059   8321  -3307   1942  -4365       C  
ATOM   2675  CD2 LEU A 378     -33.862   3.615  18.495  1.00 84.30           C  
ANISOU 2675  CD2 LEU A 378     6187  17161   8680  -3160   1969  -4707       C  
ATOM   2676  N   VAL A 379     -36.939   6.191  21.265  1.00 83.06           N  
ANISOU 2676  N   VAL A 379     6220  16871   8469  -2761   1855  -3367       N  
ATOM   2677  CA  VAL A 379     -38.031   5.655  22.077  1.00 96.97           C  
ANISOU 2677  CA  VAL A 379     7909  18627  10307  -2729   1789  -3194       C  
ATOM   2678  C   VAL A 379     -39.267   6.536  21.954  1.00103.19           C  
ANISOU 2678  C   VAL A 379     8667  19573  10969  -2656   1805  -2851       C  
ATOM   2679  O   VAL A 379     -40.401   6.040  21.869  1.00101.06           O  
ANISOU 2679  O   VAL A 379     8273  19450  10675  -2703   1734  -2717       O  
ATOM   2680  CB  VAL A 379     -37.584   5.509  23.543  1.00 90.82           C  
ANISOU 2680  CB  VAL A 379     7171  17622   9715  -2624   1797  -3167       C  
ATOM   2681  CG1 VAL A 379     -38.694   4.893  24.385  1.00 78.49           C  
ANISOU 2681  CG1 VAL A 379     5511  16088   8224  -2608   1747  -2954       C  
ATOM   2682  CG2 VAL A 379     -36.321   4.673  23.623  1.00113.52           C  
ANISOU 2682  CG2 VAL A 379    10025  20350  12757  -2679   1781  -3470       C  
ATOM   2683  N   TYR A 380     -39.065   7.858  21.940  1.00100.35           N  
ANISOU 2683  N   TYR A 380     8386  19170  10572  -2541   1908  -2698       N  
ATOM   2684  CA  TYR A 380     -40.193   8.777  21.820  1.00 96.73           C  
ANISOU 2684  CA  TYR A 380     7860  18836  10058  -2441   1959  -2361       C  
ATOM   2685  C   TYR A 380     -40.961   8.542  20.523  1.00102.06           C  
ANISOU 2685  C   TYR A 380     8388  19860  10529  -2573   1876  -2270       C  
ATOM   2686  O   TYR A 380     -42.199   8.534  20.517  1.00 99.08           O  
ANISOU 2686  O   TYR A 380     7869  19648  10128  -2549   1831  -2029       O  
ATOM   2687  CB  TYR A 380     -39.699  10.222  21.902  1.00 88.30           C  
ANISOU 2687  CB  TYR A 380     6871  17636   9044  -2318   2119  -2250       C  
ATOM   2688  CG  TYR A 380     -38.982  10.567  23.190  1.00 78.47           C  
ANISOU 2688  CG  TYR A 380     5743  16111   7961  -2215   2197  -2374       C  
ATOM   2689  CD1 TYR A 380     -39.189   9.826  24.347  1.00 77.59           C  
ANISOU 2689  CD1 TYR A 380     5641  15935   7906  -2181   2141  -2436       C  
ATOM   2690  CD2 TYR A 380     -38.098  11.636  23.248  1.00 84.86           C  
ANISOU 2690  CD2 TYR A 380     6627  16767   8851  -2177   2330  -2423       C  
ATOM   2691  CE1 TYR A 380     -38.533  10.139  25.523  1.00 76.92           C  
ANISOU 2691  CE1 TYR A 380     5637  15691   7897  -2113   2199  -2559       C  
ATOM   2692  CE2 TYR A 380     -37.439  11.957  24.419  1.00 93.34           C  
ANISOU 2692  CE2 TYR A 380     7780  17647  10039  -2119   2387  -2585       C  
ATOM   2693  CZ  TYR A 380     -37.660  11.205  25.553  1.00 82.17           C  
ANISOU 2693  CZ  TYR A 380     6375  16223   8622  -2087   2312  -2660       C  
ATOM   2694  OH  TYR A 380     -37.005  11.521  26.720  1.00 93.02           O  
ANISOU 2694  OH  TYR A 380     7804  17494  10044  -2053   2356  -2832       O  
ATOM   2695  N   THR A 381     -40.241   8.341  19.417  1.00 99.91           N  
ANISOU 2695  N   THR A 381     8125  19749  10089  -2725   1856  -2468       N  
ATOM   2696  CA  THR A 381     -40.873   8.027  18.142  1.00104.12           C  
ANISOU 2696  CA  THR A 381     8502  20714  10345  -2900   1764  -2449       C  
ATOM   2697  C   THR A 381     -41.423   6.605  18.100  1.00104.93           C  
ANISOU 2697  C   THR A 381     8492  20932  10444  -3063   1627  -2674       C  
ATOM   2698  O   THR A 381     -42.344   6.328  17.325  1.00111.54           O  
ANISOU 2698  O   THR A 381     9155  22141  11085  -3203   1521  -2604       O  
ATOM   2699  CB  THR A 381     -39.870   8.223  16.999  1.00108.91           C  
ANISOU 2699  CB  THR A 381     9145  21503  10733  -3028   1813  -2630       C  
ATOM   2700  OG1 THR A 381     -39.114   9.421  17.220  1.00111.43           O  
ANISOU 2700  OG1 THR A 381     9584  21596  11161  -2888   1961  -2464       O  
ATOM   2701  CG2 THR A 381     -40.589   8.314  15.656  1.00123.59           C  
ANISOU 2701  CG2 THR A 381    10826  23919  12213  -3195   1739  -2501       C  
ATOM   2702  N   LEU A 382     -40.876   5.694  18.903  1.00101.16           N  
ANISOU 2702  N   LEU A 382     8083  20155  10198  -3062   1624  -2928       N  
ATOM   2703  CA  LEU A 382     -41.364   4.322  18.891  1.00 96.22           C  
ANISOU 2703  CA  LEU A 382     7331  19563   9664  -3222   1516  -3128       C  
ATOM   2704  C   LEU A 382     -42.676   4.163  19.649  1.00114.93           C  
ANISOU 2704  C   LEU A 382     9593  21903  12172  -3167   1442  -2797       C  
ATOM   2705  O   LEU A 382     -43.502   3.327  19.268  1.00139.32           O  
ANISOU 2705  O   LEU A 382    12521  25141  15274  -3333   1318  -2834       O  
ATOM   2706  CB  LEU A 382     -40.308   3.380  19.470  1.00104.59           C  
ANISOU 2706  CB  LEU A 382     8455  20295  10989  -3233   1547  -3462       C  
ATOM   2707  CG  LEU A 382     -39.165   2.993  18.528  1.00102.44           C  
ANISOU 2707  CG  LEU A 382     8198  20091  10634  -3355   1607  -3915       C  
ATOM   2708  CD1 LEU A 382     -38.119   2.166  19.261  1.00 90.05           C  
ANISOU 2708  CD1 LEU A 382     6656  18148   9412  -3308   1645  -4175       C  
ATOM   2709  CD2 LEU A 382     -39.694   2.242  17.314  1.00 95.06           C  
ANISOU 2709  CD2 LEU A 382     7102  19508   9508  -3602   1541  -4197       C  
ATOM   2710  N   PHE A 383     -42.893   4.941  20.709  1.00119.06           N  
ANISOU 2710  N   PHE A 383    10188  22241  12809  -2949   1520  -2495       N  
ATOM   2711  CA  PHE A 383     -44.059   4.733  21.563  1.00127.07           C  
ANISOU 2711  CA  PHE A 383    11091  23219  13969  -2884   1490  -2201       C  
ATOM   2712  C   PHE A 383     -45.070   5.871  21.528  1.00125.39           C  
ANISOU 2712  C   PHE A 383    10798  23166  13677  -2733   1537  -1822       C  
ATOM   2713  O   PHE A 383     -46.252   5.630  21.262  1.00130.08           O  
ANISOU 2713  O   PHE A 383    11197  23961  14268  -2792   1446  -1620       O  
ATOM   2714  CB  PHE A 383     -43.603   4.476  23.006  1.00115.47           C  
ANISOU 2714  CB  PHE A 383     9717  21444  12713  -2765   1561  -2185       C  
ATOM   2715  CG  PHE A 383     -42.994   3.117  23.210  1.00123.12           C  
ANISOU 2715  CG  PHE A 383    10656  22251  13872  -2913   1491  -2438       C  
ATOM   2716  CD1 PHE A 383     -41.636   2.917  23.026  1.00115.05           C  
ANISOU 2716  CD1 PHE A 383     9742  21090  12882  -2936   1519  -2760       C  
ATOM   2717  CD2 PHE A 383     -43.782   2.037  23.574  1.00135.23           C  
ANISOU 2717  CD2 PHE A 383    12024  23745  15611  -3029   1399  -2334       C  
ATOM   2718  CE1 PHE A 383     -41.073   1.667  23.208  1.00117.37           C  
ANISOU 2718  CE1 PHE A 383     9968  21200  13429  -3049   1463  -2983       C  
ATOM   2719  CE2 PHE A 383     -43.226   0.783  23.758  1.00144.58           C  
ANISOU 2719  CE2 PHE A 383    13148  24722  17065  -3164   1331  -2537       C  
ATOM   2720  CZ  PHE A 383     -41.869   0.599  23.574  1.00138.21           C  
ANISOU 2720  CZ  PHE A 383    12439  23767  16309  -3162   1365  -2868       C  
ATOM   2721  N   ASN A 384     -44.650   7.107  21.789  1.00113.85           N  
ANISOU 2721  N   ASN A 384     9455  21603  12200  -2541   1680  -1717       N  
ATOM   2722  CA  ASN A 384     -45.596   8.212  21.924  1.00 95.10           C  
ANISOU 2722  CA  ASN A 384     6977  19305   9851  -2357   1771  -1360       C  
ATOM   2723  C   ASN A 384     -46.154   8.602  20.558  1.00105.50           C  
ANISOU 2723  C   ASN A 384     8119  20990  10977  -2446   1686  -1189       C  
ATOM   2724  O   ASN A 384     -45.404   9.029  19.675  1.00112.74           O  
ANISOU 2724  O   ASN A 384     9094  22014  11726  -2513   1698  -1274       O  
ATOM   2725  CB  ASN A 384     -44.916   9.403  22.592  1.00102.04           C  
ANISOU 2725  CB  ASN A 384     8015  19933  10821  -2147   1971  -1349       C  
ATOM   2726  CG  ASN A 384     -45.897  10.489  23.010  1.00103.48           C  
ANISOU 2726  CG  ASN A 384     8075  20119  11124  -1920   2126  -1030       C  
ATOM   2727  OD1 ASN A 384     -46.840  10.811  22.286  1.00107.14           O  
ANISOU 2727  OD1 ASN A 384     8326  20824  11557  -1908   2090   -757       O  
ATOM   2728  ND2 ASN A 384     -45.673  11.062  24.186  1.00106.21           N  
ANISOU 2728  ND2 ASN A 384     8528  20223  11604  -1741   2305  -1076       N  
ATOM   2729  N   LYS A 385     -47.479   8.492  20.407  1.00121.06           N  
ANISOU 2729  N   LYS A 385     9851  23184  12964  -2449   1603   -913       N  
ATOM   2730  CA  LYS A 385     -48.118   8.683  19.106  1.00106.92           C  
ANISOU 2730  CA  LYS A 385     7837  21836  10951  -2575   1462   -724       C  
ATOM   2731  C   LYS A 385     -47.920  10.100  18.578  1.00105.38           C  
ANISOU 2731  C   LYS A 385     7611  21736  10693  -2429   1584   -459       C  
ATOM   2732  O   LYS A 385     -47.634  10.293  17.389  1.00115.76           O  
ANISOU 2732  O   LYS A 385     8863  23392  11727  -2576   1504   -427       O  
ATOM   2733  CB  LYS A 385     -49.609   8.361  19.212  1.00117.38           C  
ANISOU 2733  CB  LYS A 385     8886  23344  12368  -2579   1345   -437       C  
ATOM   2734  CG  LYS A 385     -50.240   7.850  17.927  1.00137.36           C  
ANISOU 2734  CG  LYS A 385    11185  26366  14641  -2841   1089   -390       C  
ATOM   2735  CD  LYS A 385     -49.818   6.417  17.644  1.00142.25           C  
ANISOU 2735  CD  LYS A 385    11878  26988  15182  -3141    945   -836       C  
ATOM   2736  CE  LYS A 385     -50.601   5.825  16.482  1.00134.55           C  
ANISOU 2736  CE  LYS A 385    10661  26489  13973  -3423    679   -838       C  
ATOM   2737  NZ  LYS A 385     -50.274   4.388  16.267  1.00125.07           N  
ANISOU 2737  NZ  LYS A 385     9523  25209  12791  -3707    560  -1317       N  
ATOM   2738  N   THR A 386     -48.085  11.105  19.442  1.00 97.56           N  
ANISOU 2738  N   THR A 386     6640  20469   9961  -2149   1794   -261       N  
ATOM   2739  CA  THR A 386     -47.905  12.487  19.009  1.00 96.14           C  
ANISOU 2739  CA  THR A 386     6398  20315   9816  -2001   1947     14       C  
ATOM   2740  C   THR A 386     -46.475  12.731  18.547  1.00117.33           C  
ANISOU 2740  C   THR A 386     9308  22905  12368  -2101   2012   -219       C  
ATOM   2741  O   THR A 386     -46.244  13.446  17.563  1.00121.69           O  
ANISOU 2741  O   THR A 386     9775  23688  12775  -2144   2032      4       O  
ATOM   2742  CB  THR A 386     -48.276  13.449  20.138  1.00101.83           C  
ANISOU 2742  CB  THR A 386     7096  20707  10889  -1689   2206    160       C  
ATOM   2743  OG1 THR A 386     -47.438  13.203  21.274  1.00112.55           O  
ANISOU 2743  OG1 THR A 386     8738  21673  12355  -1645   2326   -209       O  
ATOM   2744  CG2 THR A 386     -49.733  13.263  20.540  1.00113.88           C  
ANISOU 2744  CG2 THR A 386     8365  22348  12557  -1574   2167    418       C  
ATOM   2745  N   TYR A 387     -45.502  12.145  19.249  1.00122.95           N  
ANISOU 2745  N   TYR A 387    10286  23296  13133  -2141   2043   -627       N  
ATOM   2746  CA  TYR A 387     -44.113  12.225  18.810  1.00103.84           C  
ANISOU 2746  CA  TYR A 387     8062  20785  10609  -2249   2084   -878       C  
ATOM   2747  C   TYR A 387     -43.944  11.611  17.425  1.00111.61           C  
ANISOU 2747  C   TYR A 387     8976  22200  11231  -2507   1918   -953       C  
ATOM   2748  O   TYR A 387     -43.282  12.190  16.556  1.00119.99           O  
ANISOU 2748  O   TYR A 387    10055  23407  12129  -2576   1976   -887       O  
ATOM   2749  CB  TYR A 387     -43.203  11.529  19.823  1.00 90.09           C  
ANISOU 2749  CB  TYR A 387     6556  18678   8994  -2252   2096  -1277       C  
ATOM   2750  CG  TYR A 387     -42.735  12.406  20.965  1.00 91.55           C  
ANISOU 2750  CG  TYR A 387     6867  18483   9434  -2055   2297  -1302       C  
ATOM   2751  CD1 TYR A 387     -42.392  13.735  20.756  1.00 92.99           C  
ANISOU 2751  CD1 TYR A 387     7035  18578   9720  -1960   2491  -1144       C  
ATOM   2752  CD2 TYR A 387     -42.633  11.901  22.254  1.00 90.29           C  
ANISOU 2752  CD2 TYR A 387     6816  18090   9399  -1987   2301  -1487       C  
ATOM   2753  CE1 TYR A 387     -41.957  14.534  21.801  1.00 96.14           C  
ANISOU 2753  CE1 TYR A 387     7522  18655  10351  -1811   2688  -1240       C  
ATOM   2754  CE2 TYR A 387     -42.201  12.689  23.302  1.00 99.21           C  
ANISOU 2754  CE2 TYR A 387     8048  18953  10696  -1836   2475  -1561       C  
ATOM   2755  CZ  TYR A 387     -41.865  14.004  23.071  1.00 99.14           C  
ANISOU 2755  CZ  TYR A 387     8023  18849  10797  -1753   2669  -1473       C  
ATOM   2756  OH  TYR A 387     -41.437  14.787  24.117  1.00 84.30           O  
ANISOU 2756  OH  TYR A 387     6222  16722   9084  -1630   2853  -1619       O  
ATOM   2757  N   ARG A 388     -44.543  10.436  17.200  1.00144.35           N  
ANISOU 2757  N   ARG A 388    13026  26579  15240  -2670   1725  -1099       N  
ATOM   2758  CA  ARG A 388     -44.463   9.803  15.885  1.00131.46           C  
ANISOU 2758  CA  ARG A 388    11295  25429  13225  -2946   1575  -1244       C  
ATOM   2759  C   ARG A 388     -45.002  10.728  14.806  1.00134.31           C  
ANISOU 2759  C   ARG A 388    11443  26264  13325  -2972   1548   -802       C  
ATOM   2760  O   ARG A 388     -44.356  10.942  13.775  1.00139.81           O  
ANISOU 2760  O   ARG A 388    12149  27266  13707  -3117   1559   -830       O  
ATOM   2761  CB  ARG A 388     -45.247   8.489  15.864  1.00148.27           C  
ANISOU 2761  CB  ARG A 388    13294  27738  15305  -3125   1381  -1437       C  
ATOM   2762  CG  ARG A 388     -45.063   7.588  17.060  1.00153.13           C  
ANISOU 2762  CG  ARG A 388    14044  27903  16236  -3075   1396  -1701       C  
ATOM   2763  CD  ARG A 388     -46.090   6.467  17.044  1.00163.81           C  
ANISOU 2763  CD  ARG A 388    15217  29406  17618  -3238   1216  -1751       C  
ATOM   2764  NE  ARG A 388     -45.790   5.456  16.038  1.00157.69           N  
ANISOU 2764  NE  ARG A 388    14388  28914  16611  -3542   1096  -2158       N  
ATOM   2765  CZ  ARG A 388     -45.576   4.176  16.308  1.00153.34           C  
ANISOU 2765  CZ  ARG A 388    13868  28156  16239  -3680   1046  -2534       C  
ATOM   2766  NH1 ARG A 388     -45.661   3.707  17.542  1.00151.93           N  
ANISOU 2766  NH1 ARG A 388    13754  27537  16436  -3560   1079  -2487       N  
ATOM   2767  NH2 ARG A 388     -45.278   3.344  15.314  1.00164.20           N  
ANISOU 2767  NH2 ARG A 388    15189  29780  17419  -3947    968  -2960       N  
ATOM   2768  N   SER A 389     -46.196  11.282  15.029  1.00118.95           N  
ANISOU 2768  N   SER A 389     9280  24409  11508  -2827   1516   -358       N  
ATOM   2769  CA  SER A 389     -46.831  12.117  14.014  1.00123.79           C  
ANISOU 2769  CA  SER A 389     9623  25518  11896  -2844   1456    154       C  
ATOM   2770  C   SER A 389     -46.005  13.367  13.733  1.00120.53           C  
ANISOU 2770  C   SER A 389     9292  24985  11517  -2732   1670    403       C  
ATOM   2771  O   SER A 389     -45.770  13.722  12.571  1.00127.71           O  
ANISOU 2771  O   SER A 389    10109  26349  12068  -2879   1630    627       O  
ATOM   2772  CB  SER A 389     -48.245  12.493  14.457  1.00112.85           C  
ANISOU 2772  CB  SER A 389     7962  24165  10752  -2657   1399    595       C  
ATOM   2773  OG  SER A 389     -48.906  13.255  13.461  1.00108.72           O  
ANISOU 2773  OG  SER A 389     7122  24154  10032  -2667   1301   1158       O  
ATOM   2774  N   ALA A 390     -45.545  14.042  14.791  1.00103.66           N  
ANISOU 2774  N   ALA A 390     7322  22263   9801  -2494   1904    371       N  
ATOM   2775  CA  ALA A 390     -44.772  15.265  14.603  1.00117.74           C  
ANISOU 2775  CA  ALA A 390     9159  23875  11701  -2404   2130    604       C  
ATOM   2776  C   ALA A 390     -43.459  14.986  13.884  1.00130.18           C  
ANISOU 2776  C   ALA A 390    10941  25524  12998  -2614   2149    310       C  
ATOM   2777  O   ALA A 390     -43.074  15.727  12.972  1.00132.50           O  
ANISOU 2777  O   ALA A 390    11174  26054  13114  -2683   2218    630       O  
ATOM   2778  CB  ALA A 390     -44.511  15.937  15.950  1.00108.42           C  
ANISOU 2778  CB  ALA A 390     8099  22078  11017  -2152   2379    509       C  
ATOM   2779  N   PHE A 391     -42.761  13.917  14.273  1.00122.46           N  
ANISOU 2779  N   PHE A 391    10185  24351  11995  -2712   2093   -263       N  
ATOM   2780  CA  PHE A 391     -41.464  13.629  13.670  1.00114.27           C  
ANISOU 2780  CA  PHE A 391     9321  23335  10761  -2878   2133   -578       C  
ATOM   2781  C   PHE A 391     -41.613  13.147  12.232  1.00134.05           C  
ANISOU 2781  C   PHE A 391    11696  26514  12724  -3134   1981   -560       C  
ATOM   2782  O   PHE A 391     -40.765  13.446  11.383  1.00147.13           O  
ANISOU 2782  O   PHE A 391    13404  28349  14148  -3248   2059   -548       O  
ATOM   2783  CB  PHE A 391     -40.715  12.605  14.520  1.00100.13           C  
ANISOU 2783  CB  PHE A 391     7745  21153   9146  -2888   2110  -1152       C  
ATOM   2784  CG  PHE A 391     -40.418  13.082  15.914  1.00 91.50           C  
ANISOU 2784  CG  PHE A 391     6788  19481   8499  -2671   2249  -1195       C  
ATOM   2785  CD1 PHE A 391     -40.264  14.432  16.178  1.00101.35           C  
ANISOU 2785  CD1 PHE A 391     8016  20518   9973  -2528   2456   -888       C  
ATOM   2786  CD2 PHE A 391     -40.299  12.184  16.959  1.00 88.56           C  
ANISOU 2786  CD2 PHE A 391     6532  18812   8306  -2631   2181  -1538       C  
ATOM   2787  CE1 PHE A 391     -39.994  14.873  17.455  1.00104.19           C  
ANISOU 2787  CE1 PHE A 391     8477  20412  10698  -2361   2591   -997       C  
ATOM   2788  CE2 PHE A 391     -40.028  12.621  18.243  1.00 86.39           C  
ANISOU 2788  CE2 PHE A 391     6368  18098   8358  -2455   2295  -1583       C  
ATOM   2789  CZ  PHE A 391     -39.874  13.971  18.489  1.00 94.41           C  
ANISOU 2789  CZ  PHE A 391     7370  18937   9564  -2325   2499  -1347       C  
ATOM   2790  N   SER A 392     -42.677  12.396  11.938  1.00138.02           N  
ANISOU 2790  N   SER A 392    12012  27428  13001  -3247   1769   -568       N  
ATOM   2791  CA  SER A 392     -42.951  12.019  10.557  1.00131.74           C  
ANISOU 2791  CA  SER A 392    11041  27385  11628  -3520   1613   -535       C  
ATOM   2792  C   SER A 392     -43.291  13.244   9.719  1.00136.95           C  
ANISOU 2792  C   SER A 392    11525  28438  12073  -3493   1639    158       C  
ATOM   2793  O   SER A 392     -42.945  13.313   8.533  1.00148.36           O  
ANISOU 2793  O   SER A 392    12925  30413  13032  -3690   1603    239       O  
ATOM   2794  CB  SER A 392     -44.088  11.000  10.507  1.00130.44           C  
ANISOU 2794  CB  SER A 392    10667  27581  11314  -3670   1376   -681       C  
ATOM   2795  OG  SER A 392     -43.847   9.927  11.400  1.00135.97           O  
ANISOU 2795  OG  SER A 392    11515  27846  12301  -3669   1370  -1222       O  
ATOM   2796  N   ARG A 393     -43.970  14.223  10.321  1.00134.99           N  
ANISOU 2796  N   ARG A 393    11158  27941  12192  -3246   1709    682       N  
ATOM   2797  CA  ARG A 393     -44.253  15.470   9.618  1.00142.34           C  
ANISOU 2797  CA  ARG A 393    11894  29156  13032  -3187   1760   1423       C  
ATOM   2798  C   ARG A 393     -42.969  16.194   9.234  1.00157.74           C  
ANISOU 2798  C   ARG A 393    14037  30922  14975  -3208   1983   1480       C  
ATOM   2799  O   ARG A 393     -42.891  16.810   8.165  1.00168.98           O  
ANISOU 2799  O   ARG A 393    15348  32797  16060  -3309   1973   1962       O  
ATOM   2800  CB  ARG A 393     -45.138  16.367  10.482  1.00138.54           C  
ANISOU 2800  CB  ARG A 393    11233  28325  13082  -2881   1845   1901       C  
ATOM   2801  CG  ARG A 393     -46.596  16.380  10.062  1.00140.96           C  
ANISOU 2801  CG  ARG A 393    11144  29160  13254  -2872   1607   2406       C  
ATOM   2802  CD  ARG A 393     -47.469  17.165  11.034  1.00139.91           C  
ANISOU 2802  CD  ARG A 393    10822  28605  13734  -2524   1713   2788       C  
ATOM   2803  NE  ARG A 393     -46.787  18.322  11.604  1.00148.78           N  
ANISOU 2803  NE  ARG A 393    12057  29150  15324  -2303   2044   2956       N  
ATOM   2804  CZ  ARG A 393     -46.530  19.445  10.947  1.00172.18           C  
ANISOU 2804  CZ  ARG A 393    14956  32119  18345  -2245   2129   3543       C  
ATOM   2805  NH1 ARG A 393     -46.845  19.587   9.669  1.00185.62           N  
ANISOU 2805  NH1 ARG A 393    16482  34447  19599  -2393   1917   4061       N  
ATOM   2806  NH2 ARG A 393     -45.935  20.449  11.587  1.00184.15           N  
ANISOU 2806  NH2 ARG A 393    16601  32982  20387  -2043   2416   3612       N  
ATOM   2807  N   TYR A 394     -41.951  16.135  10.093  1.00148.32           N  
ANISOU 2807  N   TYR A 394    13116  29088  14151  -3123   2174   1030       N  
ATOM   2808  CA  TYR A 394     -40.693  16.821   9.834  1.00146.86           C  
ANISOU 2808  CA  TYR A 394    13086  28677  14036  -3150   2399   1065       C  
ATOM   2809  C   TYR A 394     -39.787  16.058   8.876  1.00134.26           C  
ANISOU 2809  C   TYR A 394    11613  27428  11973  -3393   2348    674       C  
ATOM   2810  O   TYR A 394     -38.747  16.592   8.475  1.00135.58           O  
ANISOU 2810  O   TYR A 394    11872  27504  12137  -3442   2526    741       O  
ATOM   2811  CB  TYR A 394     -39.956  17.078  11.153  1.00131.15           C  
ANISOU 2811  CB  TYR A 394    11290  25914  12624  -2981   2607    742       C  
ATOM   2812  CG  TYR A 394     -40.815  17.703  12.238  1.00140.50           C  
ANISOU 2812  CG  TYR A 394    12363  26736  14283  -2734   2682    970       C  
ATOM   2813  CD1 TYR A 394     -41.845  18.581  11.924  1.00136.86           C  
ANISOU 2813  CD1 TYR A 394    11616  26497  13886  -2628   2686   1646       C  
ATOM   2814  CD2 TYR A 394     -40.597  17.408  13.577  1.00136.08           C  
ANISOU 2814  CD2 TYR A 394    11960  25636  14108  -2598   2748    528       C  
ATOM   2815  CE1 TYR A 394     -42.630  19.148  12.908  1.00130.84           C  
ANISOU 2815  CE1 TYR A 394    10714  25404  13596  -2375   2783   1826       C  
ATOM   2816  CE2 TYR A 394     -41.379  17.970  14.569  1.00126.79           C  
ANISOU 2816  CE2 TYR A 394    10674  24170  13330  -2370   2842    686       C  
ATOM   2817  CZ  TYR A 394     -42.394  18.840  14.229  1.00125.11           C  
ANISOU 2817  CZ  TYR A 394    10163  24163  13209  -2251   2875   1310       C  
ATOM   2818  OH  TYR A 394     -43.173  19.402  15.214  1.00105.25           O  
ANISOU 2818  OH  TYR A 394     7503  21359  11126  -1994   3000   1438       O  
ATOM   2819  N   ILE A 395     -40.153  14.839   8.500  1.00139.37           N  
ANISOU 2819  N   ILE A 395    12231  28470  12255  -3554   2131    261       N  
ATOM   2820  CA  ILE A 395     -39.329  14.011   7.642  1.00144.99           C  
ANISOU 2820  CA  ILE A 395    13025  29498  12567  -3780   2101   -210       C  
ATOM   2821  C   ILE A 395     -39.908  14.025   6.231  1.00158.13           C  
ANISOU 2821  C   ILE A 395    14486  32028  13569  -3996   1937     99       C  
ATOM   2822  O   ILE A 395     -41.027  14.477   5.998  1.00147.48           O  
ANISOU 2822  O   ILE A 395    12921  31045  12071  -3978   1797    640       O  
ATOM   2823  CB  ILE A 395     -39.201  12.567   8.194  1.00141.24           C  
ANISOU 2823  CB  ILE A 395    12639  28842  12184  -3843   2002   -968       C  
ATOM   2824  CG1 ILE A 395     -37.833  11.976   7.848  1.00132.26           C  
ANISOU 2824  CG1 ILE A 395    11651  27599  11003  -3948   2113  -1504       C  
ATOM   2825  CG2 ILE A 395     -40.316  11.678   7.657  1.00134.98           C  
ANISOU 2825  CG2 ILE A 395    11639  28662  10984  -4039   1749  -1096       C  
ATOM   2826  CD1 ILE A 395     -37.594  10.604   8.442  1.00117.94           C  
ANISOU 2826  CD1 ILE A 395     9901  25531   9378  -3992   2046  -2205       C  
ATOM   2827  N   GLN A 396     -39.122  13.534   5.268  1.00185.16           N  
ANISOU 2827  N   GLN A 396    17957  35803  16595  -4199   1951   -236       N  
ATOM   2828  CA  GLN A 396     -39.524  13.424   3.862  1.00192.31           C  
ANISOU 2828  CA  GLN A 396    18683  37574  16812  -4440   1788    -55       C  
ATOM   2829  C   GLN A 396     -39.797  14.800   3.248  1.00205.14           C  
ANISOU 2829  C   GLN A 396    20190  39482  18274  -4385   1814    861       C  
ATOM   2830  O   GLN A 396     -40.886  15.085   2.740  1.00206.80           O  
ANISOU 2830  O   GLN A 396    20168  40241  18165  -4436   1600   1380       O  
ATOM   2831  CB  GLN A 396     -40.731  12.495   3.701  1.00179.50           C  
ANISOU 2831  CB  GLN A 396    16862  36451  14890  -4601   1498   -267       C  
ATOM   2832  CG  GLN A 396     -40.445  11.233   2.898  1.00177.39           C  
ANISOU 2832  CG  GLN A 396    16562  36612  14225  -4890   1411   -998       C  
ATOM   2833  CD  GLN A 396     -40.165  11.516   1.433  1.00170.83           C  
ANISOU 2833  CD  GLN A 396    15643  36467  12797  -5082   1386   -804       C  
ATOM   2834  OE1 GLN A 396     -40.494  12.585   0.919  1.00173.60           O  
ANISOU 2834  OE1 GLN A 396    15899  37141  12922  -5041   1345    -36       O  
ATOM   2835  NE2 GLN A 396     -39.554  10.553   0.753  1.00166.84           N  
ANISOU 2835  NE2 GLN A 396    15152  36174  12065  -5285   1428  -1483       N  
ATOM   2836  N   CYS A 397     -38.771  15.654   3.307  1.00195.50           N  
ANISOU 2836  N   CYS A 397    19106  37870  17306  -4288   2081   1084       N  
ATOM   2837  CA  CYS A 397     -38.770  16.958   2.642  1.00178.68           C  
ANISOU 2837  CA  CYS A 397    16873  35953  15065  -4265   2158   1944       C  
ATOM   2838  C   CYS A 397     -39.937  17.830   3.118  1.00191.67           C  
ANISOU 2838  C   CYS A 397    18330  37513  16983  -4084   2075   2689       C  
ATOM   2839  O   CYS A 397     -40.752  18.310   2.329  1.00183.09           O  
ANISOU 2839  O   CYS A 397    17014  37005  15546  -4132   1892   3363       O  
ATOM   2840  CB  CYS A 397     -38.793  16.786   1.119  1.00159.72           C  
ANISOU 2840  CB  CYS A 397    14347  34430  11910  -4514   2014   2092       C  
ATOM   2841  SG  CYS A 397     -37.580  15.602   0.492  1.00203.38           S  
ANISOU 2841  SG  CYS A 397    20026  40129  17120  -4728   2115   1146       S  
ATOM   2842  N   GLN A 398     -40.004  18.035   4.435  1.00191.03           N  
ANISOU 2842  N   GLN A 398    18325  36697  17560  -3863   2209   2569       N  
ATOM   2843  CA  GLN A 398     -41.081  18.820   5.029  1.00176.54           C  
ANISOU 2843  CA  GLN A 398    16289  34683  16105  -3654   2179   3191       C  
ATOM   2844  C   GLN A 398     -40.586  19.498   6.300  1.00167.23           C  
ANISOU 2844  C   GLN A 398    15230  32604  15705  -3427   2471   3130       C  
ATOM   2845  O   GLN A 398     -39.581  19.091   6.887  1.00163.22           O  
ANISOU 2845  O   GLN A 398    14964  31637  15415  -3435   2623   2500       O  
ATOM   2846  CB  GLN A 398     -42.303  17.947   5.339  1.00154.48           C  
ANISOU 2846  CB  GLN A 398    13341  32164  13188  -3650   1911   2984       C  
ATOM   2847  CG  GLN A 398     -43.367  17.981   4.273  1.00157.12           C  
ANISOU 2847  CG  GLN A 398    13372  33369  12958  -3780   1614   3553       C  
ATOM   2848  CD  GLN A 398     -44.353  16.846   4.398  1.00151.58           C  
ANISOU 2848  CD  GLN A 398    12528  33053  12014  -3890   1342   3165       C  
ATOM   2849  OE1 GLN A 398     -44.525  16.266   5.471  1.00140.81           O  
ANISOU 2849  OE1 GLN A 398    11236  31206  11058  -3785   1385   2678       O  
ATOM   2850  NE2 GLN A 398     -45.002  16.511   3.292  1.00148.67           N  
ANISOU 2850  NE2 GLN A 398    11945  33571  10971  -4121   1049   3379       N  
ATOM   2851  N   TYR A 399     -41.298  20.547   6.718  1.00181.22           N  
ANISOU 2851  N   TYR A 399    16800  34138  17918  -3225   2545   3797       N  
ATOM   2852  CA  TYR A 399     -41.040  21.161   8.019  1.00179.07           C  
ANISOU 2852  CA  TYR A 399    16584  33052  18403  -3008   2806   3687       C  
ATOM   2853  C   TYR A 399     -41.257  20.108   9.091  1.00172.28           C  
ANISOU 2853  C   TYR A 399    15861  31911  17685  -2932   2731   2911       C  
ATOM   2854  O   TYR A 399     -42.311  19.483   9.129  1.00182.80           O  
ANISOU 2854  O   TYR A 399    17059  33546  18851  -2903   2505   2886       O  
ATOM   2855  CB  TYR A 399     -41.973  22.357   8.274  1.00190.37           C  
ANISOU 2855  CB  TYR A 399    17703  34309  20318  -2777   2882   4516       C  
ATOM   2856  CG  TYR A 399     -41.817  23.496   7.304  1.00198.54           C  
ANISOU 2856  CG  TYR A 399    18591  35502  21344  -2816   2947   5413       C  
ATOM   2857  CD1 TYR A 399     -40.833  24.457   7.495  1.00201.55           C  
ANISOU 2857  CD1 TYR A 399    19065  35325  22190  -2811   3239   5579       C  
ATOM   2858  CD2 TYR A 399     -42.659  23.628   6.203  1.00199.84           C  
ANISOU 2858  CD2 TYR A 399    18516  36353  21060  -2864   2692   6125       C  
ATOM   2859  CE1 TYR A 399     -40.688  25.503   6.610  1.00201.14           C  
ANISOU 2859  CE1 TYR A 399    18875  35366  22183  -2853   3296   6454       C  
ATOM   2860  CE2 TYR A 399     -42.515  24.681   5.321  1.00202.75           C  
ANISOU 2860  CE2 TYR A 399    18749  36859  21430  -2892   2734   7022       C  
ATOM   2861  CZ  TYR A 399     -41.531  25.604   5.526  1.00203.28           C  
ANISOU 2861  CZ  TYR A 399    18915  36335  21987  -2887   3046   7194       C  
ATOM   2862  OH  TYR A 399     -41.415  26.639   4.620  1.00207.40           O  
ANISOU 2862  OH  TYR A 399    19284  36986  22535  -2928   3081   8154       O  
TER    2863      TYR A 399                                                      
ATOM   2864  N   LYS B  74     -12.612   1.121  66.379  1.00108.38           N  
ANISOU 2864  N   LYS B  74     7708  15900  17569   4358   1670   -692       N  
ATOM   2865  CA  LYS B  74     -12.556   0.911  64.936  1.00124.08           C  
ANISOU 2865  CA  LYS B  74     9785  17786  19575   4362   1732   -681       C  
ATOM   2866  C   LYS B  74     -13.937   0.595  64.368  1.00132.24           C  
ANISOU 2866  C   LYS B  74    11032  18534  20677   4284   1768   -562       C  
ATOM   2867  O   LYS B  74     -14.869   1.388  64.506  1.00118.70           O  
ANISOU 2867  O   LYS B  74     9396  16745  18961   4124   1811   -502       O  
ATOM   2868  CB  LYS B  74     -11.577  -0.215  64.597  1.00 99.67           C  
ANISOU 2868  CB  LYS B  74     6625  14728  16516   4562   1679   -746       C  
ATOM   2869  CG  LYS B  74     -10.136   0.076  64.977  1.00100.43           C  
ANISOU 2869  CG  LYS B  74     6560  15051  16549   4588   1646   -846       C  
ATOM   2870  CD  LYS B  74      -9.221  -1.071  64.579  1.00116.34           C  
ANISOU 2870  CD  LYS B  74     8536  17061  18608   4768   1594   -900       C  
ATOM   2871  CE  LYS B  74      -7.768  -0.759  64.900  1.00113.99           C  
ANISOU 2871  CE  LYS B  74     8071  16982  18258   4787   1563  -1006       C  
ATOM   2872  NZ  LYS B  74      -6.859  -1.870  64.506  1.00106.43           N  
ANISOU 2872  NZ  LYS B  74     7066  16021  17350   4965   1512  -1068       N  
ATOM   2873  N   ASN B  75     -14.059  -0.569  63.724  1.00143.27           N  
ANISOU 2873  N   ASN B  75    12520  19773  22143   4399   1747   -532       N  
ATOM   2874  CA  ASN B  75     -15.330  -0.965  63.127  1.00140.16           C  
ANISOU 2874  CA  ASN B  75    12326  19106  21823   4334   1776   -425       C  
ATOM   2875  C   ASN B  75     -16.409  -1.231  64.169  1.00160.33           C  
ANISOU 2875  C   ASN B  75    14960  21534  24424   4295   1736   -311       C  
ATOM   2876  O   ASN B  75     -17.597  -1.188  63.832  1.00165.93           O  
ANISOU 2876  O   ASN B  75    15822  22038  25185   4187   1773   -217       O  
ATOM   2877  CB  ASN B  75     -15.141  -2.203  62.247  1.00143.20           C  
ANISOU 2877  CB  ASN B  75    12776  19368  22267   4486   1751   -432       C  
ATOM   2878  CG  ASN B  75     -14.867  -1.852  60.796  1.00153.53           C  
ANISOU 2878  CG  ASN B  75    14105  20682  23549   4448   1830   -495       C  
ATOM   2879  OD1 ASN B  75     -14.589  -0.699  60.464  1.00163.27           O  
ANISOU 2879  OD1 ASN B  75    15277  22039  24720   4323   1897   -536       O  
ATOM   2880  ND2 ASN B  75     -14.945  -2.849  59.921  1.00146.59           N  
ANISOU 2880  ND2 ASN B  75    13307  19672  22719   4559   1820   -503       N  
ATOM   2881  N   TRP B  76     -16.027  -1.513  65.418  1.00179.92           N  
ANISOU 2881  N   TRP B  76    17332  24136  26894   4379   1663   -317       N  
ATOM   2882  CA  TRP B  76     -17.025  -1.653  66.473  1.00186.39           C  
ANISOU 2882  CA  TRP B  76    18203  24874  27743   4334   1634   -209       C  
ATOM   2883  C   TRP B  76     -17.795  -0.354  66.666  1.00178.56           C  
ANISOU 2883  C   TRP B  76    17239  23903  26702   4138   1705   -200       C  
ATOM   2884  O   TRP B  76     -19.026  -0.363  66.786  1.00175.50           O  
ANISOU 2884  O   TRP B  76    16976  23346  26359   4048   1728    -95       O  
ATOM   2885  CB  TRP B  76     -16.356  -2.083  67.778  1.00179.21           C  
ANISOU 2885  CB  TRP B  76    17140  24116  26835   4454   1547   -226       C  
ATOM   2886  CG  TRP B  76     -17.314  -2.260  68.919  1.00196.96           C  
ANISOU 2886  CG  TRP B  76    19404  26288  29143   4420   1540    -80       C  
ATOM   2887  CD1 TRP B  76     -18.049  -3.373  69.206  1.00198.94           C  
ANISOU 2887  CD1 TRP B  76    19742  26338  29508   4488   1512     99       C  
ATOM   2888  CD2 TRP B  76     -17.637  -1.295  69.928  1.00194.00           C  
ANISOU 2888  CD2 TRP B  76    18947  26051  28714   4313   1565    -95       C  
ATOM   2889  NE1 TRP B  76     -18.811  -3.161  70.330  1.00182.59           N  
ANISOU 2889  NE1 TRP B  76    17643  24278  27455   4429   1526    212       N  
ATOM   2890  CE2 TRP B  76     -18.576  -1.893  70.793  1.00196.11           C  
ANISOU 2890  CE2 TRP B  76    19250  26199  29063   4325   1559     84       C  
ATOM   2891  CE3 TRP B  76     -17.223   0.016  70.184  1.00177.53           C  
ANISOU 2891  CE3 TRP B  76    16754  24184  26516   4214   1592   -240       C  
ATOM   2892  CZ2 TRP B  76     -19.107  -1.225  71.895  1.00197.06           C  
ANISOU 2892  CZ2 TRP B  76    19297  26424  29154   4243   1585    108       C  
ATOM   2893  CZ3 TRP B  76     -17.753   0.678  71.278  1.00182.57           C  
ANISOU 2893  CZ3 TRP B  76    17324  24915  27129   4134   1607   -230       C  
ATOM   2894  CH2 TRP B  76     -18.685   0.056  72.119  1.00197.92           C  
ANISOU 2894  CH2 TRP B  76    19300  26746  29153   4151   1607    -65       C  
ATOM   2895  N   SER B  77     -17.086   0.776  66.689  1.00146.90           N  
ANISOU 2895  N   SER B  77    13110  20099  22608   4072   1736   -309       N  
ATOM   2896  CA  SER B  77     -17.760   2.067  66.750  1.00141.62           C  
ANISOU 2896  CA  SER B  77    12467  19441  21903   3889   1800   -305       C  
ATOM   2897  C   SER B  77     -18.439   2.407  65.428  1.00138.36           C  
ANISOU 2897  C   SER B  77    12204  18823  21545   3765   1874   -258       C  
ATOM   2898  O   SER B  77     -19.496   3.048  65.426  1.00139.94           O  
ANISOU 2898  O   SER B  77    12495  18901  21775   3619   1915   -202       O  
ATOM   2899  CB  SER B  77     -16.765   3.161  67.136  1.00126.48           C  
ANISOU 2899  CB  SER B  77    10373  17798  19885   3860   1804   -424       C  
ATOM   2900  OG  SER B  77     -16.182   2.893  68.400  1.00115.57           O  
ANISOU 2900  OG  SER B  77     8843  16606  18461   3962   1730   -484       O  
ATOM   2901  N   ALA B  78     -17.859   1.980  64.303  1.00144.16           N  
ANISOU 2901  N   ALA B  78    12957  19518  22299   3824   1890   -286       N  
ATOM   2902  CA  ALA B  78     -18.412   2.336  62.999  1.00135.52           C  
ANISOU 2902  CA  ALA B  78    11985  18251  21256   3706   1959   -258       C  
ATOM   2903  C   ALA B  78     -19.828   1.799  62.825  1.00135.65           C  
ANISOU 2903  C   ALA B  78    12184  17988  21367   3649   1964   -141       C  
ATOM   2904  O   ALA B  78     -20.708   2.505  62.320  1.00133.70           O  
ANISOU 2904  O   ALA B  78    12032  17599  21168   3486   2015   -100       O  
ATOM   2905  CB  ALA B  78     -17.504   1.817  61.884  1.00132.44           C  
ANISOU 2905  CB  ALA B  78    11567  17896  20859   3808   1971   -321       C  
ATOM   2906  N   LEU B  79     -20.066   0.551  63.232  1.00145.94           N  
ANISOU 2906  N   LEU B  79    13534  19204  22712   3778   1908    -81       N  
ATOM   2907  CA  LEU B  79     -21.406  -0.014  63.108  1.00150.96           C  
ANISOU 2907  CA  LEU B  79    14336  19580  23441   3727   1910     42       C  
ATOM   2908  C   LEU B  79     -22.378   0.629  64.090  1.00147.05           C  
ANISOU 2908  C   LEU B  79    13859  19065  22947   3606   1921    106       C  
ATOM   2909  O   LEU B  79     -23.523   0.924  63.730  1.00132.12           O  
ANISOU 2909  O   LEU B  79    12092  16984  21123   3471   1961    177       O  
ATOM   2910  CB  LEU B  79     -21.362  -1.527  63.311  1.00157.90           C  
ANISOU 2910  CB  LEU B  79    15252  20372  24370   3901   1839     99       C  
ATOM   2911  CG  LEU B  79     -20.903  -2.345  62.104  1.00172.40           C  
ANISOU 2911  CG  LEU B  79    17136  22126  26242   4006   1832     58       C  
ATOM   2912  CD1 LEU B  79     -20.978  -3.832  62.408  1.00186.07           C  
ANISOU 2912  CD1 LEU B  79    18910  23746  28041   4174   1750    126       C  
ATOM   2913  CD2 LEU B  79     -21.739  -2.001  60.881  1.00172.36           C  
ANISOU 2913  CD2 LEU B  79    17267  21932  26291   3869   1898     80       C  
ATOM   2914  N   LEU B  80     -21.944   0.850  65.333  1.00142.90           N  
ANISOU 2914  N   LEU B  80    13204  18740  22350   3655   1886     74       N  
ATOM   2915  CA  LEU B  80     -22.839   1.420  66.336  1.00125.70           C  
ANISOU 2915  CA  LEU B  80    11025  16574  20160   3560   1896    119       C  
ATOM   2916  C   LEU B  80     -23.238   2.845  65.973  1.00118.96           C  
ANISOU 2916  C   LEU B  80    10186  15714  19298   3376   1960     74       C  
ATOM   2917  O   LEU B  80     -24.426   3.185  65.957  1.00117.23           O  
ANISOU 2917  O   LEU B  80    10068  15336  19140   3252   1993    142       O  
ATOM   2918  CB  LEU B  80     -22.179   1.389  67.715  1.00111.73           C  
ANISOU 2918  CB  LEU B  80     9093  15054  18306   3658   1841     68       C  
ATOM   2919  CG  LEU B  80     -21.822   0.032  68.319  1.00109.23           C  
ANISOU 2919  CG  LEU B  80     8738  14740  18024   3835   1768    132       C  
ATOM   2920  CD1 LEU B  80     -21.479   0.194  69.790  1.00117.66           C  
ANISOU 2920  CD1 LEU B  80     9635  16012  19057   3886   1741    121       C  
ATOM   2921  CD2 LEU B  80     -22.951  -0.968  68.131  1.00 93.51           C  
ANISOU 2921  CD2 LEU B  80     6899  12476  16156   3841   1772    307       C  
ATOM   2922  N   THR B  81     -22.251   3.693  65.672  1.00108.92           N  
ANISOU 2922  N   THR B  81     8810  14611  17966   3355   1975    -34       N  
ATOM   2923  CA  THR B  81     -22.533   5.105  65.435  1.00108.30           C  
ANISOU 2923  CA  THR B  81     8723  14536  17889   3184   2025    -74       C  
ATOM   2924  C   THR B  81     -23.380   5.307  64.186  1.00 99.22           C  
ANISOU 2924  C   THR B  81     7729  13121  16851   3050   2074    -16       C  
ATOM   2925  O   THR B  81     -24.309   6.121  64.190  1.00111.38           O  
ANISOU 2925  O   THR B  81     9328  14545  18448   2900   2104      8       O  
ATOM   2926  CB  THR B  81     -21.226   5.887  65.332  1.00122.18           C  
ANISOU 2926  CB  THR B  81    10330  16527  19567   3197   2026   -184       C  
ATOM   2927  OG1 THR B  81     -20.454   5.386  64.234  1.00141.66           O  
ANISOU 2927  OG1 THR B  81    12803  18976  22045   3262   2036   -203       O  
ATOM   2928  CG2 THR B  81     -20.428   5.734  66.614  1.00129.93           C  
ANISOU 2928  CG2 THR B  81    11149  17778  20440   3321   1972   -248       C  
ATOM   2929  N   ALA B  82     -23.082   4.572  63.111  1.00 82.80           N  
ANISOU 2929  N   ALA B  82     5710  10944  14807   3106   2080     -2       N  
ATOM   2930  CA  ALA B  82     -23.861   4.712  61.885  1.00 80.54           C  
ANISOU 2930  CA  ALA B  82     5561  10419  14622   2986   2123     46       C  
ATOM   2931  C   ALA B  82     -25.323   4.358  62.121  1.00107.37           C  
ANISOU 2931  C   ALA B  82     9098  13589  18110   2917   2125    154       C  
ATOM   2932  O   ALA B  82     -26.224   4.991  61.555  1.00108.51           O  
ANISOU 2932  O   ALA B  82     9331  13556  18340   2760   2161    188       O  
ATOM   2933  CB  ALA B  82     -23.268   3.839  60.780  1.00 89.91           C  
ANISOU 2933  CB  ALA B  82     6776  11571  15814   3088   2124     30       C  
ATOM   2934  N   VAL B  83     -25.577   3.351  62.960  1.00108.11           N  
ANISOU 2934  N   VAL B  83     9204  13683  18191   3031   2085    214       N  
ATOM   2935  CA  VAL B  83     -26.950   3.000  63.311  1.00 95.42           C  
ANISOU 2935  CA  VAL B  83     7710  11883  16663   2970   2088    327       C  
ATOM   2936  C   VAL B  83     -27.639   4.179  63.986  1.00 97.77           C  
ANISOU 2936  C   VAL B  83     7984  12202  16963   2828   2115    315       C  
ATOM   2937  O   VAL B  83     -28.778   4.526  63.655  1.00100.33           O  
ANISOU 2937  O   VAL B  83     8411  12328  17383   2692   2145    372       O  
ATOM   2938  CB  VAL B  83     -26.974   1.743  64.199  1.00 82.63           C  
ANISOU 2938  CB  VAL B  83     6079  10291  15025   3125   2036    400       C  
ATOM   2939  CG1 VAL B  83     -28.317   1.608  64.899  1.00 92.70           C  
ANISOU 2939  CG1 VAL B  83     7425  11440  16356   3057   2043    512       C  
ATOM   2940  CG2 VAL B  83     -26.688   0.504  63.367  1.00 89.02           C  
ANISOU 2940  CG2 VAL B  83     6959  10986  15880   3241   2007    433       C  
ATOM   2941  N   VAL B  84     -26.953   4.822  64.934  1.00105.35           N  
ANISOU 2941  N   VAL B  84     8800  13405  17821   2861   2101    231       N  
ATOM   2942  CA  VAL B  84     -27.542   5.966  65.626  1.00112.75           C  
ANISOU 2942  CA  VAL B  84     9700  14387  18754   2742   2120    196       C  
ATOM   2943  C   VAL B  84     -27.796   7.109  64.649  1.00105.92           C  
ANISOU 2943  C   VAL B  84     8882  13391  17973   2570   2159    161       C  
ATOM   2944  O   VAL B  84     -28.845   7.764  64.699  1.00 96.04           O  
ANISOU 2944  O   VAL B  84     7690  11998  16802   2436   2181    183       O  
ATOM   2945  CB  VAL B  84     -26.646   6.408  66.798  1.00113.72           C  
ANISOU 2945  CB  VAL B  84     9645  14821  18741   2822   2092     98       C  
ATOM   2946  CG1 VAL B  84     -27.364   7.442  67.653  1.00109.97           C  
ANISOU 2946  CG1 VAL B  84     9127  14401  18253   2721   2108     60       C  
ATOM   2947  CG2 VAL B  84     -26.244   5.209  67.640  1.00107.16           C  
ANISOU 2947  CG2 VAL B  84     8758  14116  17841   3000   2044    130       C  
ATOM   2948  N   ILE B  85     -26.843   7.364  63.747  1.00101.01           N  
ANISOU 2948  N   ILE B  85     8226  12813  17341   2572   2165    106       N  
ATOM   2949  CA  ILE B  85     -27.007   8.434  62.764  1.00 95.88           C  
ANISOU 2949  CA  ILE B  85     7608  12043  16779   2411   2198     79       C  
ATOM   2950  C   ILE B  85     -28.247   8.189  61.914  1.00102.56           C  
ANISOU 2950  C   ILE B  85     8618  12588  17761   2304   2221    170       C  
ATOM   2951  O   ILE B  85     -29.101   9.072  61.754  1.00104.10           O  
ANISOU 2951  O   ILE B  85     8860  12636  18055   2149   2238    176       O  
ATOM   2952  CB  ILE B  85     -25.751   8.556  61.881  1.00 95.18           C  
ANISOU 2952  CB  ILE B  85     7449  12065  16649   2449   2205     20       C  
ATOM   2953  CG1 ILE B  85     -24.502   8.815  62.724  1.00 96.44           C  
ANISOU 2953  CG1 ILE B  85     7437  12527  16679   2551   2180    -68       C  
ATOM   2954  CG2 ILE B  85     -25.931   9.661  60.852  1.00 80.52           C  
ANISOU 2954  CG2 ILE B  85     5619  10085  14892   2279   2236      3       C  
ATOM   2955  CD1 ILE B  85     -23.212   8.814  61.932  1.00 79.69           C  
ANISOU 2955  CD1 ILE B  85     5231  10539  14507   2608   2188   -123       C  
ATOM   2956  N   ILE B  86     -28.365   6.980  61.359  1.00110.16           N  
ANISOU 2956  N   ILE B  86     9666  13453  18737   2388   2217    237       N  
ATOM   2957  CA  ILE B  86     -29.463   6.704  60.439  1.00113.61           C  
ANISOU 2957  CA  ILE B  86    10251  13615  19300   2290   2237    320       C  
ATOM   2958  C   ILE B  86     -30.795   6.678  61.182  1.00117.83           C  
ANISOU 2958  C   ILE B  86    10855  14014  19903   2220   2239    397       C  
ATOM   2959  O   ILE B  86     -31.816   7.134  60.655  1.00116.38           O  
ANISOU 2959  O   ILE B  86    10759  13620  19839   2073   2259    438       O  
ATOM   2960  CB  ILE B  86     -29.205   5.402  59.654  1.00112.80           C  
ANISOU 2960  CB  ILE B  86    10212  13455  19192   2406   2229    360       C  
ATOM   2961  CG1 ILE B  86     -30.237   5.243  58.534  1.00131.72           C  
ANISOU 2961  CG1 ILE B  86    12747  15587  21714   2294   2250    428       C  
ATOM   2962  CG2 ILE B  86     -29.209   4.184  60.565  1.00113.09           C  
ANISOU 2962  CG2 ILE B  86    10247  13541  19179   2561   2192    413       C  
ATOM   2963  CD1 ILE B  86     -30.246   6.392  57.546  1.00117.99           C  
ANISOU 2963  CD1 ILE B  86    11007  13786  20036   2143   2281    387       C  
ATOM   2964  N   LEU B  87     -30.811   6.163  62.416  1.00104.74           N  
ANISOU 2964  N   LEU B  87     9148  12479  18170   2324   2217    416       N  
ATOM   2965  CA  LEU B  87     -32.043   6.168  63.199  1.00 87.55           C  
ANISOU 2965  CA  LEU B  87     7015  10207  16042   2266   2224    485       C  
ATOM   2966  C   LEU B  87     -32.495   7.592  63.494  1.00 91.64           C  
ANISOU 2966  C   LEU B  87     7498  10720  16602   2121   2242    419       C  
ATOM   2967  O   LEU B  87     -33.676   7.923  63.341  1.00 96.11           O  
ANISOU 2967  O   LEU B  87     8145  11091  17282   1996   2261    466       O  
ATOM   2968  CB  LEU B  87     -31.847   5.384  64.498  1.00 74.87           C  
ANISOU 2968  CB  LEU B  87     5338   8775  14334   2417   2197    513       C  
ATOM   2969  CG  LEU B  87     -31.761   3.860  64.390  1.00 75.03           C  
ANISOU 2969  CG  LEU B  87     5410   8743  14354   2553   2169    609       C  
ATOM   2970  CD1 LEU B  87     -31.605   3.229  65.766  1.00 76.20           C  
ANISOU 2970  CD1 LEU B  87     5472   9067  14413   2687   2138    641       C  
ATOM   2971  CD2 LEU B  87     -32.977   3.299  63.672  1.00 73.97           C  
ANISOU 2971  CD2 LEU B  87     5427   8324  14355   2469   2185    728       C  
ATOM   2972  N   THR B  88     -31.561   8.453  63.908  1.00 89.13           N  
ANISOU 2972  N   THR B  88     7054  10610  16201   2137   2233    305       N  
ATOM   2973  CA  THR B  88     -31.895   9.850  64.163  1.00 91.06           C  
ANISOU 2973  CA  THR B  88     7256  10849  16495   2004   2242    227       C  
ATOM   2974  C   THR B  88     -32.460  10.508  62.912  1.00 91.37           C  
ANISOU 2974  C   THR B  88     7391  10631  16694   1837   2260    243       C  
ATOM   2975  O   THR B  88     -33.523  11.144  62.950  1.00 95.52           O  
ANISOU 2975  O   THR B  88     7966  10991  17334   1709   2269    252       O  
ATOM   2976  CB  THR B  88     -30.649  10.597  64.647  1.00 83.21           C  
ANISOU 2976  CB  THR B  88     6106  10118  15391   2051   2225    106       C  
ATOM   2977  OG1 THR B  88     -30.126   9.958  65.817  1.00 91.99           O  
ANISOU 2977  OG1 THR B  88     7121  11480  16353   2209   2203     91       O  
ATOM   2978  CG2 THR B  88     -30.973  12.045  64.970  1.00 93.27           C  
ANISOU 2978  CG2 THR B  88     7327  11385  16726   1920   2226     18       C  
ATOM   2979  N   ILE B  89     -31.770  10.337  61.782  1.00 98.84           N  
ANISOU 2979  N   ILE B  89     8357  11546  17651   1841   2264    246       N  
ATOM   2980  CA  ILE B  89     -32.192  10.985  60.544  1.00100.53           C  
ANISOU 2980  CA  ILE B  89     8644  11545  18007   1689   2278    259       C  
ATOM   2981  C   ILE B  89     -33.575  10.499  60.131  1.00 95.29           C  
ANISOU 2981  C   ILE B  89     8122  10618  17467   1610   2291    364       C  
ATOM   2982  O   ILE B  89     -34.466  11.300  59.827  1.00 98.81           O  
ANISOU 2982  O   ILE B  89     8616  10878  18051   1459   2296    370       O  
ATOM   2983  CB  ILE B  89     -31.153  10.745  59.434  1.00108.25           C  
ANISOU 2983  CB  ILE B  89     9604  12578  18947   1732   2285    245       C  
ATOM   2984  CG1 ILE B  89     -29.855  11.489  59.754  1.00 98.93           C  
ANISOU 2984  CG1 ILE B  89     8275  11640  17674   1771   2276    141       C  
ATOM   2985  CG2 ILE B  89     -31.707  11.170  58.083  1.00110.02           C  
ANISOU 2985  CG2 ILE B  89     9914  12577  19310   1591   2302    281       C  
ATOM   2986  CD1 ILE B  89     -28.750  11.245  58.755  1.00105.73           C  
ANISOU 2986  CD1 ILE B  89     9095  12597  18481   1828   2288    120       C  
ATOM   2987  N   ALA B  90     -33.781   9.179  60.130  1.00 81.42           N  
ANISOU 2987  N   ALA B  90     6428   8837  15672   1710   2292    447       N  
ATOM   2988  CA  ALA B  90     -35.055   8.627  59.681  1.00 88.36           C  
ANISOU 2988  CA  ALA B  90     7433   9471  16667   1636   2303    555       C  
ATOM   2989  C   ALA B  90     -36.198   9.030  60.604  1.00 82.17           C  
ANISOU 2989  C   ALA B  90     6662   8612  15948   1559   2308    580       C  
ATOM   2990  O   ALA B  90     -37.273   9.423  60.132  1.00 72.05           O  
ANISOU 2990  O   ALA B  90     5454   7110  14810   1416   2319    622       O  
ATOM   2991  CB  ALA B  90     -34.957   7.106  59.576  1.00 88.14           C  
ANISOU 2991  CB  ALA B  90     7454   9448  16586   1771   2295    634       C  
ATOM   2992  N   GLY B  91     -35.989   8.944  61.920  1.00 79.06           N  
ANISOU 2992  N   GLY B  91     6186   8405  15446   1656   2300    550       N  
ATOM   2993  CA  GLY B  91     -37.044   9.314  62.847  1.00 75.30           C  
ANISOU 2993  CA  GLY B  91     5707   7890  15013   1601   2310    561       C  
ATOM   2994  C   GLY B  91     -37.428  10.775  62.737  1.00 76.06           C  
ANISOU 2994  C   GLY B  91     5782   7902  15213   1450   2311    474       C  
ATOM   2995  O   GLY B  91     -38.614  11.118  62.739  1.00 76.95           O  
ANISOU 2995  O   GLY B  91     5951   7833  15453   1338   2322    505       O  
ATOM   2996  N   ASN B  92     -36.435  11.659  62.617  1.00 70.36           N  
ANISOU 2996  N   ASN B  92     4976   7303  14454   1444   2297    363       N  
ATOM   2997  CA  ASN B  92     -36.762  13.075  62.524  1.00 68.31           C  
ANISOU 2997  CA  ASN B  92     4690   6953  14313   1302   2289    275       C  
ATOM   2998  C   ASN B  92     -37.366  13.430  61.170  1.00 69.68           C  
ANISOU 2998  C   ASN B  92     4966   6841  14667   1151   2291    325       C  
ATOM   2999  O   ASN B  92     -38.218  14.322  61.095  1.00 66.71           O  
ANISOU 2999  O   ASN B  92     4613   6293  14440   1019   2286    298       O  
ATOM   3000  CB  ASN B  92     -35.523  13.911  62.824  1.00 87.67           C  
ANISOU 3000  CB  ASN B  92     7011   9619  16680   1336   2270    150       C  
ATOM   3001  CG  ASN B  92     -35.036  13.715  64.244  1.00 87.69           C  
ANISOU 3001  CG  ASN B  92     6897   9911  16511   1471   2265     91       C  
ATOM   3002  OD1 ASN B  92     -35.613  14.251  65.191  1.00 78.35           O  
ANISOU 3002  OD1 ASN B  92     5665   8776  15330   1451   2265     33       O  
ATOM   3003  ND2 ASN B  92     -33.981  12.930  64.404  1.00 99.38           N  
ANISOU 3003  ND2 ASN B  92     8325  11594  17840   1614   2259    101       N  
ATOM   3004  N   ILE B  93     -36.969  12.737  60.098  1.00 75.83           N  
ANISOU 3004  N   ILE B  93     5803   7569  15439   1172   2298    392       N  
ATOM   3005  CA  ILE B  93     -37.636  12.928  58.812  1.00 78.93           C  
ANISOU 3005  CA  ILE B  93     6292   7706  15992   1036   2302    453       C  
ATOM   3006  C   ILE B  93     -39.098  12.512  58.910  1.00 88.59           C  
ANISOU 3006  C   ILE B  93     7609   8726  17327    962   2313    546       C  
ATOM   3007  O   ILE B  93     -39.991  13.193  58.389  1.00 85.53           O  
ANISOU 3007  O   ILE B  93     7270   8120  17109    813   2308    561       O  
ATOM   3008  CB  ILE B  93     -36.896  12.159  57.701  1.00 74.40           C  
ANISOU 3008  CB  ILE B  93     5748   7158  15362   1095   2311    498       C  
ATOM   3009  CG1 ILE B  93     -35.594  12.872  57.334  1.00 93.49           C  
ANISOU 3009  CG1 ILE B  93     8072   9732  17719   1118   2303    408       C  
ATOM   3010  CG2 ILE B  93     -37.777  12.002  56.469  1.00 72.68           C  
ANISOU 3010  CG2 ILE B  93     5636   6692  15287    977   2318    583       C  
ATOM   3011  CD1 ILE B  93     -34.801  12.180  56.246  1.00104.76           C  
ANISOU 3011  CD1 ILE B  93     9511  11214  19079   1187   2316    433       C  
ATOM   3012  N   LEU B  94     -39.367  11.389  59.582  1.00 76.74           N  
ANISOU 3012  N   LEU B  94     6127   7291  15739   1065   2326    614       N  
ATOM   3013  CA  LEU B  94     -40.749  10.968  59.785  1.00 64.45           C  
ANISOU 3013  CA  LEU B  94     4642   5565  14281    999   2340    708       C  
ATOM   3014  C   LEU B  94     -41.527  12.000  60.591  1.00 72.91           C  
ANISOU 3014  C   LEU B  94     5680   6589  15435    916   2338    645       C  
ATOM   3015  O   LEU B  94     -42.688  12.290  60.283  1.00 87.76           O  
ANISOU 3015  O   LEU B  94     7617   8253  17474    785   2343    688       O  
ATOM   3016  CB  LEU B  94     -40.793   9.606  60.477  1.00 65.04           C  
ANISOU 3016  CB  LEU B  94     4726   5743  14243   1139   2350    792       C  
ATOM   3017  CG  LEU B  94     -40.376   8.404  59.630  1.00 65.07           C  
ANISOU 3017  CG  LEU B  94     4785   5733  14207   1211   2349    869       C  
ATOM   3018  CD1 LEU B  94     -40.610   7.107  60.388  1.00 65.70           C  
ANISOU 3018  CD1 LEU B  94     4876   5874  14214   1336   2351    962       C  
ATOM   3019  CD2 LEU B  94     -41.124   8.400  58.307  1.00 69.57           C  
ANISOU 3019  CD2 LEU B  94     5439   6068  14927   1066   2355    930       C  
ATOM   3020  N   VAL B  95     -40.905  12.563  61.631  1.00 66.33           N  
ANISOU 3020  N   VAL B  95     4743   5964  14496    993   2330    534       N  
ATOM   3021  CA  VAL B  95     -41.580  13.580  62.437  1.00 65.56           C  
ANISOU 3021  CA  VAL B  95     4597   5847  14466    928   2326    446       C  
ATOM   3022  C   VAL B  95     -41.901  14.808  61.593  1.00 69.59           C  
ANISOU 3022  C   VAL B  95     5131   6142  15168    764   2305    390       C  
ATOM   3023  O   VAL B  95     -43.005  15.366  61.675  1.00 81.86           O  
ANISOU 3023  O   VAL B  95     6713   7518  16873    657   2303    381       O  
ATOM   3024  CB  VAL B  95     -40.728  13.943  63.668  1.00 66.89           C  
ANISOU 3024  CB  VAL B  95     4631   6316  14468   1046   2320    325       C  
ATOM   3025  CG1 VAL B  95     -41.306  15.158  64.378  1.00 67.24           C  
ANISOU 3025  CG1 VAL B  95     4611   6349  14590    973   2313    202       C  
ATOM   3026  CG2 VAL B  95     -40.655  12.766  64.619  1.00 70.24           C  
ANISOU 3026  CG2 VAL B  95     5029   6935  14725   1202   2339    392       C  
ATOM   3027  N   ILE B  96     -40.942  15.252  60.776  1.00 65.83           N  
ANISOU 3027  N   ILE B  96     4638   5680  14696    746   2286    351       N  
ATOM   3028  CA  ILE B  96     -41.163  16.414  59.918  1.00 64.27           C  
ANISOU 3028  CA  ILE B  96     4458   5278  14685    599   2259    308       C  
ATOM   3029  C   ILE B  96     -42.297  16.146  58.938  1.00 63.04           C  
ANISOU 3029  C   ILE B  96     4418   4837  14698    476   2264    423       C  
ATOM   3030  O   ILE B  96     -43.170  16.999  58.727  1.00 62.58           O  
ANISOU 3030  O   ILE B  96     4384   4566  14828    349   2244    401       O  
ATOM   3031  CB  ILE B  96     -39.864  16.795  59.185  1.00 70.91           C  
ANISOU 3031  CB  ILE B  96     5252   6211  15479    618   2244    267       C  
ATOM   3032  CG1 ILE B  96     -38.794  17.236  60.185  1.00 69.74           C  
ANISOU 3032  CG1 ILE B  96     4972   6338  15188    714   2234    143       C  
ATOM   3033  CG2 ILE B  96     -40.130  17.892  58.162  1.00 81.09           C  
ANISOU 3033  CG2 ILE B  96     6569   7270  16971    472   2214    251       C  
ATOM   3034  CD1 ILE B  96     -37.394  17.254  59.608  1.00 86.05           C  
ANISOU 3034  CD1 ILE B  96     6980   8559  17157    770   2230    123       C  
ATOM   3035  N   MET B  97     -42.302  14.961  58.322  1.00 62.59           N  
ANISOU 3035  N   MET B  97     4424   4772  14583    511   2286    543       N  
ATOM   3036  CA  MET B  97     -43.379  14.612  57.402  1.00 66.33           C  
ANISOU 3036  CA  MET B  97     4991   5006  15206    389   2292    657       C  
ATOM   3037  C   MET B  97     -44.726  14.593  58.111  1.00 77.10           C  
ANISOU 3037  C   MET B  97     6376   6253  16668    325   2303    688       C  
ATOM   3038  O   MET B  97     -45.722  15.095  57.580  1.00 82.04           O  
ANISOU 3038  O   MET B  97     7039   6649  17483    176   2292    719       O  
ATOM   3039  CB  MET B  97     -43.105  13.255  56.754  1.00 61.32           C  
ANISOU 3039  CB  MET B  97     4400   4424  14473    454   2315    764       C  
ATOM   3040  CG  MET B  97     -41.922  13.234  55.809  1.00 61.49           C  
ANISOU 3040  CG  MET B  97     4409   4533  14421    504   2309    741       C  
ATOM   3041  SD  MET B  97     -41.732  11.626  55.019  1.00 61.43           S  
ANISOU 3041  SD  MET B  97     4454   4571  14316    587   2332    844       S  
ATOM   3042  CE  MET B  97     -43.192  11.577  53.985  1.00 60.20           C  
ANISOU 3042  CE  MET B  97     4362   4153  14360    393   2336    949       C  
ATOM   3043  N   ALA B  98     -44.776  14.019  59.315  1.00 67.11           N  
ANISOU 3043  N   ALA B  98     5077   5148  15275    441   2324    683       N  
ATOM   3044  CA  ALA B  98     -46.036  13.940  60.046  1.00 71.32           C  
ANISOU 3044  CA  ALA B  98     5621   5596  15882    400   2341    715       C  
ATOM   3045  C   ALA B  98     -46.562  15.326  60.394  1.00 68.24           C  
ANISOU 3045  C   ALA B  98     5196   5098  15633    309   2318    596       C  
ATOM   3046  O   ALA B  98     -47.760  15.597  60.252  1.00 85.36           O  
ANISOU 3046  O   ALA B  98     7399   7065  17971    192   2319    628       O  
ATOM   3047  CB  ALA B  98     -45.859  13.101  61.310  1.00 69.10           C  
ANISOU 3047  CB  ALA B  98     5296   5540  15417    564   2367    729       C  
ATOM   3048  N   VAL B  99     -45.683  16.219  60.850  1.00 62.81           N  
ANISOU 3048  N   VAL B  99     4430   4546  14888    359   2295    452       N  
ATOM   3049  CA  VAL B  99     -46.135  17.555  61.227  1.00 63.14           C  
ANISOU 3049  CA  VAL B  99     4426   4494  15071    283   2268    318       C  
ATOM   3050  C   VAL B  99     -46.563  18.348  59.998  1.00 62.24           C  
ANISOU 3050  C   VAL B  99     4373   4083  15192    124   2232    333       C  
ATOM   3051  O   VAL B  99     -47.594  19.030  60.013  1.00 70.24           O  
ANISOU 3051  O   VAL B  99     5408   4973  16306     50   2195    292       O  
ATOM   3052  CB  VAL B  99     -45.044  18.290  62.025  1.00 64.33           C  
ANISOU 3052  CB  VAL B  99     4459   4883  15101    370   2252    157       C  
ATOM   3053  CG1 VAL B  99     -45.496  19.702  62.358  1.00 64.80           C  
ANISOU 3053  CG1 VAL B  99     4464   4833  15324    286   2219      5       C  
ATOM   3054  CG2 VAL B  99     -44.718  17.528  63.293  1.00 65.30           C  
ANISOU 3054  CG2 VAL B  99     4511   5305  14994    527   2286    146       C  
ATOM   3055  N   SER B 100     -45.793  18.266  58.911  1.00 69.22           N  
ANISOU 3055  N   SER B 100     5289   4941  16071    107   2217    382       N  
ATOM   3056  CA  SER B 100     -46.086  19.061  57.726  1.00 71.14           C  
ANISOU 3056  CA  SER B 100     5599   5153  16278     50   2123    369       C  
ATOM   3057  C   SER B 100     -47.208  18.484  56.871  1.00 69.89           C  
ANISOU 3057  C   SER B 100     5557   5070  15927     39   2056    464       C  
ATOM   3058  O   SER B 100     -47.727  19.197  56.005  1.00 70.44           O  
ANISOU 3058  O   SER B 100     5690   5170  15905      9   1959    444       O  
ATOM   3059  CB  SER B 100     -44.820  19.214  56.877  1.00 78.77           C  
ANISOU 3059  CB  SER B 100     6546   6118  17266     60   2128    377       C  
ATOM   3060  OG  SER B 100     -44.255  17.952  56.566  1.00 74.72           O  
ANISOU 3060  OG  SER B 100     6044   5628  16719     96   2197    490       O  
ATOM   3061  N   LEU B 101     -47.600  17.230  57.088  1.00 70.10           N  
ANISOU 3061  N   LEU B 101     5608   5125  15900     61   2105    565       N  
ATOM   3062  CA  LEU B 101     -48.635  16.585  56.288  1.00 79.20           C  
ANISOU 3062  CA  LEU B 101     6852   6353  16886     43   2046    646       C  
ATOM   3063  C   LEU B 101     -49.936  16.377  57.048  1.00 99.59           C  
ANISOU 3063  C   LEU B 101     9448   8939  19452     33   2042    657       C  
ATOM   3064  O   LEU B 101     -51.006  16.726  56.541  1.00108.12           O  
ANISOU 3064  O   LEU B 101    10586  10064  20431     -7   1959    648       O  
ATOM   3065  CB  LEU B 101     -48.126  15.238  55.756  1.00 70.67           C  
ANISOU 3065  CB  LEU B 101     5784   5307  15762     76   2098    758       C  
ATOM   3066  CG  LEU B 101     -47.086  15.299  54.633  1.00 76.09           C  
ANISOU 3066  CG  LEU B 101     6475   6004  16431     81   2091    765       C  
ATOM   3067  CD1 LEU B 101     -46.583  13.906  54.277  1.00 78.71           C  
ANISOU 3067  CD1 LEU B 101     6798   6350  16757    121   2161    866       C  
ATOM   3068  CD2 LEU B 101     -47.665  15.989  53.408  1.00 78.84           C  
ANISOU 3068  CD2 LEU B 101     6893   6408  16656     34   1981    742       C  
ATOM   3069  N   GLU B 102     -49.876  15.813  58.252  1.00101.16           N  
ANISOU 3069  N   GLU B 102     9587   9092  19758     70   2136    682       N  
ATOM   3070  CA  GLU B 102     -51.092  15.547  59.008  1.00112.14           C  
ANISOU 3070  CA  GLU B 102    10981  10477  21149     68   2146    704       C  
ATOM   3071  C   GLU B 102     -51.755  16.852  59.430  1.00115.97           C  
ANISOU 3071  C   GLU B 102    11449  10923  21692     33   2099    579       C  
ATOM   3072  O   GLU B 102     -51.104  17.744  59.983  1.00107.69           O  
ANISOU 3072  O   GLU B 102    10326   9811  20778     32   2124    469       O  
ATOM   3073  CB  GLU B 102     -50.781  14.690  60.235  1.00132.19           C  
ANISOU 3073  CB  GLU B 102    13448  12967  23810    123   2270    772       C  
ATOM   3074  CG  GLU B 102     -50.447  13.246  59.911  1.00138.72           C  
ANISOU 3074  CG  GLU B 102    14295  13832  24579    165   2314    919       C  
ATOM   3075  CD  GLU B 102     -51.646  12.473  59.400  1.00152.03           C  
ANISOU 3075  CD  GLU B 102    16046  15583  26135    149   2263   1000       C  
ATOM   3076  OE1 GLU B 102     -52.789  12.855  59.731  1.00158.55           O  
ANISOU 3076  OE1 GLU B 102    16886  16410  26944    122   2228    970       O  
ATOM   3077  OE2 GLU B 102     -51.447  11.483  58.664  1.00151.18           O  
ANISOU 3077  OE2 GLU B 102    15962  15522  25958    162   2261   1086       O  
ATOM   3078  N   LYS B 103     -53.058  16.958  59.165  1.00117.92           N  
ANISOU 3078  N   LYS B 103    11751  11206  21849      1   2033    588       N  
ATOM   3079  CA  LYS B 103     -53.816  18.137  59.560  1.00104.92           C  
ANISOU 3079  CA  LYS B 103    10087   9516  20263    -29   1990    476       C  
ATOM   3080  C   LYS B 103     -54.111  18.162  61.053  1.00 97.41           C  
ANISOU 3080  C   LYS B 103     9042   8481  19487     -4   2087    429       C  
ATOM   3081  O   LYS B 103     -54.386  19.235  61.599  1.00 97.15           O  
ANISOU 3081  O   LYS B 103     8953   8389  19572    -23   2079    299       O  
ATOM   3082  CB  LYS B 103     -55.131  18.207  58.781  1.00120.64           C  
ANISOU 3082  CB  LYS B 103    12157  11571  22108    -73   1895    509       C  
ATOM   3083  CG  LYS B 103     -55.216  17.270  57.580  1.00128.52           C  
ANISOU 3083  CG  LYS B 103    13215  12681  22934    -94   1854    619       C  
ATOM   3084  CD  LYS B 103     -54.441  17.800  56.381  1.00130.19           C  
ANISOU 3084  CD  LYS B 103    13459  12935  23071   -117   1789    601       C  
ATOM   3085  CE  LYS B 103     -54.547  16.845  55.201  1.00127.76           C  
ANISOU 3085  CE  LYS B 103    13157  12753  22631   -137   1768    694       C  
ATOM   3086  NZ  LYS B 103     -53.799  17.331  54.008  1.00116.54           N  
ANISOU 3086  NZ  LYS B 103    11750  11379  21153   -156   1717    682       N  
ATOM   3087  N   LYS B 104     -54.056  17.008  61.721  1.00 96.51           N  
ANISOU 3087  N   LYS B 104     8902   8361  19408     38   2183    532       N  
ATOM   3088  CA  LYS B 104     -54.393  16.925  63.136  1.00 97.22           C  
ANISOU 3088  CA  LYS B 104     8896   8371  19670     65   2290    509       C  
ATOM   3089  C   LYS B 104     -53.268  17.400  64.044  1.00 99.06           C  
ANISOU 3089  C   LYS B 104     9010   8529  20101     81   2381    408       C  
ATOM   3090  O   LYS B 104     -53.522  17.701  65.215  1.00113.33           O  
ANISOU 3090  O   LYS B 104    10728  10471  21861    157   2412    302       O  
ATOM   3091  CB  LYS B 104     -54.764  15.485  63.499  1.00 89.94           C  
ANISOU 3091  CB  LYS B 104     7990   7472  18713    112   2360    683       C  
ATOM   3092  CG  LYS B 104     -55.684  14.812  62.495  1.00103.68           C  
ANISOU 3092  CG  LYS B 104     9838   9301  20255     91   2271    782       C  
ATOM   3093  CD  LYS B 104     -55.908  13.347  62.841  1.00118.89           C  
ANISOU 3093  CD  LYS B 104    11767  11250  22156    139   2337    952       C  
ATOM   3094  CE  LYS B 104     -56.723  12.644  61.765  1.00127.87           C  
ANISOU 3094  CE  LYS B 104    12987  12483  23114    107   2248   1028       C  
ATOM   3095  NZ  LYS B 104     -58.062  13.269  61.575  1.00130.78           N  
ANISOU 3095  NZ  LYS B 104    13383  12864  23442     57   2176    970       N  
ATOM   3096  N   LEU B 105     -52.039  17.469  63.540  1.00 94.97           N  
ANISOU 3096  N   LEU B 105     8494   8059  19532     96   2361    393       N  
ATOM   3097  CA  LEU B 105     -50.882  17.842  64.340  1.00 88.32           C  
ANISOU 3097  CA  LEU B 105     7557   7497  18505    222   2356    253       C  
ATOM   3098  C   LEU B 105     -50.540  19.320  64.225  1.00 87.14           C  
ANISOU 3098  C   LEU B 105     7354   7278  18479    157   2307     69       C  
ATOM   3099  O   LEU B 105     -49.485  19.740  64.707  1.00 83.49           O  
ANISOU 3099  O   LEU B 105     6806   7028  17887    234   2294    -49       O  
ATOM   3100  CB  LEU B 105     -49.673  16.999  63.936  1.00 79.55           C  
ANISOU 3100  CB  LEU B 105     6468   6534  17222    303   2358    338       C  
ATOM   3101  CG  LEU B 105     -49.837  15.486  64.051  1.00 84.30           C  
ANISOU 3101  CG  LEU B 105     7116   7215  17700    383   2399    515       C  
ATOM   3102  CD1 LEU B 105     -48.586  14.792  63.546  1.00 75.02           C  
ANISOU 3102  CD1 LEU B 105     5958   6162  16382    458   2391    571       C  
ATOM   3103  CD2 LEU B 105     -50.136  15.087  65.487  1.00 89.36           C  
ANISOU 3103  CD2 LEU B 105     7678   8088  18185    517   2439    493       C  
ATOM   3104  N   GLN B 106     -51.400  20.115  63.593  1.00 86.80           N  
ANISOU 3104  N   GLN B 106     7352   6936  18690     17   2274     44       N  
ATOM   3105  CA  GLN B 106     -51.090  21.510  63.284  1.00 94.38           C  
ANISOU 3105  CA  GLN B 106     8282   7856  19724    -28   2199   -115       C  
ATOM   3106  C   GLN B 106     -51.380  22.371  64.508  1.00 91.96           C  
ANISOU 3106  C   GLN B 106     7849   7588  19504    -13   2219   -315       C  
ATOM   3107  O   GLN B 106     -52.484  22.885  64.690  1.00108.39           O  
ANISOU 3107  O   GLN B 106     9926   9531  21728    -69   2209   -372       O  
ATOM   3108  CB  GLN B 106     -51.890  21.972  62.073  1.00108.21           C  
ANISOU 3108  CB  GLN B 106    10153   9664  21297    -52   2068    -68       C  
ATOM   3109  CG  GLN B 106     -51.789  21.052  60.861  1.00112.59           C  
ANISOU 3109  CG  GLN B 106    10832  10306  21641    -40   2025    105       C  
ATOM   3110  CD  GLN B 106     -50.360  20.848  60.389  1.00101.65           C  
ANISOU 3110  CD  GLN B 106     9433   8933  20258    -23   2045    129       C  
ATOM   3111  OE1 GLN B 106     -49.761  21.738  59.784  1.00 98.08           O  
ANISOU 3111  OE1 GLN B 106     8978   8476  19814    -38   1986     67       O  
ATOM   3112  NE2 GLN B 106     -49.806  19.672  60.665  1.00 97.15           N  
ANISOU 3112  NE2 GLN B 106     8850   8372  19690     12   2133    227       N  
ATOM   3113  N   ASN B 107     -50.371  22.528  65.362  1.00 83.01           N  
ANISOU 3113  N   ASN B 107     6607   6760  18174     94   2227   -429       N  
ATOM   3114  CA  ASN B 107     -50.465  23.409  66.518  1.00 89.24           C  
ANISOU 3114  CA  ASN B 107     7257   7706  18943    131   2227   -642       C  
ATOM   3115  C   ASN B 107     -49.061  23.873  66.892  1.00 91.69           C  
ANISOU 3115  C   ASN B 107     7468   8257  19114    196   2204   -761       C  
ATOM   3116  O   ASN B 107     -48.066  23.452  66.297  1.00 93.62           O  
ANISOU 3116  O   ASN B 107     7750   8553  19268    222   2194   -673       O  
ATOM   3117  CB  ASN B 107     -51.172  22.720  67.693  1.00 85.12           C  
ANISOU 3117  CB  ASN B 107     6679   7404  18260    228   2294   -632       C  
ATOM   3118  CG  ASN B 107     -50.531  21.401  68.078  1.00 81.02           C  
ANISOU 3118  CG  ASN B 107     6164   7161  17460    364   2341   -492       C  
ATOM   3119  OD1 ASN B 107     -49.412  21.095  67.670  1.00 80.52           O  
ANISOU 3119  OD1 ASN B 107     6118   7181  17293    401   2324   -444       O  
ATOM   3120  ND2 ASN B 107     -51.242  20.610  68.874  1.00 80.03           N  
ANISOU 3120  ND2 ASN B 107     6016   7177  17215    444   2399   -426       N  
ATOM   3121  N   ALA B 108     -48.988  24.758  67.891  1.00 93.77           N  
ANISOU 3121  N   ALA B 108     7593   8672  19362    223   2197   -969       N  
ATOM   3122  CA  ALA B 108     -47.696  25.295  68.307  1.00 77.17           C  
ANISOU 3122  CA  ALA B 108     5382   6795  17145    276   2170  -1097       C  
ATOM   3123  C   ALA B 108     -46.788  24.203  68.857  1.00 87.38           C  
ANISOU 3123  C   ALA B 108     6642   8439  18122    422   2213  -1004       C  
ATOM   3124  O   ALA B 108     -45.590  24.170  68.550  1.00 88.32           O  
ANISOU 3124  O   ALA B 108     6745   8658  18154    453   2191   -990       O  
ATOM   3125  CB  ALA B 108     -47.894  26.401  69.343  1.00 78.19           C  
ANISOU 3125  CB  ALA B 108     5361   7027  17319    277   2156  -1344       C  
ATOM   3126  N   THR B 109     -47.339  23.299  69.672  1.00 92.97           N  
ANISOU 3126  N   THR B 109     7332   9334  18657    519   2274   -937       N  
ATOM   3127  CA  THR B 109     -46.519  22.271  70.309  1.00 93.82           C  
ANISOU 3127  CA  THR B 109     7394   9784  18468    672   2311   -855       C  
ATOM   3128  C   THR B 109     -45.832  21.390  69.272  1.00 91.29           C  
ANISOU 3128  C   THR B 109     7191   9381  18115    678   2302   -674       C  
ATOM   3129  O   THR B 109     -44.617  21.168  69.334  1.00 85.05           O  
ANISOU 3129  O   THR B 109     6355   8788  17171    754   2291   -672       O  
ATOM   3130  CB  THR B 109     -47.379  21.424  71.249  1.00101.95           C  
ANISOU 3130  CB  THR B 109     8396  10989  19351    766   2377   -790       C  
ATOM   3131  OG1 THR B 109     -47.843  22.232  72.338  1.00107.80           O  
ANISOU 3131  OG1 THR B 109     8998  11885  20075    784   2393   -976       O  
ATOM   3132  CG2 THR B 109     -46.577  20.252  71.797  1.00 98.73           C  
ANISOU 3132  CG2 THR B 109     7953  10902  18658    924   2409   -678       C  
ATOM   3133  N   ASN B 110     -46.591  20.895  68.293  1.00 87.51           N  
ANISOU 3133  N   ASN B 110     6856   8613  17782    597   2306   -525       N  
ATOM   3134  CA  ASN B 110     -45.993  20.016  67.295  1.00 89.55           C  
ANISOU 3134  CA  ASN B 110     7221   8798  18007    604   2301   -358       C  
ATOM   3135  C   ASN B 110     -45.103  20.783  66.326  1.00 75.31           C  
ANISOU 3135  C   ASN B 110     5431   6874  16311    527   2250   -404       C  
ATOM   3136  O   ASN B 110     -44.181  20.201  65.752  1.00 68.35           O  
ANISOU 3136  O   ASN B 110     4581   6053  15336    569   2247   -318       O  
ATOM   3137  CB  ASN B 110     -47.078  19.252  66.541  1.00 81.09           C  
ANISOU 3137  CB  ASN B 110     6288   7463  17059    537   2321   -185       C  
ATOM   3138  CG  ASN B 110     -47.824  18.277  67.430  1.00 68.81           C  
ANISOU 3138  CG  ASN B 110     4723   6043  15378    629   2375   -101       C  
ATOM   3139  OD1 ASN B 110     -47.354  17.170  67.687  1.00 68.98           O  
ANISOU 3139  OD1 ASN B 110     4749   6240  15219    744   2399      7       O  
ATOM   3140  ND2 ASN B 110     -48.995  18.685  67.905  1.00 91.83           N  
ANISOU 3140  ND2 ASN B 110     7618   8876  18397    584   2392   -152       N  
ATOM   3141  N   TYR B 111     -45.346  22.082  66.135  1.00 69.04           N  
ANISOU 3141  N   TYR B 111     4605   5911  15714    420   2209   -540       N  
ATOM   3142  CA  TYR B 111     -44.417  22.882  65.341  1.00 74.88           C  
ANISOU 3142  CA  TYR B 111     5335   6570  16547    360   2159   -592       C  
ATOM   3143  C   TYR B 111     -43.072  23.022  66.045  1.00 79.93           C  
ANISOU 3143  C   TYR B 111     5846   7535  16988    463   2154   -687       C  
ATOM   3144  O   TYR B 111     -42.014  22.905  65.412  1.00 74.48           O  
ANISOU 3144  O   TYR B 111     5160   6893  16247    478   2139   -643       O  
ATOM   3145  CB  TYR B 111     -45.022  24.252  65.040  1.00 89.20           C  
ANISOU 3145  CB  TYR B 111     7138   8117  18635    231   2110   -718       C  
ATOM   3146  CG  TYR B 111     -46.074  24.218  63.955  1.00 87.28           C  
ANISOU 3146  CG  TYR B 111     7032   7511  18619    117   2098   -604       C  
ATOM   3147  CD1 TYR B 111     -46.109  23.183  63.030  1.00 90.39           C  
ANISOU 3147  CD1 TYR B 111     7545   7821  18977    112   2119   -407       C  
ATOM   3148  CD2 TYR B 111     -47.030  25.219  63.855  1.00 97.14           C  
ANISOU 3148  CD2 TYR B 111     8287   8500  20123     17   2063   -698       C  
ATOM   3149  CE1 TYR B 111     -47.068  23.144  62.036  1.00100.40           C  
ANISOU 3149  CE1 TYR B 111     8931   8769  20448      6   2106   -299       C  
ATOM   3150  CE2 TYR B 111     -47.992  25.189  62.863  1.00116.25           C  
ANISOU 3150  CE2 TYR B 111    10830  10588  22753    -80   2047   -588       C  
ATOM   3151  CZ  TYR B 111     -48.007  24.150  61.957  1.00115.97           C  
ANISOU 3151  CZ  TYR B 111    10911  10555  22596    -70   2057   -384       C  
ATOM   3152  OH  TYR B 111     -48.964  24.116  60.968  1.00118.47           O  
ANISOU 3152  OH  TYR B 111    11356  10926  22733    -74   1972   -271       O  
ATOM   3153  N   PHE B 112     -43.091  23.260  67.359  1.00 83.80           N  
ANISOU 3153  N   PHE B 112     6214   8266  17359    537   2168   -815       N  
ATOM   3154  CA  PHE B 112     -41.848  23.257  68.123  1.00 83.32           C  
ANISOU 3154  CA  PHE B 112     6025   8543  17087    648   2167   -890       C  
ATOM   3155  C   PHE B 112     -41.186  21.884  68.080  1.00 79.88           C  
ANISOU 3155  C   PHE B 112     5624   8301  16426    772   2201   -733       C  
ATOM   3156  O   PHE B 112     -39.956  21.780  67.991  1.00 72.59           O  
ANISOU 3156  O   PHE B 112     4649   7546  15386    831   2187   -735       O  
ATOM   3157  CB  PHE B 112     -42.114  23.685  69.567  1.00 74.18           C  
ANISOU 3157  CB  PHE B 112     4729   7621  15834    712   2181  -1046       C  
ATOM   3158  CG  PHE B 112     -42.168  25.176  69.761  1.00 77.28           C  
ANISOU 3158  CG  PHE B 112     5034   7917  16411    620   2133  -1254       C  
ATOM   3159  CD1 PHE B 112     -43.347  25.875  69.564  1.00 74.92           C  
ANISOU 3159  CD1 PHE B 112     4774   7344  16349    509   2119  -1323       C  
ATOM   3160  CD2 PHE B 112     -41.040  25.878  70.150  1.00 88.69           C  
ANISOU 3160  CD2 PHE B 112     6355   9539  17805    645   2098  -1383       C  
ATOM   3161  CE1 PHE B 112     -43.400  27.244  69.745  1.00 83.19           C  
ANISOU 3161  CE1 PHE B 112     5738   8286  17584    429   2068  -1525       C  
ATOM   3162  CE2 PHE B 112     -41.086  27.249  70.333  1.00 96.82           C  
ANISOU 3162  CE2 PHE B 112     7300  10463  19022    559   2048  -1582       C  
ATOM   3163  CZ  PHE B 112     -42.268  27.932  70.130  1.00 95.87           C  
ANISOU 3163  CZ  PHE B 112     7222  10062  19144    453   2031  -1657       C  
ATOM   3164  N   LEU B 113     -41.988  20.818  68.139  1.00 83.05           N  
ANISOU 3164  N   LEU B 113     6108   8672  16773    813   2242   -598       N  
ATOM   3165  CA  LEU B 113     -41.434  19.469  68.054  1.00 79.97           C  
ANISOU 3165  CA  LEU B 113     5759   8428  16199    930   2268   -449       C  
ATOM   3166  C   LEU B 113     -40.787  19.217  66.696  1.00 77.62           C  
ANISOU 3166  C   LEU B 113     5555   7970  15969    882   2248   -354       C  
ATOM   3167  O   LEU B 113     -39.749  18.554  66.611  1.00 70.42           O  
ANISOU 3167  O   LEU B 113     4622   7231  14903    979   2250   -305       O  
ATOM   3168  CB  LEU B 113     -42.522  18.432  68.330  1.00 74.08           C  
ANISOU 3168  CB  LEU B 113     5085   7640  15422    967   2311   -321       C  
ATOM   3169  CG  LEU B 113     -43.090  18.409  69.749  1.00 72.76           C  
ANISOU 3169  CG  LEU B 113     4812   7702  15131   1050   2344   -388       C  
ATOM   3170  CD1 LEU B 113     -43.935  17.164  69.964  1.00 90.31           C  
ANISOU 3170  CD1 LEU B 113     7103   9915  17297   1108   2387   -228       C  
ATOM   3171  CD2 LEU B 113     -41.980  18.501  70.785  1.00 77.71           C  
ANISOU 3171  CD2 LEU B 113     5283   8713  15531   1181   2341   -485       C  
ATOM   3172  N   MET B 114     -41.389  19.727  65.620  1.00 77.33           N  
ANISOU 3172  N   MET B 114     5614   7610  16158    738   2229   -326       N  
ATOM   3173  CA  MET B 114     -40.793  19.571  64.297  1.00 68.26           C  
ANISOU 3173  CA  MET B 114     4540   6325  15069    690   2214   -241       C  
ATOM   3174  C   MET B 114     -39.517  20.394  64.169  1.00 73.89           C  
ANISOU 3174  C   MET B 114     5155   7161  15757    693   2182   -345       C  
ATOM   3175  O   MET B 114     -38.567  19.972  63.502  1.00 80.16           O  
ANISOU 3175  O   MET B 114     5959   8022  16477    731   2182   -286       O  
ATOM   3176  CB  MET B 114     -41.793  19.960  63.208  1.00 67.04           C  
ANISOU 3176  CB  MET B 114     4502   5809  15163    537   2200   -182       C  
ATOM   3177  CG  MET B 114     -41.277  19.716  61.793  1.00 66.14           C  
ANISOU 3177  CG  MET B 114     4465   5565  15100    493   2191    -81       C  
ATOM   3178  SD  MET B 114     -42.392  20.280  60.491  1.00 69.14           S  
ANISOU 3178  SD  MET B 114     4966   5535  15771    317   2166    -14       S  
ATOM   3179  CE  MET B 114     -42.514  22.025  60.877  1.00 65.64           C  
ANISOU 3179  CE  MET B 114     4435   4994  15510    234   2114   -198       C  
ATOM   3180  N   SER B 115     -39.478  21.575  64.791  1.00 69.90           N  
ANISOU 3180  N   SER B 115     4549   6689  15320    652   2153   -504       N  
ATOM   3181  CA  SER B 115     -38.230  22.333  64.832  1.00 70.81           C  
ANISOU 3181  CA  SER B 115     4553   6951  15402    662   2122   -606       C  
ATOM   3182  C   SER B 115     -37.148  21.553  65.570  1.00 74.42           C  
ANISOU 3182  C   SER B 115     4923   7761  15592    820   2142   -598       C  
ATOM   3183  O   SER B 115     -35.988  21.510  65.137  1.00 85.33           O  
ANISOU 3183  O   SER B 115     6263   9253  16905    852   2131   -586       O  
ATOM   3184  CB  SER B 115     -38.462  23.693  65.490  1.00 71.79           C  
ANISOU 3184  CB  SER B 115     4577   7047  15652    595   2085   -787       C  
ATOM   3185  OG  SER B 115     -37.263  24.447  65.544  1.00 72.75           O  
ANISOU 3185  OG  SER B 115     4584   7303  15756    599   2051   -883       O  
ATOM   3186  N   LEU B 116     -37.519  20.914  66.682  1.00 72.22           N  
ANISOU 3186  N   LEU B 116     4610   7668  15161    923   2170   -599       N  
ATOM   3187  CA  LEU B 116     -36.582  20.053  67.396  1.00 73.05           C  
ANISOU 3187  CA  LEU B 116     4639   8102  15014   1086   2187   -573       C  
ATOM   3188  C   LEU B 116     -36.128  18.891  66.521  1.00 77.92           C  
ANISOU 3188  C   LEU B 116     5348   8692  15565   1141   2202   -421       C  
ATOM   3189  O   LEU B 116     -34.958  18.502  66.553  1.00 90.23           O  
ANISOU 3189  O   LEU B 116     6845  10456  16982   1237   2198   -414       O  
ATOM   3190  CB  LEU B 116     -37.224  19.542  68.687  1.00 73.73           C  
ANISOU 3190  CB  LEU B 116     4679   8374  14963   1185   2217   -582       C  
ATOM   3191  CG  LEU B 116     -36.412  18.592  69.570  1.00 74.70           C  
ANISOU 3191  CG  LEU B 116     4715   8845  14822   1365   2232   -547       C  
ATOM   3192  CD1 LEU B 116     -36.643  18.918  71.031  1.00 78.81           C  
ANISOU 3192  CD1 LEU B 116     5100   9626  15218   1437   2244   -650       C  
ATOM   3193  CD2 LEU B 116     -36.773  17.137  69.295  1.00 81.27           C  
ANISOU 3193  CD2 LEU B 116     5655   9635  15589   1440   2259   -380       C  
ATOM   3194  N   ALA B 117     -37.047  18.315  65.745  1.00 84.01           N  
ANISOU 3194  N   ALA B 117     6263   9215  16442   1084   2220   -303       N  
ATOM   3195  CA  ALA B 117     -36.688  17.215  64.856  1.00 80.94           C  
ANISOU 3195  CA  ALA B 117     5964   8782  16009   1130   2234   -167       C  
ATOM   3196  C   ALA B 117     -35.718  17.673  63.774  1.00 85.80           C  
ANISOU 3196  C   ALA B 117     6571   9355  16673   1081   2216   -179       C  
ATOM   3197  O   ALA B 117     -34.792  16.940  63.411  1.00 93.15           O  
ANISOU 3197  O   ALA B 117     7494  10411  17487   1171   2222   -130       O  
ATOM   3198  CB  ALA B 117     -37.946  16.612  64.232  1.00 91.88           C  
ANISOU 3198  CB  ALA B 117     7497   9896  17516   1062   2254    -43       C  
ATOM   3199  N   ILE B 118     -35.925  18.877  63.237  1.00 90.12           N  
ANISOU 3199  N   ILE B 118     7116   9727  17399    942   2192   -242       N  
ATOM   3200  CA  ILE B 118     -34.983  19.437  62.272  1.00 81.74           C  
ANISOU 3200  CA  ILE B 118     6025   8646  16386    893   2174   -256       C  
ATOM   3201  C   ILE B 118     -33.614  19.611  62.913  1.00 74.31           C  
ANISOU 3201  C   ILE B 118     4938   8012  15286    991   2163   -340       C  
ATOM   3202  O   ILE B 118     -32.580  19.315  62.301  1.00 73.62           O  
ANISOU 3202  O   ILE B 118     4822   8028  15123   1036   2168   -309       O  
ATOM   3203  CB  ILE B 118     -35.516  20.769  61.710  1.00 77.65           C  
ANISOU 3203  CB  ILE B 118     5519   7879  16104    731   2142   -312       C  
ATOM   3204  CG1 ILE B 118     -36.803  20.539  60.918  1.00 86.14           C  
ANISOU 3204  CG1 ILE B 118     6742   8645  17342    636   2150   -213       C  
ATOM   3205  CG2 ILE B 118     -34.463  21.445  60.842  1.00 69.90           C  
ANISOU 3205  CG2 ILE B 118     4480   6913  15164    688   2121   -331       C  
ATOM   3206  CD1 ILE B 118     -37.398  21.801  60.338  1.00 98.56           C  
ANISOU 3206  CD1 ILE B 118     8334   9952  19162    487   2112   -259       C  
ATOM   3207  N   ALA B 119     -33.587  20.100  64.156  1.00 77.27           N  
ANISOU 3207  N   ALA B 119     5208   8548  15604   1026   2150   -449       N  
ATOM   3208  CA  ALA B 119     -32.319  20.235  64.867  1.00 73.62           C  
ANISOU 3208  CA  ALA B 119     4598   8393  14984   1124   2138   -525       C  
ATOM   3209  C   ALA B 119     -31.636  18.883  65.038  1.00 79.32           C  
ANISOU 3209  C   ALA B 119     5317   9324  15495   1286   2162   -442       C  
ATOM   3210  O   ALA B 119     -30.424  18.761  64.825  1.00 81.55           O  
ANISOU 3210  O   ALA B 119     5525   9777  15684   1349   2157   -448       O  
ATOM   3211  CB  ALA B 119     -32.547  20.899  66.224  1.00 74.66           C  
ANISOU 3211  CB  ALA B 119     4620   8666  15082   1142   2123   -653       C  
ATOM   3212  N   ASP B 120     -32.402  17.854  65.413  1.00 79.46           N  
ANISOU 3212  N   ASP B 120     5413   9329  15449   1356   2185   -364       N  
ATOM   3213  CA  ASP B 120     -31.831  16.520  65.581  1.00 81.71           C  
ANISOU 3213  CA  ASP B 120     5701   9785  15560   1514   2200   -286       C  
ATOM   3214  C   ASP B 120     -31.289  15.980  64.267  1.00 82.66           C  
ANISOU 3214  C   ASP B 120     5893   9808  15706   1512   2208   -207       C  
ATOM   3215  O   ASP B 120     -30.211  15.378  64.232  1.00 87.11           O  
ANISOU 3215  O   ASP B 120     6400  10560  16140   1628   2207   -199       O  
ATOM   3216  CB  ASP B 120     -32.876  15.557  66.144  1.00 90.38           C  
ANISOU 3216  CB  ASP B 120     6877  10843  16621   1571   2220   -206       C  
ATOM   3217  CG  ASP B 120     -33.419  16.002  67.475  1.00 91.46           C  
ANISOU 3217  CG  ASP B 120     6931  11115  16707   1590   2220   -282       C  
ATOM   3218  OD1 ASP B 120     -33.088  17.128  67.888  1.00 88.53           O  
ANISOU 3218  OD1 ASP B 120     6456  10827  16354   1543   2202   -404       O  
ATOM   3219  OD2 ASP B 120     -34.172  15.232  68.107  1.00 94.11           O  
ANISOU 3219  OD2 ASP B 120     7297  11475  16985   1653   2238   -222       O  
ATOM   3220  N   MET B 121     -32.033  16.170  63.176  1.00 80.21           N  
ANISOU 3220  N   MET B 121     5701   9214  15561   1386   2217   -150       N  
ATOM   3221  CA  MET B 121     -31.592  15.663  61.883  1.00 84.55           C  
ANISOU 3221  CA  MET B 121     6313   9681  16130   1384   2230    -78       C  
ATOM   3222  C   MET B 121     -30.333  16.375  61.409  1.00 86.97           C  
ANISOU 3222  C   MET B 121     6513  10116  16416   1372   2220   -142       C  
ATOM   3223  O   MET B 121     -29.423  15.739  60.864  1.00 80.02           O  
ANISOU 3223  O   MET B 121     5612   9348  15443   1456   2232   -115       O  
ATOM   3224  CB  MET B 121     -32.710  15.807  60.853  1.00 75.39           C  
ANISOU 3224  CB  MET B 121     5290   8201  15152   1246   2240     -5       C  
ATOM   3225  CG  MET B 121     -32.370  15.212  59.502  1.00 84.89           C  
ANISOU 3225  CG  MET B 121     6560   9329  16367   1249   2257     72       C  
ATOM   3226  SD  MET B 121     -33.577  15.645  58.241  1.00 79.88           S  
ANISOU 3226  SD  MET B 121     6058   8339  15953   1072   2262    145       S  
ATOM   3227  CE  MET B 121     -33.481  17.432  58.292  1.00 88.51           C  
ANISOU 3227  CE  MET B 121     7067   9376  17186    932   2230     43       C  
ATOM   3228  N   LEU B 122     -30.260  17.695  61.599  1.00 90.27           N  
ANISOU 3228  N   LEU B 122     6856  10517  16926   1267   2197   -229       N  
ATOM   3229  CA  LEU B 122     -29.056  18.425  61.214  1.00 80.57           C  
ANISOU 3229  CA  LEU B 122     5511   9416  15685   1249   2186   -285       C  
ATOM   3230  C   LEU B 122     -27.870  18.031  62.086  1.00 82.30           C  
ANISOU 3230  C   LEU B 122     5599   9962  15710   1398   2181   -333       C  
ATOM   3231  O   LEU B 122     -26.735  17.957  61.602  1.00 86.24           O  
ANISOU 3231  O   LEU B 122     6023  10604  16141   1442   2186   -336       O  
ATOM   3232  CB  LEU B 122     -29.305  19.931  61.282  1.00 73.53           C  
ANISOU 3232  CB  LEU B 122     4568   8413  14958   1102   2154   -368       C  
ATOM   3233  CG  LEU B 122     -30.236  20.505  60.212  1.00 72.36           C  
ANISOU 3233  CG  LEU B 122     4527   7945  15022    948   2150   -322       C  
ATOM   3234  CD1 LEU B 122     -30.250  22.025  60.269  1.00 72.80           C  
ANISOU 3234  CD1 LEU B 122     4508   7908  15245    820   2109   -414       C  
ATOM   3235  CD2 LEU B 122     -29.834  20.018  58.828  1.00 71.91           C  
ANISOU 3235  CD2 LEU B 122     4520   7842  14960    945   2176   -226       C  
ATOM   3236  N   LEU B 123     -28.111  17.781  63.375  1.00 99.88           N  
ANISOU 3236  N   LEU B 123     7786  12321  17842   1479   2171   -370       N  
ATOM   3237  CA  LEU B 123     -27.052  17.282  64.245  1.00 96.92           C  
ANISOU 3237  CA  LEU B 123     7290  12260  17275   1636   2164   -402       C  
ATOM   3238  C   LEU B 123     -26.565  15.914  63.784  1.00 99.01           C  
ANISOU 3238  C   LEU B 123     7599  12591  17429   1769   2182   -323       C  
ATOM   3239  O   LEU B 123     -25.359  15.639  63.787  1.00101.40           O  
ANISOU 3239  O   LEU B 123     7804  13106  17620   1867   2178   -343       O  
ATOM   3240  CB  LEU B 123     -27.560  17.219  65.686  1.00 99.18           C  
ANISOU 3240  CB  LEU B 123     7532  12673  17480   1700   2154   -445       C  
ATOM   3241  CG  LEU B 123     -26.638  16.660  66.769  1.00107.28           C  
ANISOU 3241  CG  LEU B 123     8428  14033  18299   1872   2142   -471       C  
ATOM   3242  CD1 LEU B 123     -25.464  17.592  67.014  1.00117.13           C  
ANISOU 3242  CD1 LEU B 123     9514  15473  19517   1863   2120   -557       C  
ATOM   3243  CD2 LEU B 123     -27.421  16.425  68.051  1.00101.72           C  
ANISOU 3243  CD2 LEU B 123     7707  13424  17518   1932   2141   -485       C  
ATOM   3244  N   GLY B 124     -27.493  15.043  63.382  1.00 88.40           N  
ANISOU 3244  N   GLY B 124     6400  11064  16126   1775   2200   -235       N  
ATOM   3245  CA  GLY B 124     -27.118  13.718  62.925  1.00 92.63           C  
ANISOU 3245  CA  GLY B 124     6985  11631  16580   1900   2212   -166       C  
ATOM   3246  C   GLY B 124     -26.409  13.711  61.587  1.00 93.70           C  
ANISOU 3246  C   GLY B 124     7128  11729  16744   1876   2229   -151       C  
ATOM   3247  O   GLY B 124     -25.562  12.851  61.337  1.00 85.48           O  
ANISOU 3247  O   GLY B 124     6057  10819  15603   2004   2233   -142       O  
ATOM   3248  N   PHE B 125     -26.752  14.651  60.704  1.00106.06           N  
ANISOU 3248  N   PHE B 125     8727  13121  18449   1718   2239   -151       N  
ATOM   3249  CA  PHE B 125     -26.135  14.679  59.381  1.00101.65           C  
ANISOU 3249  CA  PHE B 125     8167  12541  17914   1690   2261   -132       C  
ATOM   3250  C   PHE B 125     -24.685  15.140  59.444  1.00101.38           C  
ANISOU 3250  C   PHE B 125     7968  12761  17790   1736   2256   -200       C  
ATOM   3251  O   PHE B 125     -23.822  14.588  58.752  1.00102.01           O  
ANISOU 3251  O   PHE B 125     8011  12952  17794   1816   2276   -193       O  
ATOM   3252  CB  PHE B 125     -26.933  15.587  58.445  1.00100.65           C  
ANISOU 3252  CB  PHE B 125     8113  12163  17967   1507   2267   -105       C  
ATOM   3253  CG  PHE B 125     -27.868  14.848  57.531  1.00116.39           C  
ANISOU 3253  CG  PHE B 125    10261  13932  20030   1481   2289    -14       C  
ATOM   3254  CD1 PHE B 125     -27.395  14.238  56.380  1.00114.15           C  
ANISOU 3254  CD1 PHE B 125     9998  13665  19711   1525   2316     22       C  
ATOM   3255  CD2 PHE B 125     -29.221  14.775  57.814  1.00121.59           C  
ANISOU 3255  CD2 PHE B 125    11035  14374  20790   1414   2282     32       C  
ATOM   3256  CE1 PHE B 125     -28.254  13.561  55.534  1.00135.83           C  
ANISOU 3256  CE1 PHE B 125    12878  16212  22519   1503   2333     99       C  
ATOM   3257  CE2 PHE B 125     -30.085  14.101  56.971  1.00121.56           C  
ANISOU 3257  CE2 PHE B 125    11167  14165  20857   1384   2299    120       C  
ATOM   3258  CZ  PHE B 125     -29.601  13.493  55.831  1.00131.76           C  
ANISOU 3258  CZ  PHE B 125    12480  15473  22111   1429   2323    153       C  
ATOM   3259  N   LEU B 126     -24.397  16.156  60.257  1.00 87.48           N  
ANISOU 3259  N   LEU B 126     6099  11100  16039   1688   2231   -271       N  
ATOM   3260  CA  LEU B 126     -23.100  16.824  60.228  1.00 84.83           C  
ANISOU 3260  CA  LEU B 126     5602  10975  15654   1692   2224   -328       C  
ATOM   3261  C   LEU B 126     -22.185  16.379  61.364  1.00 90.57           C  
ANISOU 3261  C   LEU B 126     6207  11990  16216   1849   2206   -376       C  
ATOM   3262  O   LEU B 126     -21.090  15.864  61.118  1.00 96.01           O  
ANISOU 3262  O   LEU B 126     6815  12867  16798   1956   2215   -382       O  
ATOM   3263  CB  LEU B 126     -23.307  18.344  60.270  1.00 78.14           C  
ANISOU 3263  CB  LEU B 126     4702  10037  14951   1524   2201   -376       C  
ATOM   3264  CG  LEU B 126     -24.414  18.891  59.366  1.00 76.78           C  
ANISOU 3264  CG  LEU B 126     4652   9556  14964   1364   2207   -333       C  
ATOM   3265  CD1 LEU B 126     -24.514  20.400  59.499  1.00 77.00           C  
ANISOU 3265  CD1 LEU B 126     4611   9503  15144   1213   2172   -393       C  
ATOM   3266  CD2 LEU B 126     -24.190  18.492  57.916  1.00 76.43           C  
ANISOU 3266  CD2 LEU B 126     4655   9454  14931   1348   2243   -261       C  
ATOM   3267  N   VAL B 127     -22.622  16.562  62.611  1.00 79.67           N  
ANISOU 3267  N   VAL B 127     4806  10657  14810   1869   2179   -413       N  
ATOM   3268  CA  VAL B 127     -21.737  16.347  63.752  1.00 81.08           C  
ANISOU 3268  CA  VAL B 127     4845  11127  14834   2005   2157   -460       C  
ATOM   3269  C   VAL B 127     -21.436  14.865  63.943  1.00 87.63           C  
ANISOU 3269  C   VAL B 127     5700  12068  15527   2190   2160   -421       C  
ATOM   3270  O   VAL B 127     -20.287  14.478  64.190  1.00101.03           O  
ANISOU 3270  O   VAL B 127     7281  14000  17105   2314   2150   -445       O  
ATOM   3271  CB  VAL B 127     -22.352  16.970  65.018  1.00 81.19           C  
ANISOU 3271  CB  VAL B 127     4822  11172  14852   1977   2131   -512       C  
ATOM   3272  CG1 VAL B 127     -21.418  16.801  66.205  1.00 97.79           C  
ANISOU 3272  CG1 VAL B 127     6769  13596  16791   2117   2108   -554       C  
ATOM   3273  CG2 VAL B 127     -22.662  18.441  64.784  1.00 83.93           C  
ANISOU 3273  CG2 VAL B 127     5147  11378  15366   1794   2119   -566       C  
ATOM   3274  N   MET B 128     -22.462  14.014  63.845  1.00 80.43           N  
ANISOU 3274  N   MET B 128     4934  10983  14642   2211   2168   -361       N  
ATOM   3275  CA  MET B 128     -22.266  12.598  64.156  1.00 84.92           C  
ANISOU 3275  CA  MET B 128     5527  11637  15104   2386   2159   -327       C  
ATOM   3276  C   MET B 128     -21.317  11.899  63.188  1.00 81.47           C  
ANISOU 3276  C   MET B 128     5074  11250  14630   2471   2172   -319       C  
ATOM   3277  O   MET B 128     -20.446  11.145  63.657  1.00 93.22           O  
ANISOU 3277  O   MET B 128     6478  12938  16003   2632   2150   -342       O  
ATOM   3278  CB  MET B 128     -23.625  11.898  64.245  1.00107.04           C  
ANISOU 3278  CB  MET B 128     8485  14221  17963   2374   2165   -254       C  
ATOM   3279  CG  MET B 128     -24.530  12.475  65.324  1.00106.84           C  
ANISOU 3279  CG  MET B 128     8456  14187  17952   2316   2155   -271       C  
ATOM   3280  SD  MET B 128     -26.116  11.632  65.459  1.00 96.47           S  
ANISOU 3280  SD  MET B 128     7312  12636  16707   2303   2166   -174       S  
ATOM   3281  CE  MET B 128     -25.583   9.966  65.824  1.00100.16           C  
ANISOU 3281  CE  MET B 128     7772  13227  17057   2516   2142   -126       C  
ATOM   3282  N   PRO B 129     -21.427  12.056  61.862  1.00 80.78           N  
ANISOU 3282  N   PRO B 129     5058  11004  14631   2383   2206   -291       N  
ATOM   3283  CA  PRO B 129     -20.425  11.426  60.985  1.00 95.01           C  
ANISOU 3283  CA  PRO B 129     6819  12901  16379   2478   2222   -300       C  
ATOM   3284  C   PRO B 129     -19.016  11.952  61.195  1.00 93.70           C  
ANISOU 3284  C   PRO B 129     6467  13007  16127   2523   2217   -368       C  
ATOM   3285  O   PRO B 129     -18.054  11.186  61.058  1.00 84.32           O  
ANISOU 3285  O   PRO B 129     5209  11980  14850   2667   2214   -393       O  
ATOM   3286  CB  PRO B 129     -20.944  11.742  59.576  1.00 86.09           C  
ANISOU 3286  CB  PRO B 129     5788  11559  15362   2348   2263   -260       C  
ATOM   3287  CG  PRO B 129     -22.398  11.952  59.756  1.00 79.02           C  
ANISOU 3287  CG  PRO B 129     5031  10415  14577   2235   2259   -207       C  
ATOM   3288  CD  PRO B 129     -22.512  12.662  61.070  1.00 80.71           C  
ANISOU 3288  CD  PRO B 129     5172  10723  14771   2210   2229   -248       C  
ATOM   3289  N   VAL B 130     -18.859  13.237  61.523  1.00 90.50           N  
ANISOU 3289  N   VAL B 130     5974  12655  15756   2403   2211   -399       N  
ATOM   3290  CA  VAL B 130     -17.530  13.763  61.820  1.00 88.58           C  
ANISOU 3290  CA  VAL B 130     5545  12674  15436   2441   2202   -452       C  
ATOM   3291  C   VAL B 130     -16.969  13.108  63.076  1.00 87.45           C  
ANISOU 3291  C   VAL B 130     5312  12758  15158   2613   2163   -483       C  
ATOM   3292  O   VAL B 130     -15.788  12.743  63.129  1.00 96.08           O  
ANISOU 3292  O   VAL B 130     6281  14069  16157   2733   2157   -512       O  
ATOM   3293  CB  VAL B 130     -17.574  15.296  61.947  1.00 91.13           C  
ANISOU 3293  CB  VAL B 130     5799  12977  15850   2269   2197   -476       C  
ATOM   3294  CG1 VAL B 130     -16.234  15.827  62.427  1.00 87.87           C  
ANISOU 3294  CG1 VAL B 130     5186  12839  15361   2311   2182   -520       C  
ATOM   3295  CG2 VAL B 130     -17.946  15.925  60.614  1.00 90.53           C  
ANISOU 3295  CG2 VAL B 130     5787  12704  15907   2109   2230   -446       C  
ATOM   3296  N   SER B 131     -17.805  12.947  64.104  1.00 85.44           N  
ANISOU 3296  N   SER B 131     5109  12465  14892   2630   2136   -476       N  
ATOM   3297  CA  SER B 131     -17.362  12.246  65.304  1.00 86.55           C  
ANISOU 3297  CA  SER B 131     5164  12822  14901   2798   2095   -500       C  
ATOM   3298  C   SER B 131     -17.002  10.799  64.991  1.00 87.06           C  
ANISOU 3298  C   SER B 131     5264  12899  14916   2963   2084   -490       C  
ATOM   3299  O   SER B 131     -16.036  10.258  65.540  1.00 88.50           O  
ANISOU 3299  O   SER B 131     5327  13303  14998   3113   2050   -531       O  
ATOM   3300  CB  SER B 131     -18.444  12.314  66.382  1.00 95.17           C  
ANISOU 3300  CB  SER B 131     6306  13865  15990   2779   2075   -490       C  
ATOM   3301  OG  SER B 131     -18.019  11.673  67.573  1.00113.27           O  
ANISOU 3301  OG  SER B 131     8500  16387  18149   2938   2032   -516       O  
ATOM   3302  N   MET B 132     -17.774  10.156  64.111  1.00 85.97           N  
ANISOU 3302  N   MET B 132     5286  12520  14860   2939   2107   -439       N  
ATOM   3303  CA  MET B 132     -17.465   8.786  63.713  1.00 86.53           C  
ANISOU 3303  CA  MET B 132     5396  12571  14908   3092   2095   -430       C  
ATOM   3304  C   MET B 132     -16.119   8.707  63.004  1.00101.53           C  
ANISOU 3304  C   MET B 132     7181  14636  16759   3165   2108   -482       C  
ATOM   3305  O   MET B 132     -15.329   7.791  63.257  1.00107.62           O  
ANISOU 3305  O   MET B 132     7883  15542  17468   3334   2075   -520       O  
ATOM   3306  CB  MET B 132     -18.571   8.235  62.815  1.00 85.12           C  
ANISOU 3306  CB  MET B 132     5409  12098  14834   3037   2122   -357       C  
ATOM   3307  CG  MET B 132     -18.280   6.854  62.254  1.00 85.75           C  
ANISOU 3307  CG  MET B 132     5537  12133  14910   3189   2111   -346       C  
ATOM   3308  SD  MET B 132     -19.525   6.307  61.072  1.00 84.19           S  
ANISOU 3308  SD  MET B 132     5554  11601  14833   3115   2146   -260       S  
ATOM   3309  CE  MET B 132     -19.413   7.605  59.843  1.00 83.46           C  
ANISOU 3309  CE  MET B 132     5449  11473  14787   2933   2210   -278       C  
ATOM   3310  N   LEU B 133     -15.845   9.655  62.105  1.00113.60           N  
ANISOU 3310  N   LEU B 133     8680  16156  18325   3038   2155   -486       N  
ATOM   3311  CA  LEU B 133     -14.554   9.683  61.421  1.00103.01           C  
ANISOU 3311  CA  LEU B 133     7211  14997  16933   3096   2177   -532       C  
ATOM   3312  C   LEU B 133     -13.416   9.910  62.406  1.00 94.87           C  
ANISOU 3312  C   LEU B 133     5990  14256  15798   3188   2141   -584       C  
ATOM   3313  O   LEU B 133     -12.352   9.290  62.293  1.00 98.66           O  
ANISOU 3313  O   LEU B 133     6366  14908  16210   3331   2131   -630       O  
ATOM   3314  CB  LEU B 133     -14.547  10.766  60.342  1.00 98.17           C  
ANISOU 3314  CB  LEU B 133     6590  14322  16387   2923   2232   -516       C  
ATOM   3315  CG  LEU B 133     -15.413  10.526  59.104  1.00111.36           C  
ANISOU 3315  CG  LEU B 133     8417  15749  18147   2844   2273   -472       C  
ATOM   3316  CD1 LEU B 133     -15.305  11.698  58.141  1.00132.49           C  
ANISOU 3316  CD1 LEU B 133    11055  18399  20887   2670   2319   -461       C  
ATOM   3317  CD2 LEU B 133     -15.013   9.230  58.421  1.00124.43           C  
ANISOU 3317  CD2 LEU B 133    10098  17423  19757   3007   2284   -492       C  
ATOM   3318  N   THR B 134     -13.618  10.807  63.374  1.00 90.40           N  
ANISOU 3318  N   THR B 134     5371  13753  15223   3112   2120   -580       N  
ATOM   3319  CA  THR B 134     -12.592  11.053  64.382  1.00 91.95           C  
ANISOU 3319  CA  THR B 134     5385  14234  15318   3199   2084   -617       C  
ATOM   3320  C   THR B 134     -12.333   9.808  65.224  1.00101.64           C  
ANISOU 3320  C   THR B 134     6586  15568  16464   3399   2025   -655       C  
ATOM   3321  O   THR B 134     -11.179   9.486  65.530  1.00101.05           O  
ANISOU 3321  O   THR B 134     6397  15687  16310   3505   1992   -694       O  
ATOM   3322  CB  THR B 134     -13.004  12.230  65.268  1.00 94.58           C  
ANISOU 3322  CB  THR B 134     5678  14595  15664   3079   2074   -602       C  
ATOM   3323  OG1 THR B 134     -13.165  13.402  64.460  1.00 91.27           O  
ANISOU 3323  OG1 THR B 134     5270  14059  15351   2890   2114   -583       O  
ATOM   3324  CG2 THR B 134     -11.950  12.501  66.328  1.00 93.22           C  
ANISOU 3324  CG2 THR B 134     5312  14726  15383   3173   2040   -618       C  
ATOM   3325  N   ILE B 135     -13.394   9.091  65.601  1.00126.44           N  
ANISOU 3325  N   ILE B 135     9862  18540  19638   3423   2000   -635       N  
ATOM   3326  CA  ILE B 135     -13.229   7.890  66.415  1.00128.99           C  
ANISOU 3326  CA  ILE B 135    10160  18929  19920   3598   1932   -674       C  
ATOM   3327  C   ILE B 135     -12.539   6.787  65.621  1.00130.19           C  
ANISOU 3327  C   ILE B 135    10315  19060  20093   3733   1924   -704       C  
ATOM   3328  O   ILE B 135     -11.637   6.110  66.129  1.00133.17           O  
ANISOU 3328  O   ILE B 135    10620  19553  20428   3852   1860   -757       O  
ATOM   3329  CB  ILE B 135     -14.589   7.426  66.968  1.00129.87           C  
ANISOU 3329  CB  ILE B 135    10414  18848  20081   3574   1913   -624       C  
ATOM   3330  CG1 ILE B 135     -15.116   8.435  67.990  1.00136.92           C  
ANISOU 3330  CG1 ILE B 135    11264  19829  20930   3480   1910   -623       C  
ATOM   3331  CG2 ILE B 135     -14.472   6.041  67.590  1.00129.78           C  
ANISOU 3331  CG2 ILE B 135    10395  18838  20076   3745   1841   -647       C  
ATOM   3332  CD1 ILE B 135     -16.296   7.938  68.786  1.00148.77           C  
ANISOU 3332  CD1 ILE B 135    12857  21215  22453   3483   1885   -591       C  
ATOM   3333  N   LEU B 136     -12.946   6.588  64.364  1.00114.69           N  
ANISOU 3333  N   LEU B 136     8477  16899  18199   3681   1978   -661       N  
ATOM   3334  CA  LEU B 136     -12.318   5.567  63.533  1.00117.15           C  
ANISOU 3334  CA  LEU B 136     8789  17198  18525   3816   1977   -693       C  
ATOM   3335  C   LEU B 136     -10.846   5.858  63.278  1.00107.50           C  
ANISOU 3335  C   LEU B 136     7393  16222  17229   3871   1985   -765       C  
ATOM   3336  O   LEU B 136     -10.084   4.931  62.983  1.00118.76           O  
ANISOU 3336  O   LEU B 136     8794  17682  18648   4006   1958   -811       O  
ATOM   3337  CB  LEU B 136     -13.063   5.429  62.204  1.00110.02           C  
ANISOU 3337  CB  LEU B 136     8047  16059  17697   3736   2039   -639       C  
ATOM   3338  CG  LEU B 136     -14.114   4.318  62.126  1.00111.12           C  
ANISOU 3338  CG  LEU B 136     8361  15945  17913   3786   2015   -578       C  
ATOM   3339  CD1 LEU B 136     -15.237   4.541  63.131  1.00108.38           C  
ANISOU 3339  CD1 LEU B 136     8095  15490  17595   3704   1990   -511       C  
ATOM   3340  CD2 LEU B 136     -14.668   4.201  60.714  1.00122.85           C  
ANISOU 3340  CD2 LEU B 136     9979  17238  19462   3719   2075   -541       C  
ATOM   3341  N   TYR B 137     -10.429   7.118  63.382  1.00106.97           N  
ANISOU 3341  N   TYR B 137     7235  16292  17117   3748   2016   -756       N  
ATOM   3342  CA  TYR B 137      -9.019   7.475  63.308  1.00109.96           C  
ANISOU 3342  CA  TYR B 137     7471  16887  17422   3765   2015   -790       C  
ATOM   3343  C   TYR B 137      -8.325   7.404  64.662  1.00109.44           C  
ANISOU 3343  C   TYR B 137     7313  16989  17278   3828   1933   -821       C  
ATOM   3344  O   TYR B 137      -7.115   7.638  64.735  1.00100.31           O  
ANISOU 3344  O   TYR B 137     6033  16024  16057   3857   1924   -842       O  
ATOM   3345  CB  TYR B 137      -8.849   8.882  62.723  1.00 96.96           C  
ANISOU 3345  CB  TYR B 137     5756  15302  15783   3600   2086   -748       C  
ATOM   3346  CG  TYR B 137      -8.951   8.951  61.215  1.00 96.49           C  
ANISOU 3346  CG  TYR B 137     5724  15164  15775   3553   2164   -744       C  
ATOM   3347  CD1 TYR B 137      -9.689   8.015  60.501  1.00101.53           C  
ANISOU 3347  CD1 TYR B 137     6495  15617  16464   3612   2179   -750       C  
ATOM   3348  CD2 TYR B 137      -8.296   9.946  60.504  1.00 96.97           C  
ANISOU 3348  CD2 TYR B 137     5677  15333  15834   3443   2221   -728       C  
ATOM   3349  CE1 TYR B 137      -9.780   8.077  59.123  1.00107.62           C  
ANISOU 3349  CE1 TYR B 137     7315  16307  17269   3551   2246   -741       C  
ATOM   3350  CE2 TYR B 137      -8.378  10.013  59.127  1.00 96.67           C  
ANISOU 3350  CE2 TYR B 137     5653  15244  15832   3395   2291   -729       C  
ATOM   3351  CZ  TYR B 137      -9.122   9.079  58.442  1.00 95.86           C  
ANISOU 3351  CZ  TYR B 137     5709  14948  15766   3443   2302   -736       C  
ATOM   3352  OH  TYR B 137      -9.206   9.146  57.070  1.00 95.65           O  
ANISOU 3352  OH  TYR B 137     5714  14864  15763   3383   2369   -732       O  
ATOM   3353  N   GLY B 138      -9.059   7.094  65.729  1.00122.45           N  
ANISOU 3353  N   GLY B 138     9012  18580  18932   3849   1874   -824       N  
ATOM   3354  CA  GLY B 138      -8.482   7.026  67.057  1.00129.69           C  
ANISOU 3354  CA  GLY B 138     9839  19657  19779   3901   1789   -870       C  
ATOM   3355  C   GLY B 138      -8.471   8.362  67.772  1.00132.87           C  
ANISOU 3355  C   GLY B 138    10175  20202  20106   3783   1804   -816       C  
ATOM   3356  O   GLY B 138      -7.459   8.743  68.369  1.00104.23           O  
ANISOU 3356  O   GLY B 138     6427  16784  16393   3804   1775   -815       O  
ATOM   3357  N   TYR B 139      -9.597   9.077  67.716  1.00141.52           N  
ANISOU 3357  N   TYR B 139    11346  21180  21245   3664   1852   -757       N  
ATOM   3358  CA  TYR B 139      -9.723  10.413  68.304  1.00141.94           C  
ANISOU 3358  CA  TYR B 139    11340  21324  21266   3544   1876   -692       C  
ATOM   3359  C   TYR B 139      -8.644  11.353  67.770  1.00133.20           C  
ANISOU 3359  C   TYR B 139    10109  20341  20160   3481   1922   -641       C  
ATOM   3360  O   TYR B 139      -8.053  12.145  68.507  1.00128.68           O  
ANISOU 3360  O   TYR B 139     9427  19919  19546   3451   1918   -574       O  
ATOM   3361  CB  TYR B 139      -9.695  10.349  69.834  1.00156.66           C  
ANISOU 3361  CB  TYR B 139    13160  23335  23027   3593   1805   -699       C  
ATOM   3362  CG  TYR B 139     -10.753   9.441  70.423  1.00148.44           C  
ANISOU 3362  CG  TYR B 139    12219  22174  22008   3641   1753   -764       C  
ATOM   3363  CD1 TYR B 139     -12.103   9.700  70.229  1.00149.57           C  
ANISOU 3363  CD1 TYR B 139    12469  22138  22222   3557   1798   -725       C  
ATOM   3364  CD2 TYR B 139     -10.403   8.328  71.177  1.00146.43           C  
ANISOU 3364  CD2 TYR B 139    11935  21958  21743   3759   1655   -874       C  
ATOM   3365  CE1 TYR B 139     -13.072   8.873  70.761  1.00154.70           C  
ANISOU 3365  CE1 TYR B 139    13200  22674  22905   3600   1762   -754       C  
ATOM   3366  CE2 TYR B 139     -11.368   7.496  71.717  1.00149.24           C  
ANISOU 3366  CE2 TYR B 139    12361  22168  22176   3790   1612   -916       C  
ATOM   3367  CZ  TYR B 139     -12.702   7.775  71.506  1.00157.00           C  
ANISOU 3367  CZ  TYR B 139    13456  23002  23195   3716   1672   -837       C  
ATOM   3368  OH  TYR B 139     -13.670   6.954  72.039  1.00150.14           O  
ANISOU 3368  OH  TYR B 139    12651  21997  22399   3751   1641   -840       O  
ATOM   3369  N   ARG B 140      -8.386  11.260  66.467  1.00106.83           N  
ANISOU 3369  N   ARG B 140     6779  16932  16881   3461   1973   -657       N  
ATOM   3370  CA  ARG B 140      -7.381  12.068  65.789  1.00102.28           C  
ANISOU 3370  CA  ARG B 140     6079  16461  16322   3395   2020   -622       C  
ATOM   3371  C   ARG B 140      -8.060  12.889  64.703  1.00 97.55           C  
ANISOU 3371  C   ARG B 140     5510  15711  15842   3239   2087   -614       C  
ATOM   3372  O   ARG B 140      -8.776  12.337  63.860  1.00 96.43           O  
ANISOU 3372  O   ARG B 140     5480  15412  15749   3244   2115   -641       O  
ATOM   3373  CB  ARG B 140      -6.287  11.183  65.189  1.00119.89           C  
ANISOU 3373  CB  ARG B 140     8265  18789  18500   3521   2017   -659       C  
ATOM   3374  CG  ARG B 140      -4.967  11.890  64.935  1.00104.86           C  
ANISOU 3374  CG  ARG B 140     6197  17066  16577   3492   2048   -603       C  
ATOM   3375  CD  ARG B 140      -3.946  10.912  64.384  1.00103.67           C  
ANISOU 3375  CD  ARG B 140     6006  17016  16368   3632   2046   -648       C  
ATOM   3376  NE  ARG B 140      -4.341  10.414  63.072  1.00102.96           N  
ANISOU 3376  NE  ARG B 140     5996  16796  16326   3631   2094   -709       N  
ATOM   3377  CZ  ARG B 140      -3.934   9.264  62.554  1.00103.85           C  
ANISOU 3377  CZ  ARG B 140     6131  16912  16413   3771   2085   -780       C  
ATOM   3378  NH1 ARG B 140      -3.141   8.445  63.225  1.00105.45           N  
ANISOU 3378  NH1 ARG B 140     6283  17229  16554   3922   2019   -824       N  
ATOM   3379  NH2 ARG B 140      -4.341   8.923  61.334  1.00103.19           N  
ANISOU 3379  NH2 ARG B 140     6119  16712  16378   3761   2141   -809       N  
ATOM   3380  N   TRP B 141      -7.827  14.195  64.717  1.00 97.69           N  
ANISOU 3380  N   TRP B 141     5422  15772  15922   3102   2109   -576       N  
ATOM   3381  CA  TRP B 141      -8.562  15.103  63.844  1.00 96.36           C  
ANISOU 3381  CA  TRP B 141     5281  15447  15883   2930   2154   -578       C  
ATOM   3382  C   TRP B 141      -8.054  14.997  62.410  1.00 96.67           C  
ANISOU 3382  C   TRP B 141     5304  15481  15945   2900   2206   -586       C  
ATOM   3383  O   TRP B 141      -6.871  15.255  62.163  1.00120.01           O  
ANISOU 3383  O   TRP B 141     8108  18623  18869   2916   2222   -573       O  
ATOM   3384  CB  TRP B 141      -8.431  16.534  64.344  1.00 96.63           C  
ANISOU 3384  CB  TRP B 141     5215  15498  16001   2776   2139   -555       C  
ATOM   3385  CG  TRP B 141      -9.267  17.495  63.576  1.00101.32           C  
ANISOU 3385  CG  TRP B 141     5901  15852  16746   2560   2154   -569       C  
ATOM   3386  CD1 TRP B 141      -8.829  18.435  62.694  1.00 95.67           C  
ANISOU 3386  CD1 TRP B 141     5109  15118  16124   2411   2175   -563       C  
ATOM   3387  CD2 TRP B 141     -10.694  17.603  63.606  1.00110.91           C  
ANISOU 3387  CD2 TRP B 141     7295  16808  18039   2470   2146   -582       C  
ATOM   3388  NE1 TRP B 141      -9.895  19.128  62.175  1.00117.78           N  
ANISOU 3388  NE1 TRP B 141     8031  17661  19061   2236   2176   -573       N  
ATOM   3389  CE2 TRP B 141     -11.052  18.636  62.720  1.00107.46           C  
ANISOU 3389  CE2 TRP B 141     6883  16198  17750   2269   2161   -584       C  
ATOM   3390  CE3 TRP B 141     -11.704  16.929  64.300  1.00 96.27           C  
ANISOU 3390  CE3 TRP B 141     5573  14855  16148   2538   2127   -587       C  
ATOM   3391  CZ2 TRP B 141     -12.375  19.009  62.505  1.00 91.12           C  
ANISOU 3391  CZ2 TRP B 141     4971  13854  15798   2141   2157   -590       C  
ATOM   3392  CZ3 TRP B 141     -13.018  17.303  64.087  1.00 90.77           C  
ANISOU 3392  CZ3 TRP B 141     5030  13893  15564   2406   2129   -592       C  
ATOM   3393  CH2 TRP B 141     -13.341  18.335  63.199  1.00 90.12           C  
ANISOU 3393  CH2 TRP B 141     4973  13634  15633   2212   2144   -593       C  
ATOM   3394  N   PRO B 142      -8.902  14.626  61.443  1.00 95.33           N  
ANISOU 3394  N   PRO B 142     5294  15099  15829   2849   2236   -596       N  
ATOM   3395  CA  PRO B 142      -8.431  14.483  60.060  1.00 95.75           C  
ANISOU 3395  CA  PRO B 142     5323  15170  15887   2830   2294   -600       C  
ATOM   3396  C   PRO B 142      -8.686  15.702  59.185  1.00103.94           C  
ANISOU 3396  C   PRO B 142     6354  16099  17040   2608   2326   -571       C  
ATOM   3397  O   PRO B 142      -8.180  15.776  58.060  1.00134.59           O  
ANISOU 3397  O   PRO B 142    10177  20042  20918   2575   2376   -567       O  
ATOM   3398  CB  PRO B 142      -9.235  13.281  59.561  1.00 94.73           C  
ANISOU 3398  CB  PRO B 142     5371  14870  15750   2919   2304   -617       C  
ATOM   3399  CG  PRO B 142     -10.551  13.433  60.269  1.00112.83           C  
ANISOU 3399  CG  PRO B 142     7817  16942  18109   2847   2268   -595       C  
ATOM   3400  CD  PRO B 142     -10.260  14.078  61.615  1.00106.75           C  
ANISOU 3400  CD  PRO B 142     6942  16306  17312   2845   2221   -596       C  
ATOM   3401  N   LEU B 143      -9.460  16.657  59.678  1.00 95.20           N  
ANISOU 3401  N   LEU B 143     5296  14838  16036   2458   2295   -556       N  
ATOM   3402  CA  LEU B 143      -9.902  17.793  58.882  1.00111.34           C  
ANISOU 3402  CA  LEU B 143     7359  16730  18216   2242   2311   -533       C  
ATOM   3403  C   LEU B 143      -8.952  18.967  59.055  1.00 94.81           C  
ANISOU 3403  C   LEU B 143     5070  14790  16165   2141   2296   -528       C  
ATOM   3404  O   LEU B 143      -8.060  18.950  59.906  1.00 96.17           O  
ANISOU 3404  O   LEU B 143     5104  15168  16267   2234   2271   -536       O  
ATOM   3405  CB  LEU B 143     -11.324  18.177  59.284  1.00105.45           C  
ANISOU 3405  CB  LEU B 143     6778  15707  17581   2135   2280   -529       C  
ATOM   3406  CG  LEU B 143     -12.404  17.108  59.119  1.00 90.12           C  
ANISOU 3406  CG  LEU B 143     5037  13580  15625   2207   2291   -519       C  
ATOM   3407  CD1 LEU B 143     -13.762  17.664  59.513  1.00 94.11           C  
ANISOU 3407  CD1 LEU B 143     5680  13824  16252   2081   2263   -510       C  
ATOM   3408  CD2 LEU B 143     -12.429  16.587  57.693  1.00 89.87           C  
ANISOU 3408  CD2 LEU B 143     5062  13494  15590   2205   2348   -495       C  
ATOM   3409  N   PRO B 144      -9.097  20.010  58.235  1.00 94.63           N  
ANISOU 3409  N   PRO B 144     5022  14670  16263   1949   2307   -506       N  
ATOM   3410  CA  PRO B 144      -8.377  21.259  58.506  1.00 95.85           C  
ANISOU 3410  CA  PRO B 144     5004  14921  16496   1826   2276   -504       C  
ATOM   3411  C   PRO B 144      -8.781  21.845  59.852  1.00 98.09           C  
ANISOU 3411  C   PRO B 144     5293  15134  16845   1800   2207   -539       C  
ATOM   3412  O   PRO B 144      -9.855  21.563  60.388  1.00116.98           O  
ANISOU 3412  O   PRO B 144     7838  17353  19256   1819   2188   -560       O  
ATOM   3413  CB  PRO B 144      -8.798  22.171  57.349  1.00 95.36           C  
ANISOU 3413  CB  PRO B 144     4960  14703  16569   1619   2293   -471       C  
ATOM   3414  CG  PRO B 144      -9.114  21.231  56.241  1.00 94.67           C  
ANISOU 3414  CG  PRO B 144     4978  14582  16411   1676   2359   -447       C  
ATOM   3415  CD  PRO B 144      -9.706  20.010  56.891  1.00 93.67           C  
ANISOU 3415  CD  PRO B 144     5000  14394  16198   1851   2354   -475       C  
ATOM   3416  N   SER B 145      -7.887  22.671  60.402  1.00 97.11           N  
ANISOU 3416  N   SER B 145     4987  15155  16753   1757   2171   -546       N  
ATOM   3417  CA  SER B 145      -8.093  23.202  61.746  1.00105.54           C  
ANISOU 3417  CA  SER B 145     6029  16201  17869   1750   2106   -589       C  
ATOM   3418  C   SER B 145      -9.370  24.030  61.833  1.00125.92           C  
ANISOU 3418  C   SER B 145     8736  18492  20615   1592   2070   -631       C  
ATOM   3419  O   SER B 145     -10.134  23.904  62.798  1.00122.81           O  
ANISOU 3419  O   SER B 145     8427  18015  20220   1633   2041   -672       O  
ATOM   3420  CB  SER B 145      -6.886  24.039  62.169  1.00107.47           C  
ANISOU 3420  CB  SER B 145     6049  16632  18151   1709   2071   -588       C  
ATOM   3421  OG  SER B 145      -6.704  25.144  61.300  1.00127.68           O  
ANISOU 3421  OG  SER B 145     8536  19123  20854   1514   2063   -582       O  
ATOM   3422  N   LYS B 146      -9.623  24.873  60.827  1.00128.53           N  
ANISOU 3422  N   LYS B 146     9075  18674  21086   1414   2073   -617       N  
ATOM   3423  CA  LYS B 146     -10.790  25.751  60.855  1.00125.89           C  
ANISOU 3423  CA  LYS B 146     8848  18053  20933   1259   2034   -655       C  
ATOM   3424  C   LYS B 146     -12.070  24.953  61.061  1.00104.31           C  
ANISOU 3424  C   LYS B 146     6325  15142  18167   1325   2051   -662       C  
ATOM   3425  O   LYS B 146     -12.891  25.281  61.929  1.00113.46           O  
ANISOU 3425  O   LYS B 146     7548  16171  19392   1303   2010   -721       O  
ATOM   3426  CB  LYS B 146     -10.867  26.558  59.558  1.00125.82           C  
ANISOU 3426  CB  LYS B 146     8827  17917  21062   1078   2044   -609       C  
ATOM   3427  CG  LYS B 146      -9.561  27.223  59.163  1.00115.23           C  
ANISOU 3427  CG  LYS B 146     7273  16774  19736   1011   2038   -582       C  
ATOM   3428  CD  LYS B 146      -9.062  28.147  60.257  1.00108.35           C  
ANISOU 3428  CD  LYS B 146     6259  15956  18950    969   1961   -651       C  
ATOM   3429  CE  LYS B 146      -7.711  28.741  59.900  1.00133.43           C  
ANISOU 3429  CE  LYS B 146     9215  19343  22139    908   1952   -615       C  
ATOM   3430  NZ  LYS B 146      -7.180  29.592  60.999  1.00139.52           N  
ANISOU 3430  NZ  LYS B 146     9843  20170  22997    874   1871   -686       N  
ATOM   3431  N   LEU B 147     -12.227  23.864  60.300  1.00 97.56           N  
ANISOU 3431  N   LEU B 147     5569  14293  17205   1414   2111   -606       N  
ATOM   3432  CA  LEU B 147     -13.427  23.042  60.398  1.00 98.86           C  
ANISOU 3432  CA  LEU B 147     5933  14284  17345   1472   2127   -601       C  
ATOM   3433  C   LEU B 147     -13.695  22.610  61.830  1.00110.73           C  
ANISOU 3433  C   LEU B 147     7454  15852  18766   1593   2096   -647       C  
ATOM   3434  O   LEU B 147     -14.860  22.515  62.240  1.00127.18           O  
ANISOU 3434  O   LEU B 147     9673  17755  20895   1576   2084   -666       O  
ATOM   3435  CB  LEU B 147     -13.301  21.813  59.496  1.00 94.69           C  
ANISOU 3435  CB  LEU B 147     5477  13805  16696   1582   2189   -546       C  
ATOM   3436  CG  LEU B 147     -13.121  22.063  57.998  1.00 95.28           C  
ANISOU 3436  CG  LEU B 147     5543  13836  16822   1480   2233   -492       C  
ATOM   3437  CD1 LEU B 147     -13.238  20.757  57.229  1.00103.32           C  
ANISOU 3437  CD1 LEU B 147     6661  14870  17727   1602   2290   -458       C  
ATOM   3438  CD2 LEU B 147     -14.129  23.083  57.490  1.00100.40           C  
ANISOU 3438  CD2 LEU B 147     6276  14205  17667   1282   2212   -475       C  
ATOM   3439  N   CYS B 148     -12.636  22.382  62.615  1.00 96.51           N  
ANISOU 3439  N   CYS B 148     5508  14315  16847   1711   2083   -660       N  
ATOM   3440  CA  CYS B 148     -12.818  21.984  64.006  1.00102.17           C  
ANISOU 3440  CA  CYS B 148     6221  15127  17473   1832   2055   -689       C  
ATOM   3441  C   CYS B 148     -13.728  22.959  64.735  1.00108.75           C  
ANISOU 3441  C   CYS B 148     7085  15796  18439   1714   2010   -756       C  
ATOM   3442  O   CYS B 148     -14.754  22.562  65.304  1.00 97.50           O  
ANISOU 3442  O   CYS B 148     5779  14272  16993   1751   2009   -770       O  
ATOM   3443  CB  CYS B 148     -11.464  21.887  64.709  1.00100.82           C  
ANISOU 3443  CB  CYS B 148     5859  15254  17193   1945   2042   -682       C  
ATOM   3444  SG  CYS B 148     -11.602  21.816  66.505  1.00102.93           S  
ANISOU 3444  SG  CYS B 148     6075  15651  17385   2052   2000   -710       S  
ATOM   3445  N   ALA B 149     -13.403  24.253  64.668  1.00130.26           N  
ANISOU 3445  N   ALA B 149     9704  18478  21312   1566   1972   -803       N  
ATOM   3446  CA  ALA B 149     -14.257  25.252  65.297  1.00114.98           C  
ANISOU 3446  CA  ALA B 149     7791  16368  19526   1450   1924   -891       C  
ATOM   3447  C   ALA B 149     -15.683  25.114  64.790  1.00108.59           C  
ANISOU 3447  C   ALA B 149     7180  15279  18802   1382   1942   -884       C  
ATOM   3448  O   ALA B 149     -16.630  24.999  65.580  1.00111.27           O  
ANISOU 3448  O   ALA B 149     7600  15540  19140   1405   1931   -927       O  
ATOM   3449  CB  ALA B 149     -13.715  26.656  65.030  1.00137.71           C  
ANISOU 3449  CB  ALA B 149    10539  19201  22583   1286   1876   -942       C  
ATOM   3450  N   VAL B 150     -15.835  25.019  63.464  1.00 94.93           N  
ANISOU 3450  N   VAL B 150     5526  13413  17129   1310   1975   -819       N  
ATOM   3451  CA  VAL B 150     -17.161  24.880  62.869  1.00 87.16           C  
ANISOU 3451  CA  VAL B 150     4729  12151  16239   1241   1992   -794       C  
ATOM   3452  C   VAL B 150     -17.885  23.706  63.504  1.00 91.38           C  
ANISOU 3452  C   VAL B 150     5383  12699  16638   1380   2016   -777       C  
ATOM   3453  O   VAL B 150     -19.025  23.837  63.972  1.00103.08           O  
ANISOU 3453  O   VAL B 150     6964  14014  18186   1344   2004   -811       O  
ATOM   3454  CB  VAL B 150     -17.053  24.717  61.342  1.00 86.64           C  
ANISOU 3454  CB  VAL B 150     4712  11995  16210   1178   2034   -706       C  
ATOM   3455  CG1 VAL B 150     -18.399  24.326  60.751  1.00 95.89           C  
ANISOU 3455  CG1 VAL B 150     6083  12898  17452   1137   2057   -662       C  
ATOM   3456  CG2 VAL B 150     -16.538  25.998  60.706  1.00 87.52           C  
ANISOU 3456  CG2 VAL B 150     4711  12062  16480   1017   2005   -712       C  
ATOM   3457  N   TRP B 151     -17.199  22.561  63.594  1.00 86.66           N  
ANISOU 3457  N   TRP B 151     4764  12311  15853   1544   2047   -729       N  
ATOM   3458  CA  TRP B 151     -17.783  21.390  64.236  1.00 86.03           C  
ANISOU 3458  CA  TRP B 151     4782  12265  15640   1687   2063   -706       C  
ATOM   3459  C   TRP B 151     -18.379  21.776  65.580  1.00103.49           C  
ANISOU 3459  C   TRP B 151     6974  14494  17852   1695   2030   -772       C  
ATOM   3460  O   TRP B 151     -19.602  21.711  65.775  1.00109.83           O  
ANISOU 3460  O   TRP B 151     7902  15118  18711   1657   2031   -780       O  
ATOM   3461  CB  TRP B 151     -16.723  20.296  64.396  1.00 87.00           C  
ANISOU 3461  CB  TRP B 151     4834  12654  15570   1873   2081   -669       C  
ATOM   3462  CG  TRP B 151     -17.274  18.972  64.842  1.00 86.41           C  
ANISOU 3462  CG  TRP B 151     4864  12598  15369   2023   2094   -635       C  
ATOM   3463  CD1 TRP B 151     -18.099  18.149  64.134  1.00 85.10           C  
ANISOU 3463  CD1 TRP B 151     4863  12249  15222   2032   2122   -586       C  
ATOM   3464  CD2 TRP B 151     -17.025  18.312  66.091  1.00 87.21           C  
ANISOU 3464  CD2 TRP B 151     4905  12917  15316   2185   2076   -641       C  
ATOM   3465  NE1 TRP B 151     -18.385  17.021  64.864  1.00 85.05           N  
ANISOU 3465  NE1 TRP B 151     4905  12319  15093   2185   2117   -568       N  
ATOM   3466  CE2 TRP B 151     -17.739  17.097  66.070  1.00 86.34           C  
ANISOU 3466  CE2 TRP B 151     4929  12735  15143   2283   2089   -600       C  
ATOM   3467  CE3 TRP B 151     -16.272  18.632  67.225  1.00 91.76           C  
ANISOU 3467  CE3 TRP B 151     5319  13738  15805   2256   2049   -667       C  
ATOM   3468  CZ2 TRP B 151     -17.722  16.202  67.138  1.00 93.22           C  
ANISOU 3468  CZ2 TRP B 151     5774  13778  15865   2447   2072   -593       C  
ATOM   3469  CZ3 TRP B 151     -16.257  17.742  68.285  1.00 94.73           C  
ANISOU 3469  CZ3 TRP B 151     5671  14297  16023   2426   2039   -647       C  
ATOM   3470  CH2 TRP B 151     -16.976  16.541  68.233  1.00 95.36           C  
ANISOU 3470  CH2 TRP B 151     5883  14308  16040   2519   2047   -616       C  
ATOM   3471  N   ILE B 152     -17.527  22.281  66.482  1.00102.79           N  
ANISOU 3471  N   ILE B 152     6722  14618  17718   1731   1999   -822       N  
ATOM   3472  CA  ILE B 152     -17.994  22.718  67.796  1.00107.61           C  
ANISOU 3472  CA  ILE B 152     7288  15275  18323   1742   1969   -893       C  
ATOM   3473  C   ILE B 152     -19.222  23.597  67.630  1.00 96.33           C  
ANISOU 3473  C   ILE B 152     5954  13562  17085   1581   1953   -958       C  
ATOM   3474  O   ILE B 152     -20.316  23.272  68.114  1.00 92.11           O  
ANISOU 3474  O   ILE B 152     5519  12941  16538   1601   1963   -966       O  
ATOM   3475  CB  ILE B 152     -16.874  23.454  68.551  1.00107.87           C  
ANISOU 3475  CB  ILE B 152     7121  15519  18345   1752   1932   -945       C  
ATOM   3476  CG1 ILE B 152     -15.721  22.500  68.868  1.00100.02           C  
ANISOU 3476  CG1 ILE B 152     6030  14815  17156   1931   1949   -869       C  
ATOM   3477  CG2 ILE B 152     -17.415  24.089  69.825  1.00107.74           C  
ANISOU 3477  CG2 ILE B 152     7056  15523  18359   1737   1900  -1037       C  
ATOM   3478  CD1 ILE B 152     -16.092  21.388  69.824  1.00 93.04           C  
ANISOU 3478  CD1 ILE B 152     5183  14075  16093   2106   1966   -820       C  
ATOM   3479  N   TYR B 153     -19.067  24.671  66.847  1.00 87.82           N  
ANISOU 3479  N   TYR B 153     4849  12326  16191   1422   1929   -996       N  
ATOM   3480  CA  TYR B 153     -20.150  25.607  66.588  1.00 86.34           C  
ANISOU 3480  CA  TYR B 153     4740  11851  16215   1263   1905  -1060       C  
ATOM   3481  C   TYR B 153     -21.433  24.852  66.292  1.00 97.84           C  
ANISOU 3481  C   TYR B 153     6384  13122  17668   1275   1941  -1004       C  
ATOM   3482  O   TYR B 153     -22.387  24.886  67.084  1.00106.19           O  
ANISOU 3482  O   TYR B 153     7489  14123  18736   1281   1936  -1056       O  
ATOM   3483  CB  TYR B 153     -19.765  26.525  65.422  1.00 86.44           C  
ANISOU 3483  CB  TYR B 153     4724  11714  16407   1111   1887  -1053       C  
ATOM   3484  CG  TYR B 153     -20.889  27.386  64.890  1.00 85.50           C  
ANISOU 3484  CG  TYR B 153     4703  11264  16519    951   1864  -1089       C  
ATOM   3485  CD1 TYR B 153     -21.589  28.246  65.725  1.00 87.69           C  
ANISOU 3485  CD1 TYR B 153     4963  11434  16921    890   1819  -1218       C  
ATOM   3486  CD2 TYR B 153     -21.233  27.357  63.544  1.00 84.54           C  
ANISOU 3486  CD2 TYR B 153     4683  10942  16495    866   1887   -997       C  
ATOM   3487  CE1 TYR B 153     -22.609  29.042  65.239  1.00 86.01           C  
ANISOU 3487  CE1 TYR B 153     4835  10911  16934    752   1794  -1255       C  
ATOM   3488  CE2 TYR B 153     -22.252  28.149  63.048  1.00 97.14           C  
ANISOU 3488  CE2 TYR B 153     6365  12231  18311    726   1863  -1018       C  
ATOM   3489  CZ  TYR B 153     -22.936  28.990  63.901  1.00 91.73           C  
ANISOU 3489  CZ  TYR B 153     5663  11432  17757    671   1814  -1147       C  
ATOM   3490  OH  TYR B 153     -23.951  29.781  63.414  1.00 83.29           O  
ANISOU 3490  OH  TYR B 153     4677  10050  16920    542   1786  -1172       O  
ATOM   3491  N   LEU B 154     -21.412  24.063  65.212  1.00 89.07           N  
ANISOU 3491  N   LEU B 154     5371  11947  16524   1293   1981   -896       N  
ATOM   3492  CA  LEU B 154     -22.629  23.393  64.777  1.00 99.72           C  
ANISOU 3492  CA  LEU B 154     6902  13088  17902   1285   2011   -834       C  
ATOM   3493  C   LEU B 154     -23.230  22.614  65.930  1.00102.77           C  
ANISOU 3493  C   LEU B 154     7321  13575  18152   1406   2021   -842       C  
ATOM   3494  O   LEU B 154     -24.378  22.861  66.328  1.00102.17           O  
ANISOU 3494  O   LEU B 154     7318  13346  18155   1354   2016   -878       O  
ATOM   3495  CB  LEU B 154     -22.335  22.475  63.591  1.00 88.95           C  
ANISOU 3495  CB  LEU B 154     5616  11700  16483   1323   2054   -722       C  
ATOM   3496  CG  LEU B 154     -21.882  23.170  62.306  1.00 81.48           C  
ANISOU 3496  CG  LEU B 154     4647  10649  15663   1200   2055   -692       C  
ATOM   3497  CD1 LEU B 154     -21.734  22.160  61.181  1.00 88.61           C  
ANISOU 3497  CD1 LEU B 154     5634  11537  16497   1251   2104   -588       C  
ATOM   3498  CD2 LEU B 154     -22.856  24.273  61.919  1.00 80.76           C  
ANISOU 3498  CD2 LEU B 154     4616  10264  15805   1025   2027   -721       C  
ATOM   3499  N   ASP B 155     -22.414  21.761  66.559  1.00112.22           N  
ANISOU 3499  N   ASP B 155     8443  15050  19145   1569   2032   -816       N  
ATOM   3500  CA  ASP B 155     -22.891  20.956  67.674  1.00115.05           C  
ANISOU 3500  CA  ASP B 155     8816  15541  19356   1700   2041   -807       C  
ATOM   3501  C   ASP B 155     -23.618  21.842  68.670  1.00124.20           C  
ANISOU 3501  C   ASP B 155     9934  16675  20581   1640   2018   -905       C  
ATOM   3502  O   ASP B 155     -24.844  21.738  68.838  1.00133.22           O  
ANISOU 3502  O   ASP B 155    11180  17661  21775   1605   2030   -906       O  
ATOM   3503  CB  ASP B 155     -21.716  20.228  68.334  1.00118.30           C  
ANISOU 3503  CB  ASP B 155     9105  16283  19560   1875   2040   -782       C  
ATOM   3504  CG  ASP B 155     -22.156  19.056  69.195  1.00142.04           C  
ANISOU 3504  CG  ASP B 155    12147  19423  22399   2033   2054   -735       C  
ATOM   3505  OD1 ASP B 155     -23.272  19.102  69.755  1.00135.20           O  
ANISOU 3505  OD1 ASP B 155    11341  18473  21555   2009   2059   -750       O  
ATOM   3506  OD2 ASP B 155     -21.380  18.084  69.312  1.00132.02           O  
ANISOU 3506  OD2 ASP B 155    10837  18345  20980   2182   2056   -686       O  
ATOM   3507  N   VAL B 156     -22.886  22.808  69.238  1.00106.93           N  
ANISOU 3507  N   VAL B 156     7594  14614  18420   1611   1984   -996       N  
ATOM   3508  CA  VAL B 156     -23.465  23.688  70.249  1.00 95.76           C  
ANISOU 3508  CA  VAL B 156     6119  13196  17068   1563   1960  -1113       C  
ATOM   3509  C   VAL B 156     -24.798  24.213  69.751  1.00 95.50           C  
ANISOU 3509  C   VAL B 156     6215  12840  17228   1422   1958  -1152       C  
ATOM   3510  O   VAL B 156     -25.855  23.938  70.339  1.00108.37           O  
ANISOU 3510  O   VAL B 156     7908  14434  18836   1445   1977  -1162       O  
ATOM   3511  CB  VAL B 156     -22.499  24.835  70.590  1.00 95.93           C  
ANISOU 3511  CB  VAL B 156     5973  13311  17163   1506   1913  -1219       C  
ATOM   3512  CG1 VAL B 156     -23.131  25.780  71.602  1.00 90.56           C  
ANISOU 3512  CG1 VAL B 156     5232  12608  16570   1452   1883  -1366       C  
ATOM   3513  CG2 VAL B 156     -21.186  24.284  71.120  1.00115.75           C  
ANISOU 3513  CG2 VAL B 156     8351  16143  19487   1651   1916  -1167       C  
ATOM   3514  N   LEU B 157     -24.767  24.856  68.577  1.00 86.57           N  
ANISOU 3514  N   LEU B 157     5133  11476  16285   1283   1942  -1151       N  
ATOM   3515  CA  LEU B 157     -25.961  25.477  68.023  1.00101.97           C  
ANISOU 3515  CA  LEU B 157     7195  13100  18448   1140   1933  -1183       C  
ATOM   3516  C   LEU B 157     -27.143  24.531  68.131  1.00 98.79           C  
ANISOU 3516  C   LEU B 157     6935  12613  17988   1188   1974  -1110       C  
ATOM   3517  O   LEU B 157     -28.089  24.778  68.893  1.00 98.81           O  
ANISOU 3517  O   LEU B 157     6949  12572  18023   1176   1973  -1180       O  
ATOM   3518  CB  LEU B 157     -25.716  25.880  66.567  1.00 96.35           C  
ANISOU 3518  CB  LEU B 157     6536  12178  17896   1021   1925  -1125       C  
ATOM   3519  CG  LEU B 157     -26.920  26.454  65.817  1.00 86.30           C  
ANISOU 3519  CG  LEU B 157     5388  10549  16853    877   1916  -1127       C  
ATOM   3520  CD1 LEU B 157     -27.425  27.709  66.507  1.00 81.37           C  
ANISOU 3520  CD1 LEU B 157     4698   9821  16399    787   1865  -1290       C  
ATOM   3521  CD2 LEU B 157     -26.573  26.739  64.363  1.00 82.05           C  
ANISOU 3521  CD2 LEU B 157     4890   9847  16439    781   1913  -1043       C  
ATOM   3522  N   PHE B 158     -27.037  23.376  67.471  1.00 85.81           N  
ANISOU 3522  N   PHE B 158     5385  10975  16243   1258   2011   -974       N  
ATOM   3523  CA  PHE B 158     -28.184  22.483  67.405  1.00 79.03           C  
ANISOU 3523  CA  PHE B 158     4671   9993  15363   1286   2046   -893       C  
ATOM   3524  C   PHE B 158     -28.629  22.101  68.805  1.00 79.68           C  
ANISOU 3524  C   PHE B 158     4705  10268  15301   1393   2057   -930       C  
ATOM   3525  O   PHE B 158     -29.779  22.352  69.192  1.00101.07           O  
ANISOU 3525  O   PHE B 158     7463  12853  18086   1344   2063   -968       O  
ATOM   3526  CB  PHE B 158     -27.842  21.252  66.569  1.00 78.29           C  
ANISOU 3526  CB  PHE B 158     4665   9906  15174   1363   2077   -756       C  
ATOM   3527  CG  PHE B 158     -27.524  21.572  65.136  1.00 98.68           C  
ANISOU 3527  CG  PHE B 158     7298  12306  17888   1259   2077   -709       C  
ATOM   3528  CD1 PHE B 158     -28.139  22.642  64.503  1.00 87.71           C  
ANISOU 3528  CD1 PHE B 158     5950  10653  16724   1094   2056   -744       C  
ATOM   3529  CD2 PHE B 158     -26.604  20.819  64.428  1.00101.39           C  
ANISOU 3529  CD2 PHE B 158     7640  12752  18132   1333   2096   -632       C  
ATOM   3530  CE1 PHE B 158     -27.848  22.947  63.187  1.00 87.98           C  
ANISOU 3530  CE1 PHE B 158     6019  10539  16870   1005   2056   -688       C  
ATOM   3531  CE2 PHE B 158     -26.308  21.120  63.112  1.00 85.82           C  
ANISOU 3531  CE2 PHE B 158     5700  10642  16266   1243   2102   -587       C  
ATOM   3532  CZ  PHE B 158     -26.931  22.186  62.491  1.00 85.04           C  
ANISOU 3532  CZ  PHE B 158     5639  10291  16380   1079   2083   -608       C  
ATOM   3533  N   SER B 159     -27.690  21.615  69.621  1.00 80.84           N  
ANISOU 3533  N   SER B 159     4737  10735  15245   1538   2059   -927       N  
ATOM   3534  CA  SER B 159     -28.070  21.175  70.954  1.00 81.57           C  
ANISOU 3534  CA  SER B 159     4772  11045  15178   1655   2074   -941       C  
ATOM   3535  C   SER B 159     -28.666  22.330  71.737  1.00 82.26           C  
ANISOU 3535  C   SER B 159     4788  11105  15361   1576   2058  -1081       C  
ATOM   3536  O   SER B 159     -29.731  22.185  72.354  1.00 98.87           O  
ANISOU 3536  O   SER B 159     6924  13192  17451   1587   2080  -1094       O  
ATOM   3537  CB  SER B 159     -26.868  20.575  71.680  1.00104.29           C  
ANISOU 3537  CB  SER B 159     7519  14274  17834   1821   2073   -912       C  
ATOM   3538  OG  SER B 159     -26.486  19.341  71.097  1.00124.04           O  
ANISOU 3538  OG  SER B 159    10090  16803  20238   1916   2087   -796       O  
ATOM   3539  N   THR B 160     -28.046  23.512  71.639  1.00 83.01           N  
ANISOU 3539  N   THR B 160     4791  11171  15580   1484   2017  -1193       N  
ATOM   3540  CA  THR B 160     -28.579  24.671  72.340  1.00 92.28           C  
ANISOU 3540  CA  THR B 160     5893  12294  16874   1403   1992  -1353       C  
ATOM   3541  C   THR B 160     -30.038  24.872  71.965  1.00 95.31           C  
ANISOU 3541  C   THR B 160     6407  12386  17419   1299   2003  -1370       C  
ATOM   3542  O   THR B 160     -30.923  24.853  72.833  1.00 98.99           O  
ANISOU 3542  O   THR B 160     6862  12902  17848   1329   2024  -1418       O  
ATOM   3543  CB  THR B 160     -27.751  25.916  72.013  1.00 94.50           C  
ANISOU 3543  CB  THR B 160     6078  12510  17316   1295   1935  -1469       C  
ATOM   3544  OG1 THR B 160     -26.384  25.691  72.378  1.00 85.74           O  
ANISOU 3544  OG1 THR B 160     4843  11679  16057   1393   1927  -1444       O  
ATOM   3545  CG2 THR B 160     -28.272  27.123  72.772  1.00106.61           C  
ANISOU 3545  CG2 THR B 160     7532  13986  18990   1215   1899  -1662       C  
ATOM   3546  N   ALA B 161     -30.314  24.932  70.657  1.00 90.90           N  
ANISOU 3546  N   ALA B 161     5976  11537  17026   1190   1996  -1306       N  
ATOM   3547  CA  ALA B 161     -31.686  25.133  70.212  1.00 88.31           C  
ANISOU 3547  CA  ALA B 161     5774  10908  16872   1086   2004  -1307       C  
ATOM   3548  C   ALA B 161     -32.596  24.125  70.884  1.00 87.55           C  
ANISOU 3548  C   ALA B 161     5733  10901  16632   1183   2053  -1236       C  
ATOM   3549  O   ALA B 161     -33.556  24.501  71.574  1.00 80.15           O  
ANISOU 3549  O   ALA B 161     4781   9933  15739   1161   2061  -1320       O  
ATOM   3550  CB  ALA B 161     -31.770  25.018  68.689  1.00 78.70           C  
ANISOU 3550  CB  ALA B 161     4690   9409  15802    989   2001  -1198       C  
ATOM   3551  N   LYS B 162     -32.215  22.845  70.801  1.00 79.43           N  
ANISOU 3551  N   LYS B 162     4744  10018  15416   1304   2086  -1093       N  
ATOM   3552  CA  LYS B 162     -32.999  21.769  71.387  1.00 79.15           C  
ANISOU 3552  CA  LYS B 162     4760  10074  15241   1405   2130  -1006       C  
ATOM   3553  C   LYS B 162     -33.450  22.145  72.783  1.00 80.45           C  
ANISOU 3553  C   LYS B 162     4807  10440  15319   1457   2143  -1110       C  
ATOM   3554  O   LYS B 162     -34.647  22.335  73.036  1.00 89.78           O  
ANISOU 3554  O   LYS B 162     6031  11500  16580   1408   2161  -1142       O  
ATOM   3555  CB  LYS B 162     -32.181  20.477  71.432  1.00 79.23           C  
ANISOU 3555  CB  LYS B 162     4766  10301  15037   1558   2148   -880       C  
ATOM   3556  CG  LYS B 162     -31.978  19.801  70.096  1.00 77.93           C  
ANISOU 3556  CG  LYS B 162     4734   9938  14936   1529   2150   -759       C  
ATOM   3557  CD  LYS B 162     -31.732  18.320  70.309  1.00 77.91           C  
ANISOU 3557  CD  LYS B 162     4759  10096  14747   1684   2172   -638       C  
ATOM   3558  CE  LYS B 162     -32.947  17.658  70.949  1.00 80.90           C  
ANISOU 3558  CE  LYS B 162     5192  10461  15086   1723   2202   -586       C  
ATOM   3559  NZ  LYS B 162     -32.831  16.174  70.977  1.00 91.91           N  
ANISOU 3559  NZ  LYS B 162     6635  11937  16351   1854   2215   -459       N  
ATOM   3560  N   ILE B 163     -32.482  22.354  73.679  1.00 81.95           N  
ANISOU 3560  N   ILE B 163     4841  10937  15360   1551   2133  -1171       N  
ATOM   3561  CA  ILE B 163     -32.849  22.517  75.078  1.00 87.50           C  
ANISOU 3561  CA  ILE B 163     5423  11884  15938   1630   2158  -1244       C  
ATOM   3562  C   ILE B 163     -33.715  23.757  75.233  1.00 83.63           C  
ANISOU 3562  C   ILE B 163     4919  11204  15651   1497   2142  -1412       C  
ATOM   3563  O   ILE B 163     -34.799  23.701  75.832  1.00 83.82           O  
ANISOU 3563  O   ILE B 163     4948  11236  15663   1506   2176  -1436       O  
ATOM   3564  CB  ILE B 163     -31.594  22.537  75.976  1.00102.73           C  
ANISOU 3564  CB  ILE B 163     7183  14166  17684   1751   2151  -1264       C  
ATOM   3565  CG1 ILE B 163     -31.985  22.614  77.452  1.00102.05           C  
ANISOU 3565  CG1 ILE B 163     6968  14354  17454   1845   2189  -1311       C  
ATOM   3566  CG2 ILE B 163     -30.639  23.658  75.604  1.00104.66           C  
ANISOU 3566  CG2 ILE B 163     7358  14340  18069   1658   2095  -1383       C  
ATOM   3567  CD1 ILE B 163     -32.676  21.377  77.967  1.00 95.55           C  
ANISOU 3567  CD1 ILE B 163     6174  13693  16439   1971   2245  -1169       C  
ATOM   3568  N   TRP B 164     -33.320  24.860  74.590  1.00 83.60           N  
ANISOU 3568  N   TRP B 164     4907  11001  15856   1366   2087  -1525       N  
ATOM   3569  CA  TRP B 164     -34.105  26.078  74.723  1.00 84.01           C  
ANISOU 3569  CA  TRP B 164     4939  10858  16124   1240   2059  -1705       C  
ATOM   3570  C   TRP B 164     -35.479  25.890  74.107  1.00 91.94           C  
ANISOU 3570  C   TRP B 164     6092  11571  17271   1157   2080  -1655       C  
ATOM   3571  O   TRP B 164     -36.488  26.315  74.688  1.00 85.35           O  
ANISOU 3571  O   TRP B 164     5236  10694  16500   1129   2094  -1757       O  
ATOM   3572  CB  TRP B 164     -33.366  27.261  74.101  1.00 84.97           C  
ANISOU 3572  CB  TRP B 164     5019  10814  16453   1118   1988  -1827       C  
ATOM   3573  CG  TRP B 164     -32.259  27.769  74.975  1.00 98.70           C  
ANISOU 3573  CG  TRP B 164     6582  12819  18099   1177   1960  -1939       C  
ATOM   3574  CD1 TRP B 164     -30.928  27.510  74.842  1.00111.87           C  
ANISOU 3574  CD1 TRP B 164     8189  14657  19660   1235   1945  -1874       C  
ATOM   3575  CD2 TRP B 164     -32.390  28.606  76.133  1.00 87.84           C  
ANISOU 3575  CD2 TRP B 164     5067  11571  16736   1184   1943  -2140       C  
ATOM   3576  NE1 TRP B 164     -30.219  28.141  75.836  1.00122.22           N  
ANISOU 3576  NE1 TRP B 164     9331  16183  20922   1273   1918  -2012       N  
ATOM   3577  CE2 TRP B 164     -31.094  28.821  76.642  1.00113.01           C  
ANISOU 3577  CE2 TRP B 164     8116  14995  19828   1242   1915  -2182       C  
ATOM   3578  CE3 TRP B 164     -33.477  29.199  76.784  1.00 88.52           C  
ANISOU 3578  CE3 TRP B 164     5127  11595  16910   1146   1949  -2296       C  
ATOM   3579  CZ2 TRP B 164     -30.855  29.602  77.772  1.00108.89           C  
ANISOU 3579  CZ2 TRP B 164     7437  14637  19301   1260   1890  -2377       C  
ATOM   3580  CZ3 TRP B 164     -33.236  29.975  77.905  1.00 93.51           C  
ANISOU 3580  CZ3 TRP B 164     5600  12401  17529   1169   1926  -2499       C  
ATOM   3581  CH2 TRP B 164     -31.936  30.169  78.387  1.00 91.76           C  
ANISOU 3581  CH2 TRP B 164     5247  12403  17215   1224   1896  -2540       C  
ATOM   3582  N   HIS B 165     -35.546  25.191  72.968  1.00 90.90           N  
ANISOU 3582  N   HIS B 165     6105  11251  17181   1126   2087  -1494       N  
ATOM   3583  CA  HIS B 165     -36.844  24.857  72.399  1.00 86.43           C  
ANISOU 3583  CA  HIS B 165     5683  10418  16737   1058   2111  -1418       C  
ATOM   3584  C   HIS B 165     -37.702  24.178  73.451  1.00 82.39           C  
ANISOU 3584  C   HIS B 165     5147  10093  16064   1159   2167  -1392       C  
ATOM   3585  O   HIS B 165     -38.800  24.652  73.777  1.00 94.09           O  
ANISOU 3585  O   HIS B 165     6632  11464  17655   1103   2178  -1476       O  
ATOM   3586  CB  HIS B 165     -36.675  23.954  71.174  1.00 78.60           C  
ANISOU 3586  CB  HIS B 165     4839   9267  15758   1046   2120  -1228       C  
ATOM   3587  CG  HIS B 165     -36.684  24.691  69.871  1.00 77.05           C  
ANISOU 3587  CG  HIS B 165     4726   8734  15817    892   2078  -1231       C  
ATOM   3588  ND1 HIS B 165     -35.771  25.677  69.566  1.00 78.36           N  
ANISOU 3588  ND1 HIS B 165     4814   8878  16080    831   2028  -1328       N  
ATOM   3589  CD2 HIS B 165     -37.493  24.581  68.791  1.00 75.59           C  
ANISOU 3589  CD2 HIS B 165     4689   8224  15810    791   2079  -1138       C  
ATOM   3590  CE1 HIS B 165     -36.020  26.147  68.357  1.00 78.84           C  
ANISOU 3590  CE1 HIS B 165     4969   8623  16363    703   2002  -1292       C  
ATOM   3591  NE2 HIS B 165     -37.059  25.498  67.864  1.00 75.37           N  
ANISOU 3591  NE2 HIS B 165     4668   7996  15974    677   2032  -1177       N  
ATOM   3592  N   LEU B 166     -37.160  23.124  74.070  1.00 80.59           N  
ANISOU 3592  N   LEU B 166     4874  10174  15572   1315   2202  -1287       N  
ATOM   3593  CA  LEU B 166     -37.890  22.432  75.122  1.00 81.24           C  
ANISOU 3593  CA  LEU B 166     4914  10476  15478   1425   2259  -1247       C  
ATOM   3594  C   LEU B 166     -38.337  23.424  76.182  1.00 84.16           C  
ANISOU 3594  C   LEU B 166     5150  10961  15864   1415   2266  -1431       C  
ATOM   3595  O   LEU B 166     -39.528  23.507  76.513  1.00 86.31           O  
ANISOU 3595  O   LEU B 166     5439  11166  16188   1388   2299  -1461       O  
ATOM   3596  CB  LEU B 166     -37.014  21.336  75.729  1.00 84.70           C  
ANISOU 3596  CB  LEU B 166     5285  11265  15633   1601   2281  -1132       C  
ATOM   3597  CG  LEU B 166     -36.564  20.230  74.772  1.00 80.50           C  
ANISOU 3597  CG  LEU B 166     4875  10639  15072   1632   2274   -964       C  
ATOM   3598  CD1 LEU B 166     -35.455  19.406  75.398  1.00 91.14           C  
ANISOU 3598  CD1 LEU B 166     6124  12340  16166   1801   2277   -899       C  
ATOM   3599  CD2 LEU B 166     -37.736  19.343  74.388  1.00 79.31           C  
ANISOU 3599  CD2 LEU B 166     4862  10302  14969   1614   2307   -837       C  
ATOM   3600  N   CYS B 167     -37.400  24.257  76.648  1.00 88.31           N  
ANISOU 3600  N   CYS B 167     5546  11630  16376   1422   2233  -1566       N  
ATOM   3601  CA  CYS B 167     -37.728  25.245  77.666  1.00 85.79           C  
ANISOU 3601  CA  CYS B 167     5092  11417  16086   1411   2235  -1764       C  
ATOM   3602  C   CYS B 167     -38.909  26.087  77.222  1.00 99.27           C  
ANISOU 3602  C   CYS B 167     6868  12789  18063   1263   2216  -1887       C  
ATOM   3603  O   CYS B 167     -39.936  26.152  77.913  1.00110.65           O  
ANISOU 3603  O   CYS B 167     8274  14278  19488   1278   2259  -1943       O  
ATOM   3604  CB  CYS B 167     -36.508  26.121  77.955  1.00 93.85           C  
ANISOU 3604  CB  CYS B 167     5987  12547  17125   1404   2182  -1904       C  
ATOM   3605  SG  CYS B 167     -36.778  27.400  79.198  1.00 89.31           S  
ANISOU 3605  SG  CYS B 167     5240  12087  16608   1385   2171  -2185       S  
ATOM   3606  N   ALA B 168     -38.815  26.656  76.015  1.00129.78           N  
ANISOU 3606  N   ALA B 168    10830  16308  22173   1122   2157  -1907       N  
ATOM   3607  CA  ALA B 168     -39.885  27.510  75.520  1.00131.75           C  
ANISOU 3607  CA  ALA B 168    11141  16215  22705    976   2131  -2017       C  
ATOM   3608  C   ALA B 168     -41.216  26.787  75.618  1.00121.01           C  
ANISOU 3608  C   ALA B 168     9862  14798  21319    993   2192  -1917       C  
ATOM   3609  O   ALA B 168     -42.175  27.304  76.209  1.00124.27           O  
ANISOU 3609  O   ALA B 168    10225  15187  21805    968   2209  -2046       O  
ATOM   3610  CB  ALA B 168     -39.597  27.936  74.079  1.00130.53           C  
ANISOU 3610  CB  ALA B 168    11100  15706  22791    841   2071  -1977       C  
ATOM   3611  N   ILE B 169     -41.250  25.540  75.133  1.00 92.84           N  
ANISOU 3611  N   ILE B 169     6404  11237  17632   1048   2228  -1692       N  
ATOM   3612  CA  ILE B 169     -42.483  24.759  75.148  1.00 81.07           C  
ANISOU 3612  CA  ILE B 169     4998   9678  16127   1061   2283  -1575       C  
ATOM   3613  C   ILE B 169     -43.109  24.815  76.531  1.00 93.26           C  
ANISOU 3613  C   ILE B 169     6409  11501  17525   1149   2338  -1667       C  
ATOM   3614  O   ILE B 169     -44.228  25.319  76.708  1.00101.98           O  
ANISOU 3614  O   ILE B 169     7511  12471  18766   1085   2352  -1761       O  
ATOM   3615  CB  ILE B 169     -42.212  23.309  74.713  1.00 79.86           C  
ANISOU 3615  CB  ILE B 169     4945   9582  15815   1143   2313  -1336       C  
ATOM   3616  CG1 ILE B 169     -41.901  23.249  73.218  1.00 78.10           C  
ANISOU 3616  CG1 ILE B 169     4873   9031  15771   1037   2270  -1239       C  
ATOM   3617  CG2 ILE B 169     -43.399  22.424  75.047  1.00 83.49           C  
ANISOU 3617  CG2 ILE B 169     5453  10059  16212   1186   2374  -1222       C  
ATOM   3618  CD1 ILE B 169     -41.732  21.842  72.690  1.00 76.91           C  
ANISOU 3618  CD1 ILE B 169     4832   8887  15504   1105   2295  -1019       C  
ATOM   3619  N   SER B 170     -42.347  24.389  77.545  1.00 86.85           N  
ANISOU 3619  N   SER B 170     5470  11089  16439   1297   2369  -1653       N  
ATOM   3620  CA  SER B 170     -42.894  24.333  78.894  1.00 85.79           C  
ANISOU 3620  CA  SER B 170     5199  11265  16133   1398   2435  -1709       C  
ATOM   3621  C   SER B 170     -43.461  25.687  79.284  1.00 94.21           C  
ANISOU 3621  C   SER B 170     6185  12227  17383   1308   2416  -1962       C  
ATOM   3622  O   SER B 170     -44.648  25.803  79.620  1.00109.36           O  
ANISOU 3622  O   SER B 170     8095  14101  19354   1287   2458  -2008       O  
ATOM   3623  CB  SER B 170     -41.818  23.889  79.886  1.00 87.14           C  
ANISOU 3623  CB  SER B 170     5231  11867  16012   1558   2462  -1667       C  
ATOM   3624  OG  SER B 170     -40.873  24.921  80.105  1.00 99.46           O  
ANISOU 3624  OG  SER B 170     6694  13465  17630   1530   2411  -1841       O  
ATOM   3625  N   LEU B 171     -42.649  26.739  79.132  1.00 87.56           N  
ANISOU 3625  N   LEU B 171     5290  11307  16670   1241   2346  -2135       N  
ATOM   3626  CA  LEU B 171     -43.099  28.074  79.502  1.00 88.89           C  
ANISOU 3626  CA  LEU B 171     5374  11366  17034   1154   2313  -2406       C  
ATOM   3627  C   LEU B 171     -44.419  28.384  78.822  1.00 91.03           C  
ANISOU 3627  C   LEU B 171     5749  11279  17557   1031   2306  -2433       C  
ATOM   3628  O   LEU B 171     -45.422  28.678  79.487  1.00115.81           O  
ANISOU 3628  O   LEU B 171     8826  14457  20720   1034   2346  -2544       O  
ATOM   3629  CB  LEU B 171     -42.040  29.111  79.128  1.00 89.19           C  
ANISOU 3629  CB  LEU B 171     5371  11289  17229   1075   2220  -2565       C  
ATOM   3630  CG  LEU B 171     -40.783  29.173  79.996  1.00 95.96           C  
ANISOU 3630  CG  LEU B 171     6084  12490  17886   1179   2216  -2619       C  
ATOM   3631  CD1 LEU B 171     -39.660  29.883  79.260  1.00100.04           C  
ANISOU 3631  CD1 LEU B 171     6604  12849  18557   1095   2123  -2688       C  
ATOM   3632  CD2 LEU B 171     -41.088  29.880  81.304  1.00 99.30           C  
ANISOU 3632  CD2 LEU B 171     6341  13123  18267   1220   2237  -2851       C  
ATOM   3633  N   ASP B 172     -44.459  28.209  77.497  1.00 85.96           N  
ANISOU 3633  N   ASP B 172     5268  10301  17091    930   2265  -2308       N  
ATOM   3634  CA  ASP B 172     -45.661  28.544  76.747  1.00 96.37           C  
ANISOU 3634  CA  ASP B 172     6692  11245  18678    803   2251  -2319       C  
ATOM   3635  C   ASP B 172     -46.862  27.824  77.335  1.00114.85           C  
ANISOU 3635  C   ASP B 172     9034  13694  20908    865   2335  -2241       C  
ATOM   3636  O   ASP B 172     -47.869  28.455  77.685  1.00111.39           O  
ANISOU 3636  O   ASP B 172     8551  13168  20606    817   2346  -2388       O  
ATOM   3637  CB  ASP B 172     -45.476  28.190  75.270  1.00 86.16           C  
ANISOU 3637  CB  ASP B 172     5577   9627  17535    712   2212  -2139       C  
ATOM   3638  CG  ASP B 172     -46.639  28.649  74.408  1.00104.52           C  
ANISOU 3638  CG  ASP B 172     8009  11535  20168    570   2187  -2148       C  
ATOM   3639  OD1 ASP B 172     -46.949  29.859  74.421  1.00106.47           O  
ANISOU 3639  OD1 ASP B 172     8201  11603  20648    478   2135  -2356       O  
ATOM   3640  OD2 ASP B 172     -47.237  27.802  73.710  1.00 98.24           O  
ANISOU 3640  OD2 ASP B 172     7352  10582  19392    550   2215  -1948       O  
ATOM   3641  N   ARG B 173     -46.729  26.511  77.549  1.00117.67           N  
ANISOU 3641  N   ARG B 173     9424  14276  21010    982   2398  -2022       N  
ATOM   3642  CA  ARG B 173     -47.869  25.736  78.020  1.00 97.46           C  
ANISOU 3642  CA  ARG B 173     6871  11809  18352   1038   2478  -1919       C  
ATOM   3643  C   ARG B 173     -48.380  26.295  79.337  1.00 98.47           C  
ANISOU 3643  C   ARG B 173     6824  12200  18390   1099   2528  -2102       C  
ATOM   3644  O   ARG B 173     -49.586  26.522  79.500  1.00118.88           O  
ANISOU 3644  O   ARG B 173     9403  14683  21084   1058   2560  -2160       O  
ATOM   3645  CB  ARG B 173     -47.494  24.260  78.158  1.00 95.51           C  
ANISOU 3645  CB  ARG B 173     6659  11797  17832   1167   2528  -1671       C  
ATOM   3646  CG  ARG B 173     -47.424  23.522  76.832  1.00 94.69           C  
ANISOU 3646  CG  ARG B 173     6748  11392  17840   1102   2497  -1473       C  
ATOM   3647  CD  ARG B 173     -47.303  22.022  77.030  1.00101.74           C  
ANISOU 3647  CD  ARG B 173     7672  12488  18495   1224   2546  -1246       C  
ATOM   3648  NE  ARG B 173     -48.505  21.439  77.614  1.00103.06           N  
ANISOU 3648  NE  ARG B 173     7819  12740  18599   1265   2616  -1177       N  
ATOM   3649  CZ  ARG B 173     -49.503  20.918  76.913  1.00101.14           C  
ANISOU 3649  CZ  ARG B 173     7710  12213  18505   1194   2628  -1047       C  
ATOM   3650  NH1 ARG B 173     -49.478  20.890  75.590  1.00 90.84           N  
ANISOU 3650  NH1 ARG B 173     6574  10523  17418   1081   2577   -965       N  
ATOM   3651  NH2 ARG B 173     -50.552  20.412  77.555  1.00106.90           N  
ANISOU 3651  NH2 ARG B 173     8396  13056  19163   1238   2696   -991       N  
ATOM   3652  N   TYR B 174     -47.464  26.602  80.260  1.00 88.82           N  
ANISOU 3652  N   TYR B 174     5455  11302  16990   1191   2533  -2209       N  
ATOM   3653  CA  TYR B 174     -47.888  27.170  81.533  1.00 91.21           C  
ANISOU 3653  CA  TYR B 174     5586  11863  17208   1250   2585  -2394       C  
ATOM   3654  C   TYR B 174     -48.697  28.435  81.296  1.00 98.06           C  
ANISOU 3654  C   TYR B 174     6444  12425  18389   1112   2537  -2646       C  
ATOM   3655  O   TYR B 174     -49.856  28.536  81.721  1.00119.26           O  
ANISOU 3655  O   TYR B 174     9090  15114  21110   1109   2590  -2704       O  
ATOM   3656  CB  TYR B 174     -46.674  27.452  82.417  1.00 92.80           C  
ANISOU 3656  CB  TYR B 174     5642  12393  17224   1345   2581  -2487       C  
ATOM   3657  CG  TYR B 174     -47.026  27.874  83.826  1.00 95.44           C  
ANISOU 3657  CG  TYR B 174     5794  13041  17429   1427   2650  -2653       C  
ATOM   3658  N   VAL B 175     -48.136  29.369  80.524  1.00 91.17           N  
ANISOU 3658  N   VAL B 175     5613  11265  17763    993   2434  -2780       N  
ATOM   3659  CA  VAL B 175     -48.863  30.593  80.215  1.00105.86           C  
ANISOU 3659  CA  VAL B 175     7466  12805  19953    856   2375  -3016       C  
ATOM   3660  C   VAL B 175     -50.161  30.256  79.498  1.00125.28           C  
ANISOU 3660  C   VAL B 175    10050  14973  22578    780   2397  -2899       C  
ATOM   3661  O   VAL B 175     -51.230  30.787  79.833  1.00118.86           O  
ANISOU 3661  O   VAL B 175     9185  14080  21898    742   2414  -3046       O  
ATOM   3662  CB  VAL B 175     -47.979  31.548  79.391  1.00 91.09           C  
ANISOU 3662  CB  VAL B 175     5626  10662  18322    741   2258  -3133       C  
ATOM   3663  CG1 VAL B 175     -48.791  32.733  78.894  1.00 99.26           C  
ANISOU 3663  CG1 VAL B 175     6671  11312  19732    592   2189  -3339       C  
ATOM   3664  CG2 VAL B 175     -46.801  32.024  80.228  1.00 92.75           C  
ANISOU 3664  CG2 VAL B 175     5689  11159  18394    810   2233  -3293       C  
ATOM   3665  N   ALA B 176     -50.104  29.303  78.561  1.00139.23           N  
ANISOU 3665  N   ALA B 176    11976  16597  24327    765   2401  -2631       N  
ATOM   3666  CA  ALA B 176     -51.277  28.970  77.764  1.00151.48           C  
ANISOU 3666  CA  ALA B 176    13661  17835  26060    681   2412  -2507       C  
ATOM   3667  C   ALA B 176     -52.419  28.454  78.624  1.00145.64           C  
ANISOU 3667  C   ALA B 176    12857  17290  25189    757   2510  -2480       C  
ATOM   3668  O   ALA B 176     -53.570  28.450  78.173  1.00157.91           O  
ANISOU 3668  O   ALA B 176    14481  18589  26929    681   2519  -2446       O  
ATOM   3669  CB  ALA B 176     -50.915  27.940  76.694  1.00154.56           C  
ANISOU 3669  CB  ALA B 176    14225  18078  26421    667   2405  -2224       C  
ATOM   3670  N   ILE B 177     -52.131  28.033  79.853  1.00118.51           N  
ANISOU 3670  N   ILE B 177     9283  14304  21442    906   2584  -2488       N  
ATOM   3671  CA  ILE B 177     -53.170  27.558  80.753  1.00116.70           C  
ANISOU 3671  CA  ILE B 177     8968  14307  21064    989   2686  -2459       C  
ATOM   3672  C   ILE B 177     -53.435  28.533  81.891  1.00108.76           C  
ANISOU 3672  C   ILE B 177     7774  13508  20042   1022   2714  -2742       C  
ATOM   3673  O   ILE B 177     -54.522  28.480  82.490  1.00105.71           O  
ANISOU 3673  O   ILE B 177     7316  13219  19630   1051   2788  -2778       O  
ATOM   3674  CB  ILE B 177     -52.827  26.152  81.292  1.00106.92           C  
ANISOU 3674  CB  ILE B 177     7714  13440  19469   1142   2768  -2206       C  
ATOM   3675  CG1 ILE B 177     -52.652  25.204  80.102  1.00107.20           C  
ANISOU 3675  CG1 ILE B 177     7945  13227  19560   1098   2734  -1952       C  
ATOM   3676  CG2 ILE B 177     -53.911  25.606  82.211  1.00116.07           C  
ANISOU 3676  CG2 ILE B 177     8777  14858  20467   1229   2880  -2149       C  
ATOM   3677  CD1 ILE B 177     -52.225  23.817  80.470  1.00 89.01           C  
ANISOU 3677  CD1 ILE B 177     5638  11232  16948   1234   2790  -1713       C  
ATOM   3678  N   GLN B 178     -52.520  29.467  82.161  1.00105.89           N  
ANISOU 3678  N   GLN B 178     7328  13188  19719   1009   2652  -2958       N  
ATOM   3679  CA  GLN B 178     -52.768  30.412  83.243  1.00100.78           C  
ANISOU 3679  CA  GLN B 178     6501  12721  19071   1036   2672  -3252       C  
ATOM   3680  C   GLN B 178     -53.860  31.412  82.884  1.00109.67           C  
ANISOU 3680  C   GLN B 178     7628  13503  20538    906   2628  -3466       C  
ATOM   3681  O   GLN B 178     -54.524  31.945  83.782  1.00124.16           O  
ANISOU 3681  O   GLN B 178     9323  15484  22368    936   2673  -3674       O  
ATOM   3682  CB  GLN B 178     -51.477  31.139  83.623  1.00101.89           C  
ANISOU 3682  CB  GLN B 178     6551  12985  19179   1051   2607  -3436       C  
ATOM   3683  CG  GLN B 178     -51.349  31.438  85.115  1.00106.48           C  
ANISOU 3683  CG  GLN B 178     6931  13979  19548   1166   2674  -3622       C  
ATOM   3684  CD  GLN B 178     -51.101  30.194  85.960  1.00105.39           C  
ANISOU 3684  CD  GLN B 178     6741  14286  19018   1337   2797  -3371       C  
ATOM   3685  OE1 GLN B 178     -51.180  29.065  85.475  1.00100.94           O  
ANISOU 3685  OE1 GLN B 178     6285  13728  18340   1374   2834  -3065       O  
ATOM   3686  NE2 GLN B 178     -50.789  30.402  87.235  1.00104.27           N  
ANISOU 3686  NE2 GLN B 178     6416  14496  18706   1430   2863  -3532       N  
ATOM   3687  N   ASN B 179     -54.059  31.684  81.596  1.00132.36           N  
ANISOU 3687  N   ASN B 179     8834  21280  20178    918   5692  -3217       N  
ATOM   3688  CA  ASN B 179     -55.227  32.444  81.161  1.00134.46           C  
ANISOU 3688  CA  ASN B 179     8949  21503  20636   1121   5841  -3004       C  
ATOM   3689  C   ASN B 179     -56.446  31.542  81.248  1.00137.90           C  
ANISOU 3689  C   ASN B 179     9149  22163  21085   1142   5842  -2642       C  
ATOM   3690  O   ASN B 179     -56.477  30.497  80.580  1.00133.31           O  
ANISOU 3690  O   ASN B 179     8479  21650  20521    999   5606  -2433       O  
ATOM   3691  CB  ASN B 179     -55.045  32.956  79.739  1.00146.58           C  
ANISOU 3691  CB  ASN B 179    10475  22848  22373   1145   5686  -2926       C  
ATOM   3692  CG  ASN B 179     -56.187  33.847  79.289  1.00136.62           C  
ANISOU 3692  CG  ASN B 179     9066  21556  21286   1377   5844  -2735       C  
ATOM   3693  OD1 ASN B 179     -56.865  34.465  80.110  1.00138.34           O  
ANISOU 3693  OD1 ASN B 179     9255  21830  21479   1547   6119  -2763       O  
ATOM   3694  ND2 ASN B 179     -56.408  33.919  77.983  1.00140.43           N  
ANISOU 3694  ND2 ASN B 179     9459  21965  21933   1397   5675  -2541       N  
ATOM   3695  N   PRO B 180     -57.462  31.885  82.046  1.00149.76           N  
ANISOU 3695  N   PRO B 180    10544  23784  22575   1309   6107  -2556       N  
ATOM   3696  CA  PRO B 180     -58.579  30.949  82.241  1.00139.76           C  
ANISOU 3696  CA  PRO B 180     9041  22754  21307   1300   6117  -2220       C  
ATOM   3697  C   PRO B 180     -59.487  30.875  81.024  1.00144.14           C  
ANISOU 3697  C   PRO B 180     9348  23363  22057   1342   5983  -1865       C  
ATOM   3698  O   PRO B 180     -60.699  31.072  81.145  1.00142.48           O  
ANISOU 3698  O   PRO B 180     8911  23321  21904   1492   6127  -1629       O  
ATOM   3699  CB  PRO B 180     -59.308  31.513  83.470  1.00143.50           C  
ANISOU 3699  CB  PRO B 180     9492  23330  21703   1491   6464  -2265       C  
ATOM   3700  CG  PRO B 180     -58.357  32.507  84.079  1.00143.93           C  
ANISOU 3700  CG  PRO B 180     9822  23201  21665   1541   6609  -2677       C  
ATOM   3701  CD  PRO B 180     -57.565  33.050  82.935  1.00141.60           C  
ANISOU 3701  CD  PRO B 180     9620  22685  21499   1493   6421  -2782       C  
ATOM   3702  N   ILE B 181     -58.919  30.569  79.854  1.00160.43           N  
ANISOU 3702  N   ILE B 181    11441  25313  24201   1211   5703  -1823       N  
ATOM   3703  CA  ILE B 181     -59.675  30.450  78.603  1.00168.85           C  
ANISOU 3703  CA  ILE B 181    12290  26436  25431   1221   5536  -1508       C  
ATOM   3704  C   ILE B 181     -59.207  29.169  77.924  1.00168.22           C  
ANISOU 3704  C   ILE B 181    12224  26358  25334    961   5234  -1395       C  
ATOM   3705  O   ILE B 181     -58.139  29.148  77.305  1.00152.05           O  
ANISOU 3705  O   ILE B 181    10361  24128  23284    865   5057  -1553       O  
ATOM   3706  CB  ILE B 181     -59.480  31.659  77.676  1.00163.82           C  
ANISOU 3706  CB  ILE B 181    11704  25609  24930   1372   5526  -1592       C  
ATOM   3707  CG1 ILE B 181     -59.646  32.975  78.440  1.00160.11           C  
ANISOU 3707  CG1 ILE B 181    11312  25068  24454   1615   5845  -1793       C  
ATOM   3708  CG2 ILE B 181     -60.468  31.607  76.513  1.00172.77           C  
ANISOU 3708  CG2 ILE B 181    12576  26872  26198   1416   5386  -1270       C  
ATOM   3709  CD1 ILE B 181     -61.075  33.299  78.804  1.00149.39           C  
ANISOU 3709  CD1 ILE B 181     9698  23951  23114   1822   6047  -1573       C  
ATOM   3710  N   HIS B 182     -59.987  28.097  78.053  1.00176.20           N  
ANISOU 3710  N   HIS B 182    13048  27568  26332    842   5185  -1128       N  
ATOM   3711  CA  HIS B 182     -59.760  26.888  77.274  1.00177.97           C  
ANISOU 3711  CA  HIS B 182    13259  27795  26565    598   4907   -975       C  
ATOM   3712  C   HIS B 182     -60.573  26.869  75.986  1.00185.83           C  
ANISOU 3712  C   HIS B 182    14027  28861  27719    584   4736   -669       C  
ATOM   3713  O   HIS B 182     -60.433  25.932  75.192  1.00186.79           O  
ANISOU 3713  O   HIS B 182    14137  28969  27866    378   4496   -530       O  
ATOM   3714  CB  HIS B 182     -60.075  25.639  78.108  1.00156.25           C  
ANISOU 3714  CB  HIS B 182    10463  25193  23714    430   4944   -883       C  
ATOM   3715  CG  HIS B 182     -58.949  25.206  78.996  1.00149.31           C  
ANISOU 3715  CG  HIS B 182     9848  24264  22618    347   4969  -1190       C  
ATOM   3716  ND1 HIS B 182     -57.922  26.050  79.358  1.00158.99           N  
ANISOU 3716  ND1 HIS B 182    11296  25356  23756    446   5031  -1523       N  
ATOM   3717  CD2 HIS B 182     -58.683  24.016  79.586  1.00130.43           C  
ANISOU 3717  CD2 HIS B 182     7533  21964  20063    168   4936  -1220       C  
ATOM   3718  CE1 HIS B 182     -57.075  25.402  80.139  1.00129.29           C  
ANISOU 3718  CE1 HIS B 182     7715  21628  19779    338   5023  -1733       C  
ATOM   3719  NE2 HIS B 182     -57.514  24.166  80.293  1.00129.26           N  
ANISOU 3719  NE2 HIS B 182     7634  21766  19713    181   4970  -1556       N  
ATOM   3720  N   HIS B 183     -61.416  27.880  75.764  1.00189.00           N  
ANISOU 3720  N   HIS B 183    14250  29362  28200    797   4850   -580       N  
ATOM   3721  CA  HIS B 183     -62.142  28.000  74.507  1.00180.88           C  
ANISOU 3721  CA  HIS B 183    13004  28457  27265    798   4671   -357       C  
ATOM   3722  C   HIS B 183     -61.290  28.625  73.411  1.00175.02           C  
ANISOU 3722  C   HIS B 183    12442  27459  26599    833   4519   -512       C  
ATOM   3723  O   HIS B 183     -61.455  28.279  72.236  1.00177.80           O  
ANISOU 3723  O   HIS B 183    12711  27840  27004    725   4280   -372       O  
ATOM   3724  CB  HIS B 183     -63.415  28.823  74.708  1.00186.51           C  
ANISOU 3724  CB  HIS B 183    13457  29435  27974   1011   4836   -275       C  
ATOM   3725  CG  HIS B 183     -63.917  29.472  73.455  1.00188.71           C  
ANISOU 3725  CG  HIS B 183    13605  29768  28328   1083   4688   -270       C  
ATOM   3726  ND1 HIS B 183     -63.577  30.758  73.096  1.00180.99           N  
ANISOU 3726  ND1 HIS B 183    12717  28599  27451   1324   4799   -441       N  
ATOM   3727  CD2 HIS B 183     -64.726  29.009  72.472  1.00191.64           C  
ANISOU 3727  CD2 HIS B 183    13790  30315  28711    923   4442   -183       C  
ATOM   3728  CE1 HIS B 183     -64.157  31.062  71.949  1.00173.84           C  
ANISOU 3728  CE1 HIS B 183    11648  27764  26640   1348   4650   -399       C  
ATOM   3729  NE2 HIS B 183     -64.861  30.018  71.549  1.00181.61           N  
ANISOU 3729  NE2 HIS B 183    12458  28964  27581   1097   4429   -276       N  
ATOM   3730  N   SER B 184     -60.392  29.543  73.768  1.00182.58           N  
ANISOU 3730  N   SER B 184    13645  28169  27559    968   4655   -807       N  
ATOM   3731  CA  SER B 184     -59.564  30.210  72.772  1.00183.66           C  
ANISOU 3731  CA  SER B 184    13958  28038  27785   1008   4542   -957       C  
ATOM   3732  C   SER B 184     -58.737  29.191  72.001  1.00171.81           C  
ANISOU 3732  C   SER B 184    12581  26433  26264    768   4258   -932       C  
ATOM   3733  O   SER B 184     -58.083  28.327  72.593  1.00170.68           O  
ANISOU 3733  O   SER B 184    12565  26281  26005    608   4219  -1010       O  
ATOM   3734  CB  SER B 184     -58.648  31.235  73.443  1.00187.97           C  
ANISOU 3734  CB  SER B 184    14758  28348  28315   1137   4742  -1300       C  
ATOM   3735  OG  SER B 184     -57.823  30.620  74.419  1.00195.20           O  
ANISOU 3735  OG  SER B 184    15841  29242  29082   1001   4769  -1482       O  
ATOM   3736  N   ARG B 185     -58.771  29.297  70.671  1.00141.99           N  
ANISOU 3736  N   ARG B 185     8775  22583  22592    752   4066   -835       N  
ATOM   3737  CA  ARG B 185     -58.014  28.365  69.843  1.00131.05           C  
ANISOU 3737  CA  ARG B 185     7512  21091  21188    538   3802   -804       C  
ATOM   3738  C   ARG B 185     -56.519  28.496  70.101  1.00145.06           C  
ANISOU 3738  C   ARG B 185     9598  22615  22903    509   3807  -1099       C  
ATOM   3739  O   ARG B 185     -55.803  27.490  70.162  1.00145.58           O  
ANISOU 3739  O   ARG B 185     9784  22666  22864    327   3674  -1127       O  
ATOM   3740  CB  ARG B 185     -58.327  28.595  68.365  1.00126.03           C  
ANISOU 3740  CB  ARG B 185     6801  20404  20682    551   3618   -676       C  
ATOM   3741  CG  ARG B 185     -57.818  27.492  67.450  1.00134.78           C  
ANISOU 3741  CG  ARG B 185     7988  21453  21768    316   3339   -586       C  
ATOM   3742  CD  ARG B 185     -58.826  26.358  67.328  1.00123.62           C  
ANISOU 3742  CD  ARG B 185     6339  20331  20301    114   3204   -315       C  
ATOM   3743  NE  ARG B 185     -59.713  26.547  66.187  1.00121.02           N  
ANISOU 3743  NE  ARG B 185     5814  20105  20064    110   3060   -178       N  
ATOM   3744  CZ  ARG B 185     -59.493  26.047  64.978  1.00119.36           C  
ANISOU 3744  CZ  ARG B 185     5653  19793  19903    -36   2818   -122       C  
ATOM   3745  NH1 ARG B 185     -58.430  25.302  64.722  1.00121.23           N  
ANISOU 3745  NH1 ARG B 185     6122  19845  20095   -185   2694   -164       N  
ATOM   3746  NH2 ARG B 185     -60.359  26.301  64.002  1.00121.21           N  
ANISOU 3746  NH2 ARG B 185     5707  20098  20251    -26   2704    -40       N  
ATOM   3747  N   PHE B 186     -56.037  29.726  70.268  1.00148.44           N  
ANISOU 3747  N   PHE B 186    10154  22859  23386    681   3963  -1330       N  
ATOM   3748  CA  PHE B 186     -54.620  30.014  70.520  1.00153.04           C  
ANISOU 3748  CA  PHE B 186    11010  23228  23910    649   3976  -1636       C  
ATOM   3749  C   PHE B 186     -53.837  29.390  69.366  1.00150.73           C  
ANISOU 3749  C   PHE B 186    10833  22802  23638    513   3717  -1595       C  
ATOM   3750  O   PHE B 186     -54.261  29.551  68.209  1.00151.98           O  
ANISOU 3750  O   PHE B 186    10917  22900  23929    546   3603  -1436       O  
ATOM   3751  CB  PHE B 186     -54.267  29.538  71.933  1.00150.49           C  
ANISOU 3751  CB  PHE B 186    10749  23024  23405    579   4090  -1787       C  
ATOM   3752  CG  PHE B 186     -52.805  29.631  72.272  1.00158.13           C  
ANISOU 3752  CG  PHE B 186    11965  23850  24269    509   4071  -2095       C  
ATOM   3753  CD1 PHE B 186     -52.106  30.813  72.094  1.00153.55           C  
ANISOU 3753  CD1 PHE B 186    11525  23051  23765    600   4157  -2335       C  
ATOM   3754  CD2 PHE B 186     -52.132  28.528  72.774  1.00150.72           C  
ANISOU 3754  CD2 PHE B 186    11109  23010  23147    348   3971  -2146       C  
ATOM   3755  CE1 PHE B 186     -50.762  30.892  72.407  1.00133.62           C  
ANISOU 3755  CE1 PHE B 186     9199  20430  21141    515   4132  -2615       C  
ATOM   3756  CE2 PHE B 186     -50.789  28.601  73.090  1.00134.63           C  
ANISOU 3756  CE2 PHE B 186     9270  20890  20994    289   3944  -2420       C  
ATOM   3757  CZ  PHE B 186     -50.104  29.785  72.906  1.00138.19           C  
ANISOU 3757  CZ  PHE B 186     9838  21142  21527    364   4018  -2653       C  
ATOM   3758  N   ASN B 187     -52.739  28.675  69.618  1.00140.52           N  
ANISOU 3758  N   ASN B 187     9711  21472  22210    372   3623  -1729       N  
ATOM   3759  CA  ASN B 187     -51.974  27.990  68.576  1.00129.07           C  
ANISOU 3759  CA  ASN B 187     8373  19908  20759    249   3392  -1681       C  
ATOM   3760  C   ASN B 187     -51.658  28.927  67.414  1.00129.09           C  
ANISOU 3760  C   ASN B 187     8451  19661  20935    350   3352  -1721       C  
ATOM   3761  O   ASN B 187     -51.731  28.550  66.243  1.00138.84           O  
ANISOU 3761  O   ASN B 187     9677  20826  22252    303   3176  -1564       O  
ATOM   3762  CB  ASN B 187     -52.712  26.741  68.089  1.00128.21           C  
ANISOU 3762  CB  ASN B 187     8126  19958  20631    103   3223  -1390       C  
ATOM   3763  CG  ASN B 187     -52.951  25.736  69.198  1.00130.74           C  
ANISOU 3763  CG  ASN B 187     8395  20498  20783    -13   3267  -1353       C  
ATOM   3764  OD1 ASN B 187     -52.201  25.680  70.173  1.00130.66           O  
ANISOU 3764  OD1 ASN B 187     8510  20506  20630    -18   3359  -1565       O  
ATOM   3765  ND2 ASN B 187     -54.001  24.934  69.055  1.00114.95           N  
ANISOU 3765  ND2 ASN B 187     6206  18673  18797   -118   3204  -1090       N  
ATOM   3766  N   SER B 188     -51.303  30.166  67.745  1.00131.18           N  
ANISOU 3766  N   SER B 188     8798  19782  21261    483   3526  -1944       N  
ATOM   3767  CA  SER B 188     -51.048  31.190  66.735  1.00137.89           C  
ANISOU 3767  CA  SER B 188     9726  20377  22290    594   3534  -2000       C  
ATOM   3768  C   SER B 188     -49.780  30.817  65.979  1.00139.08           C  
ANISOU 3768  C   SER B 188    10066  20353  22426    491   3369  -2081       C  
ATOM   3769  O   SER B 188     -48.668  30.965  66.490  1.00126.60           O  
ANISOU 3769  O   SER B 188     8637  18708  20756    441   3406  -2317       O  
ATOM   3770  CB  SER B 188     -50.926  32.563  67.385  1.00132.18           C  
ANISOU 3770  CB  SER B 188     9062  19538  21624    737   3786  -2240       C  
ATOM   3771  OG  SER B 188     -50.673  33.566  66.417  1.00134.07           O  
ANISOU 3771  OG  SER B 188     9388  19511  22041    843   3813  -2298       O  
ATOM   3772  N   ARG B 189     -49.951  30.316  64.752  1.00134.11           N  
ANISOU 3772  N   ARG B 189     9417  19659  21879    456   3184  -1884       N  
ATOM   3773  CA  ARG B 189     -48.802  29.903  63.954  1.00132.30           C  
ANISOU 3773  CA  ARG B 189     9363  19262  21642    372   3032  -1930       C  
ATOM   3774  C   ARG B 189     -47.875  31.070  63.654  1.00125.63           C  
ANISOU 3774  C   ARG B 189     8683  18149  20901    456   3128  -2161       C  
ATOM   3775  O   ARG B 189     -46.674  30.869  63.452  1.00137.58           O  
ANISOU 3775  O   ARG B 189    10353  19558  22362    385   3062  -2283       O  
ATOM   3776  CB  ARG B 189     -49.265  29.254  62.653  1.00138.10           C  
ANISOU 3776  CB  ARG B 189    10045  19955  22473    331   2836  -1679       C  
ATOM   3777  CG  ARG B 189     -50.099  28.003  62.836  1.00145.95           C  
ANISOU 3777  CG  ARG B 189    10883  21202  23368    197   2720  -1452       C  
ATOM   3778  CD  ARG B 189     -50.391  27.375  61.487  1.00180.38           C  
ANISOU 3778  CD  ARG B 189    15217  25488  27829    124   2513  -1239       C  
ATOM   3779  NE  ARG B 189     -51.353  26.284  61.570  1.00157.22           N  
ANISOU 3779  NE  ARG B 189    12109  22794  24832    -28   2403  -1013       N  
ATOM   3780  CZ  ARG B 189     -51.872  25.670  60.516  1.00146.80           C  
ANISOU 3780  CZ  ARG B 189    10720  21460  23598   -129   2218   -805       C  
ATOM   3781  NH1 ARG B 189     -51.512  25.992  59.283  1.00166.42           N  
ANISOU 3781  NH1 ARG B 189    13301  23693  26238    -77   2121   -783       N  
ATOM   3782  NH2 ARG B 189     -52.786  24.721  60.703  1.00124.76           N  
ANISOU 3782  NH2 ARG B 189     7759  18905  20741   -297   2131   -615       N  
ATOM   3783  N   THR B 190     -48.411  32.291  63.601  1.00124.17           N  
ANISOU 3783  N   THR B 190     8461  17854  20864    607   3291  -2217       N  
ATOM   3784  CA  THR B 190     -47.555  33.465  63.475  1.00126.84           C  
ANISOU 3784  CA  THR B 190     8956  17937  21299    668   3421  -2462       C  
ATOM   3785  C   THR B 190     -46.622  33.583  64.675  1.00131.80           C  
ANISOU 3785  C   THR B 190     9674  18628  21777    579   3519  -2738       C  
ATOM   3786  O   THR B 190     -45.399  33.717  64.523  1.00141.47           O  
ANISOU 3786  O   THR B 190    11045  19727  22981    503   3489  -2913       O  
ATOM   3787  CB  THR B 190     -48.413  34.723  63.331  1.00140.66           C  
ANISOU 3787  CB  THR B 190    10647  19577  23221    855   3608  -2466       C  
ATOM   3788  OG1 THR B 190     -49.158  34.937  64.538  1.00143.49           O  
ANISOU 3788  OG1 THR B 190    10887  20131  23501    905   3775  -2503       O  
ATOM   3789  CG2 THR B 190     -49.381  34.574  62.168  1.00142.30           C  
ANISOU 3789  CG2 THR B 190    10739  19763  23567    947   3498  -2185       C  
ATOM   3790  N   LYS B 191     -47.187  33.515  65.883  1.00128.22           N  
ANISOU 3790  N   LYS B 191     9122  18383  21212    583   3635  -2779       N  
ATOM   3791  CA  LYS B 191     -46.370  33.548  67.089  1.00130.96           C  
ANISOU 3791  CA  LYS B 191     9538  18821  21401    492   3720  -3041       C  
ATOM   3792  C   LYS B 191     -45.455  32.335  67.177  1.00131.62           C  
ANISOU 3792  C   LYS B 191     9679  19028  21303    340   3531  -3029       C  
ATOM   3793  O   LYS B 191     -44.335  32.445  67.681  1.00113.66           O  
ANISOU 3793  O   LYS B 191     7503  16755  18930    255   3543  -3260       O  
ATOM   3794  CB  LYS B 191     -47.261  33.634  68.329  1.00124.17           C  
ANISOU 3794  CB  LYS B 191     8559  18162  20457    540   3884  -3060       C  
ATOM   3795  CG  LYS B 191     -48.156  34.861  68.368  1.00122.42           C  
ANISOU 3795  CG  LYS B 191     8284  17837  20394    715   4105  -3079       C  
ATOM   3796  CD  LYS B 191     -49.067  34.857  69.589  1.00116.26           C  
ANISOU 3796  CD  LYS B 191     7382  17270  19522    775   4274  -3070       C  
ATOM   3797  CE  LYS B 191     -48.270  34.932  70.881  1.00114.92           C  
ANISOU 3797  CE  LYS B 191     7301  17176  19186    675   4380  -3372       C  
ATOM   3798  NZ  LYS B 191     -49.157  34.932  72.077  1.00117.40           N  
ANISOU 3798  NZ  LYS B 191     7511  17686  19409    743   4560  -3367       N  
ATOM   3799  N   ALA B 192     -45.904  31.177  66.691  1.00148.33           N  
ANISOU 3799  N   ALA B 192    11730  21257  23373    301   3360  -2763       N  
ATOM   3800  CA  ALA B 192     -45.048  29.996  66.684  1.00139.43           C  
ANISOU 3800  CA  ALA B 192    10670  20229  22077    176   3193  -2732       C  
ATOM   3801  C   ALA B 192     -43.823  30.215  65.805  1.00130.95           C  
ANISOU 3801  C   ALA B 192     9748  18952  21056    153   3109  -2820       C  
ATOM   3802  O   ALA B 192     -42.692  29.932  66.214  1.00130.13           O  
ANISOU 3802  O   ALA B 192     9729  18903  20813     77   3075  -2968       O  
ATOM   3803  CB  ALA B 192     -45.834  28.780  66.210  1.00142.59           C  
ANISOU 3803  CB  ALA B 192    10978  20754  22446    130   3045  -2431       C  
ATOM   3804  N   PHE B 193     -44.038  30.711  64.583  1.00121.32           N  
ANISOU 3804  N   PHE B 193     8555  17506  20036    223   3078  -2723       N  
ATOM   3805  CA  PHE B 193     -42.931  31.023  63.684  1.00118.87           C  
ANISOU 3805  CA  PHE B 193     8388  16973  19804    214   3022  -2801       C  
ATOM   3806  C   PHE B 193     -41.980  32.025  64.328  1.00122.17           C  
ANISOU 3806  C   PHE B 193     8883  17320  20215    191   3161  -3116       C  
ATOM   3807  O   PHE B 193     -40.754  31.841  64.313  1.00111.34           O  
ANISOU 3807  O   PHE B 193     7600  15940  18763    115   3106  -3233       O  
ATOM   3808  CB  PHE B 193     -43.486  31.569  62.367  1.00106.41           C  
ANISOU 3808  CB  PHE B 193     6818  15153  18461    315   3005  -2662       C  
ATOM   3809  CG  PHE B 193     -42.698  31.173  61.149  1.00128.14           C  
ANISOU 3809  CG  PHE B 193     9688  17727  21272    296   2865  -2579       C  
ATOM   3810  CD1 PHE B 193     -41.432  30.621  61.262  1.00129.75           C  
ANISOU 3810  CD1 PHE B 193     9994  17965  21342    211   2796  -2663       C  
ATOM   3811  CD2 PHE B 193     -43.230  31.360  59.882  1.00135.58           C  
ANISOU 3811  CD2 PHE B 193    10635  18474  22407    375   2810  -2411       C  
ATOM   3812  CE1 PHE B 193     -40.715  30.261  60.133  1.00115.18           C  
ANISOU 3812  CE1 PHE B 193     8255  15950  19556    212   2687  -2576       C  
ATOM   3813  CE2 PHE B 193     -42.519  31.003  58.752  1.00130.18           C  
ANISOU 3813  CE2 PHE B 193    10067  17607  21789    367   2695  -2336       C  
ATOM   3814  CZ  PHE B 193     -41.259  30.452  58.878  1.00107.51           C  
ANISOU 3814  CZ  PHE B 193     7302  14762  18786    287   2641  -2417       C  
ATOM   3815  N   LEU B 194     -42.538  33.087  64.919  1.00125.48           N  
ANISOU 3815  N   LEU B 194     9258  17701  20716    251   3351  -3259       N  
ATOM   3816  CA  LEU B 194     -41.710  34.119  65.537  1.00123.11           C  
ANISOU 3816  CA  LEU B 194     9025  17322  20428    206   3504  -3584       C  
ATOM   3817  C   LEU B 194     -40.875  33.552  66.682  1.00110.82           C  
ANISOU 3817  C   LEU B 194     7464  16006  18635     78   3475  -3753       C  
ATOM   3818  O   LEU B 194     -39.675  33.828  66.784  1.00105.91           O  
ANISOU 3818  O   LEU B 194     6911  15355  17976    -13   3472  -3957       O  
ATOM   3819  CB  LEU B 194     -42.590  35.270  66.026  1.00133.51           C  
ANISOU 3819  CB  LEU B 194    10298  18567  21864    303   3732  -3692       C  
ATOM   3820  CG  LEU B 194     -43.310  36.084  64.948  1.00129.26           C  
ANISOU 3820  CG  LEU B 194     9772  17774  21566    450   3798  -3569       C  
ATOM   3821  CD1 LEU B 194     -44.171  37.167  65.578  1.00140.88           C  
ANISOU 3821  CD1 LEU B 194    11201  19207  23121    564   4046  -3671       C  
ATOM   3822  CD2 LEU B 194     -42.315  36.688  63.965  1.00111.48           C  
ANISOU 3822  CD2 LEU B 194     7661  15242  19455    424   3788  -3670       C  
ATOM   3823  N   LYS B 195     -41.489  32.740  67.546  1.00113.99           N  
ANISOU 3823  N   LYS B 195     7778  16663  18872     69   3454  -3666       N  
ATOM   3824  CA  LYS B 195     -40.769  32.205  68.698  1.00105.76           C  
ANISOU 3824  CA  LYS B 195     6727  15865  17593    -35   3438  -3827       C  
ATOM   3825  C   LYS B 195     -39.712  31.190  68.278  1.00107.18           C  
ANISOU 3825  C   LYS B 195     6963  16119  17639   -105   3244  -3747       C  
ATOM   3826  O   LYS B 195     -38.624  31.147  68.863  1.00113.03           O  
ANISOU 3826  O   LYS B 195     7728  16978  18239   -192   3228  -3941       O  
ATOM   3827  CB  LYS B 195     -41.750  31.582  69.693  1.00114.33           C  
ANISOU 3827  CB  LYS B 195     7711  17187  18543    -16   3480  -3740       C  
ATOM   3828  CG  LYS B 195     -42.654  32.591  70.388  1.00118.53           C  
ANISOU 3828  CG  LYS B 195     8185  17691  19161     57   3704  -3858       C  
ATOM   3829  CD  LYS B 195     -43.388  31.962  71.562  1.00107.38           C  
ANISOU 3829  CD  LYS B 195     6680  16539  17581     59   3761  -3819       C  
ATOM   3830  CE  LYS B 195     -44.886  32.189  71.464  1.00111.06           C  
ANISOU 3830  CE  LYS B 195     7038  16988  18174    186   3866  -3618       C  
ATOM   3831  NZ  LYS B 195     -45.463  31.519  70.266  1.00134.02           N  
ANISOU 3831  NZ  LYS B 195     9897  19844  21181    220   3703  -3289       N  
ATOM   3832  N   ILE B 196     -40.010  30.362  67.274  1.00115.26           N  
ANISOU 3832  N   ILE B 196     8002  17091  18701    -67   3101  -3463       N  
ATOM   3833  CA  ILE B 196     -39.013  29.405  66.799  1.00 99.59           C  
ANISOU 3833  CA  ILE B 196     6083  15157  16601   -111   2940  -3374       C  
ATOM   3834  C   ILE B 196     -37.819  30.139  66.202  1.00104.79           C  
ANISOU 3834  C   ILE B 196     6828  15638  17348   -134   2941  -3526       C  
ATOM   3835  O   ILE B 196     -36.659  29.787  66.464  1.00108.99           O  
ANISOU 3835  O   ILE B 196     7388  16288  17736   -194   2882  -3615       O  
ATOM   3836  CB  ILE B 196     -39.647  28.423  65.795  1.00 94.56           C  
ANISOU 3836  CB  ILE B 196     5447  14476  16007    -76   2809  -3056       C  
ATOM   3837  CG1 ILE B 196     -40.688  27.548  66.499  1.00 96.47           C  
ANISOU 3837  CG1 ILE B 196     5587  14936  16129    -91   2804  -2917       C  
ATOM   3838  CG2 ILE B 196     -38.577  27.556  65.148  1.00 92.56           C  
ANISOU 3838  CG2 ILE B 196     5279  14225  15665   -100   2671  -2969       C  
ATOM   3839  CD1 ILE B 196     -41.525  26.701  65.561  1.00 94.08           C  
ANISOU 3839  CD1 ILE B 196     5252  14597  15897    -87   2693  -2623       C  
ATOM   3840  N   ILE B 197     -38.080  31.182  65.406  1.00110.24           N  
ANISOU 3840  N   ILE B 197     7555  16055  18277    -85   3018  -3557       N  
ATOM   3841  CA  ILE B 197     -36.989  31.989  64.865  1.00103.19           C  
ANISOU 3841  CA  ILE B 197     6741  14976  17491   -118   3049  -3720       C  
ATOM   3842  C   ILE B 197     -36.201  32.649  65.991  1.00 97.72           C  
ANISOU 3842  C   ILE B 197     6018  14407  16705   -225   3153  -4050       C  
ATOM   3843  O   ILE B 197     -34.968  32.730  65.941  1.00 97.49           O  
ANISOU 3843  O   ILE B 197     6014  14401  16627   -304   3118  -4176       O  
ATOM   3844  CB  ILE B 197     -37.536  33.028  63.866  1.00103.79           C  
ANISOU 3844  CB  ILE B 197     6863  14727  17844    -37   3140  -3699       C  
ATOM   3845  CG1 ILE B 197     -37.992  32.337  62.578  1.00100.92           C  
ANISOU 3845  CG1 ILE B 197     6538  14238  17568     47   3006  -3393       C  
ATOM   3846  CG2 ILE B 197     -36.493  34.100  63.571  1.00 96.79           C  
ANISOU 3846  CG2 ILE B 197     6048  13646  17081    -93   3234  -3935       C  
ATOM   3847  CD1 ILE B 197     -38.489  33.290  61.513  1.00103.42           C  
ANISOU 3847  CD1 ILE B 197     6903  14241  18150    141   3080  -3353       C  
ATOM   3848  N   ALA B 198     -36.897  33.124  67.027  1.00102.65           N  
ANISOU 3848  N   ALA B 198     6577  15124  17301   -234   3287  -4197       N  
ATOM   3849  CA  ALA B 198     -36.220  33.774  68.144  1.00102.57           C  
ANISOU 3849  CA  ALA B 198     6532  15239  17200   -351   3398  -4539       C  
ATOM   3850  C   ALA B 198     -35.310  32.804  68.889  1.00105.02           C  
ANISOU 3850  C   ALA B 198     6803  15865  17237   -435   3271  -4575       C  
ATOM   3851  O   ALA B 198     -34.203  33.171  69.296  1.00113.72           O  
ANISOU 3851  O   ALA B 198     7886  17054  18268   -551   3281  -4814       O  
ATOM   3852  CB  ALA B 198     -37.249  34.383  69.097  1.00118.10           C  
ANISOU 3852  CB  ALA B 198     8447  17244  19183   -324   3578  -4666       C  
ATOM   3853  N   VAL B 199     -35.764  31.566  69.091  1.00130.08           N  
ANISOU 3853  N   VAL B 199     9952  19223  20248   -382   3157  -4343       N  
ATOM   3854  CA  VAL B 199     -34.931  30.593  69.792  1.00130.93           C  
ANISOU 3854  CA  VAL B 199    10029  19635  20084   -436   3045  -4358       C  
ATOM   3855  C   VAL B 199     -33.742  30.185  68.928  1.00129.80           C  
ANISOU 3855  C   VAL B 199     9934  19458  19925   -444   2913  -4267       C  
ATOM   3856  O   VAL B 199     -32.621  30.018  69.430  1.00129.52           O  
ANISOU 3856  O   VAL B 199     9862  19624  19726   -516   2864  -4401       O  
ATOM   3857  CB  VAL B 199     -35.765  29.377  70.233  1.00129.18           C  
ANISOU 3857  CB  VAL B 199     9778  19602  19701   -378   2986  -4139       C  
ATOM   3858  CG1 VAL B 199     -34.889  28.392  70.984  1.00129.05           C  
ANISOU 3858  CG1 VAL B 199     9737  19903  19394   -417   2888  -4162       C  
ATOM   3859  CG2 VAL B 199     -36.916  29.821  71.118  1.00131.04           C  
ANISOU 3859  CG2 VAL B 199     9956  19879  19955   -363   3134  -4225       C  
ATOM   3860  N   TRP B 200     -33.955  30.026  67.617  1.00118.57           N  
ANISOU 3860  N   TRP B 200     8587  17797  18669   -367   2857  -4038       N  
ATOM   3861  CA  TRP B 200     -32.818  29.820  66.724  1.00 95.32           C  
ANISOU 3861  CA  TRP B 200     5696  14780  15743   -365   2766  -3968       C  
ATOM   3862  C   TRP B 200     -31.821  30.967  66.847  1.00 96.48           C  
ANISOU 3862  C   TRP B 200     5824  14868  15967   -469   2845  -4256       C  
ATOM   3863  O   TRP B 200     -30.604  30.746  66.880  1.00 99.35           O  
ANISOU 3863  O   TRP B 200     6163  15363  16223   -518   2779  -4304       O  
ATOM   3864  CB  TRP B 200     -33.287  29.685  65.274  1.00 94.65           C  
ANISOU 3864  CB  TRP B 200     5699  14410  15855   -271   2724  -3720       C  
ATOM   3865  CG  TRP B 200     -33.817  28.331  64.896  1.00 91.53           C  
ANISOU 3865  CG  TRP B 200     5324  14089  15366   -199   2610  -3423       C  
ATOM   3866  CD1 TRP B 200     -35.077  28.040  64.461  1.00 94.88           C  
ANISOU 3866  CD1 TRP B 200     5749  14416  15885   -146   2601  -3240       C  
ATOM   3867  CD2 TRP B 200     -33.100  27.088  64.907  1.00 90.40           C  
ANISOU 3867  CD2 TRP B 200     5192  14138  15020   -179   2501  -3284       C  
ATOM   3868  NE1 TRP B 200     -35.191  26.696  64.204  1.00 95.83           N  
ANISOU 3868  NE1 TRP B 200     5881  14648  15882   -120   2494  -3014       N  
ATOM   3869  CE2 TRP B 200     -33.992  26.089  64.470  1.00 89.21           C  
ANISOU 3869  CE2 TRP B 200     5058  13980  14858   -129   2440  -3037       C  
ATOM   3870  CE3 TRP B 200     -31.794  26.724  65.246  1.00 90.49           C  
ANISOU 3870  CE3 TRP B 200     5188  14338  14855   -197   2455  -3343       C  
ATOM   3871  CZ2 TRP B 200     -33.621  24.750  64.363  1.00 88.08           C  
ANISOU 3871  CZ2 TRP B 200     4934  13992  14539    -97   2354  -2866       C  
ATOM   3872  CZ3 TRP B 200     -31.427  25.393  65.139  1.00 89.34           C  
ANISOU 3872  CZ3 TRP B 200     5060  14358  14528   -138   2366  -3150       C  
ATOM   3873  CH2 TRP B 200     -32.337  24.423  64.702  1.00 88.14           C  
ANISOU 3873  CH2 TRP B 200     4941  14175  14372    -88   2326  -2924       C  
ATOM   3874  N   THR B 201     -32.326  32.200  66.927  1.00 97.94           N  
ANISOU 3874  N   THR B 201     6010  14864  16340   -505   2997  -4452       N  
ATOM   3875  CA  THR B 201     -31.455  33.366  67.022  1.00 99.55           C  
ANISOU 3875  CA  THR B 201     6197  14986  16644   -629   3101  -4754       C  
ATOM   3876  C   THR B 201     -30.672  33.379  68.331  1.00101.46           C  
ANISOU 3876  C   THR B 201     6329  15556  16665   -768   3106  -5022       C  
ATOM   3877  O   THR B 201     -29.483  33.709  68.339  1.00108.96           O  
ANISOU 3877  O   THR B 201     7236  16575  17590   -881   3092  -5182       O  
ATOM   3878  CB  THR B 201     -32.281  34.645  66.872  1.00100.91           C  
ANISOU 3878  CB  THR B 201     6402  14878  17061   -625   3292  -4906       C  
ATOM   3879  OG1 THR B 201     -32.899  34.665  65.580  1.00 99.27           O  
ANISOU 3879  OG1 THR B 201     6286  14377  17054   -494   3275  -4659       O  
ATOM   3880  CG2 THR B 201     -31.400  35.874  67.024  1.00109.35           C  
ANISOU 3880  CG2 THR B 201     7456  15853  18240   -780   3431  -5252       C  
ATOM   3881  N   ILE B 202     -31.318  33.042  69.449  1.00105.17           N  
ANISOU 3881  N   ILE B 202     6745  16245  16972   -769   3129  -5079       N  
ATOM   3882  CA  ILE B 202     -30.600  33.046  70.723  1.00113.46           C  
ANISOU 3882  CA  ILE B 202     7687  17628  17794   -902   3131  -5347       C  
ATOM   3883  C   ILE B 202     -29.557  31.932  70.750  1.00103.39           C  
ANISOU 3883  C   ILE B 202     6371  16626  16288   -891   2945  -5203       C  
ATOM   3884  O   ILE B 202     -28.469  32.095  71.317  1.00104.86           O  
ANISOU 3884  O   ILE B 202     6463  17044  16336  -1015   2914  -5408       O  
ATOM   3885  CB  ILE B 202     -31.571  32.957  71.921  1.00115.49           C  
ANISOU 3885  CB  ILE B 202     7905  18050  17927   -893   3217  -5444       C  
ATOM   3886  CG1 ILE B 202     -32.230  31.580  72.023  1.00110.35           C  
ANISOU 3886  CG1 ILE B 202     7269  17544  17116   -760   3099  -5127       C  
ATOM   3887  CG2 ILE B 202     -32.604  34.066  71.865  1.00107.03           C  
ANISOU 3887  CG2 ILE B 202     6874  16706  17086   -876   3419  -5561       C  
ATOM   3888  CD1 ILE B 202     -33.003  31.360  73.308  1.00105.68           C  
ANISOU 3888  CD1 ILE B 202     6625  17169  16358   -760   3174  -5222       C  
ATOM   3889  N   SER B 203     -29.857  30.791  70.122  1.00101.06           N  
ANISOU 3889  N   SER B 203     6138  16315  15944   -746   2825  -4852       N  
ATOM   3890  CA  SER B 203     -28.860  29.731  70.020  1.00108.08           C  
ANISOU 3890  CA  SER B 203     7004  17431  16632   -707   2673  -4691       C  
ATOM   3891  C   SER B 203     -27.674  30.163  69.163  1.00112.38           C  
ANISOU 3891  C   SER B 203     7547  17869  17283   -748   2642  -4705       C  
ATOM   3892  O   SER B 203     -26.520  29.867  69.494  1.00102.06           O  
ANISOU 3892  O   SER B 203     6155  16818  15806   -793   2564  -4752       O  
ATOM   3893  CB  SER B 203     -29.503  28.463  69.464  1.00103.83           C  
ANISOU 3893  CB  SER B 203     6544  16862  16042   -551   2586  -4330       C  
ATOM   3894  OG  SER B 203     -30.543  28.026  70.319  1.00104.93           O  
ANISOU 3894  OG  SER B 203     6669  17129  16071   -528   2619  -4319       O  
ATOM   3895  N   VAL B 204     -27.941  30.869  68.061  1.00120.70           N  
ANISOU 3895  N   VAL B 204     8688  18559  18614   -729   2706  -4660       N  
ATOM   3896  CA  VAL B 204     -26.861  31.403  67.232  1.00 98.96           C  
ANISOU 3896  CA  VAL B 204     5937  15676  15988   -777   2706  -4692       C  
ATOM   3897  C   VAL B 204     -26.025  32.403  68.023  1.00101.70           C  
ANISOU 3897  C   VAL B 204     6163  16166  16312   -978   2778  -5066       C  
ATOM   3898  O   VAL B 204     -24.790  32.403  67.947  1.00116.17           O  
ANISOU 3898  O   VAL B 204     7917  18143  18077  -1048   2723  -5108       O  
ATOM   3899  CB  VAL B 204     -27.438  32.033  65.949  1.00 97.70           C  
ANISOU 3899  CB  VAL B 204     5902  15087  16133   -715   2782  -4595       C  
ATOM   3900  CG1 VAL B 204     -26.442  32.998  65.322  1.00 98.50           C  
ANISOU 3900  CG1 VAL B 204     5996  15024  16404   -814   2848  -4745       C  
ATOM   3901  CG2 VAL B 204     -27.826  30.950  64.952  1.00 95.04           C  
ANISOU 3901  CG2 VAL B 204     5666  14645  15800   -543   2680  -4219       C  
ATOM   3902  N   GLY B 205     -26.685  33.278  68.783  1.00103.51           N  
ANISOU 3902  N   GLY B 205     6368  16361  16598  -1079   2913  -5347       N  
ATOM   3903  CA  GLY B 205     -25.965  34.252  69.586  1.00106.39           C  
ANISOU 3903  CA  GLY B 205     6619  16867  16939  -1297   3002  -5742       C  
ATOM   3904  C   GLY B 205     -25.137  33.627  70.689  1.00107.79           C  
ANISOU 3904  C   GLY B 205     6650  17511  16795  -1376   2887  -5837       C  
ATOM   3905  O   GLY B 205     -24.087  34.159  71.059  1.00109.88           O  
ANISOU 3905  O   GLY B 205     6795  17951  17004  -1557   2889  -6079       O  
ATOM   3906  N   ILE B 206     -25.608  32.513  71.252  1.00128.40           N  
ANISOU 3906  N   ILE B 206     9260  20340  19185  -1252   2790  -5657       N  
ATOM   3907  CA  ILE B 206     -24.810  31.781  72.230  1.00129.58           C  
ANISOU 3907  CA  ILE B 206     9279  20947  19010  -1288   2668  -5701       C  
ATOM   3908  C   ILE B 206     -23.615  31.119  71.555  1.00131.63           C  
ANISOU 3908  C   ILE B 206     9502  21316  19197  -1227   2526  -5477       C  
ATOM   3909  O   ILE B 206     -22.491  31.159  72.071  1.00135.74           O  
ANISOU 3909  O   ILE B 206     9876  22148  19551  -1336   2457  -5611       O  
ATOM   3910  CB  ILE B 206     -25.685  30.749  72.967  1.00128.87           C  
ANISOU 3910  CB  ILE B 206     9215  21036  18713  -1158   2626  -5560       C  
ATOM   3911  CG1 ILE B 206     -26.675  31.450  73.899  1.00130.55           C  
ANISOU 3911  CG1 ILE B 206     9422  21234  18947  -1240   2776  -5830       C  
ATOM   3912  CG2 ILE B 206     -24.822  29.763  73.745  1.00129.60           C  
ANISOU 3912  CG2 ILE B 206     9196  21584  18461  -1136   2481  -5515       C  
ATOM   3913  CD1 ILE B 206     -27.550  30.496  74.683  1.00130.14           C  
ANISOU 3913  CD1 ILE B 206     9388  21364  18693  -1126   2754  -5706       C  
ATOM   3914  N   SER B 207     -23.833  30.513  70.387  1.00116.77           N  
ANISOU 3914  N   SER B 207     7743  19189  17435  -1053   2486  -5134       N  
ATOM   3915  CA  SER B 207     -22.781  29.730  69.749  1.00106.99           C  
ANISOU 3915  CA  SER B 207     6481  18057  16112   -957   2369  -4883       C  
ATOM   3916  C   SER B 207     -21.702  30.625  69.150  1.00114.63           C  
ANISOU 3916  C   SER B 207     7384  18936  17233  -1082   2397  -4999       C  
ATOM   3917  O   SER B 207     -20.558  30.620  69.612  1.00135.81           O  
ANISOU 3917  O   SER B 207     9914  21928  19761  -1171   2331  -5090       O  
ATOM   3918  CB  SER B 207     -23.388  28.816  68.686  1.00109.28           C  
ANISOU 3918  CB  SER B 207     6928  18112  16482   -745   2338  -4505       C  
ATOM   3919  OG  SER B 207     -24.285  27.891  69.275  1.00115.47           O  
ANISOU 3919  OG  SER B 207     7753  19018  17101   -646   2308  -4392       O  
ATOM   3920  N   MET B 208     -22.068  31.446  68.150  1.00111.24           N  
ANISOU 3920  N   MET B 208     7062  18095  17107  -1099   2503  -5009       N  
ATOM   3921  CA  MET B 208     -21.175  32.236  67.295  1.00118.92           C  
ANISOU 3921  CA  MET B 208     8016  18896  18273  -1186   2551  -5061       C  
ATOM   3922  C   MET B 208     -19.936  32.796  67.999  1.00128.91           C  
ANISOU 3922  C   MET B 208     9086  20464  19428  -1399   2535  -5325       C  
ATOM   3923  O   MET B 208     -18.840  32.766  67.417  1.00120.18           O  
ANISOU 3923  O   MET B 208     7915  19406  18343  -1409   2495  -5224       O  
ATOM   3924  CB  MET B 208     -21.965  33.378  66.646  1.00106.64           C  
ANISOU 3924  CB  MET B 208     6582  16901  17035  -1240   2713  -5200       C  
ATOM   3925  CG  MET B 208     -21.153  34.252  65.702  1.00118.79           C  
ANISOU 3925  CG  MET B 208     8124  18210  18799  -1330   2793  -5264       C  
ATOM   3926  SD  MET B 208     -20.773  33.435  64.141  1.00135.51           S  
ANISOU 3926  SD  MET B 208    10354  20127  21005  -1107   2723  -4829       S  
ATOM   3927  CE  MET B 208     -22.413  33.258  63.444  1.00 98.99           C  
ANISOU 3927  CE  MET B 208     5942  15126  16545   -931   2767  -4653       C  
ATOM   3928  N   PRO B 209     -20.048  33.330  69.226  1.00122.37           N  
ANISOU 3928  N   PRO B 209     8154  19857  18484  -1581   2570  -5667       N  
ATOM   3929  CA  PRO B 209     -18.820  33.709  69.945  1.00128.25           C  
ANISOU 3929  CA  PRO B 209     8694  20960  19075  -1793   2523  -5900       C  
ATOM   3930  C   PRO B 209     -17.830  32.569  70.103  1.00133.69           C  
ANISOU 3930  C   PRO B 209     9263  22032  19500  -1677   2343  -5647       C  
ATOM   3931  O   PRO B 209     -16.618  32.812  70.057  1.00134.44           O  
ANISOU 3931  O   PRO B 209     9209  22319  19554  -1792   2295  -5690       O  
ATOM   3932  CB  PRO B 209     -19.352  34.195  71.299  1.00115.04           C  
ANISOU 3932  CB  PRO B 209     6955  19482  17273  -1962   2582  -6268       C  
ATOM   3933  CG  PRO B 209     -20.683  34.740  70.982  1.00115.98           C  
ANISOU 3933  CG  PRO B 209     7244  19195  17627  -1916   2741  -6325       C  
ATOM   3934  CD  PRO B 209     -21.247  33.833  69.924  1.00110.56           C  
ANISOU 3934  CD  PRO B 209     6716  18263  17028  -1635   2683  -5893       C  
ATOM   3935  N   ILE B 210     -18.297  31.336  70.288  1.00139.02           N  
ANISOU 3935  N   ILE B 210     9996  22829  19997  -1454   2252  -5382       N  
ATOM   3936  CA  ILE B 210     -17.388  30.203  70.457  1.00133.24           C  
ANISOU 3936  CA  ILE B 210     9159  22459  19006  -1317   2102  -5136       C  
ATOM   3937  C   ILE B 210     -16.559  30.002  69.190  1.00138.04           C  
ANISOU 3937  C   ILE B 210     9782  22912  19756  -1210   2091  -4857       C  
ATOM   3938  O   ILE B 210     -15.323  29.996  69.283  1.00154.43           O  
ANISOU 3938  O   ILE B 210    11685  25257  21732  -1266   2024  -4845       O  
ATOM   3939  CB  ILE B 210     -18.139  28.917  70.842  1.00133.38           C  
ANISOU 3939  CB  ILE B 210     9263  22595  18820  -1095   2039  -4912       C  
ATOM   3940  CG1 ILE B 210     -19.123  29.183  71.978  1.00136.18           C  
ANISOU 3940  CG1 ILE B 210     9626  23036  19079  -1189   2082  -5177       C  
ATOM   3941  CG2 ILE B 210     -17.155  27.822  71.230  1.00132.18           C  
ANISOU 3941  CG2 ILE B 210     8987  22872  18363   -964   1902  -4717       C  
ATOM   3942  CD1 ILE B 210     -20.294  28.236  71.973  1.00135.51           C  
ANISOU 3942  CD1 ILE B 210     9697  22847  18944   -992   2087  -4960       C  
ATOM   3943  N   PRO B 211     -17.154  29.832  67.997  1.00119.35           N  
ANISOU 3943  N   PRO B 211     7602  20137  17610  -1059   2154  -4625       N  
ATOM   3944  CA  PRO B 211     -16.307  29.721  66.801  1.00118.80           C  
ANISOU 3944  CA  PRO B 211     7537  19927  17674   -970   2162  -4386       C  
ATOM   3945  C   PRO B 211     -15.493  30.965  66.511  1.00124.92           C  
ANISOU 3945  C   PRO B 211     8210  20626  18629  -1194   2231  -4606       C  
ATOM   3946  O   PRO B 211     -14.375  30.834  66.007  1.00118.64           O  
ANISOU 3946  O   PRO B 211     7310  19931  17835  -1169   2204  -4461       O  
ATOM   3947  CB  PRO B 211     -17.309  29.426  65.676  1.00105.46           C  
ANISOU 3947  CB  PRO B 211     6083  17804  16183   -795   2227  -4160       C  
ATOM   3948  CG  PRO B 211     -18.591  29.912  66.176  1.00115.24           C  
ANISOU 3948  CG  PRO B 211     7416  18885  17487   -872   2284  -4364       C  
ATOM   3949  CD  PRO B 211     -18.569  29.625  67.640  1.00110.89           C  
ANISOU 3949  CD  PRO B 211     6735  18741  16657   -945   2213  -4536       C  
ATOM   3950  N   VAL B 212     -15.994  32.166  66.810  1.00142.39           N  
ANISOU 3950  N   VAL B 212    10444  22665  20993  -1411   2334  -4953       N  
ATOM   3951  CA  VAL B 212     -15.197  33.361  66.533  1.00147.74           C  
ANISOU 3951  CA  VAL B 212    11030  23263  21842  -1645   2419  -5181       C  
ATOM   3952  C   VAL B 212     -13.936  33.377  67.394  1.00147.89           C  
ANISOU 3952  C   VAL B 212    10790  23763  21638  -1807   2318  -5303       C  
ATOM   3953  O   VAL B 212     -12.813  33.504  66.885  1.00146.69           O  
ANISOU 3953  O   VAL B 212    10520  23687  21526  -1849   2302  -5210       O  
ATOM   3954  CB  VAL B 212     -16.041  34.632  66.736  1.00151.18           C  
ANISOU 3954  CB  VAL B 212    11552  23410  22479  -1841   2578  -5549       C  
ATOM   3955  CG1 VAL B 212     -15.151  35.863  66.728  1.00145.88           C  
ANISOU 3955  CG1 VAL B 212    10763  22731  21933  -2133   2671  -5850       C  
ATOM   3956  CG2 VAL B 212     -17.099  34.739  65.648  1.00151.65           C  
ANISOU 3956  CG2 VAL B 212    11848  22974  22800  -1679   2681  -5399       C  
ATOM   3957  N   PHE B 213     -14.097  33.207  68.710  1.00144.91           N  
ANISOU 3957  N   PHE B 213    10314  23734  21010  -1894   2244  -5498       N  
ATOM   3958  CA  PHE B 213     -12.952  33.201  69.611  1.00151.63           C  
ANISOU 3958  CA  PHE B 213    10914  25081  21619  -2053   2131  -5623       C  
ATOM   3959  C   PHE B 213     -12.080  31.963  69.435  1.00140.26           C  
ANISOU 3959  C   PHE B 213     9368  23942  19981  -1823   1987  -5244       C  
ATOM   3960  O   PHE B 213     -10.919  31.979  69.857  1.00148.76           O  
ANISOU 3960  O   PHE B 213    10221  25396  20905  -1929   1895  -5273       O  
ATOM   3961  CB  PHE B 213     -13.421  33.309  71.064  1.00167.20           C  
ANISOU 3961  CB  PHE B 213    12819  27351  23358  -2192   2095  -5934       C  
ATOM   3962  CG  PHE B 213     -13.616  34.726  71.542  1.00163.84           C  
ANISOU 3962  CG  PHE B 213    12374  26827  23052  -2530   2226  -6401       C  
ATOM   3963  CD1 PHE B 213     -12.544  35.460  72.024  1.00151.81           C  
ANISOU 3963  CD1 PHE B 213    10650  25577  21452  -2827   2200  -6656       C  
ATOM   3964  CD2 PHE B 213     -14.871  35.316  71.524  1.00156.30           C  
ANISOU 3964  CD2 PHE B 213    11596  25512  22278  -2554   2384  -6585       C  
ATOM   3965  CE1 PHE B 213     -12.715  36.759  72.470  1.00146.83           C  
ANISOU 3965  CE1 PHE B 213    10016  24848  20923  -3159   2340  -7103       C  
ATOM   3966  CE2 PHE B 213     -15.049  36.616  71.969  1.00155.16           C  
ANISOU 3966  CE2 PHE B 213    11441  25268  22245  -2860   2536  -7026       C  
ATOM   3967  CZ  PHE B 213     -13.969  37.337  72.442  1.00154.76           C  
ANISOU 3967  CZ  PHE B 213    11208  25478  22114  -3171   2519  -7294       C  
ATOM   3968  N   GLY B 214     -12.603  30.898  68.827  1.00128.91           N  
ANISOU 3968  N   GLY B 214     8084  22353  18541  -1516   1972  -4894       N  
ATOM   3969  CA  GLY B 214     -11.794  29.729  68.544  1.00142.93           C  
ANISOU 3969  CA  GLY B 214     9785  24367  20155  -1277   1874  -4528       C  
ATOM   3970  C   GLY B 214     -10.973  29.875  67.280  1.00142.25           C  
ANISOU 3970  C   GLY B 214     9683  24086  20279  -1219   1930  -4306       C  
ATOM   3971  O   GLY B 214      -9.813  29.458  67.231  1.00133.68           O  
ANISOU 3971  O   GLY B 214     8420  23289  19082  -1160   1863  -4136       O  
ATOM   3972  N   LEU B 215     -11.573  30.458  66.239  1.00135.44           N  
ANISOU 3972  N   LEU B 215     9004  22740  19719  -1222   2060  -4298       N  
ATOM   3973  CA  LEU B 215     -10.813  30.810  65.047  1.00113.64           C  
ANISOU 3973  CA  LEU B 215     6227  19773  17177  -1207   2137  -4145       C  
ATOM   3974  C   LEU B 215      -9.740  31.837  65.369  1.00137.84           C  
ANISOU 3974  C   LEU B 215     9066  23029  20277  -1502   2141  -4390       C  
ATOM   3975  O   LEU B 215      -8.682  31.851  64.730  1.00117.97           O  
ANISOU 3975  O   LEU B 215     6428  20570  17827  -1484   2153  -4223       O  
ATOM   3976  CB  LEU B 215     -11.750  31.342  63.961  1.00110.66           C  
ANISOU 3976  CB  LEU B 215     6098  18845  17102  -1174   2276  -4141       C  
ATOM   3977  CG  LEU B 215     -12.744  30.354  63.347  1.00107.03           C  
ANISOU 3977  CG  LEU B 215     5869  18150  16649   -888   2280  -3858       C  
ATOM   3978  CD1 LEU B 215     -13.865  31.105  62.647  1.00129.77           C  
ANISOU 3978  CD1 LEU B 215     8970  20537  19797   -925   2398  -3969       C  
ATOM   3979  CD2 LEU B 215     -12.045  29.412  62.381  1.00105.78           C  
ANISOU 3979  CD2 LEU B 215     5719  17995  16477   -632   2280  -3459       C  
ATOM   3980  N   GLN B 216      -9.995  32.706  66.351  1.00150.33           N  
ANISOU 3980  N   GLN B 216    10589  24716  21816  -1782   2141  -4789       N  
ATOM   3981  CA  GLN B 216      -8.943  33.598  66.828  1.00150.96           C  
ANISOU 3981  CA  GLN B 216    10436  25047  21874  -2090   2126  -5041       C  
ATOM   3982  C   GLN B 216      -7.820  32.811  67.499  1.00155.77           C  
ANISOU 3982  C   GLN B 216    10786  26209  22190  -2040   1959  -4890       C  
ATOM   3983  O   GLN B 216      -6.662  32.866  67.069  1.00139.20           O  
ANISOU 3983  O   GLN B 216     8512  24252  20124  -2067   1942  -4750       O  
ATOM   3984  CB  GLN B 216      -9.526  34.638  67.787  1.00137.29           C  
ANISOU 3984  CB  GLN B 216     8715  23314  20135  -2397   2176  -5516       C  
ATOM   3985  CG  GLN B 216     -10.275  35.766  67.097  1.00128.69           C  
ANISOU 3985  CG  GLN B 216     7822  21702  19374  -2524   2374  -5729       C  
ATOM   3986  CD  GLN B 216     -10.164  37.079  67.847  1.00127.54           C  
ANISOU 3986  CD  GLN B 216     7603  21598  19258  -2917   2459  -6213       C  
ATOM   3987  OE1 GLN B 216     -10.082  37.101  69.076  1.00131.80           O  
ANISOU 3987  OE1 GLN B 216     8018  22504  19557  -3073   2375  -6441       O  
ATOM   3988  NE2 GLN B 216     -10.146  38.183  67.109  1.00128.04           N  
ANISOU 3988  NE2 GLN B 216     7752  21286  19611  -3084   2637  -6379       N  
ATOM   3989  N   ASP B 217      -8.147  32.063  68.553  1.00212.62           N  
ANISOU 3989  N   ASP B 217    18350  32348  30087   1723   4152  -3927       N  
ATOM   3990  CA  ASP B 217      -7.166  31.315  69.335  1.00212.82           C  
ANISOU 3990  CA  ASP B 217    18275  32475  30112   1758   4024  -4084       C  
ATOM   3991  C   ASP B 217      -7.419  29.824  69.146  1.00212.02           C  
ANISOU 3991  C   ASP B 217    18195  32371  29992   1904   3875  -4055       C  
ATOM   3992  O   ASP B 217      -8.438  29.298  69.608  1.00210.40           O  
ANISOU 3992  O   ASP B 217    18058  32099  29783   1939   3787  -3949       O  
ATOM   3993  CB  ASP B 217      -7.244  31.702  70.811  1.00216.47           C  
ANISOU 3993  CB  ASP B 217    18707  32955  30586   1670   3970  -4132       C  
ATOM   3994  CG  ASP B 217      -6.221  30.975  71.665  1.00213.96           C  
ANISOU 3994  CG  ASP B 217    18281  32753  30261   1707   3839  -4293       C  
ATOM   3995  OD1 ASP B 217      -5.245  30.432  71.106  1.00215.34           O  
ANISOU 3995  OD1 ASP B 217    18388  33005  30427   1774   3819  -4394       O  
ATOM   3996  OD2 ASP B 217      -6.398  30.940  72.902  1.00213.64           O  
ANISOU 3996  OD2 ASP B 217    18222  32732  30220   1674   3756  -4318       O  
ATOM   3997  N   ASP B 218      -6.480  29.141  68.485  1.00160.92           N  
ANISOU 3997  N   ASP B 218    11661  25971  23509   1989   3845  -4153       N  
ATOM   3998  CA  ASP B 218      -6.623  27.708  68.255  1.00154.42           C  
ANISOU 3998  CA  ASP B 218    10854  25148  22673   2132   3704  -4141       C  
ATOM   3999  C   ASP B 218      -6.534  26.897  69.541  1.00149.75           C  
ANISOU 3999  C   ASP B 218    10221  24595  22081   2167   3538  -4193       C  
ATOM   4000  O   ASP B 218      -7.004  25.755  69.569  1.00139.85           O  
ANISOU 4000  O   ASP B 218     9000  23310  20826   2276   3413  -4143       O  
ATOM   4001  CB  ASP B 218      -5.564  27.223  67.262  1.00145.29           C  
ANISOU 4001  CB  ASP B 218     9635  24067  21502   2214   3715  -4245       C  
ATOM   4002  CG  ASP B 218      -5.789  27.756  65.859  1.00135.85           C  
ANISOU 4002  CG  ASP B 218     8490  22828  20300   2217   3862  -4169       C  
ATOM   4003  OD1 ASP B 218      -6.688  28.603  65.678  1.00134.83           O  
ANISOU 4003  OD1 ASP B 218     8439  22615  20177   2146   3964  -4043       O  
ATOM   4004  OD2 ASP B 218      -5.068  27.323  64.934  1.00141.18           O  
ANISOU 4004  OD2 ASP B 218     9126  23555  20960   2294   3874  -4234       O  
ATOM   4005  N   SER B 219      -5.959  27.456  70.604  1.00152.96           N  
ANISOU 4005  N   SER B 219    10556  25070  22493   2081   3533  -4290       N  
ATOM   4006  CA  SER B 219      -5.818  26.732  71.863  1.00136.35           C  
ANISOU 4006  CA  SER B 219     8405  23016  20384   2118   3381  -4341       C  
ATOM   4007  C   SER B 219      -7.114  26.665  72.662  1.00146.56           C  
ANISOU 4007  C   SER B 219     9780  24220  21687   2101   3326  -4198       C  
ATOM   4008  O   SER B 219      -7.110  26.117  73.769  1.00156.78           O  
ANISOU 4008  O   SER B 219    11040  25550  22978   2129   3205  -4220       O  
ATOM   4009  CB  SER B 219      -4.718  27.368  72.718  1.00138.86           C  
ANISOU 4009  CB  SER B 219     8612  23450  20699   2033   3395  -4505       C  
ATOM   4010  OG  SER B 219      -5.128  28.626  73.223  1.00142.98           O  
ANISOU 4010  OG  SER B 219     9155  23936  21236   1893   3495  -4476       O  
ATOM   4011  N   LYS B 220      -8.210  27.213  72.138  1.00151.30           N  
ANISOU 4011  N   LYS B 220    10481  24708  22296   2059   3414  -4051       N  
ATOM   4012  CA  LYS B 220      -9.522  27.128  72.770  1.00139.46           C  
ANISOU 4012  CA  LYS B 220     9065  23118  20804   2048   3368  -3902       C  
ATOM   4013  C   LYS B 220     -10.359  25.966  72.257  1.00127.10           C  
ANISOU 4013  C   LYS B 220     7570  21477  19245   2170   3278  -3786       C  
ATOM   4014  O   LYS B 220     -11.114  25.371  73.031  1.00126.01           O  
ANISOU 4014  O   LYS B 220     7462  21298  19117   2204   3173  -3703       O  
ATOM   4015  CB  LYS B 220     -10.293  28.436  72.569  1.00139.27           C  
ANISOU 4015  CB  LYS B 220     9114  23018  20786   1930   3514  -3805       C  
ATOM   4016  CG  LYS B 220      -9.615  29.651  73.184  1.00150.57           C  
ANISOU 4016  CG  LYS B 220    10481  24506  22221   1798   3602  -3911       C  
ATOM   4017  CD  LYS B 220     -10.405  30.923  72.933  1.00146.83           C  
ANISOU 4017  CD  LYS B 220    10084  23950  21756   1689   3748  -3809       C  
ATOM   4018  CE  LYS B 220      -9.749  32.107  73.625  1.00152.83           C  
ANISOU 4018  CE  LYS B 220    10778  24761  22529   1557   3827  -3923       C  
ATOM   4019  NZ  LYS B 220     -10.528  33.359  73.426  1.00154.54           N  
ANISOU 4019  NZ  LYS B 220    11069  24892  22757   1452   3968  -3824       N  
ATOM   4020  N   VAL B 221     -10.246  25.632  70.970  1.00127.32           N  
ANISOU 4020  N   VAL B 221     7622  21485  19267   2236   3316  -3778       N  
ATOM   4021  CA  VAL B 221     -10.940  24.475  70.416  1.00126.36           C  
ANISOU 4021  CA  VAL B 221     7558  21298  19154   2357   3227  -3692       C  
ATOM   4022  C   VAL B 221     -10.015  23.283  70.203  1.00128.21           C  
ANISOU 4022  C   VAL B 221     7724  21602  19387   2480   3114  -3806       C  
ATOM   4023  O   VAL B 221     -10.509  22.164  69.989  1.00126.73           O  
ANISOU 4023  O   VAL B 221     7571  21367  19215   2589   3009  -3752       O  
ATOM   4024  CB  VAL B 221     -11.650  24.827  69.091  1.00125.72           C  
ANISOU 4024  CB  VAL B 221     7564  21137  19066   2361   3337  -3589       C  
ATOM   4025  CG1 VAL B 221     -12.828  25.753  69.349  1.00132.08           C  
ANISOU 4025  CG1 VAL B 221     8454  21856  19873   2265   3418  -3444       C  
ATOM   4026  CG2 VAL B 221     -10.672  25.461  68.120  1.00127.18           C  
ANISOU 4026  CG2 VAL B 221     7707  21382  19233   2338   3461  -3683       C  
ATOM   4027  N   PHE B 222      -8.699  23.484  70.243  1.00149.30           N  
ANISOU 4027  N   PHE B 222    10300  24384  22044   2468   3134  -3962       N  
ATOM   4028  CA  PHE B 222      -7.721  22.402  70.180  1.00130.69           C  
ANISOU 4028  CA  PHE B 222     7868  22108  19681   2582   3024  -4083       C  
ATOM   4029  C   PHE B 222      -7.063  22.272  71.549  1.00130.91           C  
ANISOU 4029  C   PHE B 222     7808  22225  19705   2566   2935  -4175       C  
ATOM   4030  O   PHE B 222      -6.248  23.118  71.934  1.00132.00           O  
ANISOU 4030  O   PHE B 222     7878  22447  19830   2477   3001  -4280       O  
ATOM   4031  CB  PHE B 222      -6.670  22.657  69.100  1.00131.70           C  
ANISOU 4031  CB  PHE B 222     7947  22306  19789   2594   3111  -4195       C  
ATOM   4032  CG  PHE B 222      -7.118  22.300  67.712  1.00131.31           C  
ANISOU 4032  CG  PHE B 222     7964  22192  19736   2666   3150  -4130       C  
ATOM   4033  CD1 PHE B 222      -7.187  20.975  67.312  1.00131.22           C  
ANISOU 4033  CD1 PHE B 222     7963  22166  19729   2807   3028  -4137       C  
ATOM   4034  CD2 PHE B 222      -7.448  23.288  66.799  1.00131.16           C  
ANISOU 4034  CD2 PHE B 222     7995  22131  19709   2598   3308  -4069       C  
ATOM   4035  CE1 PHE B 222      -7.591  20.643  66.033  1.00131.03           C  
ANISOU 4035  CE1 PHE B 222     7993  22095  19698   2875   3059  -4102       C  
ATOM   4036  CE2 PHE B 222      -7.853  22.962  65.519  1.00130.88           C  
ANISOU 4036  CE2 PHE B 222     8019  22046  19665   2670   3344  -4012       C  
ATOM   4037  CZ  PHE B 222      -7.924  21.638  65.136  1.00130.76           C  
ANISOU 4037  CZ  PHE B 222     8013  22018  19652   2808   3219  -4027       C  
ATOM   4038  N   LYS B 223      -7.417  21.216  72.283  1.00140.59           N  
ANISOU 4038  N   LYS B 223     9033  23439  20944   2653   2786  -4142       N  
ATOM   4039  CA  LYS B 223      -6.769  20.911  73.558  1.00138.47           C  
ANISOU 4039  CA  LYS B 223     8676  23270  20667   2664   2685  -4234       C  
ATOM   4040  C   LYS B 223      -5.595  19.978  73.275  1.00144.82           C  
ANISOU 4040  C   LYS B 223     9388  24182  21453   2779   2600  -4393       C  
ATOM   4041  O   LYS B 223      -5.675  18.755  73.414  1.00156.26           O  
ANISOU 4041  O   LYS B 223    10817  25645  22909   2905   2461  -4417       O  
ATOM   4042  CB  LYS B 223      -7.760  20.302  74.543  1.00150.38           C  
ANISOU 4042  CB  LYS B 223    10210  24731  22195   2698   2569  -4141       C  
ATOM   4043  CG  LYS B 223      -7.165  20.020  75.918  1.00156.32           C  
ANISOU 4043  CG  LYS B 223    10874  25587  22934   2714   2468  -4220       C  
ATOM   4044  CD  LYS B 223      -8.198  19.452  76.881  1.00170.07           C  
ANISOU 4044  CD  LYS B 223    12643  27279  24697   2748   2361  -4109       C  
ATOM   4045  CE  LYS B 223      -9.188  20.515  77.326  1.00169.06           C  
ANISOU 4045  CE  LYS B 223    12590  27069  24578   2620   2450  -3974       C  
ATOM   4046  NZ  LYS B 223     -10.236  19.962  78.228  1.00151.81           N  
ANISOU 4046  NZ  LYS B 223    10432  24834  22416   2654   2350  -3857       N  
ATOM   4047  N   GLU B 224      -4.484  20.586  72.854  1.00153.38           N  
ANISOU 4047  N   GLU B 224    10417  25345  22517   2736   2687  -4500       N  
ATOM   4048  CA  GLU B 224      -3.255  19.873  72.506  1.00135.86           C  
ANISOU 4048  CA  GLU B 224     8106  23239  20274   2831   2628  -4658       C  
ATOM   4049  C   GLU B 224      -3.511  18.842  71.404  1.00135.83           C  
ANISOU 4049  C   GLU B 224     8137  23194  20276   2961   2574  -4652       C  
ATOM   4050  O   GLU B 224      -3.278  17.641  71.563  1.00136.45           O  
ANISOU 4050  O   GLU B 224     8177  23315  20353   3091   2433  -4716       O  
ATOM   4051  CB  GLU B 224      -2.628  19.226  73.746  1.00136.81           C  
ANISOU 4051  CB  GLU B 224     8134  23469  20378   2887   2491  -4756       C  
ATOM   4052  CG  GLU B 224      -2.133  20.227  74.776  1.00137.24           C  
ANISOU 4052  CG  GLU B 224     8134  23592  20417   2767   2542  -4802       C  
ATOM   4053  CD  GLU B 224      -1.541  19.559  76.000  1.00144.76           C  
ANISOU 4053  CD  GLU B 224     8994  24662  21346   2832   2404  -4896       C  
ATOM   4054  OE1 GLU B 224      -1.874  18.382  76.254  1.00138.10           O  
ANISOU 4054  OE1 GLU B 224     8152  23813  20508   2958   2269  -4875       O  
ATOM   4055  OE2 GLU B 224      -0.740  20.208  76.705  1.00169.82           O  
ANISOU 4055  OE2 GLU B 224    12092  27936  24496   2760   2431  -4993       O  
ATOM   4056  N   GLY B 225      -4.003  19.342  70.270  1.00140.48           N  
ANISOU 4056  N   GLY B 225     8803  23701  20873   2926   2689  -4574       N  
ATOM   4057  CA  GLY B 225      -4.252  18.521  69.107  1.00140.49           C  
ANISOU 4057  CA  GLY B 225     8840  23664  20876   3036   2658  -4572       C  
ATOM   4058  C   GLY B 225      -5.614  17.864  69.055  1.00155.69           C  
ANISOU 4058  C   GLY B 225    10851  25476  22830   3089   2585  -4452       C  
ATOM   4059  O   GLY B 225      -5.950  17.256  68.030  1.00158.66           O  
ANISOU 4059  O   GLY B 225    11266  25808  23208   3173   2567  -4444       O  
ATOM   4060  N   SER B 226      -6.413  17.973  70.113  1.00152.79           N  
ANISOU 4060  N   SER B 226    10510  25060  22483   3042   2542  -4361       N  
ATOM   4061  CA  SER B 226      -7.729  17.352  70.169  1.00131.24           C  
ANISOU 4061  CA  SER B 226     7855  22225  19787   3087   2468  -4243       C  
ATOM   4062  C   SER B 226      -8.801  18.416  69.986  1.00131.13           C  
ANISOU 4062  C   SER B 226     7936  22106  19780   2968   2595  -4087       C  
ATOM   4063  O   SER B 226      -8.800  19.432  70.688  1.00129.30           O  
ANISOU 4063  O   SER B 226     7706  21878  19543   2850   2673  -4046       O  
ATOM   4064  CB  SER B 226      -7.932  16.621  71.497  1.00131.17           C  
ANISOU 4064  CB  SER B 226     7807  22234  19797   3134   2323  -4237       C  
ATOM   4065  OG  SER B 226      -9.139  15.878  71.488  1.00134.34           O  
ANISOU 4065  OG  SER B 226     8270  22536  20237   3194   2239  -4131       O  
ATOM   4066  N   CYS B 227      -9.719  18.176  69.051  1.00139.42           N  
ANISOU 4066  N   CYS B 227     9065  23066  20842   3003   2613  -4004       N  
ATOM   4067  CA  CYS B 227     -10.763  19.145  68.724  1.00127.33           C  
ANISOU 4067  CA  CYS B 227     7630  21436  19313   2903   2737  -3851       C  
ATOM   4068  C   CYS B 227     -11.878  19.043  69.756  1.00125.97           C  
ANISOU 4068  C   CYS B 227     7497  21196  19169   2873   2671  -3733       C  
ATOM   4069  O   CYS B 227     -12.862  18.323  69.578  1.00125.14           O  
ANISOU 4069  O   CYS B 227     7438  21019  19089   2934   2596  -3663       O  
ATOM   4070  CB  CYS B 227     -11.291  18.917  67.314  1.00127.01           C  
ANISOU 4070  CB  CYS B 227     7655  21337  19268   2958   2780  -3814       C  
ATOM   4071  SG  CYS B 227     -12.593  20.076  66.844  1.00125.30           S  
ANISOU 4071  SG  CYS B 227     7558  21003  19047   2850   2933  -3620       S  
ATOM   4072  N   LEU B 228     -11.719  19.779  70.853  1.00133.35           N  
ANISOU 4072  N   LEU B 228     8410  22158  20101   2778   2699  -3715       N  
ATOM   4073  CA  LEU B 228     -12.752  19.881  71.875  1.00137.51           C  
ANISOU 4073  CA  LEU B 228     8973  22625  20648   2733   2658  -3594       C  
ATOM   4074  C   LEU B 228     -12.527  21.166  72.657  1.00124.37           C  
ANISOU 4074  C   LEU B 228     7305  20982  18968   2598   2758  -3570       C  
ATOM   4075  O   LEU B 228     -11.450  21.766  72.601  1.00125.46           O  
ANISOU 4075  O   LEU B 228     7391  21195  19084   2553   2827  -3670       O  
ATOM   4076  CB  LEU B 228     -12.759  18.656  72.801  1.00135.67           C  
ANISOU 4076  CB  LEU B 228     8684  22425  20441   2832   2479  -3630       C  
ATOM   4077  CG  LEU B 228     -11.465  18.225  73.497  1.00126.44           C  
ANISOU 4077  CG  LEU B 228     7405  21379  19257   2880   2400  -3780       C  
ATOM   4078  CD1 LEU B 228     -11.291  18.928  74.834  1.00126.39           C  
ANISOU 4078  CD1 LEU B 228     7363  21419  19239   2789   2411  -3769       C  
ATOM   4079  CD2 LEU B 228     -11.439  16.715  73.678  1.00127.02           C  
ANISOU 4079  CD2 LEU B 228     7436  21469  19358   3032   2228  -3824       C  
ATOM   4080  N   LEU B 229     -13.563  21.584  73.381  1.00129.00           N  
ANISOU 4080  N   LEU B 229     7946  21502  19566   2533   2765  -3439       N  
ATOM   4081  CA  LEU B 229     -13.493  22.817  74.157  1.00142.24           C  
ANISOU 4081  CA  LEU B 229     9627  23188  21228   2405   2857  -3408       C  
ATOM   4082  C   LEU B 229     -12.365  22.744  75.177  1.00145.30           C  
ANISOU 4082  C   LEU B 229     9908  23695  21604   2401   2795  -3549       C  
ATOM   4083  O   LEU B 229     -12.364  21.881  76.060  1.00130.47           O  
ANISOU 4083  O   LEU B 229     7982  21855  19736   2467   2660  -3570       O  
ATOM   4084  CB  LEU B 229     -14.829  23.075  74.851  1.00138.62           C  
ANISOU 4084  CB  LEU B 229     9238  22645  20784   2356   2847  -3248       C  
ATOM   4085  CG  LEU B 229     -15.918  23.738  74.006  1.00120.64           C  
ANISOU 4085  CG  LEU B 229     7067  20267  18505   2305   2958  -3114       C  
ATOM   4086  CD1 LEU B 229     -17.221  23.801  74.780  1.00118.42           C  
ANISOU 4086  CD1 LEU B 229     6847  19908  18240   2274   2925  -2955       C  
ATOM   4087  CD2 LEU B 229     -15.479  25.130  73.577  1.00120.63           C  
ANISOU 4087  CD2 LEU B 229     7067  20293  18475   2193   3120  -3171       C  
ATOM   4088  N   ALA B 230     -11.404  23.659  75.053  1.00163.20           N  
ANISOU 4088  N   ALA B 230    12120  26041  23847   2322   2891  -3677       N  
ATOM   4089  CA  ALA B 230     -10.210  23.656  75.889  1.00165.14           C  
ANISOU 4089  CA  ALA B 230    12255  26414  24075   2315   2844  -3835       C  
ATOM   4090  C   ALA B 230     -10.227  24.728  76.969  1.00169.20           C  
ANISOU 4090  C   ALA B 230    12745  26964  24578   2191   2891  -3860       C  
ATOM   4091  O   ALA B 230      -9.870  24.444  78.116  1.00181.01           O  
ANISOU 4091  O   ALA B 230    14177  28535  26065   2205   2800  -3915       O  
ATOM   4092  CB  ALA B 230      -8.960  23.829  75.021  1.00163.72           C  
ANISOU 4092  CB  ALA B 230    12012  26315  23879   2323   2906  -3986       C  
ATOM   4093  N   ASP B 231     -10.625  25.955  76.634  1.00147.70           N  
ANISOU 4093  N   ASP B 231    10071  24193  21855   2074   3030  -3823       N  
ATOM   4094  CA  ASP B 231     -10.663  27.020  77.627  1.00147.41           C  
ANISOU 4094  CA  ASP B 231    10014  24185  21811   1953   3079  -3854       C  
ATOM   4095  C   ASP B 231     -11.724  26.717  78.676  1.00141.17           C  
ANISOU 4095  C   ASP B 231     9266  23347  21026   1962   2993  -3727       C  
ATOM   4096  O   ASP B 231     -12.863  26.377  78.344  1.00154.38           O  
ANISOU 4096  O   ASP B 231    11028  24914  22714   1996   2982  -3566       O  
ATOM   4097  CB  ASP B 231     -10.943  28.366  76.960  1.00138.57           C  
ANISOU 4097  CB  ASP B 231     8945  23008  20695   1834   3250  -3826       C  
ATOM   4098  CG  ASP B 231     -10.803  29.538  77.921  1.00139.97           C  
ANISOU 4098  CG  ASP B 231     9090  23221  20870   1703   3309  -3889       C  
ATOM   4099  OD1 ASP B 231     -10.432  29.317  79.093  1.00139.16           O  
ANISOU 4099  OD1 ASP B 231     8920  23198  20756   1704   3218  -3964       O  
ATOM   4100  OD2 ASP B 231     -11.061  30.686  77.502  1.00133.58           O  
ANISOU 4100  OD2 ASP B 231     8323  22363  20070   1601   3447  -3864       O  
ATOM   4101  N   ASP B 232     -11.347  26.849  79.949  1.00140.59           N  
ANISOU 4101  N   ASP B 232     9124  23356  20938   1934   2934  -3801       N  
ATOM   4102  CA  ASP B 232     -12.269  26.524  81.031  1.00151.10           C  
ANISOU 4102  CA  ASP B 232    10482  24657  22273   1949   2847  -3687       C  
ATOM   4103  C   ASP B 232     -13.346  27.587  81.198  1.00142.40           C  
ANISOU 4103  C   ASP B 232     9463  23468  21175   1840   2942  -3574       C  
ATOM   4104  O   ASP B 232     -14.477  27.263  81.576  1.00128.20           O  
ANISOU 4104  O   ASP B 232     7728  21595  19388   1864   2895  -3419       O  
ATOM   4105  CB  ASP B 232     -11.495  26.336  82.335  1.00157.30           C  
ANISOU 4105  CB  ASP B 232    11164  25569  23033   1960   2755  -3805       C  
ATOM   4106  CG  ASP B 232     -10.539  25.160  82.277  1.00167.18           C  
ANISOU 4106  CG  ASP B 232    12338  26904  24278   2085   2645  -3896       C  
ATOM   4107  OD1 ASP B 232     -10.969  24.065  81.856  1.00163.74           O  
ANISOU 4107  OD1 ASP B 232    11939  26410  23866   2197   2568  -3798       O  
ATOM   4108  OD2 ASP B 232      -9.357  25.333  82.642  1.00172.23           O  
ANISOU 4108  OD2 ASP B 232    12878  27669  24891   2072   2635  -4068       O  
ATOM   4109  N   ASN B 233     -13.019  28.853  80.929  1.00150.91           N  
ANISOU 4109  N   ASN B 233    10539  24554  22247   1722   3075  -3648       N  
ATOM   4110  CA  ASN B 233     -13.998  29.925  81.090  1.00144.61           C  
ANISOU 4110  CA  ASN B 233     9818  23677  21453   1618   3170  -3548       C  
ATOM   4111  C   ASN B 233     -15.175  29.742  80.138  1.00146.02           C  
ANISOU 4111  C   ASN B 233    10111  23725  21644   1649   3210  -3364       C  
ATOM   4112  O   ASN B 233     -16.342  29.856  80.540  1.00141.47           O  
ANISOU 4112  O   ASN B 233     9605  23075  21070   1633   3200  -3218       O  
ATOM   4113  CB  ASN B 233     -13.325  31.280  80.867  1.00140.28           C  
ANISOU 4113  CB  ASN B 233     9239  23157  20903   1492   3310  -3671       C  
ATOM   4114  CG  ASN B 233     -14.234  32.446  81.199  1.00124.51           C  
ANISOU 4114  CG  ASN B 233     7310  21088  18909   1381   3404  -3589       C  
ATOM   4115  OD1 ASN B 233     -15.138  32.328  82.025  1.00143.81           O  
ANISOU 4115  OD1 ASN B 233     9792  23501  21347   1384   3346  -3485       O  
ATOM   4116  ND2 ASN B 233     -13.998  33.583  80.553  1.00124.34           N  
ANISOU 4116  ND2 ASN B 233     7303  21040  18900   1285   3550  -3631       N  
ATOM   4117  N   PHE B 234     -14.884  29.451  78.866  1.00146.20           N  
ANISOU 4117  N   PHE B 234    10152  23725  21673   1696   3252  -3370       N  
ATOM   4118  CA  PHE B 234     -15.948  29.229  77.892  1.00134.77           C  
ANISOU 4118  CA  PHE B 234     8808  22165  20233   1734   3287  -3206       C  
ATOM   4119  C   PHE B 234     -16.820  28.051  78.299  1.00140.60           C  
ANISOU 4119  C   PHE B 234     9579  22857  20985   1831   3153  -3080       C  
ATOM   4120  O   PHE B 234     -18.052  28.127  78.241  1.00142.88           O  
ANISOU 4120  O   PHE B 234     9954  23055  21280   1823   3165  -2920       O  
ATOM   4121  CB  PHE B 234     -15.358  28.995  76.500  1.00127.54           C  
ANISOU 4121  CB  PHE B 234     7891  21250  19318   1783   3342  -3253       C  
ATOM   4122  CG  PHE B 234     -14.883  30.245  75.818  1.00133.42           C  
ANISOU 4122  CG  PHE B 234     8635  22001  20056   1687   3503  -3314       C  
ATOM   4123  CD1 PHE B 234     -15.787  31.133  75.261  1.00125.58           C  
ANISOU 4123  CD1 PHE B 234     7734  20922  19059   1625   3623  -3192       C  
ATOM   4124  CD2 PHE B 234     -13.532  30.523  75.716  1.00155.98           C  
ANISOU 4124  CD2 PHE B 234    11399  24952  22913   1661   3537  -3488       C  
ATOM   4125  CE1 PHE B 234     -15.353  32.282  74.629  1.00126.72           C  
ANISOU 4125  CE1 PHE B 234     7876  21069  19203   1541   3775  -3239       C  
ATOM   4126  CE2 PHE B 234     -13.090  31.670  75.086  1.00158.93           C  
ANISOU 4126  CE2 PHE B 234    11768  25328  23290   1572   3689  -3539       C  
ATOM   4127  CZ  PHE B 234     -14.002  32.550  74.540  1.00154.53           C  
ANISOU 4127  CZ  PHE B 234    11303  24680  22733   1513   3809  -3412       C  
ATOM   4128  N   VAL B 235     -16.192  26.948  78.717  1.00130.23           N  
ANISOU 4128  N   VAL B 235     8196  21606  19680   1925   3024  -3147       N  
ATOM   4129  CA  VAL B 235     -16.953  25.760  79.097  1.00138.33           C  
ANISOU 4129  CA  VAL B 235     9243  22586  20729   2023   2892  -3029       C  
ATOM   4130  C   VAL B 235     -17.857  26.067  80.281  1.00150.86           C  
ANISOU 4130  C   VAL B 235    10854  24147  22318   1974   2862  -2925       C  
ATOM   4131  O   VAL B 235     -19.051  25.751  80.267  1.00139.92           O  
ANISOU 4131  O   VAL B 235     9540  22670  20952   1996   2836  -2761       O  
ATOM   4132  CB  VAL B 235     -16.009  24.585  79.404  1.00119.96           C  
ANISOU 4132  CB  VAL B 235     6829  20340  18412   2133   2763  -3129       C  
ATOM   4133  CG1 VAL B 235     -16.815  23.382  79.863  1.00119.07           C  
ANISOU 4133  CG1 VAL B 235     6731  20179  18332   2232   2626  -3011       C  
ATOM   4134  CG2 VAL B 235     -15.187  24.235  78.184  1.00130.53           C  
ANISOU 4134  CG2 VAL B 235     8149  21698  19748   2188   2790  -3224       C  
ATOM   4135  N   LEU B 236     -17.305  26.700  81.319  1.00150.80           N  
ANISOU 4135  N   LEU B 236    10784  24223  22290   1907   2865  -3022       N  
ATOM   4136  CA  LEU B 236     -18.112  27.044  82.486  1.00127.41           C  
ANISOU 4136  CA  LEU B 236     7839  21246  19324   1860   2839  -2934       C  
ATOM   4137  C   LEU B 236     -19.308  27.898  82.087  1.00128.62           C  
ANISOU 4137  C   LEU B 236     8097  21294  19477   1783   2943  -2793       C  
ATOM   4138  O   LEU B 236     -20.461  27.548  82.377  1.00129.89           O  
ANISOU 4138  O   LEU B 236     8317  21382  19655   1807   2899  -2632       O  
ATOM   4139  CB  LEU B 236     -17.255  27.772  83.523  1.00131.05           C  
ANISOU 4139  CB  LEU B 236     8217  21820  19758   1788   2848  -3083       C  
ATOM   4140  CG  LEU B 236     -16.176  26.975  84.260  1.00148.00           C  
ANISOU 4140  CG  LEU B 236    10253  24087  21894   1862   2732  -3212       C  
ATOM   4141  CD1 LEU B 236     -15.306  27.899  85.101  1.00155.47           C  
ANISOU 4141  CD1 LEU B 236    11120  25145  22806   1773   2767  -3378       C  
ATOM   4142  CD2 LEU B 236     -16.803  25.893  85.125  1.00132.09           C  
ANISOU 4142  CD2 LEU B 236     8232  22060  19895   1956   2592  -3095       C  
ATOM   4143  N   ILE B 237     -19.053  28.999  81.370  1.00136.69           N  
ANISOU 4143  N   ILE B 237     9145  22306  20484   1696   3081  -2848       N  
ATOM   4144  CA  ILE B 237     -20.129  29.930  81.039  1.00141.91           C  
ANISOU 4144  CA  ILE B 237     9904  22878  21140   1620   3188  -2722       C  
ATOM   4145  C   ILE B 237     -21.195  29.238  80.201  1.00141.74           C  
ANISOU 4145  C   ILE B 237     9967  22755  21133   1690   3170  -2553       C  
ATOM   4146  O   ILE B 237     -22.386  29.273  80.531  1.00148.69           O  
ANISOU 4146  O   ILE B 237    10913  23567  22018   1681   3158  -2401       O  
ATOM   4147  CB  ILE B 237     -19.568  31.170  80.319  1.00140.73           C  
ANISOU 4147  CB  ILE B 237     9760  22736  20976   1525   3342  -2812       C  
ATOM   4148  CG1 ILE B 237     -18.700  31.998  81.269  1.00142.81           C  
ANISOU 4148  CG1 ILE B 237     9944  23088  21230   1436   3365  -2969       C  
ATOM   4149  CG2 ILE B 237     -20.700  32.015  79.755  1.00121.54           C  
ANISOU 4149  CG2 ILE B 237     7437  20206  18536   1468   3453  -2667       C  
ATOM   4150  CD1 ILE B 237     -18.151  33.263  80.642  1.00140.65           C  
ANISOU 4150  CD1 ILE B 237     9669  22816  20955   1335   3519  -3059       C  
ATOM   4151  N   GLY B 238     -20.783  28.577  79.118  1.00137.86           N  
ANISOU 4151  N   GLY B 238     9474  22257  20651   1764   3164  -2583       N  
ATOM   4152  CA  GLY B 238     -21.757  28.004  78.204  1.00144.03           C  
ANISOU 4152  CA  GLY B 238    10336  22945  21444   1827   3159  -2440       C  
ATOM   4153  C   GLY B 238     -22.505  26.821  78.789  1.00139.74           C  
ANISOU 4153  C   GLY B 238     9797  22365  20934   1910   3018  -2329       C  
ATOM   4154  O   GLY B 238     -23.734  26.747  78.701  1.00127.83           O  
ANISOU 4154  O   GLY B 238     8362  20773  19435   1912   3016  -2170       O  
ATOM   4155  N   SER B 239     -21.776  25.874  79.386  1.00145.73           N  
ANISOU 4155  N   SER B 239    10474  23184  21713   1982   2897  -2408       N  
ATOM   4156  CA  SER B 239     -22.420  24.719  79.997  1.00144.60           C  
ANISOU 4156  CA  SER B 239    10324  23008  21609   2066   2760  -2305       C  
ATOM   4157  C   SER B 239     -23.389  25.148  81.088  1.00135.05           C  
ANISOU 4157  C   SER B 239     9143  21768  20402   2008   2749  -2182       C  
ATOM   4158  O   SER B 239     -24.448  24.534  81.262  1.00127.62           O  
ANISOU 4158  O   SER B 239     8231  20766  19491   2046   2683  -2055       O  
ATOM   4159  CB  SER B 239     -21.362  23.769  80.556  1.00141.51           C  
ANISOU 4159  CB  SER B 239     9823  22715  21230   2146   2637  -2448       C  
ATOM   4160  OG  SER B 239     -21.952  22.724  81.309  1.00147.17           O  
ANISOU 4160  OG  SER B 239    10509  23427  21984   2221   2499  -2385       O  
ATOM   4161  N   PHE B 240     -23.052  26.207  81.830  1.00140.49           N  
ANISOU 4161  N   PHE B 240     9809  22513  21057   1914   2810  -2250       N  
ATOM   4162  CA  PHE B 240     -23.957  26.665  82.878  1.00136.58           C  
ANISOU 4162  CA  PHE B 240     9339  21996  20560   1858   2803  -2143       C  
ATOM   4163  C   PHE B 240     -25.206  27.319  82.293  1.00125.57           C  
ANISOU 4163  C   PHE B 240     8051  20502  19159   1805   2895  -1994       C  
ATOM   4164  O   PHE B 240     -26.308  27.141  82.825  1.00125.10           O  
ANISOU 4164  O   PHE B 240     8030  20385  19117   1807   2856  -1844       O  
ATOM   4165  CB  PHE B 240     -23.231  27.625  83.818  1.00142.21           C  
ANISOU 4165  CB  PHE B 240     9996  22800  21238   1774   2842  -2271       C  
ATOM   4166  CG  PHE B 240     -23.783  27.631  85.213  1.00142.98           C  
ANISOU 4166  CG  PHE B 240    10075  22914  21338   1759   2776  -2203       C  
ATOM   4167  CD1 PHE B 240     -23.909  26.448  85.922  1.00147.15           C  
ANISOU 4167  CD1 PHE B 240    10557  23453  21899   1853   2636  -2146       C  
ATOM   4168  CD2 PHE B 240     -24.169  28.814  85.819  1.00143.43           C  
ANISOU 4168  CD2 PHE B 240    10156  22974  21365   1655   2852  -2195       C  
ATOM   4169  CE1 PHE B 240     -24.416  26.442  87.207  1.00155.20           C  
ANISOU 4169  CE1 PHE B 240    11557  24491  22922   1844   2576  -2078       C  
ATOM   4170  CE2 PHE B 240     -24.675  28.816  87.106  1.00154.69           C  
ANISOU 4170  CE2 PHE B 240    11563  24420  22791   1646   2791  -2135       C  
ATOM   4171  CZ  PHE B 240     -24.799  27.628  87.801  1.00153.70           C  
ANISOU 4171  CZ  PHE B 240    11392  24309  22698   1741   2653  -2075       C  
ATOM   4172  N   VAL B 241     -25.063  28.071  81.201  1.00130.42           N  
ANISOU 4172  N   VAL B 241     8712  21096  19747   1761   3017  -2028       N  
ATOM   4173  CA  VAL B 241     -26.198  28.814  80.663  1.00133.41           C  
ANISOU 4173  CA  VAL B 241     9190  21392  20108   1709   3114  -1892       C  
ATOM   4174  C   VAL B 241     -27.001  27.973  79.675  1.00132.62           C  
ANISOU 4174  C   VAL B 241     9148  21211  20029   1787   3086  -1770       C  
ATOM   4175  O   VAL B 241     -28.232  28.060  79.638  1.00131.15           O  
ANISOU 4175  O   VAL B 241     9032  20953  19846   1777   3096  -1613       O  
ATOM   4176  CB  VAL B 241     -25.727  30.139  80.029  1.00126.35           C  
ANISOU 4176  CB  VAL B 241     8319  20514  19174   1620   3268  -1973       C  
ATOM   4177  CG1 VAL B 241     -24.873  29.890  78.789  1.00123.93           C  
ANISOU 4177  CG1 VAL B 241     7997  20225  18866   1663   3307  -2069       C  
ATOM   4178  CG2 VAL B 241     -26.921  31.015  79.682  1.00118.46           C  
ANISOU 4178  CG2 VAL B 241     7420  19440  18150   1563   3367  -1828       C  
ATOM   4179  N   SER B 242     -26.333  27.152  78.856  1.00128.79           N  
ANISOU 4179  N   SER B 242     8634  20740  19561   1867   3048  -1844       N  
ATOM   4180  CA  SER B 242     -27.046  26.439  77.803  1.00122.35           C  
ANISOU 4180  CA  SER B 242     7873  19851  18762   1937   3032  -1748       C  
ATOM   4181  C   SER B 242     -27.860  25.278  78.358  1.00117.48           C  
ANISOU 4181  C   SER B 242     7244  19196  18197   2006   2893  -1651       C  
ATOM   4182  O   SER B 242     -28.986  25.037  77.910  1.00116.07           O  
ANISOU 4182  O   SER B 242     7122  18949  18031   2022   2889  -1531       O  
ATOM   4183  CB  SER B 242     -26.063  25.949  76.742  1.00114.52           C  
ANISOU 4183  CB  SER B 242     6850  18890  17771   2001   3037  -1871       C  
ATOM   4184  OG  SER B 242     -25.485  27.039  76.044  1.00109.46           O  
ANISOU 4184  OG  SER B 242     6223  18278  17086   1938   3176  -1952       O  
ATOM   4185  N   PHE B 243     -27.315  24.544  79.327  1.00122.65           N  
ANISOU 4185  N   PHE B 243     7811  19910  18882   2046   2775  -1725       N  
ATOM   4186  CA  PHE B 243     -27.965  23.327  79.800  1.00122.41           C  
ANISOU 4186  CA  PHE B 243     7743  19861  18906   2123   2631  -1671       C  
ATOM   4187  C   PHE B 243     -28.667  23.483  81.142  1.00125.43           C  
ANISOU 4187  C   PHE B 243     8119  20235  19304   2084   2587  -1563       C  
ATOM   4188  O   PHE B 243     -29.713  22.864  81.350  1.00125.95           O  
ANISOU 4188  O   PHE B 243     8196  20248  19412   2115   2516  -1445       O  
ATOM   4189  CB  PHE B 243     -26.948  22.186  79.900  1.00124.81           C  
ANISOU 4189  CB  PHE B 243     7949  20234  19238   2222   2512  -1814       C  
ATOM   4190  CG  PHE B 243     -27.562  20.858  80.245  1.00138.10           C  
ANISOU 4190  CG  PHE B 243     9592  21895  20983   2315   2361  -1760       C  
ATOM   4191  CD1 PHE B 243     -28.235  20.123  79.282  1.00140.47           C  
ANISOU 4191  CD1 PHE B 243     9923  22136  21316   2377   2324  -1721       C  
ATOM   4192  CD2 PHE B 243     -27.463  20.342  81.526  1.00137.06           C  
ANISOU 4192  CD2 PHE B 243     9391  21804  20881   2345   2253  -1748       C  
ATOM   4193  CE1 PHE B 243     -28.802  18.901  79.593  1.00140.42           C  
ANISOU 4193  CE1 PHE B 243     9876  22104  21373   2464   2183  -1670       C  
ATOM   4194  CE2 PHE B 243     -28.028  19.120  81.844  1.00138.20           C  
ANISOU 4194  CE2 PHE B 243     9497  21924  21090   2436   2115  -1686       C  
ATOM   4195  CZ  PHE B 243     -28.698  18.398  80.875  1.00139.47           C  
ANISOU 4195  CZ  PHE B 243     9687  22019  21287   2494   2078  -1647       C  
ATOM   4196  N   PHE B 244     -28.129  24.291  82.057  1.00120.11           N  
ANISOU 4196  N   PHE B 244     7423  19611  18601   2018   2626  -1601       N  
ATOM   4197  CA  PHE B 244     -28.648  24.306  83.420  1.00106.79           C  
ANISOU 4197  CA  PHE B 244     5713  17931  16932   1997   2567  -1521       C  
ATOM   4198  C   PHE B 244     -29.729  25.357  83.640  1.00105.47           C  
ANISOU 4198  C   PHE B 244     5633  17696  16743   1905   2660  -1373       C  
ATOM   4199  O   PHE B 244     -30.682  25.102  84.382  1.00113.07           O  
ANISOU 4199  O   PHE B 244     6602  18623  17739   1905   2604  -1251       O  
ATOM   4200  CB  PHE B 244     -27.502  24.505  84.415  1.00109.79           C  
ANISOU 4200  CB  PHE B 244     6011  18413  17291   1986   2539  -1651       C  
ATOM   4201  CG  PHE B 244     -26.539  23.353  84.455  1.00135.43           C  
ANISOU 4201  CG  PHE B 244     9163  21733  20561   2088   2424  -1778       C  
ATOM   4202  CD1 PHE B 244     -26.935  22.121  84.950  1.00123.08           C  
ANISOU 4202  CD1 PHE B 244     7548  20166  19050   2180   2283  -1726       C  
ATOM   4203  CD2 PHE B 244     -25.241  23.498  83.996  1.00131.76           C  
ANISOU 4203  CD2 PHE B 244     8658  21338  20066   2095   2456  -1944       C  
ATOM   4204  CE1 PHE B 244     -26.054  21.056  84.985  1.00139.34           C  
ANISOU 4204  CE1 PHE B 244     9522  22291  21129   2283   2176  -1837       C  
ATOM   4205  CE2 PHE B 244     -24.355  22.438  84.028  1.00111.75           C  
ANISOU 4205  CE2 PHE B 244     6037  18873  17549   2194   2350  -2060       C  
ATOM   4206  CZ  PHE B 244     -24.761  21.216  84.524  1.00111.84           C  
ANISOU 4206  CZ  PHE B 244     6003  18881  17611   2291   2209  -2006       C  
ATOM   4207  N   ILE B 245     -29.607  26.540  83.033  1.00105.33           N  
ANISOU 4207  N   ILE B 245     5677  17670  16674   1829   2799  -1395       N  
ATOM   4208  CA  ILE B 245     -30.697  27.516  83.101  1.00110.03           C  
ANISOU 4208  CA  ILE B 245     6352  18212  17242   1750   2887  -1275       C  
ATOM   4209  C   ILE B 245     -31.975  26.969  82.472  1.00111.29           C  
ANISOU 4209  C   ILE B 245     6580  18272  17432   1788   2868  -1100       C  
ATOM   4210  O   ILE B 245     -33.031  27.016  83.126  1.00108.90           O  
ANISOU 4210  O   ILE B 245     6306  17922  17150   1767   2846   -960       O  
ATOM   4211  CB  ILE B 245     -30.254  28.854  82.490  1.00104.78           C  
ANISOU 4211  CB  ILE B 245     5723  17574  16515   1666   3036  -1365       C  
ATOM   4212  CG1 ILE B 245     -29.284  29.582  83.423  1.00105.95           C  
ANISOU 4212  CG1 ILE B 245     5806  17811  16638   1604   3055  -1512       C  
ATOM   4213  CG2 ILE B 245     -31.462  29.725  82.163  1.00103.63           C  
ANISOU 4213  CG2 ILE B 245     5675  17360  16340   1607   3132  -1224       C  
ATOM   4214  CD1 ILE B 245     -28.839  30.933  82.903  1.00106.56           C  
ANISOU 4214  CD1 ILE B 245     5912  17910  16667   1514   3200  -1602       C  
ATOM   4215  N   PRO B 246     -31.963  26.444  81.239  1.00102.85           N  
ANISOU 4215  N   PRO B 246     5537  17173  16371   1843   2875  -1104       N  
ATOM   4216  CA  PRO B 246     -33.178  25.794  80.734  1.00101.90           C  
ANISOU 4216  CA  PRO B 246     5454  16981  16282   1882   2834   -979       C  
ATOM   4217  C   PRO B 246     -33.582  24.583  81.544  1.00102.25           C  
ANISOU 4217  C   PRO B 246     5428  17023  16398   1942   2679   -947       C  
ATOM   4218  O   PRO B 246     -34.776  24.295  81.624  1.00124.94           O  
ANISOU 4218  O   PRO B 246     8332  19835  19305   1945   2647   -811       O  
ATOM   4219  CB  PRO B 246     -32.807  25.418  79.294  1.00102.31           C  
ANISOU 4219  CB  PRO B 246     5520  17031  16323   1935   2860  -1054       C  
ATOM   4220  CG  PRO B 246     -31.697  26.322  78.942  1.00103.07           C  
ANISOU 4220  CG  PRO B 246     5623  17172  16367   1894   2967  -1161       C  
ATOM   4221  CD  PRO B 246     -30.914  26.465  80.205  1.00109.16           C  
ANISOU 4221  CD  PRO B 246     6323  18010  17145   1867   2923  -1244       C  
ATOM   4222  N   LEU B 247     -32.638  23.862  82.152  1.00103.08           N  
ANISOU 4222  N   LEU B 247     5440  17196  16530   1994   2582  -1063       N  
ATOM   4223  CA  LEU B 247     -33.016  22.737  83.003  1.00103.22           C  
ANISOU 4223  CA  LEU B 247     5389  17214  16617   2058   2433  -1018       C  
ATOM   4224  C   LEU B 247     -33.861  23.205  84.182  1.00117.46           C  
ANISOU 4224  C   LEU B 247     7206  18988  18435   1998   2431   -887       C  
ATOM   4225  O   LEU B 247     -34.936  22.653  84.452  1.00123.94           O  
ANISOU 4225  O   LEU B 247     8029  19750  19311   2017   2366   -759       O  
ATOM   4226  CB  LEU B 247     -31.768  22.003  83.493  1.00104.68           C  
ANISOU 4226  CB  LEU B 247     5473  17486  16816   2126   2339  -1165       C  
ATOM   4227  CG  LEU B 247     -31.984  20.869  84.496  1.00105.08           C  
ANISOU 4227  CG  LEU B 247     5442  17550  16935   2201   2183  -1124       C  
ATOM   4228  CD1 LEU B 247     -33.023  19.885  83.984  1.00104.54           C  
ANISOU 4228  CD1 LEU B 247     5383  17408  16931   2263   2103  -1019       C  
ATOM   4229  CD2 LEU B 247     -30.670  20.161  84.784  1.00119.61           C  
ANISOU 4229  CD2 LEU B 247     7188  19482  18777   2280   2100  -1277       C  
ATOM   4230  N   THR B 248     -33.388  24.231  84.893  1.00118.63           N  
ANISOU 4230  N   THR B 248     7360  19176  18537   1927   2502   -921       N  
ATOM   4231  CA  THR B 248     -34.141  24.761  86.024  1.00120.16           C  
ANISOU 4231  CA  THR B 248     7569  19344  18742   1869   2508   -810       C  
ATOM   4232  C   THR B 248     -35.496  25.286  85.575  1.00116.47           C  
ANISOU 4232  C   THR B 248     7199  18779  18276   1819   2581   -648       C  
ATOM   4233  O   THR B 248     -36.528  24.978  86.188  1.00116.22           O  
ANISOU 4233  O   THR B 248     7168  18690  18301   1815   2528   -522       O  
ATOM   4234  CB  THR B 248     -33.346  25.867  86.722  1.00118.41           C  
ANISOU 4234  CB  THR B 248     7343  19187  18462   1799   2581   -893       C  
ATOM   4235  OG1 THR B 248     -33.045  26.908  85.784  1.00118.33           O  
ANISOU 4235  OG1 THR B 248     7400  19174  18386   1742   2719   -940       O  
ATOM   4236  CG2 THR B 248     -32.052  25.314  87.301  1.00131.91           C  
ANISOU 4236  CG2 THR B 248     8949  21001  20171   1850   2500  -1051       C  
ATOM   4237  N   ILE B 249     -35.517  26.073  84.494  1.00107.22           N  
ANISOU 4237  N   ILE B 249     6107  17584  17046   1782   2702   -647       N  
ATOM   4238  CA  ILE B 249     -36.783  26.644  84.040  1.00101.09           C  
ANISOU 4238  CA  ILE B 249     5426  16723  16260   1738   2779   -491       C  
ATOM   4239  C   ILE B 249     -37.747  25.539  83.622  1.00106.62           C  
ANISOU 4239  C   ILE B 249     6124  17361  17024   1794   2688   -406       C  
ATOM   4240  O   ILE B 249     -38.932  25.571  83.969  1.00128.11           O  
ANISOU 4240  O   ILE B 249     8927  19996  19752   1752   2655   -287       O  
ATOM   4241  CB  ILE B 249     -36.548  27.660  82.907  1.00 98.94           C  
ANISOU 4241  CB  ILE B 249     5230  16459  15904   1699   2922   -525       C  
ATOM   4242  CG1 ILE B 249     -35.644  28.795  83.391  1.00106.39           C  
ANISOU 4242  CG1 ILE B 249     6156  17484  16784   1629   3001   -660       C  
ATOM   4243  CG2 ILE B 249     -37.874  28.230  82.430  1.00 97.72           C  
ANISOU 4243  CG2 ILE B 249     5192  16224  15713   1655   2984   -383       C  
ATOM   4244  CD1 ILE B 249     -35.446  29.901  82.375  1.00101.24           C  
ANISOU 4244  CD1 ILE B 249     5566  16847  16055   1580   3144   -709       C  
ATOM   4245  N   MET B 250     -37.251  24.534  82.895  1.00 98.87           N  
ANISOU 4245  N   MET B 250     5090  16408  16066   1875   2620   -492       N  
ATOM   4246  CA  MET B 250     -38.092  23.433  82.444  1.00105.57           C  
ANISOU 4246  CA  MET B 250     5923  17209  16979   1937   2526   -426       C  
ATOM   4247  C   MET B 250     -38.692  22.677  83.617  1.00120.11           C  
ANISOU 4247  C   MET B 250     7723  19017  18895   1948   2393   -353       C  
ATOM   4248  O   MET B 250     -39.901  22.431  83.653  1.00118.71           O  
ANISOU 4248  O   MET B 250     7616  18750  18738   1922   2345   -244       O  
ATOM   4249  CB  MET B 250     -37.279  22.481  81.567  1.00 99.57           C  
ANISOU 4249  CB  MET B 250     5115  16493  16226   2026   2463   -559       C  
ATOM   4250  CG  MET B 250     -37.205  22.879  80.116  1.00 99.43           C  
ANISOU 4250  CG  MET B 250     5163  16465  16150   2026   2562   -599       C  
ATOM   4251  SD  MET B 250     -35.900  22.016  79.226  1.00127.38           S  
ANISOU 4251  SD  MET B 250     8643  20065  19691   2119   2510   -797       S  
ATOM   4252  CE  MET B 250     -36.314  20.312  79.579  1.00101.29           C  
ANISOU 4252  CE  MET B 250     5252  16750  16485   2224   2313   -781       C  
ATOM   4253  N   VAL B 251     -37.860  22.288  84.585  1.00121.08           N  
ANISOU 4253  N   VAL B 251     7743  19207  19054   1985   2324   -420       N  
ATOM   4254  CA  VAL B 251     -38.358  21.490  85.704  1.00137.02           C  
ANISOU 4254  CA  VAL B 251     9704  21199  21157   2011   2194   -351       C  
ATOM   4255  C   VAL B 251     -39.361  22.291  86.526  1.00123.81           C  
ANISOU 4255  C   VAL B 251     8127  19442  19474   1908   2225   -246       C  
ATOM   4256  O   VAL B 251     -40.441  21.794  86.882  1.00119.12           O  
ANISOU 4256  O   VAL B 251     7568  18753  18940   1894   2142   -153       O  
ATOM   4257  CB  VAL B 251     -37.188  20.983  86.565  1.00136.80           C  
ANISOU 4257  CB  VAL B 251     9571  21265  21143   2069   2113   -460       C  
ATOM   4258  CG1 VAL B 251     -37.711  20.243  87.783  1.00148.35           C  
ANISOU 4258  CG1 VAL B 251    10966  22702  22700   2100   1988   -376       C  
ATOM   4259  CG2 VAL B 251     -36.284  20.078  85.745  1.00116.28           C  
ANISOU 4259  CG2 VAL B 251     6925  18719  18537   2164   2052   -583       C  
ATOM   4260  N   ILE B 252     -39.032  23.553  86.823  1.00101.15           N  
ANISOU 4260  N   ILE B 252     5297  16597  16536   1833   2344   -267       N  
ATOM   4261  CA  ILE B 252     -39.921  24.381  87.632  1.00 99.67           C  
ANISOU 4261  CA  ILE B 252     5198  16331  16340   1739   2378   -181       C  
ATOM   4262  C   ILE B 252     -41.251  24.589  86.917  1.00107.61           C  
ANISOU 4262  C   ILE B 252     6342  17207  17339   1686   2407    -75       C  
ATOM   4263  O   ILE B 252     -42.325  24.426  87.510  1.00119.97           O  
ANISOU 4263  O   ILE B 252     7952  18660  18971   1644   2352     -6       O  
ATOM   4264  CB  ILE B 252     -39.241  25.721  87.968  1.00 97.39           C  
ANISOU 4264  CB  ILE B 252     4926  16105  15973   1678   2504   -229       C  
ATOM   4265  CG1 ILE B 252     -38.082  25.503  88.943  1.00 98.64           C  
ANISOU 4265  CG1 ILE B 252     4940  16382  16156   1721   2462   -331       C  
ATOM   4266  CG2 ILE B 252     -40.244  26.702  88.549  1.00 97.26           C  
ANISOU 4266  CG2 ILE B 252     5024  15996  15935   1582   2559   -136       C  
ATOM   4267  CD1 ILE B 252     -37.322  26.767  89.277  1.00 98.96           C  
ANISOU 4267  CD1 ILE B 252     4991  16492  16117   1661   2573   -403       C  
ATOM   4268  N   THR B 253     -41.201  24.939  85.628  1.00 95.72           N  
ANISOU 4268  N   THR B 253     4899  15708  15764   1688   2492    -79       N  
ATOM   4269  CA  THR B 253     -42.427  25.201  84.886  1.00 94.58           C  
ANISOU 4269  CA  THR B 253     4883  15449  15603   1642   2527     18       C  
ATOM   4270  C   THR B 253     -43.254  23.936  84.708  1.00101.76           C  
ANISOU 4270  C   THR B 253     5769  16286  16609   1683   2399     56       C  
ATOM   4271  O   THR B 253     -44.483  23.992  84.756  1.00111.55           O  
ANISOU 4271  O   THR B 253     7092  17386  17905   1624   2386    122       O  
ATOM   4272  CB  THR B 253     -42.104  25.824  83.529  1.00 94.49           C  
ANISOU 4272  CB  THR B 253     4934  15477  15491   1646   2643     -2       C  
ATOM   4273  OG1 THR B 253     -41.083  25.058  82.878  1.00 95.54           O  
ANISOU 4273  OG1 THR B 253     4962  15705  15633   1735   2612   -112       O  
ATOM   4274  CG2 THR B 253     -41.634  27.259  83.704  1.00 94.39           C  
ANISOU 4274  CG2 THR B 253     4979  15499  15387   1583   2776    -11       C  
ATOM   4275  N   TYR B 254     -42.605  22.787  84.504  1.00 95.42           N  
ANISOU 4275  N   TYR B 254     4852  15561  15844   1783   2302     -3       N  
ATOM   4276  CA  TYR B 254     -43.348  21.539  84.366  1.00102.08           C  
ANISOU 4276  CA  TYR B 254     5663  16344  16777   1832   2168     37       C  
ATOM   4277  C   TYR B 254     -44.060  21.173  85.662  1.00109.44           C  
ANISOU 4277  C   TYR B 254     6579  17173  17831   1793   2068     69       C  
ATOM   4278  O   TYR B 254     -45.225  20.752  85.639  1.00113.21           O  
ANISOU 4278  O   TYR B 254     7097  17509  18410   1754   2003     86       O  
ATOM   4279  CB  TYR B 254     -42.411  20.412  83.935  1.00 96.69           C  
ANISOU 4279  CB  TYR B 254     4857  15771  16111   1957   2083    -40       C  
ATOM   4280  CG  TYR B 254     -43.130  19.119  83.625  1.00 97.34           C  
ANISOU 4280  CG  TYR B 254     4908  15811  16267   2023   1946      8       C  
ATOM   4281  CD1 TYR B 254     -43.735  18.922  82.392  1.00 98.00           C  
ANISOU 4281  CD1 TYR B 254     5041  15877  16318   2040   1961     28       C  
ATOM   4282  CD2 TYR B 254     -43.206  18.098  84.564  1.00 99.07           C  
ANISOU 4282  CD2 TYR B 254     5044  16010  16587   2073   1800     32       C  
ATOM   4283  CE1 TYR B 254     -44.396  17.747  82.102  1.00 96.71           C  
ANISOU 4283  CE1 TYR B 254     4843  15691  16211   2105   1833     74       C  
ATOM   4284  CE2 TYR B 254     -43.866  16.915  84.281  1.00 97.73           C  
ANISOU 4284  CE2 TYR B 254     4846  15802  16484   2137   1671     85       C  
ATOM   4285  CZ  TYR B 254     -44.459  16.746  83.047  1.00 97.34           C  
ANISOU 4285  CZ  TYR B 254     4845  15753  16389   2154   1687    108       C  
ATOM   4286  OH  TYR B 254     -45.118  15.573  82.755  1.00 97.68           O  
ANISOU 4286  OH  TYR B 254     4855  15785  16473   2226   1556    168       O  
ATOM   4287  N   PHE B 255     -43.379  21.317  86.802  1.00124.24           N  
ANISOU 4287  N   PHE B 255     8385  19102  19716   1795   2048     30       N  
ATOM   4288  CA  PHE B 255     -44.028  21.002  88.071  1.00106.39           C  
ANISOU 4288  CA  PHE B 255     6102  16750  17571   1757   1950     18       C  
ATOM   4289  C   PHE B 255     -45.163  21.977  88.366  1.00103.85           C  
ANISOU 4289  C   PHE B 255     5898  16287  17274   1623   2015     -9       C  
ATOM   4290  O   PHE B 255     -46.246  21.564  88.804  1.00111.19           O  
ANISOU 4290  O   PHE B 255     6836  17112  18297   1571   1915   -126       O  
ATOM   4291  CB  PHE B 255     -42.998  20.990  89.200  1.00128.57           C  
ANISOU 4291  CB  PHE B 255     8808  19676  20368   1798   1920    -21       C  
ATOM   4292  CG  PHE B 255     -42.042  19.828  89.135  1.00149.42           C  
ANISOU 4292  CG  PHE B 255    11320  22423  23029   1926   1819    -48       C  
ATOM   4293  CD1 PHE B 255     -42.268  18.777  88.258  1.00146.64           C  
ANISOU 4293  CD1 PHE B 255    10950  22050  22716   2000   1740    -22       C  
ATOM   4294  CD2 PHE B 255     -40.925  19.781  89.952  1.00153.45           C  
ANISOU 4294  CD2 PHE B 255    11726  23054  23525   1977   1800   -107       C  
ATOM   4295  CE1 PHE B 255     -41.395  17.707  88.193  1.00138.55           C  
ANISOU 4295  CE1 PHE B 255     9812  21119  21714   2125   1646    -56       C  
ATOM   4296  CE2 PHE B 255     -40.050  18.711  89.894  1.00153.13           C  
ANISOU 4296  CE2 PHE B 255    11568  23099  23514   2097   1706   -149       C  
ATOM   4297  CZ  PHE B 255     -40.285  17.675  89.013  1.00152.53           C  
ANISOU 4297  CZ  PHE B 255    11481  22994  23477   2172   1629   -123       C  
ATOM   4298  N   LEU B 256     -44.952  23.270  88.104  1.00 93.88           N  
ANISOU 4298  N   LEU B 256     4721  15044  15907   1566   2169     30       N  
ATOM   4299  CA  LEU B 256     -46.027  24.237  88.298  1.00 92.68           C  
ANISOU 4299  CA  LEU B 256     4688  14753  15773   1441   2239    -10       C  
ATOM   4300  C   LEU B 256     -47.193  23.962  87.355  1.00 91.83           C  
ANISOU 4300  C   LEU B 256     4654  14511  15726   1389   2219    -97       C  
ATOM   4301  O   LEU B 256     -48.356  24.131  87.733  1.00100.53           O  
ANISOU 4301  O   LEU B 256     5799  15563  16835   1287   2168   -309       O  
ATOM   4302  CB  LEU B 256     -45.504  25.661  88.109  1.00 92.44           C  
ANISOU 4302  CB  LEU B 256     4736  14776  15611   1406   2406     69       C  
ATOM   4303  CG  LEU B 256     -44.479  26.145  89.138  1.00 93.20           C  
ANISOU 4303  CG  LEU B 256     4760  15006  15647   1424   2427     62       C  
ATOM   4304  CD1 LEU B 256     -44.277  27.650  89.033  1.00 92.81           C  
ANISOU 4304  CD1 LEU B 256     4803  14979  15482   1366   2579    104       C  
ATOM   4305  CD2 LEU B 256     -44.890  25.748  90.548  1.00 98.40           C  
ANISOU 4305  CD2 LEU B 256     5358  15632  16399   1402   2321     -3       C  
ATOM   4306  N   THR B 257     -46.901  23.531  86.127  1.00 92.09           N  
ANISOU 4306  N   THR B 257     4688  14573  15729   1462   2240      2       N  
ATOM   4307  CA  THR B 257     -47.954  23.242  85.162  1.00 91.40           C  
ANISOU 4307  CA  THR B 257     4659  14369  15702   1416   2219   -106       C  
ATOM   4308  C   THR B 257     -48.781  22.037  85.585  1.00 91.49           C  
ANISOU 4308  C   THR B 257     4588  14397  15779   1408   2009   -371       C  
ATOM   4309  O   THR B 257     -50.013  22.078  85.528  1.00103.28           O  
ANISOU 4309  O   THR B 257     6112  16005  17126   1336   1928   -621       O  
ATOM   4310  CB  THR B 257     -47.344  23.014  83.777  1.00 92.03           C  
ANISOU 4310  CB  THR B 257     4741  14551  15675   1527   2280     88       C  
ATOM   4311  OG1 THR B 257     -46.841  24.255  83.265  1.00 94.05           O  
ANISOU 4311  OG1 THR B 257     5081  14886  15767   1517   2440    178       O  
ATOM   4312  CG2 THR B 257     -48.382  22.457  82.815  1.00 91.38           C  
ANISOU 4312  CG2 THR B 257     4689  14348  15684   1501   2233    -13       C  
ATOM   4313  N   ILE B 258     -48.125  20.953  86.009  1.00 92.56           N  
ANISOU 4313  N   ILE B 258     4609  14575  15984   1517   1900   -283       N  
ATOM   4314  CA  ILE B 258     -48.881  19.780  86.439  1.00 92.79           C  
ANISOU 4314  CA  ILE B 258     4557  14706  15992   1546   1679   -512       C  
ATOM   4315  C   ILE B 258     -49.680  20.099  87.696  1.00 92.23           C  
ANISOU 4315  C   ILE B 258     4483  14804  15757   1498   1609   -604       C  
ATOM   4316  O   ILE B 258     -50.806  19.621  87.869  1.00102.88           O  
ANISOU 4316  O   ILE B 258     5815  16326  16948   1519   1495   -615       O  
ATOM   4317  CB  ILE B 258     -47.957  18.561  86.636  1.00103.76           C  
ANISOU 4317  CB  ILE B 258     5833  16076  17517   1680   1584   -370       C  
ATOM   4318  CG1 ILE B 258     -46.966  18.782  87.780  1.00123.71           C  
ANISOU 4318  CG1 ILE B 258     8303  18652  20050   1715   1611   -236       C  
ATOM   4319  CG2 ILE B 258     -47.230  18.234  85.345  1.00102.99           C  
ANISOU 4319  CG2 ILE B 258     5735  15968  17428   1783   1673    -76       C  
ATOM   4320  CD1 ILE B 258     -46.126  17.566  88.107  1.00113.93           C  
ANISOU 4320  CD1 ILE B 258     6943  17472  18872   1851   1496   -143       C  
ATOM   4321  N   LYS B 259     -49.126  20.933  88.580  1.00 92.24           N  
ANISOU 4321  N   LYS B 259     4498  14751  15796   1455   1702   -533       N  
ATOM   4322  CA  LYS B 259     -49.862  21.333  89.773  1.00 94.36           C  
ANISOU 4322  CA  LYS B 259     4769  15147  15935   1413   1664   -549       C  
ATOM   4323  C   LYS B 259     -51.093  22.164  89.417  1.00 97.10           C  
ANISOU 4323  C   LYS B 259     5220  15556  16117   1320   1727   -573       C  
ATOM   4324  O   LYS B 259     -52.184  21.949  89.963  1.00 92.01           O  
ANISOU 4324  O   LYS B 259     4563  15041  15355   1325   1652   -496       O  
ATOM   4325  CB  LYS B 259     -48.931  22.111  90.695  1.00102.42           C  
ANISOU 4325  CB  LYS B 259     5784  16101  17030   1391   1761   -474       C  
ATOM   4326  CG  LYS B 259     -49.131  21.844  92.162  1.00127.47           C  
ANISOU 4326  CG  LYS B 259     8882  19396  20155   1421   1659   -457       C  
ATOM   4327  CD  LYS B 259     -48.481  22.964  92.931  1.00136.41           C  
ANISOU 4327  CD  LYS B 259    10038  20487  21306   1371   1784   -404       C  
ATOM   4328  CE  LYS B 259     -49.119  24.287  92.549  1.00128.70           C  
ANISOU 4328  CE  LYS B 259     9196  19451  20254   1252   1927   -432       C  
ATOM   4329  NZ  LYS B 259     -48.145  25.415  92.554  1.00123.00           N  
ANISOU 4329  NZ  LYS B 259     8521  18636  19576   1222   2096   -334       N  
ATOM   4330  N   SER B 260     -50.936  23.125  88.503  1.00 89.84           N  
ANISOU 4330  N   SER B 260     4404  14523  15208   1241   1877   -618       N  
ATOM   4331  CA  SER B 260     -52.066  23.942  88.081  1.00 88.64           C  
ANISOU 4331  CA  SER B 260     4355  14429  14893   1155   1941   -636       C  
ATOM   4332  C   SER B 260     -53.114  23.111  87.354  1.00 88.32           C  
ANISOU 4332  C   SER B 260     4294  14507  14756   1201   1844   -591       C  
ATOM   4333  O   SER B 260     -54.311  23.394  87.466  1.00103.43           O  
ANISOU 4333  O   SER B 260     6248  16494  16557   1165   1848   -493       O  
ATOM   4334  CB  SER B 260     -51.584  25.090  87.195  1.00 88.29           C  
ANISOU 4334  CB  SER B 260     4425  14226  14896   1073   2121   -690       C  
ATOM   4335  OG  SER B 260     -52.655  25.956  86.858  1.00 87.17           O  
ANISOU 4335  OG  SER B 260     4387  14152  14582    988   2183   -715       O  
ATOM   4336  N   LEU B 261     -52.689  22.094  86.601  1.00 89.06           N  
ANISOU 4336  N   LEU B 261     4325  14593  14920   1285   1767   -627       N  
ATOM   4337  CA  LEU B 261     -53.645  21.200  85.953  1.00 88.94           C  
ANISOU 4337  CA  LEU B 261     4276  14673  14844   1346   1669   -551       C  
ATOM   4338  C   LEU B 261     -54.397  20.356  86.974  1.00 91.12           C  
ANISOU 4338  C   LEU B 261     4468  15037  15117   1407   1535   -390       C  
ATOM   4339  O   LEU B 261     -55.600  20.112  86.820  1.00103.29           O  
ANISOU 4339  O   LEU B 261     6010  16618  16617   1408   1503   -250       O  
ATOM   4340  CB  LEU B 261     -52.927  20.309  84.942  1.00 89.83           C  
ANISOU 4340  CB  LEU B 261     4340  14753  15039   1428   1613   -642       C  
ATOM   4341  CG  LEU B 261     -52.437  21.029  83.687  1.00 89.63           C  
ANISOU 4341  CG  LEU B 261     4397  14617  15043   1374   1750   -755       C  
ATOM   4342  CD1 LEU B 261     -51.757  20.061  82.732  1.00 93.45           C  
ANISOU 4342  CD1 LEU B 261     4823  15032  15651   1462   1694   -813       C  
ATOM   4343  CD2 LEU B 261     -53.601  21.728  83.011  1.00 97.28           C  
ANISOU 4343  CD2 LEU B 261     5455  15648  15860   1308   1821   -714       C  
ATOM   4344  N   GLN B 262     -53.703  19.889  88.017  1.00 90.49           N  
ANISOU 4344  N   GLN B 262     4311  14967  15105   1460   1460   -391       N  
ATOM   4345  CA  GLN B 262     -54.377  19.155  89.084  1.00 93.01           C  
ANISOU 4345  CA  GLN B 262     4550  15358  15430   1518   1340   -228       C  
ATOM   4346  C   GLN B 262     -55.402  20.034  89.789  1.00 91.85           C  
ANISOU 4346  C   GLN B 262     4495  15225  15180   1428   1401    -94       C  
ATOM   4347  O   GLN B 262     -56.504  19.578  90.116  1.00 89.40           O  
ANISOU 4347  O   GLN B 262     4234  14922  14814   1438   1327    120       O  
ATOM   4348  CB  GLN B 262     -53.351  18.617  90.082  1.00105.60           C  
ANISOU 4348  CB  GLN B 262     6058  16960  17104   1589   1260   -263       C  
ATOM   4349  CG  GLN B 262     -52.461  17.513  89.531  1.00131.13           C  
ANISOU 4349  CG  GLN B 262     9220  20175  20429   1695   1164   -342       C  
ATOM   4350  CD  GLN B 262     -51.156  17.379  90.295  1.00151.34           C  
ANISOU 4350  CD  GLN B 262    11723  22691  23089   1734   1145   -417       C  
ATOM   4351  OE1 GLN B 262     -50.815  18.229  91.118  1.00152.45           O  
ANISOU 4351  OE1 GLN B 262    11882  22806  23235   1673   1223   -422       O  
ATOM   4352  NE2 GLN B 262     -50.416  16.310  90.021  1.00145.63           N  
ANISOU 4352  NE2 GLN B 262    10926  21949  22457   1840   1043   -461       N  
ATOM   4353  N   LYS B 263     -55.052  21.298  90.038  1.00103.41           N  
ANISOU 4353  N   LYS B 263     6006  16665  16619   1338   1537   -200       N  
ATOM   4354  CA  LYS B 263     -56.024  22.235  90.596  1.00 87.52           C  
ANISOU 4354  CA  LYS B 263     4103  14659  14492   1250   1603    -87       C  
ATOM   4355  C   LYS B 263     -57.195  22.441  89.641  1.00 86.58           C  
ANISOU 4355  C   LYS B 263     4088  14521  14288   1205   1639     13       C  
ATOM   4356  O   LYS B 263     -58.353  22.498  90.069  1.00 99.66           O  
ANISOU 4356  O   LYS B 263     5825  16180  15863   1180   1613    209       O  
ATOM   4357  CB  LYS B 263     -55.345  23.567  90.913  1.00 90.55           C  
ANISOU 4357  CB  LYS B 263     4529  15000  14877   1163   1746   -232       C  
ATOM   4358  CG  LYS B 263     -56.299  24.694  91.281  1.00 86.13           C  
ANISOU 4358  CG  LYS B 263     4074  14444  14207   1068   1839   -161       C  
ATOM   4359  CD  LYS B 263     -57.119  24.358  92.514  1.00101.29           C  
ANISOU 4359  CD  LYS B 263     6016  16418  16053   1092   1741     48       C  
ATOM   4360  CE  LYS B 263     -58.005  25.526  92.913  1.00120.20           C  
ANISOU 4360  CE  LYS B 263     8533  18805  18334    999   1831    117       C  
ATOM   4361  NZ  LYS B 263     -58.885  25.965  91.794  1.00118.77           N  
ANISOU 4361  NZ  LYS B 263     8459  18587  18083    944   1900    153       N  
ATOM   4362  N   GLU B 264     -56.909  22.550  88.343  1.00107.81           N  
ANISOU 4362  N   GLU B 264     6776  17184  17001   1198   1701   -115       N  
ATOM   4363  CA  GLU B 264     -57.954  22.784  87.355  1.00108.45           C  
ANISOU 4363  CA  GLU B 264     6953  17245  17008   1159   1743    -33       C  
ATOM   4364  C   GLU B 264     -58.879  21.578  87.207  1.00107.21           C  
ANISOU 4364  C   GLU B 264     6786  17087  16863   1225   1607    170       C  
ATOM   4365  O   GLU B 264     -60.044  21.733  86.824  1.00106.49           O  
ANISOU 4365  O   GLU B 264     6783  16969  16710   1188   1621    314       O  
ATOM   4366  CB  GLU B 264     -57.312  23.140  86.010  1.00108.52           C  
ANISOU 4366  CB  GLU B 264     6960  17230  17041   1145   1838   -222       C  
ATOM   4367  CG  GLU B 264     -58.289  23.413  84.881  1.00129.76           C  
ANISOU 4367  CG  GLU B 264     9733  19907  19663   1112   1892   -162       C  
ATOM   4368  CD  GLU B 264     -57.591  23.586  83.547  1.00129.49           C  
ANISOU 4368  CD  GLU B 264     9725  19843  19634   1116   1958   -322       C  
ATOM   4369  OE1 GLU B 264     -56.368  23.845  83.537  1.00124.04           O  
ANISOU 4369  OE1 GLU B 264     9040  19113  18977   1111   1993   -473       O  
ATOM   4370  OE2 GLU B 264     -58.264  23.456  82.504  1.00136.47           O  
ANISOU 4370  OE2 GLU B 264    10631  20729  20494   1124   1973   -285       O  
ATOM   4371  N   ALA B 265     -58.390  20.377  87.515  1.00 98.83           N  
ANISOU 4371  N   ALA B 265     5618  16042  15892   1323   1476    186       N  
ATOM   4372  CA  ALA B 265     -59.175  19.164  87.311  1.00 87.36           C  
ANISOU 4372  CA  ALA B 265     4145  14568  14482   1388   1345    366       C  
ATOM   4373  C   ALA B 265     -60.139  18.908  88.466  1.00 87.91           C  
ANISOU 4373  C   ALA B 265     4256  14625  14521   1377   1274    611       C  
ATOM   4374  O   ALA B 265     -61.308  18.576  88.242  1.00102.62           O  
ANISOU 4374  O   ALA B 265     6173  16444  16373   1362   1237    796       O  
ATOM   4375  CB  ALA B 265     -58.244  17.963  87.121  1.00 90.21           C  
ANISOU 4375  CB  ALA B 265     4376  14943  14956   1503   1232    282       C  
ATOM   4376  N   ALA B1001     -59.666  19.054  89.708  1.00 90.30           N  
ANISOU 4376  N   ALA B1001     4532  14965  14813   1385   1254    615       N  
ATOM   4377  CA  ALA B1001     -60.496  18.715  90.861  1.00 87.48           C  
ANISOU 4377  CA  ALA B1001     4204  14606  14429   1388   1177    848       C  
ATOM   4378  C   ALA B1001     -61.684  19.655  91.005  1.00 91.58           C  
ANISOU 4378  C   ALA B1001     4852  15107  14836   1291   1258    979       C  
ATOM   4379  O   ALA B1001     -62.746  19.235  91.479  1.00106.17           O  
ANISOU 4379  O   ALA B1001     6740  16930  16668   1288   1194   1208       O  
ATOM   4380  CB  ALA B1001     -59.657  18.722  92.138  1.00 88.13           C  
ANISOU 4380  CB  ALA B1001     4223  14744  14517   1423   1145    806       C  
ATOM   4381  N   ASP B1002     -61.527  20.922  90.616  1.00 85.40           N  
ANISOU 4381  N   ASP B1002     4136  14332  13980   1213   1397    840       N  
ATOM   4382  CA  ASP B1002     -62.644  21.858  90.693  1.00 85.57           C  
ANISOU 4382  CA  ASP B1002     4286  14335  13892   1128   1476    953       C  
ATOM   4383  C   ASP B1002     -63.798  21.410  89.807  1.00 85.31           C  
ANISOU 4383  C   ASP B1002     4305  14249  13861   1121   1448   1104       C  
ATOM   4384  O   ASP B1002     -64.966  21.483  90.209  1.00105.96           O  
ANISOU 4384  O   ASP B1002     6995  16844  16421   1089   1431   1306       O  
ATOM   4385  CB  ASP B1002     -62.185  23.262  90.297  1.00 84.26           C  
ANISOU 4385  CB  ASP B1002     4179  14173  13665   1050   1631    760       C  
ATOM   4386  CG  ASP B1002     -61.204  23.859  91.288  1.00 83.84           C  
ANISOU 4386  CG  ASP B1002     4085  14160  13613   1039   1669    627       C  
ATOM   4387  OD1 ASP B1002     -60.619  23.098  92.087  1.00 84.74           O  
ANISOU 4387  OD1 ASP B1002     4103  14308  13785   1107   1574    639       O  
ATOM   4388  OD2 ASP B1002     -61.027  25.095  91.272  1.00 83.25           O  
ANISOU 4388  OD2 ASP B1002     4070  14076  13484    963   1795    510       O  
ATOM   4389  N   LEU B1003     -63.488  20.944  88.596  1.00 84.21           N  
ANISOU 4389  N   LEU B1003     4122  14088  13786   1153   1444   1005       N  
ATOM   4390  CA  LEU B1003     -64.535  20.551  87.662  1.00 91.92           C  
ANISOU 4390  CA  LEU B1003     5138  15016  14772   1146   1424   1124       C  
ATOM   4391  C   LEU B1003     -65.345  19.376  88.190  1.00103.40           C  
ANISOU 4391  C   LEU B1003     6563  16434  16293   1187   1284   1357       C  
ATOM   4392  O   LEU B1003     -66.577  19.370  88.095  1.00105.23           O  
ANISOU 4392  O   LEU B1003     6864  16628  16493   1149   1275   1536       O  
ATOM   4393  CB  LEU B1003     -63.926  20.204  86.309  1.00 84.36           C  
ANISOU 4393  CB  LEU B1003     4122  14052  13879   1186   1438    958       C  
ATOM   4394  CG  LEU B1003     -64.962  19.725  85.299  1.00 86.24           C  
ANISOU 4394  CG  LEU B1003     4386  14243  14139   1188   1410   1067       C  
ATOM   4395  CD1 LEU B1003     -65.908  20.855  84.945  1.00 91.09           C  
ANISOU 4395  CD1 LEU B1003     5131  14846  14633   1102   1524   1120       C  
ATOM   4396  CD2 LEU B1003     -64.273  19.206  84.078  1.00 84.88           C  
ANISOU 4396  CD2 LEU B1003     4135  14074  14043   1247   1401    904       C  
ATOM   4397  N   GLU B1004     -64.672  18.364  88.739  1.00 99.74           N  
ANISOU 4397  N   GLU B1004     5996  15977  15926   1265   1174   1361       N  
ATOM   4398  CA  GLU B1004     -65.392  17.200  89.241  1.00 98.81           C  
ANISOU 4398  CA  GLU B1004     5847  15810  15888   1304   1040   1584       C  
ATOM   4399  C   GLU B1004     -66.220  17.555  90.471  1.00114.63           C  
ANISOU 4399  C   GLU B1004     7920  17823  17811   1259   1036   1785       C  
ATOM   4400  O   GLU B1004     -67.343  17.062  90.635  1.00128.50           O  
ANISOU 4400  O   GLU B1004     9708  19528  19587   1243    978   2002       O  
ATOM   4401  CB  GLU B1004     -64.410  16.067  89.538  1.00 89.89           C  
ANISOU 4401  CB  GLU B1004     4593  14682  14879   1405    926   1533       C  
ATOM   4402  CG  GLU B1004     -65.022  14.684  89.440  1.00 88.54           C  
ANISOU 4402  CG  GLU B1004     4373  14429  14839   1455    788   1708       C  
ATOM   4403  CD  GLU B1004     -65.921  14.381  90.607  1.00 88.62           C  
ANISOU 4403  CD  GLU B1004     4418  14413  14840   1436    727   1966       C  
ATOM   4404  OE1 GLU B1004     -65.489  14.621  91.752  1.00 88.75           O  
ANISOU 4404  OE1 GLU B1004     4429  14486  14806   1449    726   1983       O  
ATOM   4405  OE2 GLU B1004     -67.061  13.927  90.376  1.00126.03           O  
ANISOU 4405  OE2 GLU B1004     9188  19079  19620   1406    683   2148       O  
ATOM   4406  N   ASP B1005     -65.689  18.420  91.341  1.00123.04           N  
ANISOU 4406  N   ASP B1005     9008  18953  18790   1237   1099   1712       N  
ATOM   4407  CA  ASP B1005     -66.467  18.883  92.486  1.00134.84           C  
ANISOU 4407  CA  ASP B1005    10573  20467  20192   1196   1106   1887       C  
ATOM   4408  C   ASP B1005     -67.712  19.638  92.037  1.00131.62           C  
ANISOU 4408  C   ASP B1005    10286  20030  19693   1116   1179   1990       C  
ATOM   4409  O   ASP B1005     -68.795  19.462  92.609  1.00134.84           O  
ANISOU 4409  O   ASP B1005    10744  20419  20070   1095   1139   2214       O  
ATOM   4410  CB  ASP B1005     -65.604  19.762  93.393  1.00130.93           C  
ANISOU 4410  CB  ASP B1005    10075  20048  19624   1187   1168   1756       C  
ATOM   4411  CG  ASP B1005     -64.688  18.954  94.293  1.00149.22           C  
ANISOU 4411  CG  ASP B1005    12283  22404  22009   1270   1073   1741       C  
ATOM   4412  OD1 ASP B1005     -64.733  17.708  94.229  1.00154.23           O  
ANISOU 4412  OD1 ASP B1005    12851  23002  22749   1336    959   1840       O  
ATOM   4413  OD2 ASP B1005     -63.925  19.568  95.069  1.00160.63           O  
ANISOU 4413  OD2 ASP B1005    13709  23915  23409   1270   1112   1629       O  
ATOM   4414  N   ASN B1006     -67.582  20.480  91.010  1.00 95.54           N  
ANISOU 4414  N   ASN B1006     5765  15457  15078   1073   1287   1834       N  
ATOM   4415  CA  ASN B1006     -68.742  21.213  90.512  1.00106.28           C  
ANISOU 4415  CA  ASN B1006     7243  16791  16349   1005   1358   1923       C  
ATOM   4416  C   ASN B1006     -69.742  20.281  89.837  1.00102.61           C  
ANISOU 4416  C   ASN B1006     6771  16264  15953   1015   1281   2085       C  
ATOM   4417  O   ASN B1006     -70.956  20.486  89.941  1.00102.43           O  
ANISOU 4417  O   ASN B1006     6827  16219  15871    972   1285   2260       O  
ATOM   4418  CB  ASN B1006     -68.292  22.318  89.559  1.00103.61           C  
ANISOU 4418  CB  ASN B1006     6954  16460  15951    962   1493   1712       C  
ATOM   4419  CG  ASN B1006     -67.502  23.403  90.264  1.00100.24           C  
ANISOU 4419  CG  ASN B1006     6551  16081  15456    931   1580   1567       C  
ATOM   4420  OD1 ASN B1006     -67.070  23.230  91.405  1.00 97.55           O  
ANISOU 4420  OD1 ASN B1006     6165  15777  15122    955   1533   1589       O  
ATOM   4421  ND2 ASN B1006     -67.308  24.528  89.589  1.00 98.50           N  
ANISOU 4421  ND2 ASN B1006     6398  15856  15172    877   1708   1417       N  
ATOM   4422  N   TRP B1007     -69.253  19.253  89.139  1.00 94.04           N  
ANISOU 4422  N   TRP B1007     5588  15150  14994   1072   1210   2024       N  
ATOM   4423  CA  TRP B1007     -70.143  18.250  88.560  1.00 92.73           C  
ANISOU 4423  CA  TRP B1007     5396  14918  14919   1085   1122   2170       C  
ATOM   4424  C   TRP B1007     -70.932  17.530  89.647  1.00100.15           C  
ANISOU 4424  C   TRP B1007     6332  15827  15893   1087   1021   2423       C  
ATOM   4425  O   TRP B1007     -72.145  17.308  89.513  1.00108.65           O  
ANISOU 4425  O   TRP B1007     7452  16860  16970   1051    993   2603       O  
ATOM   4426  CB  TRP B1007     -69.320  17.261  87.731  1.00 84.62           C  
ANISOU 4426  CB  TRP B1007     4254  13866  14033   1156   1056   2040       C  
ATOM   4427  CG  TRP B1007     -70.109  16.189  87.039  1.00 88.02           C  
ANISOU 4427  CG  TRP B1007     4643  14221  14580   1173    961   2155       C  
ATOM   4428  CD1 TRP B1007     -70.910  16.338  85.943  1.00 84.84           C  
ANISOU 4428  CD1 TRP B1007     4276  13794  14165   1141    995   2163       C  
ATOM   4429  CD2 TRP B1007     -70.146  14.796  87.376  1.00 87.59           C  
ANISOU 4429  CD2 TRP B1007     4498  14101  14681   1228    815   2270       C  
ATOM   4430  NE1 TRP B1007     -71.455  15.128  85.587  1.00 88.01           N  
ANISOU 4430  NE1 TRP B1007     4610  14121  14709   1168    877   2270       N  
ATOM   4431  CE2 TRP B1007     -71.001  14.165  86.451  1.00 95.21           C  
ANISOU 4431  CE2 TRP B1007     5446  14998  15731   1220    765   2339       C  
ATOM   4432  CE3 TRP B1007     -69.546  14.024  88.376  1.00 87.45           C  
ANISOU 4432  CE3 TRP B1007     4413  14073  14743   1285    722   2323       C  
ATOM   4433  CZ2 TRP B1007     -71.270  12.798  86.496  1.00101.66           C  
ANISOU 4433  CZ2 TRP B1007     6182  15724  16720   1259    624   2455       C  
ATOM   4434  CZ3 TRP B1007     -69.814  12.667  88.418  1.00 88.67           C  
ANISOU 4434  CZ3 TRP B1007     4492  14138  15062   1330    585   2447       C  
ATOM   4435  CH2 TRP B1007     -70.669  12.069  87.484  1.00 91.90           C  
ANISOU 4435  CH2 TRP B1007     4887  14466  15564   1313    537   2510       C  
ATOM   4436  N   GLU B1008     -70.256  17.170  90.741  1.00 86.98           N  
ANISOU 4436  N   GLU B1008     4611  14186  14251   1130    966   2441       N  
ATOM   4437  CA  GLU B1008     -70.943  16.564  91.876  1.00 93.27           C  
ANISOU 4437  CA  GLU B1008     5408  14963  15068   1134    879   2684       C  
ATOM   4438  C   GLU B1008     -71.976  17.515  92.465  1.00101.45           C  
ANISOU 4438  C   GLU B1008     6561  16027  15959   1064    945   2824       C  
ATOM   4439  O   GLU B1008     -73.092  17.102  92.794  1.00109.21           O  
ANISOU 4439  O   GLU B1008     7573  16970  16951   1039    893   3049       O  
ATOM   4440  CB  GLU B1008     -69.936  16.152  92.947  1.00102.93           C  
ANISOU 4440  CB  GLU B1008     6557  16228  16325   1198    824   2656       C  
ATOM   4441  CG  GLU B1008     -69.067  14.978  92.561  1.00105.34           C  
ANISOU 4441  CG  GLU B1008     6743  16494  16788   1281    728   2575       C  
ATOM   4442  CD  GLU B1008     -68.228  14.482  93.719  1.00124.75           C  
ANISOU 4442  CD  GLU B1008     9132  18991  19277   1351    661   2588       C  
ATOM   4443  OE1 GLU B1008     -68.481  14.913  94.863  1.00135.24           O  
ANISOU 4443  OE1 GLU B1008    10500  20372  20513   1334    676   2697       O  
ATOM   4444  OE2 GLU B1008     -67.318  13.661  93.486  1.00128.12           O  
ANISOU 4444  OE2 GLU B1008     9463  19401  19816   1429    593   2488       O  
ATOM   4445  N   THR B1009     -71.614  18.791  92.619  1.00 93.64           N  
ANISOU 4445  N   THR B1009     5638  15103  14840   1031   1057   2692       N  
ATOM   4446  CA  THR B1009     -72.559  19.775  93.141  1.00102.14           C  
ANISOU 4446  CA  THR B1009     6829  16204  15774    971   1121   2806       C  
ATOM   4447  C   THR B1009     -73.797  19.856  92.258  1.00 92.76           C  
ANISOU 4447  C   THR B1009     5712  14966  14568    924   1139   2913       C  
ATOM   4448  O   THR B1009     -74.934  19.848  92.752  1.00102.47           O  
ANISOU 4448  O   THR B1009     6999  16184  15750    894   1114   3123       O  
ATOM   4449  CB  THR B1009     -71.886  21.145  93.245  1.00 90.08           C  
ANISOU 4449  CB  THR B1009     5357  14737  14133    943   1242   2611       C  
ATOM   4450  OG1 THR B1009     -70.815  21.085  94.195  1.00 81.92           O  
ANISOU 4450  OG1 THR B1009     4256  13759  13112    984   1221   2525       O  
ATOM   4451  CG2 THR B1009     -72.889  22.210  93.677  1.00 89.81           C  
ANISOU 4451  CG2 THR B1009     5448  14720  13955    884   1309   2717       C  
ATOM   4452  N   LEU B1010     -73.590  19.909  90.941  1.00 81.38           N  
ANISOU 4452  N   LEU B1010     4261  13499  13162    920   1179   2768       N  
ATOM   4453  CA  LEU B1010     -74.708  20.003  90.011  1.00 80.89           C  
ANISOU 4453  CA  LEU B1010     4257  13398  13079    882   1199   2848       C  
ATOM   4454  C   LEU B1010     -75.621  18.791  90.128  1.00 93.77           C  
ANISOU 4454  C   LEU B1010     5843  14969  14815    887   1080   3067       C  
ATOM   4455  O   LEU B1010     -76.840  18.935  90.254  1.00105.82           O  
ANISOU 4455  O   LEU B1010     7437  16482  16289    846   1076   3243       O  
ATOM   4456  CB  LEU B1010     -74.198  20.158  88.578  1.00 80.81           C  
ANISOU 4456  CB  LEU B1010     4226  13379  13099    889   1256   2645       C  
ATOM   4457  CG  LEU B1010     -73.444  21.450  88.258  1.00 84.90           C  
ANISOU 4457  CG  LEU B1010     4802  13942  13514    869   1389   2432       C  
ATOM   4458  CD1 LEU B1010     -73.391  21.696  86.760  1.00 79.82           C  
ANISOU 4458  CD1 LEU B1010     4167  13288  12874    865   1455   2293       C  
ATOM   4459  CD2 LEU B1010     -74.066  22.631  88.971  1.00 90.11           C  
ANISOU 4459  CD2 LEU B1010     5584  14628  14025    817   1464   2504       C  
ATOM   4460  N   ASN B1011     -75.049  17.584  90.099  1.00 99.75           N  
ANISOU 4460  N   ASN B1011     6485  15686  15729    939    979   3058       N  
ATOM   4461  CA  ASN B1011     -75.892  16.391  90.162  1.00108.96           C  
ANISOU 4461  CA  ASN B1011     7603  16777  17019    940    863   3259       C  
ATOM   4462  C   ASN B1011     -76.610  16.278  91.505  1.00107.51           C  
ANISOU 4462  C   ASN B1011     7455  16597  16796    920    821   3499       C  
ATOM   4463  O   ASN B1011     -77.800  15.929  91.554  1.00107.19           O  
ANISOU 4463  O   ASN B1011     7441  16514  16773    882    780   3696       O  
ATOM   4464  CB  ASN B1011     -75.063  15.141  89.880  1.00107.26           C  
ANISOU 4464  CB  ASN B1011     7259  16508  16988   1006    761   3191       C  
ATOM   4465  CG  ASN B1011     -74.649  15.038  88.426  1.00114.72           C  
ANISOU 4465  CG  ASN B1011     8162  17438  17991   1025    782   2995       C  
ATOM   4466  OD1 ASN B1011     -74.424  16.049  87.761  1.00101.12           O  
ANISOU 4466  OD1 ASN B1011     6494  15768  16159   1006    894   2842       O  
ATOM   4467  ND2 ASN B1011     -74.558  13.813  87.921  1.00130.35           N  
ANISOU 4467  ND2 ASN B1011    10041  19340  20145   1066    675   3001       N  
ATOM   4468  N   ASP B1012     -75.913  16.578  92.605  1.00 94.09           N  
ANISOU 4468  N   ASP B1012     5754  14954  15040    947    831   3484       N  
ATOM   4469  CA  ASP B1012     -76.537  16.512  93.922  1.00 94.10           C  
ANISOU 4469  CA  ASP B1012     5788  14974  14992    936    797   3706       C  
ATOM   4470  C   ASP B1012     -77.715  17.469  94.016  1.00 92.96           C  
ANISOU 4470  C   ASP B1012     5764  14857  14699    873    865   3818       C  
ATOM   4471  O   ASP B1012     -78.802  17.090  94.466  1.00 95.29           O  
ANISOU 4471  O   ASP B1012     6084  15125  14997    845    817   4048       O  
ATOM   4472  CB  ASP B1012     -75.511  16.828  95.012  1.00 94.28           C  
ANISOU 4472  CB  ASP B1012     5789  15073  14961    979    809   3634       C  
ATOM   4473  CG  ASP B1012     -74.391  15.815  95.073  1.00106.85           C  
ANISOU 4473  CG  ASP B1012     7260  16642  16696   1052    730   3549       C  
ATOM   4474  OD1 ASP B1012     -74.561  14.704  94.529  1.00119.49           O  
ANISOU 4474  OD1 ASP B1012     8794  18156  18451   1070    644   3605       O  
ATOM   4475  OD2 ASP B1012     -73.336  16.131  95.662  1.00104.08           O  
ANISOU 4475  OD2 ASP B1012     6878  16359  16307   1092    750   3420       O  
ATOM   4476  N   ASN B1013     -77.527  18.716  93.579  1.00 84.75           N  
ANISOU 4476  N   ASN B1013     4803  13867  13531    849    976   3660       N  
ATOM   4477  CA  ASN B1013     -78.611  19.683  93.697  1.00 80.56           C  
ANISOU 4477  CA  ASN B1013     4394  13362  12854    799   1040   3759       C  
ATOM   4478  C   ASN B1013     -79.721  19.415  92.687  1.00 89.52           C  
ANISOU 4478  C   ASN B1013     5554  14442  14016    763   1027   3845       C  
ATOM   4479  O   ASN B1013     -80.881  19.761  92.941  1.00106.46           O  
ANISOU 4479  O   ASN B1013     7778  16594  16078    727   1034   4010       O  
ATOM   4480  CB  ASN B1013     -78.061  21.100  93.554  1.00 79.52           C  
ANISOU 4480  CB  ASN B1013     4338  13288  12589    786   1160   3562       C  
ATOM   4481  CG  ASN B1013     -77.193  21.501  94.731  1.00 85.21           C  
ANISOU 4481  CG  ASN B1013     5044  14072  13260    811   1174   3503       C  
ATOM   4482  OD1 ASN B1013     -77.634  22.225  95.624  1.00 93.14           O  
ANISOU 4482  OD1 ASN B1013     6119  15123  14148    796   1201   3586       O  
ATOM   4483  ND2 ASN B1013     -75.955  21.017  94.748  1.00100.84           N  
ANISOU 4483  ND2 ASN B1013     6927  16059  15329    854   1150   3357       N  
ATOM   4484  N   LEU B1014     -79.397  18.794  91.549  1.00 80.86           N  
ANISOU 4484  N   LEU B1014     4389  13299  13037    774   1006   3735       N  
ATOM   4485  CA  LEU B1014     -80.440  18.347  90.632  1.00 93.62           C  
ANISOU 4485  CA  LEU B1014     6005  14863  14703    744    976   3823       C  
ATOM   4486  C   LEU B1014     -81.321  17.292  91.286  1.00101.03           C  
ANISOU 4486  C   LEU B1014     6903  15747  15734    730    865   4076       C  
ATOM   4487  O   LEU B1014     -82.551  17.331  91.160  1.00 98.94           O  
ANISOU 4487  O   LEU B1014     6689  15470  15436    688    856   4231       O  
ATOM   4488  CB  LEU B1014     -79.815  17.797  89.349  1.00 96.39           C  
ANISOU 4488  CB  LEU B1014     6272  15178  15174    769    963   3645       C  
ATOM   4489  CG  LEU B1014     -79.249  18.786  88.330  1.00 80.68           C  
ANISOU 4489  CG  LEU B1014     4326  13231  13099    772   1078   3413       C  
ATOM   4490  CD1 LEU B1014     -78.390  18.047  87.320  1.00 81.48           C  
ANISOU 4490  CD1 LEU B1014     4319  13303  13337    814   1046   3241       C  
ATOM   4491  CD2 LEU B1014     -80.362  19.547  87.634  1.00 79.80           C  
ANISOU 4491  CD2 LEU B1014     4312  13134  12875    728   1144   3458       C  
ATOM   4492  N   LYS B1015     -80.705  16.338  91.988  1.00 95.94           N  
ANISOU 4492  N   LYS B1015     6169  15071  15212    767    781   4123       N  
ATOM   4493  CA  LYS B1015     -81.485  15.365  92.747  1.00 93.21           C  
ANISOU 4493  CA  LYS B1015     5788  14669  14957    753    681   4376       C  
ATOM   4494  C   LYS B1015     -82.263  16.029  93.877  1.00 92.59           C  
ANISOU 4494  C   LYS B1015     5802  14648  14729    726    711   4560       C  
ATOM   4495  O   LYS B1015     -83.381  15.606  94.192  1.00 99.20           O  
ANISOU 4495  O   LYS B1015     6653  15451  15588    690    663   4780       O  
ATOM   4496  CB  LYS B1015     -80.570  14.274  93.299  1.00100.34           C  
ANISOU 4496  CB  LYS B1015     6581  15528  16016    807    591   4380       C  
ATOM   4497  CG  LYS B1015     -80.338  13.120  92.342  1.00110.90           C  
ANISOU 4497  CG  LYS B1015     7813  16766  17559    826    505   4318       C  
ATOM   4498  CD  LYS B1015     -81.420  12.067  92.493  1.00109.85           C  
ANISOU 4498  CD  LYS B1015     7642  16535  17563    789    406   4554       C  
ATOM   4499  CE  LYS B1015     -81.274  10.969  91.459  1.00108.34           C  
ANISOU 4499  CE  LYS B1015     7346  16236  17583    803    318   4481       C  
ATOM   4500  NZ  LYS B1015     -81.532   9.639  92.066  1.00108.93           N  
ANISOU 4500  NZ  LYS B1015     7340  16196  17851    808    193   4673       N  
ATOM   4501  N   VAL B1016     -81.684  17.058  94.499  1.00 85.24           N  
ANISOU 4501  N   VAL B1016     4931  13803  13653    744    787   4469       N  
ATOM   4502  CA  VAL B1016     -82.388  17.799  95.544  1.00 88.91           C  
ANISOU 4502  CA  VAL B1016     5487  14330  13964    726    819   4622       C  
ATOM   4503  C   VAL B1016     -83.639  18.460  94.977  1.00 99.41           C  
ANISOU 4503  C   VAL B1016     6914  15663  15193    677    862   4694       C  
ATOM   4504  O   VAL B1016     -84.687  18.508  95.634  1.00101.84           O  
ANISOU 4504  O   VAL B1016     7272  15984  15440    654    841   4905       O  
ATOM   4505  CB  VAL B1016     -81.443  18.827  96.199  1.00 81.12           C  
ANISOU 4505  CB  VAL B1016     4538  13431  12852    755    893   4471       C  
ATOM   4506  CG1 VAL B1016     -82.217  19.775  97.100  1.00 95.84           C  
ANISOU 4506  CG1 VAL B1016     6507  15364  14545    737    934   4595       C  
ATOM   4507  CG2 VAL B1016     -80.360  18.116  96.994  1.00 82.15           C  
ANISOU 4507  CG2 VAL B1016     4571  13573  13069    808    838   4445       C  
ATOM   4508  N   ILE B1017     -83.553  18.973  93.747  1.00 84.42           N  
ANISOU 4508  N   ILE B1017     5043  13758  13274    665    923   4521       N  
ATOM   4509  CA  ILE B1017     -84.724  19.559  93.096  1.00 84.61           C  
ANISOU 4509  CA  ILE B1017     5154  13787  13207    627    961   4578       C  
ATOM   4510  C   ILE B1017     -85.817  18.512  92.915  1.00104.03           C  
ANISOU 4510  C   ILE B1017     7569  16184  15772    595    872   4781       C  
ATOM   4511  O   ILE B1017     -87.009  18.802  93.081  1.00126.65           O  
ANISOU 4511  O   ILE B1017    10502  19064  18555    565    870   4941       O  
ATOM   4512  CB  ILE B1017     -84.328  20.193  91.749  1.00 85.87           C  
ANISOU 4512  CB  ILE B1017     5336  13950  13339    626   1042   4349       C  
ATOM   4513  CG1 ILE B1017     -83.479  21.444  91.974  1.00 91.62           C  
ANISOU 4513  CG1 ILE B1017     6133  14738  13942    643   1143   4169       C  
ATOM   4514  CG2 ILE B1017     -85.564  20.523  90.919  1.00 78.24           C  
ANISOU 4514  CG2 ILE B1017     4436  12982  12311    592   1063   4415       C  
ATOM   4515  CD1 ILE B1017     -83.068  22.143  90.697  1.00 77.28           C  
ANISOU 4515  CD1 ILE B1017     4347  12925  12093    641   1233   3950       C  
ATOM   4516  N   GLU B1018     -85.429  17.280  92.580  1.00109.09           N  
ANISOU 4516  N   GLU B1018     8093  16752  16603    602    791   4776       N  
ATOM   4517  CA  GLU B1018     -86.404  16.259  92.204  1.00118.63           C  
ANISOU 4517  CA  GLU B1018     9247  17887  17941    565    706   4932       C  
ATOM   4518  C   GLU B1018     -87.359  15.942  93.352  1.00122.99           C  
ANISOU 4518  C   GLU B1018     9822  18434  18477    539    654   5210       C  
ATOM   4519  O   GLU B1018     -88.574  15.843  93.152  1.00141.68           O  
ANISOU 4519  O   GLU B1018    12216  20785  20830    495    632   5356       O  
ATOM   4520  CB  GLU B1018     -85.677  14.997  91.736  1.00116.95           C  
ANISOU 4520  CB  GLU B1018     8899  17586  17949    586    621   4861       C  
ATOM   4521  CG  GLU B1018     -86.506  14.098  90.829  1.00122.76           C  
ANISOU 4521  CG  GLU B1018     9571  18242  18830    547    548   4920       C  
ATOM   4522  CD  GLU B1018     -86.744  12.724  91.425  1.00129.02           C  
ANISOU 4522  CD  GLU B1018    10269  18932  19821    535    425   5102       C  
ATOM   4523  OE1 GLU B1018     -86.588  12.573  92.653  1.00121.97           O  
ANISOU 4523  OE1 GLU B1018     9382  18045  18916    549    406   5241       O  
ATOM   4524  OE2 GLU B1018     -87.083  11.793  90.664  1.00120.08           O  
ANISOU 4524  OE2 GLU B1018     9053  17711  18860    514    348   5106       O  
ATOM   4525  N   LYS B1019     -86.830  15.786  94.566  1.00110.67           N  
ANISOU 4525  N   LYS B1019     7131  16199  18719    640    317   -445       N  
ATOM   4526  CA  LYS B1019     -87.644  15.436  95.731  1.00116.30           C  
ANISOU 4526  CA  LYS B1019     7934  16813  19442    459    690   -188       C  
ATOM   4527  C   LYS B1019     -87.930  16.712  96.522  1.00111.52           C  
ANISOU 4527  C   LYS B1019     7525  16416  18430    564    970   -124       C  
ATOM   4528  O   LYS B1019     -87.264  17.034  97.505  1.00110.00           O  
ANISOU 4528  O   LYS B1019     7742  16200  17852    598   1015     53       O  
ATOM   4529  CB  LYS B1019     -86.934  14.381  96.576  1.00123.38           C  
ANISOU 4529  CB  LYS B1019     9161  17408  20309    310    621     84       C  
ATOM   4530  CG  LYS B1019     -86.448  13.179  95.777  1.00122.34           C  
ANISOU 4530  CG  LYS B1019     8850  17049  20585    247    262    -26       C  
ATOM   4531  CD  LYS B1019     -85.689  12.196  96.653  1.00136.65           C  
ANISOU 4531  CD  LYS B1019    11035  18524  22361    134    133    245       C  
ATOM   4532  CE  LYS B1019     -85.380  10.911  95.897  1.00144.45           C  
ANISOU 4532  CE  LYS B1019    11788  19247  23847     55   -214    117       C  
ATOM   4533  NZ  LYS B1019     -85.086   9.778  96.817  1.00150.15           N  
ANISOU 4533  NZ  LYS B1019    12828  19564  24660   -112   -271    442       N  
ATOM   4534  N   ALA B1020     -88.945  17.450  96.075  1.00110.80           N  
ANISOU 4534  N   ALA B1020     7125  16527  18446    640   1124   -309       N  
ATOM   4535  CA  ALA B1020     -89.232  18.760  96.639  1.00117.41           C  
ANISOU 4535  CA  ALA B1020     8084  17570  18956    781   1327   -330       C  
ATOM   4536  C   ALA B1020     -90.732  18.978  96.765  1.00139.17           C  
ANISOU 4536  C   ALA B1020    10491  20446  21940    728   1670   -439       C  
ATOM   4537  O   ALA B1020     -91.501  18.608  95.874  1.00140.89           O  
ANISOU 4537  O   ALA B1020    10290  20664  22577    709   1608   -639       O  
ATOM   4538  CB  ALA B1020     -88.616  19.878  95.783  1.00112.96           C  
ANISOU 4538  CB  ALA B1020     7544  17144  18231   1032   1041   -523       C  
ATOM   4539  N   ASP B1021     -91.139  19.581  97.884  1.00148.96           N  
ANISOU 4539  N   ASP B1021    11889  21797  22913    719   2022   -349       N  
ATOM   4540  CA  ASP B1021     -92.495  20.079  98.060  1.00145.28           C  
ANISOU 4540  CA  ASP B1021    11086  21494  22620    716   2354   -526       C  
ATOM   4541  C   ASP B1021     -92.540  21.571  98.347  1.00148.18           C  
ANISOU 4541  C   ASP B1021    11547  22073  22682    963   2376   -673       C  
ATOM   4542  O   ASP B1021     -93.629  22.156  98.320  1.00169.11           O  
ANISOU 4542  O   ASP B1021    13877  24869  25508   1026   2564   -903       O  
ATOM   4543  CB  ASP B1021     -93.212  19.326  99.194  1.00156.46           C  
ANISOU 4543  CB  ASP B1021    12515  22861  24071    431   2865   -324       C  
ATOM   4544  CG  ASP B1021     -92.691  19.702 100.569  1.00158.64           C  
ANISOU 4544  CG  ASP B1021    13297  23202  23777    434   3096    -78       C  
ATOM   4545  OD1 ASP B1021     -93.180  20.697 101.147  1.00186.16           O  
ANISOU 4545  OD1 ASP B1021    16772  26911  27048    549   3337   -209       O  
ATOM   4546  OD2 ASP B1021     -91.791  19.000 101.074  1.00139.34           O  
ANISOU 4546  OD2 ASP B1021    11261  20582  21102    344   3007    218       O  
ATOM   4547  N   ASN B1022     -91.399  22.194  98.624  1.00122.29           N  
ANISOU 4547  N   ASN B1022     8670  18795  19001   1109   2175   -580       N  
ATOM   4548  CA  ASN B1022     -91.295  23.621  98.868  1.00119.11           C  
ANISOU 4548  CA  ASN B1022     8374  18542  18341   1352   2140   -722       C  
ATOM   4549  C   ASN B1022     -90.818  24.322  97.597  1.00117.01           C  
ANISOU 4549  C   ASN B1022     8037  18256  18163   1556   1721   -880       C  
ATOM   4550  O   ASN B1022     -90.525  23.691  96.580  1.00117.25           O  
ANISOU 4550  O   ASN B1022     7959  18196  18396   1517   1476   -885       O  
ATOM   4551  CB  ASN B1022     -90.341  23.878 100.039  1.00126.00           C  
ANISOU 4551  CB  ASN B1022     9729  19407  18739   1383   2188   -542       C  
ATOM   4552  CG  ASN B1022     -90.462  25.280 100.601  1.00136.56           C  
ANISOU 4552  CG  ASN B1022    11143  20908  19836   1606   2252   -711       C  
ATOM   4553  OD1 ASN B1022     -90.049  26.252  99.969  1.00145.18           O  
ANISOU 4553  OD1 ASN B1022    12227  21993  20942   1808   1969   -859       O  
ATOM   4554  ND2 ASN B1022     -91.018  25.389 101.801  1.00145.30           N  
ANISOU 4554  ND2 ASN B1022    12334  22155  20717   1568   2633   -690       N  
ATOM   4555  N   ALA B1023     -90.752  25.651  97.656  1.00120.46           N  
ANISOU 4555  N   ALA B1023     8547  18778  18444   1778   1646  -1012       N  
ATOM   4556  CA  ALA B1023     -90.099  26.439  96.619  1.00100.33           C  
ANISOU 4556  CA  ALA B1023     6055  16179  15886   1959   1282  -1088       C  
ATOM   4557  C   ALA B1023     -88.681  26.839  96.996  1.00 97.88           C  
ANISOU 4557  C   ALA B1023     6134  15781  15274   2000   1138   -971       C  
ATOM   4558  O   ALA B1023     -87.827  26.987  96.112  1.00103.95           O  
ANISOU 4558  O   ALA B1023     6983  16464  16048   2039    871   -961       O  
ATOM   4559  CB  ALA B1023     -90.916  27.700  96.315  1.00106.98           C  
ANISOU 4559  CB  ALA B1023     6723  17106  16817   2186   1237  -1312       C  
ATOM   4560  N   ALA B1024     -88.418  27.006  98.295  1.00106.71           N  
ANISOU 4560  N   ALA B1024     7486  16926  16132   1995   1317   -908       N  
ATOM   4561  CA  ALA B1024     -87.076  27.341  98.751  1.00 92.60           C  
ANISOU 4561  CA  ALA B1024     6046  15043  14095   2052   1156   -848       C  
ATOM   4562  C   ALA B1024     -86.087  26.233  98.432  1.00113.95           C  
ANISOU 4562  C   ALA B1024     8873  17604  16819   1907    985   -710       C  
ATOM   4563  O   ALA B1024     -84.912  26.511  98.183  1.00119.25           O  
ANISOU 4563  O   ALA B1024     9708  18171  17431   1955    753   -733       O  
ATOM   4564  CB  ALA B1024     -87.082  27.625 100.253  1.00 94.90           C  
ANISOU 4564  CB  ALA B1024     6569  15412  14078   2101   1363   -834       C  
ATOM   4565  N   GLN B1025     -86.537  24.978  98.428  1.00131.50           N  
ANISOU 4565  N   GLN B1025    10994  19804  19167   1725   1092   -592       N  
ATOM   4566  CA  GLN B1025     -85.652  23.884  98.042  1.00138.21           C  
ANISOU 4566  CA  GLN B1025    11919  20497  20098   1601    887   -498       C  
ATOM   4567  C   GLN B1025     -85.159  24.063  96.610  1.00138.30           C  
ANISOU 4567  C   GLN B1025    11771  20485  20292   1644    619   -626       C  
ATOM   4568  O   GLN B1025     -83.949  24.021  96.345  1.00138.92           O  
ANISOU 4568  O   GLN B1025    11990  20467  20326   1655    400   -654       O  
ATOM   4569  CB  GLN B1025     -86.376  22.549  98.204  1.00136.29           C  
ANISOU 4569  CB  GLN B1025    11549  20202  20032   1395   1050   -362       C  
ATOM   4570  CG  GLN B1025     -86.674  22.178  99.644  1.00146.38           C  
ANISOU 4570  CG  GLN B1025    13072  21475  21073   1308   1336   -168       C  
ATOM   4571  CD  GLN B1025     -87.620  20.999  99.753  1.00151.01           C  
ANISOU 4571  CD  GLN B1025    13481  22001  21894   1073   1581    -26       C  
ATOM   4572  OE1 GLN B1025     -88.521  20.837  98.934  1.00157.69           O  
ANISOU 4572  OE1 GLN B1025    13931  22895  23091   1018   1643   -151       O  
ATOM   4573  NE2 GLN B1025     -87.420  20.171 100.767  1.00145.18           N  
ANISOU 4573  NE2 GLN B1025    13046  21138  20977    938   1710    231       N  
ATOM   4574  N   VAL B1026     -86.088  24.292  95.678  1.00101.72           N  
ANISOU 4574  N   VAL B1026     6845  15948  15855   1681    635   -727       N  
ATOM   4575  CA  VAL B1026     -85.715  24.493  94.280  1.00 87.87           C  
ANISOU 4575  CA  VAL B1026     4977  14202  14205   1741    399   -834       C  
ATOM   4576  C   VAL B1026     -84.833  25.725  94.132  1.00 92.44           C  
ANISOU 4576  C   VAL B1026     5759  14760  14603   1869    294   -871       C  
ATOM   4577  O   VAL B1026     -83.819  25.695  93.426  1.00100.03           O  
ANISOU 4577  O   VAL B1026     6785  15669  15554   1849    128   -903       O  
ATOM   4578  CB  VAL B1026     -86.975  24.590  93.399  1.00 87.53           C  
ANISOU 4578  CB  VAL B1026     4618  14266  14372   1807    404   -950       C  
ATOM   4579  CG1 VAL B1026     -86.634  25.180  92.039  1.00 86.20           C  
ANISOU 4579  CG1 VAL B1026     4434  14135  14185   1933    170  -1041       C  
ATOM   4580  CG2 VAL B1026     -87.612  23.221  93.239  1.00 93.84           C  
ANISOU 4580  CG2 VAL B1026     5165  15044  15447   1655    443   -958       C  
ATOM   4581  N   LYS B1027     -85.199  26.827  94.793  1.00 88.13           N  
ANISOU 4581  N   LYS B1027     5296  14246  13943   1993    403   -889       N  
ATOM   4582  CA  LYS B1027     -84.425  28.054  94.623  1.00 92.86           C  
ANISOU 4582  CA  LYS B1027     6063  14783  14438   2108    301   -931       C  
ATOM   4583  C   LYS B1027     -83.014  27.914  95.188  1.00100.35           C  
ANISOU 4583  C   LYS B1027     7236  15611  15283   2053    223   -922       C  
ATOM   4584  O   LYS B1027     -82.047  28.369  94.568  1.00107.34           O  
ANISOU 4584  O   LYS B1027     8189  16413  16184   2051    100   -966       O  
ATOM   4585  CB  LYS B1027     -85.143  29.240  95.265  1.00 91.74           C  
ANISOU 4585  CB  LYS B1027     5936  14678  14243   2270    403   -992       C  
ATOM   4586  CG  LYS B1027     -84.559  30.560  94.804  1.00 85.63           C  
ANISOU 4586  CG  LYS B1027     5283  13799  13453   2391    272  -1032       C  
ATOM   4587  CD  LYS B1027     -85.099  31.762  95.542  1.00 87.19           C  
ANISOU 4587  CD  LYS B1027     5507  13993  13627   2566    326  -1128       C  
ATOM   4588  CE  LYS B1027     -84.193  32.954  95.275  1.00 96.45           C  
ANISOU 4588  CE  LYS B1027     6846  14987  14813   2643    191  -1148       C  
ATOM   4589  NZ  LYS B1027     -84.826  34.261  95.582  1.00117.75           N  
ANISOU 4589  NZ  LYS B1027     9531  17638  17570   2842    168  -1255       N  
ATOM   4590  N   ASP B1028     -82.873  27.292  96.363  1.00 94.89           N  
ANISOU 4590  N   ASP B1028     6669  14899  14486   2009    291   -874       N  
ATOM   4591  CA  ASP B1028     -81.555  27.094  96.955  1.00 97.75           C  
ANISOU 4591  CA  ASP B1028     7246  15132  14763   1995    155   -903       C  
ATOM   4592  C   ASP B1028     -80.697  26.176  96.093  1.00 94.49           C  
ANISOU 4592  C   ASP B1028     6765  14641  14495   1870    -18   -931       C  
ATOM   4593  O   ASP B1028     -79.509  26.452  95.864  1.00 85.26           O  
ANISOU 4593  O   ASP B1028     5659  13371  13364   1872   -162  -1046       O  
ATOM   4594  CB  ASP B1028     -81.712  26.526  98.367  1.00 91.49           C  
ANISOU 4594  CB  ASP B1028     6645  14340  13778   1996    243   -817       C  
ATOM   4595  CG  ASP B1028     -80.673  27.058  99.334  1.00 98.59           C  
ANISOU 4595  CG  ASP B1028     7807  15145  14507   2117    115   -914       C  
ATOM   4596  OD1 ASP B1028     -80.469  28.290  99.371  1.00101.72           O  
ANISOU 4596  OD1 ASP B1028     8215  15536  14899   2245     96  -1045       O  
ATOM   4597  OD2 ASP B1028     -80.078  26.247 100.074  1.00 93.45           O  
ANISOU 4597  OD2 ASP B1028     7358  14406  13743   2100      8   -869       O  
ATOM   4598  N   ALA B1029     -81.284  25.082  95.597  1.00 96.49           N  
ANISOU 4598  N   ALA B1029     6856  14935  14869   1761     -4   -864       N  
ATOM   4599  CA  ALA B1029     -80.533  24.181  94.730  1.00 91.66           C  
ANISOU 4599  CA  ALA B1029     6143  14267  14416   1660   -182   -937       C  
ATOM   4600  C   ALA B1029     -80.110  24.881  93.445  1.00 87.18           C  
ANISOU 4600  C   ALA B1029     5473  13756  13896   1680   -234  -1050       C  
ATOM   4601  O   ALA B1029     -78.988  24.687  92.966  1.00 84.98           O  
ANISOU 4601  O   ALA B1029     5189  13419  13679   1628   -358  -1174       O  
ATOM   4602  CB  ALA B1029     -81.363  22.936  94.422  1.00 90.31           C  
ANISOU 4602  CB  ALA B1029     5786  14119  14406   1554   -164   -870       C  
ATOM   4603  N   LEU B1030     -80.993  25.703  92.873  1.00100.62           N  
ANISOU 4603  N   LEU B1030     7101  15564  15566   1759   -138  -1016       N  
ATOM   4604  CA  LEU B1030     -80.644  26.429  91.657  1.00 95.49           C  
ANISOU 4604  CA  LEU B1030     6427  14955  14902   1784   -173  -1067       C  
ATOM   4605  C   LEU B1030     -79.556  27.461  91.919  1.00 91.15           C  
ANISOU 4605  C   LEU B1030     6049  14286  14300   1798   -166  -1111       C  
ATOM   4606  O   LEU B1030     -78.679  27.666  91.075  1.00102.40           O  
ANISOU 4606  O   LEU B1030     7472  15690  15744   1732   -188  -1180       O  
ATOM   4607  CB  LEU B1030     -81.886  27.092  91.062  1.00102.78           C  
ANISOU 4607  CB  LEU B1030     7273  15981  15798   1901   -126  -1013       C  
ATOM   4608  CG  LEU B1030     -82.846  26.138  90.349  1.00101.72           C  
ANISOU 4608  CG  LEU B1030     6906  15967  15775   1895   -177  -1043       C  
ATOM   4609  CD1 LEU B1030     -84.054  26.887  89.813  1.00 96.65           C  
ANISOU 4609  CD1 LEU B1030     6188  15408  15127   2054   -181  -1039       C  
ATOM   4610  CD2 LEU B1030     -82.130  25.397  89.229  1.00116.78           C  
ANISOU 4610  CD2 LEU B1030     8736  17925  17709   1819   -301  -1137       C  
ATOM   4611  N   THR B1031     -79.595  28.122  93.077  1.00 80.44           N  
ANISOU 4611  N   THR B1031     4825  12850  12887   1878   -121  -1095       N  
ATOM   4612  CA  THR B1031     -78.528  29.051  93.435  1.00 81.85           C  
ANISOU 4612  CA  THR B1031     5135  12884  13081   1898   -143  -1185       C  
ATOM   4613  C   THR B1031     -77.186  28.332  93.512  1.00 95.90           C  
ANISOU 4613  C   THR B1031     6910  14572  14956   1793   -258  -1334       C  
ATOM   4614  O   THR B1031     -76.186  28.784  92.934  1.00 91.53           O  
ANISOU 4614  O   THR B1031     6338  13938  14500   1723   -260  -1446       O  
ATOM   4615  CB  THR B1031     -78.854  29.731  94.767  1.00 82.46           C  
ANISOU 4615  CB  THR B1031     5340  12915  13077   2033   -112  -1192       C  
ATOM   4616  OG1 THR B1031     -79.879  30.713  94.568  1.00 82.07           O  
ANISOU 4616  OG1 THR B1031     5271  12912  13001   2145    -27  -1125       O  
ATOM   4617  CG2 THR B1031     -77.617  30.400  95.352  1.00 99.41           C  
ANISOU 4617  CG2 THR B1031     7599  14888  15285   2061   -194  -1349       C  
ATOM   4618  N   LYS B1032     -77.153  27.191  94.207  1.00 93.65           N  
ANISOU 4618  N   LYS B1032     6637  14281  14665   1775   -353  -1344       N  
ATOM   4619  CA  LYS B1032     -75.905  26.443  94.327  1.00 79.89           C  
ANISOU 4619  CA  LYS B1032     4883  12427  13044   1709   -526  -1520       C  
ATOM   4620  C   LYS B1032     -75.422  25.945  92.969  1.00 79.35           C  
ANISOU 4620  C   LYS B1032     4622  12420  13109   1579   -541  -1622       C  
ATOM   4621  O   LYS B1032     -74.222  25.989  92.674  1.00 91.62           O  
ANISOU 4621  O   LYS B1032     6115  13893  14801   1515   -603  -1833       O  
ATOM   4622  CB  LYS B1032     -76.081  25.278  95.300  1.00 86.52           C  
ANISOU 4622  CB  LYS B1032     5816  13220  13838   1727   -651  -1464       C  
ATOM   4623  CG  LYS B1032     -76.504  25.712  96.693  1.00 94.17           C  
ANISOU 4623  CG  LYS B1032     7013  14162  14604   1858   -614  -1371       C  
ATOM   4624  CD  LYS B1032     -76.286  24.616  97.719  1.00 84.38           C  
ANISOU 4624  CD  LYS B1032     5954  12823  13285   1879   -772  -1323       C  
ATOM   4625  CE  LYS B1032     -76.682  25.097  99.102  1.00 84.67           C  
ANISOU 4625  CE  LYS B1032     6256  12872  13044   2023   -709  -1237       C  
ATOM   4626  NZ  LYS B1032     -76.122  26.449  99.380  1.00 84.63           N  
ANISOU 4626  NZ  LYS B1032     6293  12837  13024   2157   -734  -1426       N  
ATOM   4627  N   MET B1033     -76.343  25.466  92.129  1.00 92.64           N  
ANISOU 4627  N   MET B1033     6185  14253  14761   1547   -482  -1513       N  
ATOM   4628  CA  MET B1033     -75.966  24.991  90.801  1.00 87.08           C  
ANISOU 4628  CA  MET B1033     5306  13649  14130   1452   -497  -1629       C  
ATOM   4629  C   MET B1033     -75.431  26.122  89.934  1.00 83.90           C  
ANISOU 4629  C   MET B1033     4928  13273  13677   1415   -351  -1661       C  
ATOM   4630  O   MET B1033     -74.465  25.935  89.185  1.00 95.62           O  
ANISOU 4630  O   MET B1033     6313  14781  15238   1309   -337  -1840       O  
ATOM   4631  CB  MET B1033     -77.162  24.323  90.126  1.00 86.33           C  
ANISOU 4631  CB  MET B1033     5083  13709  14010   1466   -494  -1529       C  
ATOM   4632  CG  MET B1033     -77.423  22.909  90.595  1.00 83.89           C  
ANISOU 4632  CG  MET B1033     4681  13352  13842   1432   -638  -1546       C  
ATOM   4633  SD  MET B1033     -78.932  22.228  89.893  1.00 89.88           S  
ANISOU 4633  SD  MET B1033     5243  14257  14652   1449   -625  -1463       S  
ATOM   4634  CE  MET B1033     -78.788  22.787  88.199  1.00 83.24           C  
ANISOU 4634  CE  MET B1033     4400  13573  13655   1458   -588  -1531       C  
ATOM   4635  N   ARG B1034     -76.053  27.299  90.012  1.00 79.73           N  
ANISOU 4635  N   ARG B1034     4530  12731  13031   1493   -232  -1492       N  
ATOM   4636  CA  ARG B1034     -75.580  28.442  89.243  1.00 88.12           C  
ANISOU 4636  CA  ARG B1034     5667  13762  14052   1448    -87  -1466       C  
ATOM   4637  C   ARG B1034     -74.194  28.868  89.702  1.00101.07           C  
ANISOU 4637  C   ARG B1034     7315  15223  15865   1359    -64  -1653       C  
ATOM   4638  O   ARG B1034     -73.352  29.252  88.883  1.00106.81           O  
ANISOU 4638  O   ARG B1034     8007  15934  16642   1227     70  -1734       O  
ATOM   4639  CB  ARG B1034     -76.569  29.598  89.369  1.00 83.82           C  
ANISOU 4639  CB  ARG B1034     5267  13186  13396   1577    -22  -1258       C  
ATOM   4640  CG  ARG B1034     -76.457  30.626  88.264  1.00 89.52           C  
ANISOU 4640  CG  ARG B1034     6100  13889  14024   1545    107  -1140       C  
ATOM   4641  CD  ARG B1034     -76.173  32.004  88.822  1.00 85.89           C  
ANISOU 4641  CD  ARG B1034     5785  13201  13648   1574    173  -1086       C  
ATOM   4642  NE  ARG B1034     -76.110  33.002  87.763  1.00 96.25           N  
ANISOU 4642  NE  ARG B1034     7249  14448  14872   1532    300   -918       N  
ATOM   4643  CZ  ARG B1034     -75.742  34.262  87.944  1.00105.36           C  
ANISOU 4643  CZ  ARG B1034     8536  15362  16135   1515    380   -850       C  
ATOM   4644  NH1 ARG B1034     -75.393  34.714  89.137  1.00105.40           N  
ANISOU 4644  NH1 ARG B1034     8513  15188  16347   1557    331   -982       N  
ATOM   4645  NH2 ARG B1034     -75.721  35.087  86.902  1.00106.48           N  
ANISOU 4645  NH2 ARG B1034     8857  15428  16173   1462    501   -647       N  
ATOM   4646  N   ALA B1035     -73.940  28.810  91.013  1.00109.32           N  
ANISOU 4646  N   ALA B1035     8402  16132  17002   1433   -187  -1741       N  
ATOM   4647  CA  ALA B1035     -72.606  29.133  91.512  1.00110.10           C  
ANISOU 4647  CA  ALA B1035     8475  16047  17313   1382   -229  -1988       C  
ATOM   4648  C   ALA B1035     -71.556  28.181  90.948  1.00101.72           C  
ANISOU 4648  C   ALA B1035     7222  15013  16414   1247   -284  -2247       C  
ATOM   4649  O   ALA B1035     -70.465  28.609  90.556  1.00110.48           O  
ANISOU 4649  O   ALA B1035     8231  16036  17709   1122   -188  -2452       O  
ATOM   4650  CB  ALA B1035     -72.593  29.100  93.040  1.00118.68           C  
ANISOU 4650  CB  ALA B1035     9670  17010  18413   1534   -411  -2053       C  
ATOM   4651  N   ALA B1036     -71.867  26.885  90.902  1.00 91.82           N  
ANISOU 4651  N   ALA B1036     5893  13866  15131   1262   -435  -2267       N  
ATOM   4652  CA  ALA B1036     -70.925  25.914  90.352  1.00 81.75           C  
ANISOU 4652  CA  ALA B1036     4407  12618  14034   1157   -526  -2554       C  
ATOM   4653  C   ALA B1036     -70.776  26.070  88.844  1.00 83.65           C  
ANISOU 4653  C   ALA B1036     4527  13041  14217   1014   -297  -2577       C  
ATOM   4654  O   ALA B1036     -69.661  25.975  88.314  1.00 96.15           O  
ANISOU 4654  O   ALA B1036     5939  14624  15971    883   -229  -2861       O  
ATOM   4655  CB  ALA B1036     -71.366  24.497  90.701  1.00 81.26           C  
ANISOU 4655  CB  ALA B1036     4307  12585  13984   1218   -769  -2553       C  
ATOM   4656  N   ALA B1037     -71.883  26.308  88.134  1.00 81.77           N  
ANISOU 4656  N   ALA B1037     4374  12966  13728   1046   -177  -2302       N  
ATOM   4657  CA  ALA B1037     -71.821  26.381  86.677  1.00 89.91           C  
ANISOU 4657  CA  ALA B1037     5344  14197  14619    945     12  -2306       C  
ATOM   4658  C   ALA B1037     -70.975  27.551  86.186  1.00102.04           C  
ANISOU 4658  C   ALA B1037     6941  15664  16168    802    293  -2319       C  
ATOM   4659  O   ALA B1037     -70.559  27.553  85.023  1.00128.08           O  
ANISOU 4659  O   ALA B1037    10184  19118  19364    675    491  -2384       O  
ATOM   4660  CB  ALA B1037     -73.230  26.465  86.093  1.00 87.23           C  
ANISOU 4660  CB  ALA B1037     5115  14021  14009   1058     21  -2021       C  
ATOM   4661  N   LEU B1038     -70.717  28.549  87.038  1.00 98.04           N  
ANISOU 4661  N   LEU B1038     6546  14923  15783    815    329  -2264       N  
ATOM   4662  CA  LEU B1038     -69.886  29.679  86.624  1.00100.05           C  
ANISOU 4662  CA  LEU B1038     6837  15050  16126    653    607  -2279       C  
ATOM   4663  C   LEU B1038     -68.496  29.219  86.201  1.00105.39           C  
ANISOU 4663  C   LEU B1038     7257  15745  17042    456    719  -2663       C  
ATOM   4664  O   LEU B1038     -67.934  29.733  85.228  1.00117.98           O  
ANISOU 4664  O   LEU B1038     8839  17386  18601    262   1042  -2668       O  
ATOM   4665  CB  LEU B1038     -69.788  30.704  87.752  1.00 95.11           C  
ANISOU 4665  CB  LEU B1038     6318  14142  15679    722    561  -2240       C  
ATOM   4666  CG  LEU B1038     -71.078  31.387  88.211  1.00 92.75           C  
ANISOU 4666  CG  LEU B1038     6248  13804  15188    910    488  -1910       C  
ATOM   4667  CD1 LEU B1038     -70.824  32.231  89.450  1.00 91.11           C  
ANISOU 4667  CD1 LEU B1038     6091  13333  15192    998    399  -1983       C  
ATOM   4668  CD2 LEU B1038     -71.672  32.232  87.095  1.00 87.74           C  
ANISOU 4668  CD2 LEU B1038     5799  13217  14320    872    698  -1596       C  
ATOM   4669  N   ASP B1039     -67.924  28.260  86.923  1.00 99.43           N  
ANISOU 4669  N   ASP B1039     6302  14943  16535    504    459  -2994       N  
ATOM   4670  CA  ASP B1039     -66.613  27.719  86.579  1.00 89.58           C  
ANISOU 4670  CA  ASP B1039     4757  13708  15572    348    506  -3439       C  
ATOM   4671  C   ASP B1039     -66.696  26.820  85.351  1.00 90.24           C  
ANISOU 4671  C   ASP B1039     4708  14101  15478    275    593  -3522       C  
ATOM   4672  O   ASP B1039     -66.503  25.608  85.446  1.00 89.60           O  
ANISOU 4672  O   ASP B1039     4645  14004  15393    324    327  -3685       O  
ATOM   4673  CB  ASP B1039     -66.031  26.942  87.759  1.00 95.76           C  
ANISOU 4673  CB  ASP B1039     5532  14269  16582    461    115  -3708       C  
ATOM   4674  CG  ASP B1039     -65.938  27.780  89.017  1.00118.41           C  
ANISOU 4674  CG  ASP B1039     8456  16891  19645    579     -9  -3716       C  
ATOM   4675  OD1 ASP B1039     -66.996  28.180  89.548  1.00105.24           O  
ANISOU 4675  OD1 ASP B1039     6989  15223  17775    729    -66  -3388       O  
ATOM   4676  OD2 ASP B1039     -64.806  28.051  89.470  1.00138.49           O  
ANISOU 4676  OD2 ASP B1039    10940  19205  22477    525    -56  -4031       O  
ATOM   4677  N   ASP B1046     -72.384  30.636  79.809  1.00127.79           N  
ANISOU 4677  N   ASP B1046    11226  19628  17701    623   1391  -1198       N  
ATOM   4678  CA  ASP B1046     -73.473  31.605  79.773  1.00126.37           C  
ANISOU 4678  CA  ASP B1046    11374  19316  17325    806   1287   -812       C  
ATOM   4679  C   ASP B1046     -74.764  30.948  79.291  1.00123.96           C  
ANISOU 4679  C   ASP B1046    11091  19247  16762   1080    982   -775       C  
ATOM   4680  O   ASP B1046     -75.848  31.255  79.787  1.00135.02           O  
ANISOU 4680  O   ASP B1046    12563  20543  18195   1292    745   -628       O  
ATOM   4681  CB  ASP B1046     -73.113  32.786  78.870  1.00135.72           C  
ANISOU 4681  CB  ASP B1046    12920  20404  18242    672   1606   -503       C  
ATOM   4682  CG  ASP B1046     -73.396  34.126  79.522  1.00141.04           C  
ANISOU 4682  CG  ASP B1046    13821  20693  19073    705   1598   -213       C  
ATOM   4683  OD1 ASP B1046     -73.667  34.151  80.741  1.00135.10           O  
ANISOU 4683  OD1 ASP B1046    12906  19769  18655    800   1395   -312       O  
ATOM   4684  OD2 ASP B1046     -73.348  35.155  78.815  1.00148.76           O  
ANISOU 4684  OD2 ASP B1046    15155  21535  19834    640   1793    114       O  
ATOM   4685  N   ILE B1047     -74.635  30.046  78.315  1.00107.35           N  
ANISOU 4685  N   ILE B1047     8749  16765  15275  -1655   6187    640       N  
ATOM   4686  CA  ILE B1047     -75.800  29.330  77.799  1.00113.29           C  
ANISOU 4686  CA  ILE B1047     9541  17593  15912  -1654   6222    551       C  
ATOM   4687  C   ILE B1047     -76.446  28.506  78.904  1.00108.19           C  
ANISOU 4687  C   ILE B1047     9017  16730  15359  -1644   6169    370       C  
ATOM   4688  O   ILE B1047     -77.662  28.561  79.121  1.00105.34           O  
ANISOU 4688  O   ILE B1047     8671  16338  15014  -1687   6123    347       O  
ATOM   4689  CB  ILE B1047     -75.399  28.442  76.608  1.00116.47           C  
ANISOU 4689  CB  ILE B1047     9933  18216  16104  -1614   6362    494       C  
ATOM   4690  CG1 ILE B1047     -74.715  29.273  75.522  1.00111.11           C  
ANISOU 4690  CG1 ILE B1047     9108  17804  15304  -1633   6414    696       C  
ATOM   4691  CG2 ILE B1047     -76.615  27.710  76.057  1.00112.70           C  
ANISOU 4691  CG2 ILE B1047     9503  17816  15500  -1661   6415    380       C  
ATOM   4692  CD1 ILE B1047     -74.144  28.442  74.394  1.00113.17           C  
ANISOU 4692  CD1 ILE B1047     9354  18297  15347  -1572   6577    637       C  
ATOM   4693  N   LEU B1048     -75.634  27.724  79.616  1.00106.97           N  
ANISOU 4693  N   LEU B1048     8928  16450  15265  -1592   6178    260       N  
ATOM   4694  CA  LEU B1048     -76.152  26.887  80.690  1.00103.95           C  
ANISOU 4694  CA  LEU B1048     8645  15879  14970  -1596   6135    110       C  
ATOM   4695  C   LEU B1048     -76.716  27.728  81.828  1.00114.18           C  
ANISOU 4695  C   LEU B1048     9940  17041  16400  -1643   6007    154       C  
ATOM   4696  O   LEU B1048     -77.769  27.399  82.387  1.00117.86           O  
ANISOU 4696  O   LEU B1048    10454  17435  16891  -1676   5962     75       O  
ATOM   4697  CB  LEU B1048     -75.046  25.969  81.198  1.00104.03           C  
ANISOU 4697  CB  LEU B1048     8688  15807  15031  -1525   6185     37       C  
ATOM   4698  CG  LEU B1048     -75.459  24.997  82.294  1.00103.06           C  
ANISOU 4698  CG  LEU B1048     8648  15504  15006  -1535   6159    -91       C  
ATOM   4699  CD1 LEU B1048     -76.533  24.073  81.761  1.00108.49           C  
ANISOU 4699  CD1 LEU B1048     9417  16177  15626  -1584   6237   -249       C  
ATOM   4700  CD2 LEU B1048     -74.248  24.222  82.765  1.00103.56           C  
ANISOU 4700  CD2 LEU B1048     8699  15510  15140  -1451   6222   -102       C  
ATOM   4701  N   VAL B1049     -76.024  28.812  82.188  1.00114.60           N  
ANISOU 4701  N   VAL B1049     9938  17064  16541  -1659   5966    267       N  
ATOM   4702  CA  VAL B1049     -76.511  29.691  83.247  1.00117.07           C  
ANISOU 4702  CA  VAL B1049    10258  17232  16992  -1709   5889    275       C  
ATOM   4703  C   VAL B1049     -77.849  30.304  82.855  1.00123.35           C  
ANISOU 4703  C   VAL B1049    11029  18045  17793  -1724   5889    311       C  
ATOM   4704  O   VAL B1049     -78.768  30.400  83.677  1.00142.12           O  
ANISOU 4704  O   VAL B1049    13435  20327  20237  -1735   5847    248       O  
ATOM   4705  CB  VAL B1049     -75.461  30.771  83.571  1.00116.20           C  
ANISOU 4705  CB  VAL B1049    10093  17073  16986  -1757   5884    374       C  
ATOM   4706  CG1 VAL B1049     -76.061  31.854  84.456  1.00138.49           C  
ANISOU 4706  CG1 VAL B1049    12924  19725  19969  -1818   5861    360       C  
ATOM   4707  CG2 VAL B1049     -74.251  30.143  84.245  1.00112.66           C  
ANISOU 4707  CG2 VAL B1049     9638  16631  16535  -1754   5865    351       C  
ATOM   4708  N   GLY B1050     -77.983  30.715  81.591  1.00108.88           N  
ANISOU 4708  N   GLY B1050     9122  16369  15880  -1723   5944    432       N  
ATOM   4709  CA  GLY B1050     -79.237  31.299  81.140  1.00117.36           C  
ANISOU 4709  CA  GLY B1050    10131  17505  16954  -1734   5951    512       C  
ATOM   4710  C   GLY B1050     -80.419  30.362  81.311  1.00132.88           C  
ANISOU 4710  C   GLY B1050    12129  19521  18836  -1739   5923    407       C  
ATOM   4711  O   GLY B1050     -81.499  30.783  81.730  1.00130.23           O  
ANISOU 4711  O   GLY B1050    11760  19154  18567  -1739   5897    425       O  
ATOM   4712  N   GLN B1051     -80.230  29.080  80.988  1.00125.95           N  
ANISOU 4712  N   GLN B1051    11314  18713  17830  -1748   5947    293       N  
ATOM   4713  CA  GLN B1051     -81.283  28.096  81.229  1.00121.33           C  
ANISOU 4713  CA  GLN B1051    10772  18140  17187  -1791   5931    174       C  
ATOM   4714  C   GLN B1051     -81.586  27.965  82.717  1.00116.31           C  
ANISOU 4714  C   GLN B1051    10197  17316  16678  -1787   5851     86       C  
ATOM   4715  O   GLN B1051     -82.752  27.834  83.111  1.00125.01           O  
ANISOU 4715  O   GLN B1051    11280  18440  17780  -1820   5812     68       O  
ATOM   4716  CB  GLN B1051     -80.885  26.741  80.647  1.00110.74           C  
ANISOU 4716  CB  GLN B1051     9509  16838  15728  -1819   6016     27       C  
ATOM   4717  CG  GLN B1051     -81.175  26.550  79.172  1.00133.78           C  
ANISOU 4717  CG  GLN B1051    12373  19998  18458  -1873   6111     53       C  
ATOM   4718  CD  GLN B1051     -80.900  25.126  78.719  1.00136.62           C  
ANISOU 4718  CD  GLN B1051    12844  20350  18716  -1926   6231   -178       C  
ATOM   4719  OE1 GLN B1051     -80.274  24.345  79.437  1.00125.72           O  
ANISOU 4719  OE1 GLN B1051    11563  18773  17434  -1889   6257   -316       O  
ATOM   4720  NE2 GLN B1051     -81.372  24.781  77.527  1.00148.73           N  
ANISOU 4720  NE2 GLN B1051    14355  22104  20052  -2027   6323   -230       N  
ATOM   4721  N   ILE B1052     -80.548  27.980  83.558  1.00120.85           N  
ANISOU 4721  N   ILE B1052    10827  17746  17346  -1758   5829     45       N  
ATOM   4722  CA  ILE B1052     -80.753  27.936  85.004  1.00111.33           C  
ANISOU 4722  CA  ILE B1052     9660  16404  16237  -1770   5760    -23       C  
ATOM   4723  C   ILE B1052     -81.564  29.140  85.458  1.00109.52           C  
ANISOU 4723  C   ILE B1052     9375  16142  16094  -1763   5738     28       C  
ATOM   4724  O   ILE B1052     -82.462  29.024  86.302  1.00119.54           O  
ANISOU 4724  O   ILE B1052    10646  17388  17385  -1777   5700    -26       O  
ATOM   4725  CB  ILE B1052     -79.399  27.865  85.737  1.00120.68           C  
ANISOU 4725  CB  ILE B1052    10873  17494  17485  -1758   5748    -39       C  
ATOM   4726  CG1 ILE B1052     -78.677  26.556  85.421  1.00117.37           C  
ANISOU 4726  CG1 ILE B1052    10495  17086  17013  -1737   5798    -95       C  
ATOM   4727  CG2 ILE B1052     -79.592  28.015  87.237  1.00121.92           C  
ANISOU 4727  CG2 ILE B1052    11044  17560  17720  -1793   5682    -92       C  
ATOM   4728  CD1 ILE B1052     -77.258  26.498  85.934  1.00105.01           C  
ANISOU 4728  CD1 ILE B1052     8911  15488  15499  -1710   5799    -59       C  
ATOM   4729  N   ASP B1053     -81.261  30.315  84.903  1.00105.10           N  
ANISOU 4729  N   ASP B1053     8758  15575  15600  -1741   5783    136       N  
ATOM   4730  CA  ASP B1053     -81.949  31.535  85.309  1.00112.29           C  
ANISOU 4730  CA  ASP B1053     9616  16398  16651  -1721   5813    177       C  
ATOM   4731  C   ASP B1053     -83.430  31.483  84.954  1.00122.23           C  
ANISOU 4731  C   ASP B1053    10797  17783  17861  -1696   5815    226       C  
ATOM   4732  O   ASP B1053     -84.274  31.974  85.713  1.00123.99           O  
ANISOU 4732  O   ASP B1053    10990  17942  18177  -1665   5829    198       O  
ATOM   4733  CB  ASP B1053     -81.274  32.746  84.665  1.00121.83           C  
ANISOU 4733  CB  ASP B1053    10773  17544  17973  -1715   5887    306       C  
ATOM   4734  CG  ASP B1053     -79.788  32.823  84.980  1.00126.65           C  
ANISOU 4734  CG  ASP B1053    11430  18072  18620  -1761   5883    283       C  
ATOM   4735  OD1 ASP B1053     -79.358  32.226  85.989  1.00120.90           O  
ANISOU 4735  OD1 ASP B1053    10764  17296  17878  -1791   5831    163       O  
ATOM   4736  OD2 ASP B1053     -79.049  33.484  84.219  1.00116.66           O  
ANISOU 4736  OD2 ASP B1053    10117  16817  17392  -1777   5931    408       O  
ATOM   4737  N   ASP B1054     -83.767  30.900  83.800  1.00141.98           N  
ANISOU 4737  N   ASP B1054    13249  20488  20210  -1717   5815    299       N  
ATOM   4738  CA  ASP B1054     -85.172  30.735  83.442  1.00131.28           C  
ANISOU 4738  CA  ASP B1054    11792  19311  18778  -1726   5809    363       C  
ATOM   4739  C   ASP B1054     -85.888  29.830  84.436  1.00121.30           C  
ANISOU 4739  C   ASP B1054    10575  18033  17481  -1759   5747    237       C  
ATOM   4740  O   ASP B1054     -87.021  30.113  84.843  1.00127.10           O  
ANISOU 4740  O   ASP B1054    11223  18829  18240  -1737   5740    272       O  
ATOM   4741  CB  ASP B1054     -85.289  30.176  82.025  1.00147.06           C  
ANISOU 4741  CB  ASP B1054    13727  21558  20590  -1787   5831    448       C  
ATOM   4742  CG  ASP B1054     -84.420  30.921  81.034  1.00166.70           C  
ANISOU 4742  CG  ASP B1054    16168  24095  23075  -1771   5889    577       C  
ATOM   4743  OD1 ASP B1054     -84.216  32.138  81.221  1.00173.84           O  
ANISOU 4743  OD1 ASP B1054    17032  24870  24150  -1716   5923    672       O  
ATOM   4744  OD2 ASP B1054     -83.931  30.287  80.076  1.00166.20           O  
ANISOU 4744  OD2 ASP B1054    16111  24183  22852  -1818   5921    578       O  
ATOM   4745  N   ALA B1055     -85.242  28.731  84.837  1.00101.05           N  
ANISOU 4745  N   ALA B1055     8130  15396  14869  -1809   5713    104       N  
ATOM   4746  CA  ALA B1055     -85.793  27.892  85.895  1.00 99.96           C  
ANISOU 4746  CA  ALA B1055     8035  15222  14722  -1854   5658      0       C  
ATOM   4747  C   ALA B1055     -85.882  28.660  87.205  1.00102.90           C  
ANISOU 4747  C   ALA B1055     8407  15477  15211  -1803   5640    -36       C  
ATOM   4748  O   ALA B1055     -86.857  28.521  87.954  1.00119.44           O  
ANISOU 4748  O   ALA B1055    10460  17623  17299  -1812   5613    -55       O  
ATOM   4749  CB  ALA B1055     -84.943  26.635  86.068  1.00 99.27           C  
ANISOU 4749  CB  ALA B1055     8065  15050  14603  -1911   5653   -117       C  
ATOM   4750  N   LEU B1056     -84.865  29.473  87.501  1.00 99.99           N  
ANISOU 4750  N   LEU B1056     8078  14965  14948  -1765   5670    -51       N  
ATOM   4751  CA  LEU B1056     -84.901  30.300  88.700  1.00100.94           C  
ANISOU 4751  CA  LEU B1056     8201  14964  15186  -1743   5692   -119       C  
ATOM   4752  C   LEU B1056     -86.021  31.328  88.634  1.00100.67           C  
ANISOU 4752  C   LEU B1056     8064  14945  15239  -1668   5765    -66       C  
ATOM   4753  O   LEU B1056     -86.607  31.672  89.667  1.00101.01           O  
ANISOU 4753  O   LEU B1056     8088  14950  15339  -1645   5794   -145       O  
ATOM   4754  CB  LEU B1056     -83.552  30.991  88.895  1.00100.29           C  
ANISOU 4754  CB  LEU B1056     8169  14730  15206  -1756   5727   -144       C  
ATOM   4755  CG  LEU B1056     -83.292  31.595  90.272  1.00 99.59           C  
ANISOU 4755  CG  LEU B1056     8105  14518  15215  -1792   5757   -264       C  
ATOM   4756  CD1 LEU B1056     -83.716  30.616  91.345  1.00125.51           C  
ANISOU 4756  CD1 LEU B1056    11405  17889  18396  -1834   5682   -343       C  
ATOM   4757  CD2 LEU B1056     -81.824  31.913  90.398  1.00 99.59           C  
ANISOU 4757  CD2 LEU B1056     8144  14428  15269  -1854   5767   -274       C  
ATOM   4758  N   LYS B1057     -86.320  31.839  87.438  1.00101.68           N  
ANISOU 4758  N   LYS B1057     8109  15142  15383  -1623   5810     77       N  
ATOM   4759  CA  LYS B1057     -87.474  32.716  87.275  1.00103.26           C  
ANISOU 4759  CA  LYS B1057     8175  15382  15675  -1532   5889    173       C  
ATOM   4760  C   LYS B1057     -88.759  31.996  87.662  1.00111.50           C  
ANISOU 4760  C   LYS B1057     9143  16624  16599  -1540   5834    170       C  
ATOM   4761  O   LYS B1057     -89.588  32.535  88.403  1.00113.03           O  
ANISOU 4761  O   LYS B1057     9267  16803  16877  -1463   5894    146       O  
ATOM   4762  CB  LYS B1057     -87.561  33.218  85.834  1.00104.54           C  
ANISOU 4762  CB  LYS B1057     8233  15644  15842  -1504   5932    373       C  
ATOM   4763  CG  LYS B1057     -86.967  34.595  85.598  1.00105.84           C  
ANISOU 4763  CG  LYS B1057     8384  15583  16246  -1435   6058    454       C  
ATOM   4764  CD  LYS B1057     -87.579  35.237  84.358  1.00109.96           C  
ANISOU 4764  CD  LYS B1057     8740  16231  16807  -1371   6118    710       C  
ATOM   4765  CE  LYS B1057     -86.519  35.638  83.343  1.00116.55           C  
ANISOU 4765  CE  LYS B1057     9584  17039  17661  -1410   6142    841       C  
ATOM   4766  NZ  LYS B1057     -87.122  36.278  82.138  1.00110.53           N  
ANISOU 4766  NZ  LYS B1057     8644  16422  16931  -1355   6197   1130       N  
ATOM   4767  N   LEU B1058     -88.932  30.764  87.177  1.00103.15           N  
ANISOU 4767  N   LEU B1058     8093  15744  15355  -1638   5740    189       N  
ATOM   4768  CA  LEU B1058     -90.143  30.006  87.478  1.00102.81           C  
ANISOU 4768  CA  LEU B1058     7965  15897  15200  -1683   5688    210       C  
ATOM   4769  C   LEU B1058     -90.294  29.771  88.975  1.00102.13           C  
ANISOU 4769  C   LEU B1058     7933  15732  15140  -1682   5665     80       C  
ATOM   4770  O   LEU B1058     -91.398  29.884  89.520  1.00132.87           O  
ANISOU 4770  O   LEU B1058    11713  19750  19019  -1647   5676    109       O  
ATOM   4771  CB  LEU B1058     -90.126  28.676  86.726  1.00102.43           C  
ANISOU 4771  CB  LEU B1058     7950  15975  14992  -1822   5623    220       C  
ATOM   4772  CG  LEU B1058     -90.772  28.604  85.340  1.00103.88           C  
ANISOU 4772  CG  LEU B1058     7996  16406  15067  -1874   5638    378       C  
ATOM   4773  CD1 LEU B1058     -90.468  29.835  84.496  1.00104.92           C  
ANISOU 4773  CD1 LEU B1058     8044  16557  15263  -1781   5708    506       C  
ATOM   4774  CD2 LEU B1058     -90.302  27.347  84.630  1.00103.60           C  
ANISOU 4774  CD2 LEU B1058     8065  16384  14914  -2023   5623    298       C  
ATOM   4775  N   ALA B1059     -89.196  29.436  89.656  1.00100.86           N  
ANISOU 4775  N   ALA B1059     7919  15401  15001  -1725   5637    -48       N  
ATOM   4776  CA  ALA B1059     -89.259  29.188  91.094  1.00100.44           C  
ANISOU 4776  CA  ALA B1059     7900  15314  14947  -1748   5615   -157       C  
ATOM   4777  C   ALA B1059     -89.609  30.458  91.862  1.00101.57           C  
ANISOU 4777  C   ALA B1059     7993  15387  15211  -1646   5722   -219       C  
ATOM   4778  O   ALA B1059     -90.463  30.438  92.757  1.00112.61           O  
ANISOU 4778  O   ALA B1059     9324  16882  16579  -1627   5738   -253       O  
ATOM   4779  CB  ALA B1059     -87.932  28.611  91.584  1.00 99.20           C  
ANISOU 4779  CB  ALA B1059     7878  15026  14788  -1821   5569   -246       C  
ATOM   4780  N   ASN B1060     -88.952  31.572  91.531  1.00102.13           N  
ANISOU 4780  N   ASN B1060     8092  15278  15435  -1584   5819   -240       N  
ATOM   4781  CA  ASN B1060     -89.200  32.821  92.247  1.00103.67           C  
ANISOU 4781  CA  ASN B1060     8257  15334  15800  -1496   5972   -336       C  
ATOM   4782  C   ASN B1060     -90.625  33.314  92.029  1.00105.40           C  
ANISOU 4782  C   ASN B1060     8315  15671  16063  -1362   6054   -242       C  
ATOM   4783  O   ASN B1060     -91.262  33.823  92.959  1.00106.72           O  
ANISOU 4783  O   ASN B1060     8432  15825  16292  -1289   6159   -341       O  
ATOM   4784  CB  ASN B1060     -88.187  33.882  91.815  1.00114.77           C  
ANISOU 4784  CB  ASN B1060     9721  16486  17400  -1480   6078   -355       C  
ATOM   4785  CG  ASN B1060     -86.842  33.715  92.499  1.00103.28           C  
ANISOU 4785  CG  ASN B1060     8392  14916  15935  -1608   6044   -491       C  
ATOM   4786  OD1 ASN B1060     -86.365  34.620  93.183  1.00104.37           O  
ANISOU 4786  OD1 ASN B1060     8565  14868  16221  -1637   6170   -632       O  
ATOM   4787  ND2 ASN B1060     -86.232  32.549  92.328  1.00101.57           N  
ANISOU 4787  ND2 ASN B1060     8230  14809  15553  -1692   5892   -449       N  
ATOM   4788  N   GLU B1061     -91.140  33.183  90.803  1.00116.39           N  
ANISOU 4788  N   GLU B1061     9604  17205  17414  -1330   6018    -49       N  
ATOM   4789  CA  GLU B1061     -92.527  33.558  90.544  1.00125.50           C  
ANISOU 4789  CA  GLU B1061    10563  18533  18587  -1211   6079     83       C  
ATOM   4790  C   GLU B1061     -93.489  32.682  91.337  1.00112.39           C  
ANISOU 4790  C   GLU B1061     8830  17123  16750  -1255   6001     63       C  
ATOM   4791  O   GLU B1061     -94.509  33.167  91.843  1.00127.52           O  
ANISOU 4791  O   GLU B1061    10610  19133  18710  -1136   6093     75       O  
ATOM   4792  CB  GLU B1061     -92.824  33.488  89.045  1.00126.45           C  
ANISOU 4792  CB  GLU B1061    10570  18820  18657  -1218   6039    307       C  
ATOM   4793  CG  GLU B1061     -92.003  34.470  88.219  1.00114.28           C  
ANISOU 4793  CG  GLU B1061     9060  17055  17305  -1157   6133    385       C  
ATOM   4794  CD  GLU B1061     -92.413  34.503  86.761  1.00135.18           C  
ANISOU 4794  CD  GLU B1061    11559  19912  19891  -1161   6109    631       C  
ATOM   4795  OE1 GLU B1061     -93.434  35.149  86.446  1.00161.99           O  
ANISOU 4795  OE1 GLU B1061    14765  23399  23384  -1031   6189    802       O  
ATOM   4796  OE2 GLU B1061     -91.719  33.878  85.931  1.00130.88           O  
ANISOU 4796  OE2 GLU B1061    11076  19454  19199  -1290   6019    659       O  
ATOM   4797  N   GLY B1062     -93.185  31.392  91.463  1.00105.67           N  
ANISOU 4797  N   GLY B1062     8060  16370  15719  -1416   5849     45       N  
ATOM   4798  CA  GLY B1062     -93.916  30.569  92.405  1.00105.58           C  
ANISOU 4798  CA  GLY B1062     8002  16535  15577  -1475   5787     29       C  
ATOM   4799  C   GLY B1062     -94.239  29.147  91.992  1.00110.82           C  
ANISOU 4799  C   GLY B1062     8652  17376  16078  -1637   5647    134       C  
ATOM   4800  O   GLY B1062     -94.360  28.275  92.857  1.00133.98           O  
ANISOU 4800  O   GLY B1062    11618  20351  18938  -1730   5583     98       O  
ATOM   4801  N   LYS B1063     -94.387  28.887  90.695  1.00104.96           N  
ANISOU 4801  N   LYS B1063     7858  16729  15292  -1687   5614    262       N  
ATOM   4802  CA  LYS B1063     -94.844  27.571  90.247  1.00121.43           C  
ANISOU 4802  CA  LYS B1063     9922  18959  17257  -1860   5520    347       C  
ATOM   4803  C   LYS B1063     -93.723  26.554  90.421  1.00115.52           C  
ANISOU 4803  C   LYS B1063     9387  18009  16497  -1992   5461    206       C  
ATOM   4804  O   LYS B1063     -92.812  26.459  89.596  1.00110.79           O  
ANISOU 4804  O   LYS B1063     8893  17293  15910  -2018   5467    163       O  
ATOM   4805  CB  LYS B1063     -95.330  27.628  88.802  1.00107.94           C  
ANISOU 4805  CB  LYS B1063     8085  17430  15498  -1896   5526    515       C  
ATOM   4806  CG  LYS B1063     -94.592  28.598  87.899  1.00106.12           C  
ANISOU 4806  CG  LYS B1063     7873  17120  15326  -1804   5586    525       C  
ATOM   4807  CD  LYS B1063     -95.230  28.604  86.518  1.00107.74           C  
ANISOU 4807  CD  LYS B1063     7901  17591  15443  -1862   5590    730       C  
ATOM   4808  CE  LYS B1063     -94.668  29.702  85.635  1.00113.03           C  
ANISOU 4808  CE  LYS B1063     8542  18236  16168  -1774   5658    770       C  
ATOM   4809  NZ  LYS B1063     -95.333  29.720  84.302  1.00116.64           N  
ANISOU 4809  NZ  LYS B1063     8793  19036  16490  -1869   5655    966       N  
ATOM   4810  N   VAL B1064     -93.794  25.785  91.510  1.00131.44           N  
ANISOU 4810  N   VAL B1064     8998  20600  20341    303   2345   -258       N  
ATOM   4811  CA  VAL B1064     -92.794  24.755  91.773  1.00120.07           C  
ANISOU 4811  CA  VAL B1064     7602  19201  18819    306   2427   -168       C  
ATOM   4812  C   VAL B1064     -92.947  23.593  90.798  1.00118.61           C  
ANISOU 4812  C   VAL B1064     7385  18960  18720    249   2386   -234       C  
ATOM   4813  O   VAL B1064     -91.954  23.034  90.316  1.00119.25           O  
ANISOU 4813  O   VAL B1064     7523  19038  18749    263   2365   -196       O  
ATOM   4814  CB  VAL B1064     -92.890  24.281  93.234  1.00128.48           C  
ANISOU 4814  CB  VAL B1064     8638  20364  19813    311   2608    -85       C  
ATOM   4815  CG1 VAL B1064     -91.768  23.303  93.552  1.00 99.89           C  
ANISOU 4815  CG1 VAL B1064     5106  16771  16075    322   2683     -9       C  
ATOM   4816  CG2 VAL B1064     -92.857  25.470  94.180  1.00140.98           C  
ANISOU 4816  CG2 VAL B1064    10262  21962  21341    375   2638    -44       C  
ATOM   4817  N   LYS B1065     -94.190  23.207  90.497  1.00130.61           N  
ANISOU 4817  N   LYS B1065     8812  20420  20392    186   2375   -335       N  
ATOM   4818  CA  LYS B1065     -94.435  22.059  89.630  1.00131.30           C  
ANISOU 4818  CA  LYS B1065     8858  20423  20609    130   2343   -409       C  
ATOM   4819  C   LYS B1065     -93.878  22.258  88.226  1.00124.51           C  
ANISOU 4819  C   LYS B1065     8045  19505  19761    166   2177   -460       C  
ATOM   4820  O   LYS B1065     -93.633  21.271  87.524  1.00121.20           O  
ANISOU 4820  O   LYS B1065     7616  19029  19405    144   2150   -495       O  
ATOM   4821  CB  LYS B1065     -95.937  21.771  89.555  1.00145.19           C  
ANISOU 4821  CB  LYS B1065    10501  22103  22561     61   2352   -514       C  
ATOM   4822  CG  LYS B1065     -96.585  21.474  90.899  1.00154.18           C  
ANISOU 4822  CG  LYS B1065    11580  23294  23708     23   2526   -466       C  
ATOM   4823  CD  LYS B1065     -96.040  20.192  91.510  1.00150.87           C  
ANISOU 4823  CD  LYS B1065    11168  22895  23262    -11   2673   -395       C  
ATOM   4824  CE  LYS B1065     -96.348  18.987  90.635  1.00163.00           C  
ANISOU 4824  CE  LYS B1065    12652  24288  24993    -81   2648   -473       C  
ATOM   4825  NZ  LYS B1065     -95.818  17.723  91.218  1.00169.70           N  
ANISOU 4825  NZ  LYS B1065    13511  25132  25834   -117   2799   -404       N  
ATOM   4826  N   GLU B1066     -93.668  23.504  87.805  1.00119.67           N  
ANISOU 4826  N   GLU B1066     7480  18900  19092    223   2070   -468       N  
ATOM   4827  CA  GLU B1066     -93.156  23.784  86.470  1.00115.37           C  
ANISOU 4827  CA  GLU B1066     6978  18309  18548    268   1918   -514       C  
ATOM   4828  C   GLU B1066     -91.634  23.801  86.412  1.00108.63           C  
ANISOU 4828  C   GLU B1066     6225  17499  17550    320   1921   -405       C  
ATOM   4829  O   GLU B1066     -91.060  23.514  85.355  1.00113.28           O  
ANISOU 4829  O   GLU B1066     6844  18057  18141    350   1828   -426       O  
ATOM   4830  CB  GLU B1066     -93.708  25.124  85.970  1.00119.40           C  
ANISOU 4830  CB  GLU B1066     7488  18799  19081    306   1803   -583       C  
ATOM   4831  CG  GLU B1066     -93.384  25.434  84.518  1.00100.26           C  
ANISOU 4831  CG  GLU B1066     5093  16329  16670    361   1644   -646       C  
ATOM   4832  CD  GLU B1066     -93.910  24.378  83.567  1.00123.01           C  
ANISOU 4832  CD  GLU B1066     7911  19143  19685    339   1580   -753       C  
ATOM   4833  OE1 GLU B1066     -95.062  23.931  83.750  1.00163.30           O  
ANISOU 4833  OE1 GLU B1066    12922  24200  24923    282   1605   -837       O  
ATOM   4834  OE2 GLU B1066     -93.167  23.989  82.642  1.00 96.97           O  
ANISOU 4834  OE2 GLU B1066     4650  15831  16365    381   1504   -756       O  
ATOM   4835  N   ALA B1067     -90.966  24.118  87.524  1.00116.85           N  
ANISOU 4835  N   ALA B1067     7317  18607  18475    338   2025   -290       N  
ATOM   4836  CA  ALA B1067     -89.511  24.215  87.521  1.00110.76           C  
ANISOU 4836  CA  ALA B1067     6641  17856  17589    390   2032   -186       C  
ATOM   4837  C   ALA B1067     -88.829  22.870  87.303  1.00112.45           C  
ANISOU 4837  C   ALA B1067     6865  18081  17779    380   2075   -149       C  
ATOM   4838  O   ALA B1067     -87.651  22.843  86.929  1.00111.08           O  
ANISOU 4838  O   ALA B1067     6764  17899  17541    425   2051    -83       O  
ATOM   4839  CB  ALA B1067     -89.025  24.837  88.832  1.00 92.01           C  
ANISOU 4839  CB  ALA B1067     4309  15521  15131    417   2140    -84       C  
ATOM   4840  N   GLN B1068     -89.536  21.759  87.529  1.00114.21           N  
ANISOU 4840  N   GLN B1068     7017  18308  18071    319   2143   -196       N  
ATOM   4841  CA  GLN B1068     -88.923  20.442  87.378  1.00104.60           C  
ANISOU 4841  CA  GLN B1068     5806  17098  16841    305   2192   -175       C  
ATOM   4842  C   GLN B1068     -88.502  20.184  85.936  1.00100.61           C  
ANISOU 4842  C   GLN B1068     5316  16530  16382    334   2054   -231       C  
ATOM   4843  O   GLN B1068     -87.416  19.647  85.685  1.00108.61           O  
ANISOU 4843  O   GLN B1068     6382  17563  17321    369   2060   -171       O  
ATOM   4844  CB  GLN B1068     -89.893  19.357  87.847  1.00109.23           C  
ANISOU 4844  CB  GLN B1068     6304  17657  17543    223   2293   -234       C  
ATOM   4845  CG  GLN B1068     -90.838  19.799  88.952  1.00111.35           C  
ANISOU 4845  CG  GLN B1068     6523  17960  17827    190   2390   -229       C  
ATOM   4846  CD  GLN B1068     -90.131  20.046  90.268  1.00104.34           C  
ANISOU 4846  CD  GLN B1068     5687  17198  16759    230   2519   -106       C  
ATOM   4847  OE1 GLN B1068     -89.486  19.153  90.817  1.00 98.42           O  
ANISOU 4847  OE1 GLN B1068     4961  16509  15925    227   2627    -56       O  
ATOM   4848  NE2 GLN B1068     -90.249  21.264  90.783  1.00107.08           N  
ANISOU 4848  NE2 GLN B1068     6053  17580  17053    273   2508    -67       N  
ATOM   4849  N   ALA B1069     -89.352  20.556  84.975  1.00 95.97           N  
ANISOU 4849  N   ALA B1069     4681  15871  15914    331   1927   -349       N  
ATOM   4850  CA  ALA B1069     -89.062  20.280  83.571  1.00 97.35           C  
ANISOU 4850  CA  ALA B1069     4859  15992  16136    373   1790   -417       C  
ATOM   4851  C   ALA B1069     -87.802  20.999  83.114  1.00117.76           C  
ANISOU 4851  C   ALA B1069     7540  18612  18590    455   1730   -331       C  
ATOM   4852  O   ALA B1069     -87.007  20.448  82.344  1.00127.19           O  
ANISOU 4852  O   ALA B1069     8764  19798  19763    498   1680   -322       O  
ATOM   4853  CB  ALA B1069     -90.250  20.681  82.699  1.00 97.43           C  
ANISOU 4853  CB  ALA B1069     4801  15930  16289    370   1665   -561       C  
ATOM   4854  N   ALA B1070     -87.609  22.238  83.569  1.00115.57           N  
ANISOU 4854  N   ALA B1070     7311  18358  18243    478   1735   -273       N  
ATOM   4855  CA  ALA B1070     -86.387  22.960  83.236  1.00112.14           C  
ANISOU 4855  CA  ALA B1070     6967  17918  17723    543   1696   -191       C  
ATOM   4856  C   ALA B1070     -85.162  22.262  83.813  1.00100.28           C  
ANISOU 4856  C   ALA B1070     5531  16421  16150    551   1799    -78       C  
ATOM   4857  O   ALA B1070     -84.109  22.210  83.169  1.00107.75           O  
ANISOU 4857  O   ALA B1070     6551  17318  17071    597   1754    -54       O  
ATOM   4858  CB  ALA B1070     -86.475  24.400  83.736  1.00103.11           C  
ANISOU 4858  CB  ALA B1070     5854  16770  16554    554   1694   -168       C  
ATOM   4859  N   ALA B1071     -85.283  21.714  85.025  1.00 99.38           N  
ANISOU 4859  N   ALA B1071     5423  16335  16001    507   1932    -33       N  
ATOM   4860  CA  ALA B1071     -84.142  21.078  85.678  1.00 98.90           C  
ANISOU 4860  CA  ALA B1071     5466  16235  15876    516   2034     54       C  
ATOM   4861  C   ALA B1071     -83.647  19.865  84.896  1.00103.85           C  
ANISOU 4861  C   ALA B1071     6084  16866  16507    529   2012     46       C  
ATOM   4862  O   ALA B1071     -82.435  19.672  84.740  1.00103.55           O  
ANISOU 4862  O   ALA B1071     6143  16728  16474    560   2028     75       O  
ATOM   4863  CB  ALA B1071     -84.512  20.682  87.105  1.00 89.62           C  
ANISOU 4863  CB  ALA B1071     4286  15111  14654    479   2183    103       C  
ATOM   4864  N   GLU B1072     -84.567  19.033  84.400  1.00107.54           N  
ANISOU 4864  N   GLU B1072     6426  17401  17034    497   1982    -37       N  
ATOM   4865  CA  GLU B1072     -84.162  17.812  83.706  1.00117.55           C  
ANISOU 4865  CA  GLU B1072     7666  18672  18325    510   1964    -64       C  
ATOM   4866  C   GLU B1072     -83.465  18.126  82.387  1.00117.29           C  
ANISOU 4866  C   GLU B1072     7672  18587  18307    586   1826    -78       C  
ATOM   4867  O   GLU B1072     -82.399  17.573  82.090  1.00117.20           O  
ANISOU 4867  O   GLU B1072     7731  18537  18263    626   1832    -39       O  
ATOM   4868  CB  GLU B1072     -85.375  16.911  83.474  1.00127.37           C  
ANISOU 4868  CB  GLU B1072     8794  19885  19716    443   1958   -198       C  
ATOM   4869  CG  GLU B1072     -85.067  15.640  82.688  1.00157.45           C  
ANISOU 4869  CG  GLU B1072    12576  23648  23598    454   1924   -256       C  
ATOM   4870  CD  GLU B1072     -84.227  14.644  83.471  1.00153.67           C  
ANISOU 4870  CD  GLU B1072    12129  23227  23032    443   2067   -175       C  
ATOM   4871  OE1 GLU B1072     -84.212  14.722  84.717  1.00162.41           O  
ANISOU 4871  OE1 GLU B1072    13254  24405  24049    408   2205   -109       O  
ATOM   4872  OE2 GLU B1072     -83.581  13.782  82.837  1.00143.74           O  
ANISOU 4872  OE2 GLU B1072    10877  21949  21787    479   2038   -188       O  
ATOM   4873  N   GLN B1073     -84.055  19.009  81.575  1.00109.20           N  
ANISOU 4873  N   GLN B1073     6620  17540  17331    609   1699   -154       N  
ATOM   4874  CA  GLN B1073     -83.404  19.406  80.331  1.00108.34           C  
ANISOU 4874  CA  GLN B1073     6553  17396  17215    692   1570   -174       C  
ATOM   4875  C   GLN B1073     -82.118  20.175  80.601  1.00100.01           C  
ANISOU 4875  C   GLN B1073     5614  16282  16102    722   1606    -90       C  
ATOM   4876  O   GLN B1073     -81.190  20.140  79.785  1.00 91.43           O  
ANISOU 4876  O   GLN B1073     4576  15163  15001    781   1545   -109       O  
ATOM   4877  CB  GLN B1073     -84.357  20.236  79.469  1.00118.48           C  
ANISOU 4877  CB  GLN B1073     7797  18667  18555    716   1434   -282       C  
ATOM   4878  CG  GLN B1073     -84.746  21.582  80.061  1.00111.13           C  
ANISOU 4878  CG  GLN B1073     6884  17737  17605    695   1453   -255       C  
ATOM   4879  CD  GLN B1073     -85.639  22.389  79.136  1.00108.18           C  
ANISOU 4879  CD  GLN B1073     6471  17345  17287    730   1319   -362       C  
ATOM   4880  OE1 GLN B1073     -86.347  21.833  78.296  1.00101.57           O  
ANISOU 4880  OE1 GLN B1073     5572  16486  16533    748   1229   -479       O  
ATOM   4881  NE2 GLN B1073     -85.604  23.709  79.282  1.00107.10           N  
ANISOU 4881  NE2 GLN B1073     6370  17206  17117    747   1305   -331       N  
ATOM   4882  N   LEU B1074     -82.050  20.876  81.735  1.00103.60           N  
ANISOU 4882  N   LEU B1074     6125  16708  16530    678   1698    -47       N  
ATOM   4883  CA  LEU B1074     -80.791  21.470  82.168  1.00 85.65           C  
ANISOU 4883  CA  LEU B1074     3965  14354  14222    682   1743    -52       C  
ATOM   4884  C   LEU B1074     -79.752  20.397  82.455  1.00 88.91           C  
ANISOU 4884  C   LEU B1074     4431  14749  14602    676   1822    -79       C  
ATOM   4885  O   LEU B1074     -78.566  20.571  82.151  1.00 95.22           O  
ANISOU 4885  O   LEU B1074     5291  15572  15316    708   1798   -122       O  
ATOM   4886  CB  LEU B1074     -81.023  22.333  83.406  1.00 93.96           C  
ANISOU 4886  CB  LEU B1074     5047  15390  15265    639   1826    -30       C  
ATOM   4887  CG  LEU B1074     -81.242  23.817  83.138  1.00105.02           C  
ANISOU 4887  CG  LEU B1074     6447  16792  16662    659   1746    -40       C  
ATOM   4888  CD1 LEU B1074     -81.997  24.479  84.278  1.00115.50           C  
ANISOU 4888  CD1 LEU B1074     7757  18139  17990    622   1812    -13       C  
ATOM   4889  CD2 LEU B1074     -79.890  24.449  82.958  1.00103.59           C  
ANISOU 4889  CD2 LEU B1074     6350  16579  16431    682   1727    -82       C  
ATOM   4890  N   LYS B1075     -80.181  19.279  83.044  1.00 91.36           N  
ANISOU 4890  N   LYS B1075     4709  15060  14944    640   1916    -44       N  
ATOM   4891  CA  LYS B1075     -79.252  18.211  83.395  1.00 91.09           C  
ANISOU 4891  CA  LYS B1075     4717  15024  14867    632   2003    -89       C  
ATOM   4892  C   LYS B1075     -78.577  17.628  82.158  1.00 86.61           C  
ANISOU 4892  C   LYS B1075     4141  14503  14264    696   1903   -119       C  
ATOM   4893  O   LYS B1075     -77.374  17.345  82.176  1.00 98.84           O  
ANISOU 4893  O   LYS B1075     5775  16121  15657    724   1913   -135       O  
ATOM   4894  CB  LYS B1075     -79.992  17.124  84.176  1.00 89.52           C  
ANISOU 4894  CB  LYS B1075     4475  14805  14736    585   2126    -33       C  
ATOM   4895  CG  LYS B1075     -79.248  15.809  84.299  1.00 91.81           C  
ANISOU 4895  CG  LYS B1075     4780  15108  14995    577   2202   -105       C  
ATOM   4896  CD  LYS B1075     -79.900  14.738  83.443  1.00103.33           C  
ANISOU 4896  CD  LYS B1075     6145  16591  16526    605   2148     -1       C  
ATOM   4897  CE  LYS B1075     -79.185  13.410  83.591  1.00 95.14           C  
ANISOU 4897  CE  LYS B1075     5117  15549  15483    585   2230   -136       C  
ATOM   4898  NZ  LYS B1075     -79.145  12.973  85.013  1.00 97.07           N  
ANISOU 4898  NZ  LYS B1075     5385  15876  15621    506   2397   -242       N  
ATOM   4899  N   THR B1076     -79.334  17.442  81.074  1.00 89.92           N  
ANISOU 4899  N   THR B1076     4480  14928  14756    733   1789   -100       N  
ATOM   4900  CA  THR B1076     -78.760  16.869  79.859  1.00 92.50           C  
ANISOU 4900  CA  THR B1076     4798  15298  15049    810   1683   -140       C  
ATOM   4901  C   THR B1076     -77.679  17.774  79.277  1.00 88.54           C  
ANISOU 4901  C   THR B1076     4410  14840  14392    868   1595   -166       C  
ATOM   4902  O   THR B1076     -76.597  17.306  78.900  1.00 89.98           O  
ANISOU 4902  O   THR B1076     4669  15095  14424    920   1569   -158       O  
ATOM   4903  CB  THR B1076     -79.860  16.616  78.829  1.00100.93           C  
ANISOU 4903  CB  THR B1076     5756  16399  16195    847   1560   -151       C  
ATOM   4904  OG1 THR B1076     -80.331  17.868  78.314  1.00117.39           O  
ANISOU 4904  OG1 THR B1076     7841  18482  18278    871   1461   -174       O  
ATOM   4905  CG2 THR B1076     -81.022  15.872  79.469  1.00108.78           C  
ANISOU 4905  CG2 THR B1076     6644  17442  17245    778   1629   -137       C  
ATOM   4906  N   THR B1077     -77.955  19.078  79.197  1.00 84.44           N  
ANISOU 4906  N   THR B1077     3900  14294  13888    865   1550   -166       N  
ATOM   4907  CA  THR B1077     -76.946  20.020  78.720  1.00 83.48           C  
ANISOU 4907  CA  THR B1077     3877  14216  13625    914   1483   -166       C  
ATOM   4908  C   THR B1077     -75.788  20.137  79.700  1.00 86.26           C  
ANISOU 4908  C   THR B1077     4337  14613  13823    883   1575   -133       C  
ATOM   4909  O   THR B1077     -74.646  20.364  79.285  1.00 99.39           O  
ANISOU 4909  O   THR B1077     6089  16347  15327    934   1532    -99       O  
ATOM   4910  CB  THR B1077     -77.569  21.391  78.470  1.00 83.47           C  
ANISOU 4910  CB  THR B1077     3848  14170  13694    916   1427   -173       C  
ATOM   4911  OG1 THR B1077     -78.195  21.858  79.673  1.00114.61           O  
ANISOU 4911  OG1 THR B1077     7766  18062  17718    836   1525   -156       O  
ATOM   4912  CG2 THR B1077     -78.612  21.310  77.361  1.00 95.76           C  
ANISOU 4912  CG2 THR B1077     5314  15720  15350    971   1313   -194       C  
ATOM   4913  N   ILE B1078     -76.066  19.996  80.999  1.00 91.44           N  
ANISOU 4913  N   ILE B1078     4985  15239  14517    810   1699   -131       N  
ATOM   4914  CA  ILE B1078     -74.999  19.992  81.997  1.00 84.79           C  
ANISOU 4914  CA  ILE B1078     4244  14455  13517    793   1785    -98       C  
ATOM   4915  C   ILE B1078     -74.047  18.831  81.746  1.00 82.24           C  
ANISOU 4915  C   ILE B1078     3980  14217  13048    838   1792    -53       C  
ATOM   4916  O   ILE B1078     -72.821  18.988  81.786  1.00 89.17           O  
ANISOU 4916  O   ILE B1078     4959  15171  13750    873   1782     -1       O  
ATOM   4917  CB  ILE B1078     -75.592  19.936  83.418  1.00 88.54           C  
ANISOU 4917  CB  ILE B1078     4692  14889  14060    723   1919   -108       C  
ATOM   4918  CG1 ILE B1078     -75.996  21.333  83.890  1.00 99.56           C  
ANISOU 4918  CG1 ILE B1078     6077  16235  15517    697   1915   -124       C  
ATOM   4919  CG2 ILE B1078     -74.612  19.292  84.391  1.00 82.78           C  
ANISOU 4919  CG2 ILE B1078     4050  14238  13165    724   2019    -68       C  
ATOM   4920  CD1 ILE B1078     -76.863  21.338  85.132  1.00106.05           C  
ANISOU 4920  CD1 ILE B1078     6849  17009  16435    642   2034   -130       C  
ATOM   4921  N   ASN B1079     -74.601  17.646  81.478  1.00 97.21           N  
ANISOU 4921  N   ASN B1079     5808  16101  15024    840   1809    -65       N  
ATOM   4922  CA  ASN B1079     -73.769  16.466  81.263  1.00103.83           C  
ANISOU 4922  CA  ASN B1079     6696  17020  15736    889   1821    -14       C  
ATOM   4923  C   ASN B1079     -72.866  16.635  80.046  1.00111.59           C  
ANISOU 4923  C   ASN B1079     7740  18072  16589    980   1694     20       C  
ATOM   4924  O   ASN B1079     -71.688  16.262  80.080  1.00102.47           O  
ANISOU 4924  O   ASN B1079     6680  17001  15252   1026   1703     90       O  
ATOM   4925  CB  ASN B1079     -74.651  15.227  81.109  1.00104.80           C  
ANISOU 4925  CB  ASN B1079     6708  17104  16005    875   1855    -44       C  
ATOM   4926  CG  ASN B1079     -75.292  14.800  82.416  1.00107.57           C  
ANISOU 4926  CG  ASN B1079     7016  17409  16446    791   2014    -53       C  
ATOM   4927  OD1 ASN B1079     -75.425  15.595  83.346  1.00111.86           O  
ANISOU 4927  OD1 ASN B1079     7586  17929  16987    744   2080    -59       O  
ATOM   4928  ND2 ASN B1079     -75.686  13.534  82.494  1.00100.03           N  
ANISOU 4928  ND2 ASN B1079     5990  16444  15573    779   2079    -56       N  
ATOM   4929  N   ALA B1080     -73.402  17.196  78.961  1.00118.65           N  
ANISOU 4929  N   ALA B1080     8580  18933  17567   1017   1577    -24       N  
ATOM   4930  CA  ALA B1080     -72.626  17.329  77.732  1.00112.65           C  
ANISOU 4930  CA  ALA B1080     7874  18243  16688   1118   1459      8       C  
ATOM   4931  C   ALA B1080     -71.476  18.317  77.898  1.00100.74           C  
ANISOU 4931  C   ALA B1080     6475  16782  15021   1128   1459     68       C  
ATOM   4932  O   ALA B1080     -70.331  18.016  77.538  1.00100.47           O  
ANISOU 4932  O   ALA B1080     6524  16832  14817   1191   1437    138       O  
ATOM   4933  CB  ALA B1080     -73.539  17.756  76.585  1.00114.24           C  
ANISOU 4933  CB  ALA B1080     7991  18400  17015   1165   1338    -54       C  
ATOM   4934  N   TYR B1081     -71.762  19.505  78.435  1.00 86.43           N  
ANISOU 4934  N   TYR B1081     4656  14915  13270   1069   1482     42       N  
ATOM   4935  CA  TYR B1081     -70.731  20.533  78.559  1.00 85.35           C  
ANISOU 4935  CA  TYR B1081     4602  14811  13017   1075   1477     87       C  
ATOM   4936  C   TYR B1081     -69.621  20.097  79.508  1.00 88.13           C  
ANISOU 4936  C   TYR B1081     5042  15228  13215   1059   1559    145       C  
ATOM   4937  O   TYR B1081     -68.432  20.224  79.191  1.00109.37           O  
ANISOU 4937  O   TYR B1081     7811  17989  15756   1107   1534    209       O  
ATOM   4938  CB  TYR B1081     -71.351  21.850  79.030  1.00 84.69           C  
ANISOU 4938  CB  TYR B1081     4479  14649  13051   1015   1488     38       C  
ATOM   4939  CG  TYR B1081     -70.356  22.790  79.678  1.00 84.27           C  
ANISOU 4939  CG  TYR B1081     4494  14617  12908    991   1521     69       C  
ATOM   4940  CD1 TYR B1081     -69.512  23.581  78.908  1.00 97.43           C  
ANISOU 4940  CD1 TYR B1081     6202  16316  14502   1039   1459    111       C  
ATOM   4941  CD2 TYR B1081     -70.259  22.884  81.061  1.00 79.49           C  
ANISOU 4941  CD2 TYR B1081     3906  14001  12296    928   1615     57       C  
ATOM   4942  CE1 TYR B1081     -68.599  24.439  79.499  1.00 89.90           C  
ANISOU 4942  CE1 TYR B1081     5294  15376  13490   1013   1488    133       C  
ATOM   4943  CE2 TYR B1081     -69.351  23.736  81.658  1.00 82.22           C  
ANISOU 4943  CE2 TYR B1081     4302  14368  12570    913   1635     75       C  
ATOM   4944  CZ  TYR B1081     -68.524  24.512  80.874  1.00 83.44           C  
ANISOU 4944  CZ  TYR B1081     4486  14546  12672    951   1570    109       C  
ATOM   4945  OH  TYR B1081     -67.620  25.362  81.471  1.00 78.48           O  
ANISOU 4945  OH  TYR B1081     3892  13932  11996    932   1590    120       O  
ATOM   4946  N   ILE B1082     -69.992  19.588  80.685  1.00 79.90           N  
ANISOU 4946  N   ILE B1082     3986  14166  12206   1000   1661    127       N  
ATOM   4947  CA  ILE B1082     -68.994  19.207  81.681  1.00 79.62           C  
ANISOU 4947  CA  ILE B1082     4034  14196  12023    994   1742    178       C  
ATOM   4948  C   ILE B1082     -68.119  18.076  81.158  1.00 92.34           C  
ANISOU 4948  C   ILE B1082     5702  15895  13487   1066   1726    249       C  
ATOM   4949  O   ILE B1082     -66.900  18.065  81.369  1.00 94.10           O  
ANISOU 4949  O   ILE B1082     6013  16194  13547   1098   1734    309       O  
ATOM   4950  CB  ILE B1082     -69.681  18.830  83.007  1.00 80.17           C  
ANISOU 4950  CB  ILE B1082     4072  14231  12158    931   1861    148       C  
ATOM   4951  CG1 ILE B1082     -70.360  20.055  83.622  1.00 80.28           C  
ANISOU 4951  CG1 ILE B1082     4043  14172  12289    872   1876     88       C  
ATOM   4952  CG2 ILE B1082     -68.676  18.234  83.982  1.00 82.65           C  
ANISOU 4952  CG2 ILE B1082     4472  14627  12304    947   1943    206       C  
ATOM   4953  CD1 ILE B1082     -69.397  21.134  84.064  1.00 79.74           C  
ANISOU 4953  CD1 ILE B1082     4036  14134  12128    874   1864    100       C  
ATOM   4954  N   GLN B1083     -68.725  17.106  80.468  1.00103.34           N  
ANISOU 4954  N   GLN B1083     7042  17281  14943   1096   1700    240       N  
ATOM   4955  CA  GLN B1083     -67.955  16.000  79.908  1.00119.57           C  
ANISOU 4955  CA  GLN B1083     9144  19418  16868   1176   1678    305       C  
ATOM   4956  C   GLN B1083     -66.930  16.493  78.894  1.00111.16           C  
ANISOU 4956  C   GLN B1083     8146  18418  15672   1253   1581    356       C  
ATOM   4957  O   GLN B1083     -65.785  16.024  78.881  1.00111.99           O  
ANISOU 4957  O   GLN B1083     8334  18609  15608   1306   1587    430       O  
ATOM   4958  CB  GLN B1083     -68.896  14.980  79.267  1.00128.38           C  
ANISOU 4958  CB  GLN B1083    10168  20504  18106   1199   1652    269       C  
ATOM   4959  CG  GLN B1083     -68.205  13.910  78.428  1.00139.60           C  
ANISOU 4959  CG  GLN B1083    11622  22006  19412   1301   1601    323       C  
ATOM   4960  CD  GLN B1083     -67.590  12.797  79.260  1.00129.95           C  
ANISOU 4960  CD  GLN B1083    10451  20839  18083   1309   1704    389       C  
ATOM   4961  OE1 GLN B1083     -67.099  13.023  80.367  1.00105.21           O  
ANISOU 4961  OE1 GLN B1083     7382  17723  14871   1266   1795    422       O  
ATOM   4962  NE2 GLN B1083     -67.620  11.581  78.727  1.00130.94           N  
ANISOU 4962  NE2 GLN B1083    10549  20995  18209   1374   1687    406       N  
ATOM   4963  N   LYS B1084     -67.323  17.433  78.031  1.00100.13           N  
ANISOU 4963  N   LYS B1084     6712  16982  14350   1266   1496    323       N  
ATOM   4964  CA  LYS B1084     -66.388  17.977  77.050  1.00 90.22           C  
ANISOU 4964  CA  LYS B1084     5515  15786  12980   1342   1416    380       C  
ATOM   4965  C   LYS B1084     -65.242  18.715  77.729  1.00 89.91           C  
ANISOU 4965  C   LYS B1084     5554  15781  12827   1313   1459    428       C  
ATOM   4966  O   LYS B1084     -64.073  18.538  77.366  1.00103.79           O  
ANISOU 4966  O   LYS B1084     7385  17621  14431   1374   1441    503       O  
ATOM   4967  CB  LYS B1084     -67.127  18.901  76.079  1.00 94.46           C  
ANISOU 4967  CB  LYS B1084     5991  16269  13629   1364   1330    336       C  
ATOM   4968  CG  LYS B1084     -66.216  19.749  75.194  1.00 96.51           C  
ANISOU 4968  CG  LYS B1084     6306  16577  13788   1432   1269    400       C  
ATOM   4969  CD  LYS B1084     -66.083  21.176  75.721  1.00101.26           C  
ANISOU 4969  CD  LYS B1084     6906  17127  14442   1361   1300    389       C  
ATOM   4970  CE  LYS B1084     -64.973  21.933  75.011  1.00 93.50           C  
ANISOU 4970  CE  LYS B1084     5976  16195  13353   1418   1267    469       C  
ATOM   4971  NZ  LYS B1084     -64.776  23.294  75.585  1.00 79.96           N  
ANISOU 4971  NZ  LYS B1084     4250  14428  11703   1346   1301    453       N  
ATOM   4972  N   TYR B1085     -65.561  19.557  78.716  1.00 78.12           N  
ANISOU 4972  N   TYR B1085     4040  14227  11415   1226   1514    381       N  
ATOM   4973  CA  TYR B1085     -64.536  20.368  79.365  1.00 90.21           C  
ANISOU 4973  CA  TYR B1085     5626  15784  12866   1200   1544    407       C  
ATOM   4974  C   TYR B1085     -63.511  19.493  80.078  1.00 95.85           C  
ANISOU 4974  C   TYR B1085     6417  16583  13417   1220   1599    461       C  
ATOM   4975  O   TYR B1085     -62.304  19.757  80.014  1.00 92.89           O  
ANISOU 4975  O   TYR B1085     6103  16272  12920   1249   1588    513       O  
ATOM   4976  CB  TYR B1085     -65.192  21.348  80.340  1.00 90.67           C  
ANISOU 4976  CB  TYR B1085     5638  15761  13052   1113   1588    334       C  
ATOM   4977  CG  TYR B1085     -64.308  22.501  80.772  1.00107.51           C  
ANISOU 4977  CG  TYR B1085     7796  17898  15153   1089   1593    339       C  
ATOM   4978  CD1 TYR B1085     -64.240  23.670  80.023  1.00106.17           C  
ANISOU 4978  CD1 TYR B1085     7599  17692  15049   1093   1538    338       C  
ATOM   4979  CD2 TYR B1085     -63.555  22.426  81.937  1.00104.06           C  
ANISOU 4979  CD2 TYR B1085     7403  17505  14631   1068   1654    343       C  
ATOM   4980  CE1 TYR B1085     -63.438  24.730  80.418  1.00109.17           C  
ANISOU 4980  CE1 TYR B1085     7986  18068  15425   1068   1546    338       C  
ATOM   4981  CE2 TYR B1085     -62.751  23.480  82.339  1.00 92.66           C  
ANISOU 4981  CE2 TYR B1085     5966  16063  13176   1048   1653    335       C  
ATOM   4982  CZ  TYR B1085     -62.696  24.628  81.577  1.00 91.80           C  
ANISOU 4982  CZ  TYR B1085     5821  15907  13150   1043   1600    332       C  
ATOM   4983  OH  TYR B1085     -61.897  25.677  81.975  1.00 87.00           O  
ANISOU 4983  OH  TYR B1085     5205  15295  12555   1020   1602    321       O  
ATOM   4984  N   GLY B1086     -63.972  18.442  80.760  1.00 95.90           N  
ANISOU 4984  N   GLY B1086     6418  16595  13426   1207   1664    450       N  
ATOM   4985  CA  GLY B1086     -63.046  17.529  81.412  1.00 85.46           C  
ANISOU 4985  CA  GLY B1086     5169  15359  11943   1240   1719    506       C  
ATOM   4986  C   GLY B1086     -62.214  16.724  80.434  1.00 91.22           C  
ANISOU 4986  C   GLY B1086     5950  16172  12536   1332   1666    582       C  
ATOM   4987  O   GLY B1086     -61.020  16.505  80.657  1.00 92.04           O  
ANISOU 4987  O   GLY B1086     6129  16360  12481   1372   1676    639       O  
ATOM   4988  N   GLN B 313     -62.835  16.262  79.344  1.00111.64           N  
ANISOU 4988  N   GLN B 313     8494  18742  15182   1376   1606    579       N  
ATOM   4989  CA  GLN B 313     -62.106  15.509  78.327  1.00109.09           C  
ANISOU 4989  CA  GLN B 313     8216  18502  14732   1480   1547    646       C  
ATOM   4990  C   GLN B 313     -60.953  16.322  77.757  1.00 99.24           C  
ANISOU 4990  C   GLN B 313     7027  17307  13372   1520   1496    702       C  
ATOM   4991  O   GLN B 313     -59.918  15.757  77.382  1.00111.43           O  
ANISOU 4991  O   GLN B 313     8638  18943  14758   1597   1478    773       O  
ATOM   4992  CB  GLN B 313     -63.059  15.080  77.210  1.00118.91           C  
ANISOU 4992  CB  GLN B 313     9389  19712  16078   1529   1474    614       C  
ATOM   4993  CG  GLN B 313     -62.466  14.110  76.193  1.00114.32           C  
ANISOU 4993  CG  GLN B 313     8845  19217  15375   1652   1412    671       C  
ATOM   4994  CD  GLN B 313     -62.849  12.668  76.468  1.00129.67           C  
ANISOU 4994  CD  GLN B 313    10763  21172  17333   1676   1451    666       C  
ATOM   4995  OE1 GLN B 313     -63.424  12.355  77.509  1.00160.40           O  
ANISOU 4995  OE1 GLN B 313    14621  25016  21307   1598   1543    636       O  
ATOM   4996  NE2 GLN B 313     -62.537  11.782  75.528  1.00130.73           N  
ANISOU 4996  NE2 GLN B 313    10911  21368  17391   1791   1385    696       N  
ATOM   4997  N   SER B 314     -61.109  17.646  77.691  1.00 89.11           N  
ANISOU 4997  N   SER B 314     5715  15968  12175   1470   1477    671       N  
ATOM   4998  CA  SER B 314     -60.035  18.498  77.190  1.00 89.83           C  
ANISOU 4998  CA  SER B 314     5847  16098  12185   1498   1443    726       C  
ATOM   4999  C   SER B 314     -58.887  18.594  78.189  1.00 86.45           C  
ANISOU 4999  C   SER B 314     5477  15723  11646   1471   1497    751       C  
ATOM   5000  O   SER B 314     -57.715  18.606  77.796  1.00 89.68           O  
ANISOU 5000  O   SER B 314     5939  16207  11926   1524   1477    819       O  
ATOM   5001  CB  SER B 314     -60.583  19.887  76.864  1.00 78.78           C  
ANISOU 5001  CB  SER B 314     4390  14616  10927   1453   1415    686       C  
ATOM   5002  OG  SER B 314     -61.698  19.801  75.993  1.00 88.49           O  
ANISOU 5002  OG  SER B 314     5561  15800  12260   1484   1361    653       O  
ATOM   5003  N   ILE B 315     -59.204  18.670  79.484  1.00 80.81           N  
ANISOU 5003  N   ILE B 315     4750  14975  10978   1398   1564    694       N  
ATOM   5004  CA  ILE B 315     -58.162  18.797  80.500  1.00 82.75           C  
ANISOU 5004  CA  ILE B 315     5044  15276  11123   1383   1608    703       C  
ATOM   5005  C   ILE B 315     -57.322  17.527  80.569  1.00 76.93           C  
ANISOU 5005  C   ILE B 315     4380  14646  10205   1457   1623    769       C  
ATOM   5006  O   ILE B 315     -56.101  17.581  80.767  1.00 89.03           O  
ANISOU 5006  O   ILE B 315     5964  16254  11610   1487   1622    807       O  
ATOM   5007  CB  ILE B 315     -58.789  19.141  81.863  1.00 98.40           C  
ANISOU 5007  CB  ILE B 315     6993  17205  13191   1305   1675    625       C  
ATOM   5008  CG1 ILE B 315     -59.665  20.391  81.745  1.00101.64           C  
ANISOU 5008  CG1 ILE B 315     7327  17508  13783   1239   1655    559       C  
ATOM   5009  CG2 ILE B 315     -57.707  19.355  82.909  1.00 97.78           C  
ANISOU 5009  CG2 ILE B 315     6954  17190  13007   1303   1710    623       C  
ATOM   5010  CD1 ILE B 315     -60.362  20.772  83.033  1.00100.43           C  
ANISOU 5010  CD1 ILE B 315     7136  17303  13719   1171   1717    482       C  
ATOM   5011  N   SER B 316     -57.958  16.364  80.410  1.00 77.94           N  
ANISOU 5011  N   SER B 316     4508  14780  10326   1491   1638    780       N  
ATOM   5012  CA  SER B 316     -57.208  15.113  80.386  1.00 76.57           C  
ANISOU 5012  CA  SER B 316     4402  14705   9986   1573   1652    846       C  
ATOM   5013  C   SER B 316     -56.271  15.060  79.185  1.00 76.60           C  
ANISOU 5013  C   SER B 316     4448  14779   9878   1657   1578    917       C  
ATOM   5014  O   SER B 316     -55.143  14.568  79.291  1.00 82.43           O  
ANISOU 5014  O   SER B 316     5254  15614  10453   1716   1581    973       O  
ATOM   5015  CB  SER B 316     -58.166  13.923  80.377  1.00 86.41           C  
ANISOU 5015  CB  SER B 316     5622  15930  11281   1592   1684    840       C  
ATOM   5016  OG  SER B 316     -57.454  12.699  80.433  1.00 83.64           O  
ANISOU 5016  OG  SER B 316     5335  15671  10774   1674   1705    904       O  
ATOM   5017  N   ASN B 317     -56.720  15.559  78.032  1.00 76.33           N  
ANISOU 5017  N   ASN B 317     4374  14705   9923   1674   1512    918       N  
ATOM   5018  CA  ASN B 317     -55.842  15.624  76.867  1.00 76.21           C  
ANISOU 5018  CA  ASN B 317     4397  14758   9801   1761   1448    992       C  
ATOM   5019  C   ASN B 317     -54.682  16.587  77.100  1.00 79.45           C  
ANISOU 5019  C   ASN B 317     4834  15198  10154   1737   1454   1021       C  
ATOM   5020  O   ASN B 317     -53.546  16.311  76.690  1.00 82.41           O  
ANISOU 5020  O   ASN B 317     5265  15664  10382   1806   1436   1092       O  
ATOM   5021  CB  ASN B 317     -56.644  16.026  75.631  1.00 76.39           C  
ANISOU 5021  CB  ASN B 317     4369  14732   9924   1793   1380    985       C  
ATOM   5022  CG  ASN B 317     -57.698  14.998  75.262  1.00 76.74           C  
ANISOU 5022  CG  ASN B 317     4376  14755  10025   1834   1358    951       C  
ATOM   5023  OD1 ASN B 317     -57.943  14.050  76.008  1.00 76.87           O  
ANISOU 5023  OD1 ASN B 317     4396  14778  10033   1821   1408    932       O  
ATOM   5024  ND2 ASN B 317     -58.329  15.184  74.108  1.00 77.00           N  
ANISOU 5024  ND2 ASN B 317     4368  14764  10122   1889   1284    941       N  
ATOM   5025  N   GLU B 318     -54.950  17.722  77.753  1.00 82.43           N  
ANISOU 5025  N   GLU B 318     5165  15500  10654   1641   1479    962       N  
ATOM   5026  CA  GLU B 318     -53.879  18.654  78.098  1.00 75.90           C  
ANISOU 5026  CA  GLU B 318     4345  14692   9802   1611   1489    971       C  
ATOM   5027  C   GLU B 318     -52.838  17.983  78.982  1.00 75.84           C  
ANISOU 5027  C   GLU B 318     4397  14777   9641   1633   1523    987       C  
ATOM   5028  O   GLU B 318     -51.630  18.096  78.739  1.00 96.93           O  
ANISOU 5028  O   GLU B 318     7100  17520  12207   1672   1508   1038       O  
ATOM   5029  CB  GLU B 318     -54.454  19.886  78.803  1.00 88.47           C  
ANISOU 5029  CB  GLU B 318     5869  16182  11563   1508   1513    888       C  
ATOM   5030  CG  GLU B 318     -55.275  20.817  77.925  1.00 98.47           C  
ANISOU 5030  CG  GLU B 318     7074  17361  12979   1488   1478    876       C  
ATOM   5031  CD  GLU B 318     -55.818  22.010  78.696  1.00110.26           C  
ANISOU 5031  CD  GLU B 318     8500  18756  14636   1390   1503    790       C  
ATOM   5032  OE1 GLU B 318     -56.038  21.884  79.920  1.00 99.00           O  
ANISOU 5032  OE1 GLU B 318     7071  17319  13228   1340   1547    726       O  
ATOM   5033  OE2 GLU B 318     -56.019  23.078  78.079  1.00120.10           O  
ANISOU 5033  OE2 GLU B 318     9698  19943  15992   1372   1480    790       O  
ATOM   5034  N   GLN B 319     -53.290  17.267  80.014  1.00 75.89           N  
ANISOU 5034  N   GLN B 319     4416  14787   9633   1615   1570    945       N  
ATOM   5035  CA  GLN B 319     -52.341  16.615  80.908  1.00 75.92           C  
ANISOU 5035  CA  GLN B 319     4478  14886   9484   1649   1604    959       C  
ATOM   5036  C   GLN B 319     -51.619  15.464  80.216  1.00 84.86           C  
ANISOU 5036  C   GLN B 319     5679  16120  10443   1755   1580   1044       C  
ATOM   5037  O   GLN B 319     -50.453  15.206  80.519  1.00 95.03           O  
ANISOU 5037  O   GLN B 319     7016  17501  11589   1799   1582   1076       O  
ATOM   5038  CB  GLN B 319     -53.042  16.141  82.185  1.00 76.13           C  
ANISOU 5038  CB  GLN B 319     4501  14894   9533   1615   1672    903       C  
ATOM   5039  CG  GLN B 319     -53.783  14.824  82.075  1.00 86.10           C  
ANISOU 5039  CG  GLN B 319     5784  16162  10770   1658   1700    930       C  
ATOM   5040  CD  GLN B 319     -54.460  14.434  83.373  1.00 92.36           C  
ANISOU 5040  CD  GLN B 319     6568  16931  11593   1624   1784    885       C  
ATOM   5041  OE1 GLN B 319     -54.455  15.195  84.341  1.00 76.98           O  
ANISOU 5041  OE1 GLN B 319     4599  14965   9685   1571   1814    828       O  
ATOM   5042  NE2 GLN B 319     -55.046  13.243  83.400  1.00108.84           N  
ANISOU 5042  NE2 GLN B 319     8667  19021  13665   1660   1827    913       N  
ATOM   5043  N   LYS B 320     -52.275  14.782  79.274  1.00 75.87           N  
ANISOU 5043  N   LYS B 320     4540  14969   9317   1804   1553   1077       N  
ATOM   5044  CA  LYS B 320     -51.602  13.740  78.501  1.00 79.59           C  
ANISOU 5044  CA  LYS B 320     5073  15538   9629   1918   1522   1156       C  
ATOM   5045  C   LYS B 320     -50.483  14.324  77.647  1.00 83.25           C  
ANISOU 5045  C   LYS B 320     5559  16059  10015   1961   1473   1217       C  
ATOM   5046  O   LYS B 320     -49.371  13.777  77.597  1.00 77.20           O  
ANISOU 5046  O   LYS B 320     4853  15397   9083   2032   1466   1272       O  
ATOM   5047  CB  LYS B 320     -52.621  13.007  77.629  1.00 77.19           C  
ANISOU 5047  CB  LYS B 320     4746  15202   9381   1964   1494   1162       C  
ATOM   5048  CG  LYS B 320     -52.027  12.062  76.599  1.00 91.09           C  
ANISOU 5048  CG  LYS B 320     6559  17055  10996   2095   1444   1236       C  
ATOM   5049  CD  LYS B 320     -51.526  10.776  77.235  1.00116.38           C  
ANISOU 5049  CD  LYS B 320     9824  20340  14056   2158   1484   1264       C  
ATOM   5050  CE  LYS B 320     -51.046   9.793  76.176  1.00117.72           C  
ANISOU 5050  CE  LYS B 320    10042  20596  14091   2297   1431   1329       C  
ATOM   5051  NZ  LYS B 320     -50.634   8.490  76.767  1.00124.04           N  
ANISOU 5051  NZ  LYS B 320    10900  21469  14761   2367   1472   1356       N  
ATOM   5052  N   ALA B 321     -50.761  15.439  76.967  1.00 83.33           N  
ANISOU 5052  N   ALA B 321     5517  16002  10142   1921   1444   1212       N  
ATOM   5053  CA  ALA B 321     -49.718  16.114  76.202  1.00 75.79           C  
ANISOU 5053  CA  ALA B 321     4572  15091   9134   1954   1416   1277       C  
ATOM   5054  C   ALA B 321     -48.587  16.569  77.113  1.00 76.13           C  
ANISOU 5054  C   ALA B 321     4623  15174   9128   1913   1445   1263       C  
ATOM   5055  O   ALA B 321     -47.407  16.474  76.750  1.00 91.15           O  
ANISOU 5055  O   ALA B 321     6561  17164  10909   1970   1432   1326       O  
ATOM   5056  CB  ALA B 321     -50.306  17.299  75.438  1.00 75.91           C  
ANISOU 5056  CB  ALA B 321     4522  15017   9303   1915   1394   1273       C  
ATOM   5057  N   CYS B 322     -48.930  17.062  78.305  1.00 83.28           N  
ANISOU 5057  N   CYS B 322     5493  16023  10127   1822   1484   1177       N  
ATOM   5058  CA  CYS B 322     -47.904  17.455  79.264  1.00 87.00           C  
ANISOU 5058  CA  CYS B 322     5963  16539  10555   1792   1507   1146       C  
ATOM   5059  C   CYS B 322     -47.046  16.266  79.677  1.00 97.76           C  
ANISOU 5059  C   CYS B 322     7403  18027  11715   1874   1513   1180       C  
ATOM   5060  O   CYS B 322     -45.826  16.392  79.797  1.00102.51           O  
ANISOU 5060  O   CYS B 322     8019  18705  12224   1900   1505   1200       O  
ATOM   5061  CB  CYS B 322     -48.542  18.108  80.488  1.00 85.54           C  
ANISOU 5061  CB  CYS B 322     5726  16278  10498   1698   1544   1041       C  
ATOM   5062  SG  CYS B 322     -49.001  19.837  80.242  1.00119.60           S  
ANISOU 5062  SG  CYS B 322     9941  20462  15041   1599   1539    990       S  
ATOM   5063  N   LYS B 323     -47.665  15.103  79.900  1.00 89.20           N  
ANISOU 5063  N   LYS B 323     6362  16962  10567   1918   1529   1186       N  
ATOM   5064  CA  LYS B 323     -46.892  13.917  80.264  1.00 87.35           C  
ANISOU 5064  CA  LYS B 323     6204  16846  10139   2007   1537   1225       C  
ATOM   5065  C   LYS B 323     -45.943  13.513  79.142  1.00 83.75           C  
ANISOU 5065  C   LYS B 323     5794  16478   9550   2102   1490   1315       C  
ATOM   5066  O   LYS B 323     -44.785  13.160  79.395  1.00 78.36           O  
ANISOU 5066  O   LYS B 323     5156  15899   8719   2157   1485   1343       O  
ATOM   5067  CB  LYS B 323     -47.819  12.750  80.612  1.00 84.52           C  
ANISOU 5067  CB  LYS B 323     5875  16478   9762   2038   1573   1222       C  
ATOM   5068  CG  LYS B 323     -48.822  13.018  81.723  1.00 82.70           C  
ANISOU 5068  CG  LYS B 323     5603  16166   9655   1955   1630   1143       C  
ATOM   5069  CD  LYS B 323     -48.215  13.759  82.903  1.00 90.01           C  
ANISOU 5069  CD  LYS B 323     6513  17113  10573   1910   1654   1082       C  
ATOM   5070  CE  LYS B 323     -49.293  14.124  83.916  1.00 76.42           C  
ANISOU 5070  CE  LYS B 323     4747  15309   8981   1833   1708   1005       C  
ATOM   5071  NZ  LYS B 323     -48.771  14.945  85.043  1.00 76.67           N  
ANISOU 5071  NZ  LYS B 323     4752  15362   9017   1796   1724    933       N  
ATOM   5072  N   VAL B 324     -46.418  13.552  77.895  1.00 84.89           N  
ANISOU 5072  N   VAL B 324     5928  16589   9738   2131   1455   1362       N  
ATOM   5073  CA  VAL B 324     -45.562  13.179  76.768  1.00 75.86           C  
ANISOU 5073  CA  VAL B 324     4828  15535   8461   2234   1411   1453       C  
ATOM   5074  C   VAL B 324     -44.382  14.140  76.652  1.00 76.01           C  
ANISOU 5074  C   VAL B 324     4827  15586   8467   2212   1405   1477       C  
ATOM   5075  O   VAL B 324     -43.223  13.725  76.488  1.00 76.14           O  
ANISOU 5075  O   VAL B 324     4889  15710   8330   2284   1392   1529       O  
ATOM   5076  CB  VAL B 324     -46.380  13.129  75.465  1.00 86.40           C  
ANISOU 5076  CB  VAL B 324     6147  16827   9852   2279   1372   1490       C  
ATOM   5077  CG1 VAL B 324     -45.469  12.858  74.278  1.00 93.11           C  
ANISOU 5077  CG1 VAL B 324     7042  17774  10561   2395   1329   1588       C  
ATOM   5078  CG2 VAL B 324     -47.464  12.066  75.561  1.00 84.66           C  
ANISOU 5078  CG2 VAL B 324     5936  16581   9649   2309   1376   1461       C  
ATOM   5079  N   LEU B 325     -44.657  15.443  76.745  1.00 76.08           N  
ANISOU 5079  N   LEU B 325     4761  15500   8646   2113   1418   1436       N  
ATOM   5080  CA  LEU B 325     -43.579  16.421  76.656  1.00 77.27           C  
ANISOU 5080  CA  LEU B 325     4873  15666   8819   2083   1421   1452       C  
ATOM   5081  C   LEU B 325     -42.622  16.308  77.837  1.00 76.51           C  
ANISOU 5081  C   LEU B 325     4785  15638   8648   2067   1439   1401       C  
ATOM   5082  O   LEU B 325     -41.417  16.529  77.678  1.00 76.81           O  
ANISOU 5082  O   LEU B 325     4819  15745   8620   2092   1433   1435       O  
ATOM   5083  CB  LEU B 325     -44.157  17.832  76.554  1.00 76.51           C  
ANISOU 5083  CB  LEU B 325     4689  15444   8938   1982   1435   1413       C  
ATOM   5084  CG  LEU B 325     -45.051  18.052  75.329  1.00 76.49           C  
ANISOU 5084  CG  LEU B 325     4673  15382   9007   2008   1414   1465       C  
ATOM   5085  CD1 LEU B 325     -45.493  19.499  75.226  1.00 81.53           C  
ANISOU 5085  CD1 LEU B 325     5223  15904   9850   1917   1430   1433       C  
ATOM   5086  CD2 LEU B 325     -44.353  17.607  74.051  1.00 76.68           C  
ANISOU 5086  CD2 LEU B 325     4743  15498   8892   2127   1386   1585       C  
ATOM   5087  N   GLY B 326     -43.130  15.956  79.018  1.00 76.39           N  
ANISOU 5087  N   GLY B 326     4777  15609   8638   2034   1463   1322       N  
ATOM   5088  CA  GLY B 326     -42.251  15.719  80.149  1.00 76.60           C  
ANISOU 5088  CA  GLY B 326     4819  15719   8568   2045   1476   1275       C  
ATOM   5089  C   GLY B 326     -41.369  14.504  79.949  1.00 76.61           C  
ANISOU 5089  C   GLY B 326     4906  15858   8346   2163   1457   1342       C  
ATOM   5090  O   GLY B 326     -40.215  14.489  80.380  1.00 76.91           O  
ANISOU 5090  O   GLY B 326     4949  15986   8287   2191   1450   1333       O  
ATOM   5091  N   ILE B 327     -41.899  13.467  79.298  1.00 76.37           N  
ANISOU 5091  N   ILE B 327     4937  15845   8235   2237   1446   1403       N  
ATOM   5092  CA  ILE B 327     -41.071  12.314  78.951  1.00 76.42           C  
ANISOU 5092  CA  ILE B 327     5025  15979   8032   2361   1423   1474       C  
ATOM   5093  C   ILE B 327     -39.951  12.733  78.009  1.00 82.56           C  
ANISOU 5093  C   ILE B 327     5797  16818   8756   2399   1391   1542       C  
ATOM   5094  O   ILE B 327     -38.797  12.313  78.162  1.00 77.22           O  
ANISOU 5094  O   ILE B 327     5156  16254   7929   2465   1377   1566       O  
ATOM   5095  CB  ILE B 327     -41.936  11.192  78.345  1.00 76.23           C  
ANISOU 5095  CB  ILE B 327     5054  15949   7960   2435   1416   1520       C  
ATOM   5096  CG1 ILE B 327     -42.699  10.459  79.449  1.00 93.68           C  
ANISOU 5096  CG1 ILE B 327     7285  18138  10172   2426   1461   1467       C  
ATOM   5097  CG2 ILE B 327     -41.080  10.222  77.541  1.00 77.10           C  
ANISOU 5097  CG2 ILE B 327     5238  16180   7876   2571   1379   1606       C  
ATOM   5098  CD1 ILE B 327     -43.428   9.228  78.971  1.00 88.47           C  
ANISOU 5098  CD1 ILE B 327     6670  17479   9466   2506   1464   1507       C  
ATOM   5099  N   VAL B 328     -40.276  13.569  77.020  1.00 87.99           N  
ANISOU 5099  N   VAL B 328     6436  17431   9563   2364   1383   1578       N  
ATOM   5100  CA  VAL B 328     -39.249  14.063  76.100  1.00 76.95           C  
ANISOU 5100  CA  VAL B 328     5025  16083   8131   2397   1367   1653       C  
ATOM   5101  C   VAL B 328     -38.189  14.858  76.859  1.00 77.35           C  
ANISOU 5101  C   VAL B 328     5018  16155   8216   2336   1384   1604       C  
ATOM   5102  O   VAL B 328     -36.979  14.663  76.668  1.00 77.68           O  
ANISOU 5102  O   VAL B 328     5075  16299   8141   2394   1373   1647       O  
ATOM   5103  CB  VAL B 328     -39.890  14.903  74.981  1.00 77.01           C  
ANISOU 5103  CB  VAL B 328     4985  16000   8275   2371   1365   1700       C  
ATOM   5104  CG1 VAL B 328     -38.818  15.496  74.079  1.00 82.40           C  
ANISOU 5104  CG1 VAL B 328     5645  16729   8935   2405   1364   1788       C  
ATOM   5105  CG2 VAL B 328     -40.861  14.054  74.176  1.00 90.67           C  
ANISOU 5105  CG2 VAL B 328     6766  17725   9959   2450   1338   1741       C  
ATOM   5106  N   PHE B 329     -38.635  15.771  77.730  1.00 79.58           N  
ANISOU 5106  N   PHE B 329     5228  16343   8667   2222   1410   1507       N  
ATOM   5107  CA  PHE B 329     -37.713  16.544  78.559  1.00 77.88           C  
ANISOU 5107  CA  PHE B 329     4943  16142   8504   2164   1424   1437       C  
ATOM   5108  C   PHE B 329     -36.800  15.624  79.353  1.00 78.00           C  
ANISOU 5108  C   PHE B 329     5014  16295   8328   2237   1411   1415       C  
ATOM   5109  O   PHE B 329     -35.576  15.803  79.375  1.00 84.24           O  
ANISOU 5109  O   PHE B 329     5780  17164   9063   2259   1404   1420       O  
ATOM   5110  CB  PHE B 329     -38.485  17.444  79.529  1.00 91.13           C  
ANISOU 5110  CB  PHE B 329     6549  17709  10369   2050   1450   1322       C  
ATOM   5111  CG  PHE B 329     -39.389  18.448  78.869  1.00 89.46           C  
ANISOU 5111  CG  PHE B 329     6276  17359  10358   1974   1462   1330       C  
ATOM   5112  CD1 PHE B 329     -39.099  18.963  77.618  1.00 94.69           C  
ANISOU 5112  CD1 PHE B 329     6912  17998  11066   1987   1461   1423       C  
ATOM   5113  CD2 PHE B 329     -40.531  18.887  79.520  1.00 77.63           C  
ANISOU 5113  CD2 PHE B 329     4743  15756   8999   1896   1479   1248       C  
ATOM   5114  CE1 PHE B 329     -39.940  19.891  77.027  1.00 93.77           C  
ANISOU 5114  CE1 PHE B 329     6741  17760  11129   1928   1474   1433       C  
ATOM   5115  CE2 PHE B 329     -41.372  19.812  78.935  1.00 77.62           C  
ANISOU 5115  CE2 PHE B 329     4684  15630   9179   1832   1487   1251       C  
ATOM   5116  CZ  PHE B 329     -41.076  20.315  77.687  1.00 82.36           C  
ANISOU 5116  CZ  PHE B 329     5262  16211   9821   1849   1484   1343       C  
ATOM   5117  N   PHE B 330     -37.393  14.639  80.031  1.00 77.66           N  
ANISOU 5117  N   PHE B 330     5040  16282   8187   2279   1412   1389       N  
ATOM   5118  CA  PHE B 330     -36.634  13.760  80.908  1.00 84.11           C  
ANISOU 5118  CA  PHE B 330     5911  17227   8822   2355   1403   1363       C  
ATOM   5119  C   PHE B 330     -35.612  12.958  80.125  1.00 88.17           C  
ANISOU 5119  C   PHE B 330     6488  17863   9149   2468   1371   1456       C  
ATOM   5120  O   PHE B 330     -34.456  12.853  80.537  1.00 90.46           O  
ANISOU 5120  O   PHE B 330     6776  18258   9336   2509   1357   1438       O  
ATOM   5121  CB  PHE B 330     -37.585  12.833  81.664  1.00 93.18           C  
ANISOU 5121  CB  PHE B 330     7122  18369   9913   2384   1422   1337       C  
ATOM   5122  CG  PHE B 330     -36.912  12.001  82.717  1.00 98.16           C  
ANISOU 5122  CG  PHE B 330     7805  19123  10368   2465   1421   1305       C  
ATOM   5123  CD1 PHE B 330     -36.538  12.563  83.926  1.00100.02           C  
ANISOU 5123  CD1 PHE B 330     7991  19385  10628   2429   1432   1203       C  
ATOM   5124  CD2 PHE B 330     -36.665  10.655  82.504  1.00102.62           C  
ANISOU 5124  CD2 PHE B 330     8470  19781  10742   2587   1408   1375       C  
ATOM   5125  CE1 PHE B 330     -35.923  11.801  84.901  1.00106.38           C  
ANISOU 5125  CE1 PHE B 330     8845  20313  11261   2517   1429   1174       C  
ATOM   5126  CE2 PHE B 330     -36.050   9.886  83.475  1.00111.48           C  
ANISOU 5126  CE2 PHE B 330     9643  21015  11698   2671   1408   1350       C  
ATOM   5127  CZ  PHE B 330     -35.679  10.461  84.675  1.00114.41           C  
ANISOU 5127  CZ  PHE B 330     9966  21418  12088   2638   1418   1251       C  
ATOM   5128  N   LEU B 331     -36.009  12.400  78.980  1.00 86.88           N  
ANISOU 5128  N   LEU B 331     6378  17694   8940   2527   1356   1552       N  
ATOM   5129  CA  LEU B 331     -35.070  11.610  78.193  1.00 87.52           C  
ANISOU 5129  CA  LEU B 331     6522  17896   8835   2647   1323   1643       C  
ATOM   5130  C   LEU B 331     -33.913  12.467  77.693  1.00 86.35           C  
ANISOU 5130  C   LEU B 331     6312  17781   8715   2628   1319   1671       C  
ATOM   5131  O   LEU B 331     -32.743  12.096  77.847  1.00 87.64           O  
ANISOU 5131  O   LEU B 331     6493  18064   8740   2693   1301   1683       O  
ATOM   5132  CB  LEU B 331     -35.794  10.933  77.030  1.00 86.94           C  
ANISOU 5132  CB  LEU B 331     6507  17806   8721   2719   1307   1731       C  
ATOM   5133  CG  LEU B 331     -36.760   9.826  77.453  1.00 85.33           C  
ANISOU 5133  CG  LEU B 331     6367  17589   8464   2763   1313   1713       C  
ATOM   5134  CD1 LEU B 331     -37.243   9.052  76.244  1.00 81.01           C  
ANISOU 5134  CD1 LEU B 331     5874  17053   7855   2860   1287   1794       C  
ATOM   5135  CD2 LEU B 331     -36.106   8.894  78.464  1.00 80.57           C  
ANISOU 5135  CD2 LEU B 331     5825  17093   7696   2835   1312   1687       C  
ATOM   5136  N   PHE B 332     -34.218  13.638  77.121  1.00 91.79           N  
ANISOU 5136  N   PHE B 332     6920  18364   9591   2540   1340   1681       N  
ATOM   5137  CA  PHE B 332     -33.155  14.498  76.605  1.00 79.03           C  
ANISOU 5137  CA  PHE B 332     5234  16767   8028   2518   1350   1717       C  
ATOM   5138  C   PHE B 332     -32.193  14.915  77.714  1.00 79.88           C  
ANISOU 5138  C   PHE B 332     5278  16920   8153   2474   1357   1620       C  
ATOM   5139  O   PHE B 332     -30.970  14.755  77.588  1.00104.35           O  
ANISOU 5139  O   PHE B 332     8371  20125  11153   2526   1347   1645       O  
ATOM   5140  CB  PHE B 332     -33.762  15.728  75.926  1.00 79.16           C  
ANISOU 5140  CB  PHE B 332     5168  16646   8262   2428   1380   1738       C  
ATOM   5141  CG  PHE B 332     -32.749  16.766  75.521  1.00 79.97           C  
ANISOU 5141  CG  PHE B 332     5175  16742   8466   2387   1408   1767       C  
ATOM   5142  CD1 PHE B 332     -32.113  16.691  74.293  1.00 92.01           C  
ANISOU 5142  CD1 PHE B 332     6716  18325   9919   2465   1409   1896       C  
ATOM   5143  CD2 PHE B 332     -32.440  17.822  76.364  1.00 80.45           C  
ANISOU 5143  CD2 PHE B 332     5127  16739   8704   2276   1435   1664       C  
ATOM   5144  CE1 PHE B 332     -31.182  17.645  73.919  1.00 98.10           C  
ANISOU 5144  CE1 PHE B 332     7391  19085  10796   2427   1446   1930       C  
ATOM   5145  CE2 PHE B 332     -31.511  18.775  75.995  1.00 94.54           C  
ANISOU 5145  CE2 PHE B 332     6810  18508  10604   2236   1467   1687       C  
ATOM   5146  CZ  PHE B 332     -30.883  18.688  74.771  1.00 97.07           C  
ANISOU 5146  CZ  PHE B 332     7144  18881  10856   2308   1477   1823       C  
ATOM   5147  N   VAL B 333     -32.732  15.444  78.815  1.00 79.51           N  
ANISOU 5147  N   VAL B 333     5180  16801   8231   2384   1374   1503       N  
ATOM   5148  CA  VAL B 333     -31.885  15.948  79.890  1.00 92.77           C  
ANISOU 5148  CA  VAL B 333     6785  18520   9944   2344   1378   1395       C  
ATOM   5149  C   VAL B 333     -31.107  14.813  80.544  1.00 98.41           C  
ANISOU 5149  C   VAL B 333     7574  19395  10423   2452   1347   1378       C  
ATOM   5150  O   VAL B 333     -29.916  14.954  80.835  1.00105.87           O  
ANISOU 5150  O   VAL B 333     8476  20430  11320   2472   1337   1346       O  
ATOM   5151  CB  VAL B 333     -32.728  16.725  80.916  1.00 97.82           C  
ANISOU 5151  CB  VAL B 333     7358  19052  10756   2240   1399   1273       C  
ATOM   5152  CG1 VAL B 333     -31.904  17.023  82.157  1.00 92.32           C  
ANISOU 5152  CG1 VAL B 333     6598  18424  10055   2228   1393   1149       C  
ATOM   5153  CG2 VAL B 333     -33.248  18.016  80.301  1.00102.26           C  
ANISOU 5153  CG2 VAL B 333     7827  19462  11567   2133   1428   1280       C  
ATOM   5154  N   VAL B 334     -31.758  13.675  80.788  1.00 88.62           N  
ANISOU 5154  N   VAL B 334     6442  18192   9039   2525   1333   1399       N  
ATOM   5155  CA  VAL B 334     -31.096  12.560  81.452  1.00 93.93           C  
ANISOU 5155  CA  VAL B 334     7191  19011   9487   2637   1306   1387       C  
ATOM   5156  C   VAL B 334     -29.985  11.994  80.580  1.00106.35           C  
ANISOU 5156  C   VAL B 334     8805  20701  10902   2736   1276   1479       C  
ATOM   5157  O   VAL B 334     -28.937  11.583  81.088  1.00110.85           O  
ANISOU 5157  O   VAL B 334     9385  21400  11333   2804   1251   1451       O  
ATOM   5158  CB  VAL B 334     -32.133  11.489  81.838  1.00100.08           C  
ANISOU 5158  CB  VAL B 334     8069  19782  10174   2692   1309   1400       C  
ATOM   5159  CG1 VAL B 334     -31.481  10.122  81.994  1.00 81.62           C  
ANISOU 5159  CG1 VAL B 334     5835  17591   7588   2839   1278   1443       C  
ATOM   5160  CG2 VAL B 334     -32.833  11.885  83.128  1.00110.52           C  
ANISOU 5160  CG2 VAL B 334     9355  21050  11590   2625   1337   1287       C  
ATOM   5161  N   MET B 335     -30.182  11.961  79.260  1.00107.84           N  
ANISOU 5161  N   MET B 335     9016  20856  11104   2754   1275   1590       N  
ATOM   5162  CA  MET B 335     -29.132  11.427  78.402  1.00104.24           C  
ANISOU 5162  CA  MET B 335     8600  20516  10492   2857   1247   1683       C  
ATOM   5163  C   MET B 335     -27.995  12.419  78.187  1.00104.18           C  
ANISOU 5163  C   MET B 335     8485  20527  10570   2807   1262   1675       C  
ATOM   5164  O   MET B 335     -26.857  11.999  77.945  1.00117.07           O  
ANISOU 5164  O   MET B 335    10134  22285  12062   2888   1240   1712       O  
ATOM   5165  CB  MET B 335     -29.725  10.973  77.070  1.00103.00           C  
ANISOU 5165  CB  MET B 335     8507  20333  10296   2917   1239   1805       C  
ATOM   5166  CG  MET B 335     -30.613   9.746  77.218  1.00 98.69           C  
ANISOU 5166  CG  MET B 335     8068  19796   9633   2996   1221   1818       C  
ATOM   5167  SD  MET B 335     -30.912   8.852  75.684  1.00133.79           S  
ANISOU 5167  SD  MET B 335    12604  24276  13956   3125   1192   1952       S  
ATOM   5168  CE  MET B 335     -31.862   7.461  76.289  1.00101.76           C  
ANISOU 5168  CE  MET B 335     8645  20221   9798   3199   1182   1925       C  
ATOM   5169  N   TRP B 336     -28.262  13.725  78.272  1.00108.14           N  
ANISOU 5169  N   TRP B 336     8874  20906  11308   2677   1300   1626       N  
ATOM   5170  CA  TRP B 336     -27.158  14.680  78.264  1.00116.30           C  
ANISOU 5170  CA  TRP B 336     9789  21950  12450   2623   1321   1598       C  
ATOM   5171  C   TRP B 336     -26.518  14.864  79.637  1.00115.43           C  
ANISOU 5171  C   TRP B 336     9618  21898  12341   2598   1312   1454       C  
ATOM   5172  O   TRP B 336     -25.454  15.486  79.726  1.00116.15           O  
ANISOU 5172  O   TRP B 336     9609  22023  12498   2570   1322   1417       O  
ATOM   5173  CB  TRP B 336     -27.622  16.041  77.734  1.00111.26           C  
ANISOU 5173  CB  TRP B 336     9042  21153  12078   2502   1370   1608       C  
ATOM   5174  CG  TRP B 336     -27.527  16.184  76.240  1.00110.33           C  
ANISOU 5174  CG  TRP B 336     8935  21020  11967   2537   1388   1759       C  
ATOM   5175  CD1 TRP B 336     -28.558  16.158  75.349  1.00111.80           C  
ANISOU 5175  CD1 TRP B 336     9169  21129  12180   2548   1394   1845       C  
ATOM   5176  CD2 TRP B 336     -26.333  16.374  75.467  1.00122.14           C  
ANISOU 5176  CD2 TRP B 336    10388  22586  13435   2578   1404   1842       C  
ATOM   5177  NE1 TRP B 336     -28.083  16.322  74.069  1.00117.15           N  
ANISOU 5177  NE1 TRP B 336     9843  21832  12839   2600   1411   1980       N  
ATOM   5178  CE2 TRP B 336     -26.721  16.455  74.114  1.00123.06           C  
ANISOU 5178  CE2 TRP B 336    10536  22668  13554   2618   1421   1985       C  
ATOM   5179  CE3 TRP B 336     -24.976  16.482  75.787  1.00120.65           C  
ANISOU 5179  CE3 TRP B 336    10133  22490  13218   2589   1407   1808       C  
ATOM   5180  CZ2 TRP B 336     -25.802  16.641  73.083  1.00119.95           C  
ANISOU 5180  CZ2 TRP B 336    10114  22330  13132   2672   1446   2105       C  
ATOM   5181  CZ3 TRP B 336     -24.065  16.667  74.760  1.00123.36           C  
ANISOU 5181  CZ3 TRP B 336    10442  22882  13546   2632   1433   1922       C  
ATOM   5182  CH2 TRP B 336     -24.482  16.743  73.426  1.00112.37           C  
ANISOU 5182  CH2 TRP B 336     9087  21455  12153   2674   1454   2074       C  
ATOM   5183  N   CYS B 337     -27.135  14.339  80.703  1.00113.86           N  
ANISOU 5183  N   CYS B 337     9473  21715  12073   2614   1294   1372       N  
ATOM   5184  CA  CYS B 337     -26.635  14.612  82.051  1.00122.01           C  
ANISOU 5184  CA  CYS B 337    10443  22802  13115   2596   1285   1227       C  
ATOM   5185  C   CYS B 337     -25.308  13.932  82.362  1.00133.85           C  
ANISOU 5185  C   CYS B 337    11962  24480  14415   2700   1248   1211       C  
ATOM   5186  O   CYS B 337     -24.384  14.628  82.814  1.00128.42           O  
ANISOU 5186  O   CYS B 337    11162  23827  13804   2665   1250   1123       O  
ATOM   5187  CB  CYS B 337     -27.706  14.249  83.084  1.00122.05           C  
ANISOU 5187  CB  CYS B 337    10501  22778  13094   2594   1283   1155       C  
ATOM   5188  SG  CYS B 337     -28.723  15.645  83.620  1.00116.74           S  
ANISOU 5188  SG  CYS B 337     9714  21927  12715   2439   1321   1053       S  
ATOM   5189  N   PRO B 338     -25.144  12.609  82.203  1.00150.14           N  
ANISOU 5189  N   PRO B 338    14155  26660  16232   2832   1213   1282       N  
ATOM   5190  CA  PRO B 338     -23.859  12.001  82.597  1.00143.79           C  
ANISOU 5190  CA  PRO B 338    13365  26031  15238   2936   1174   1254       C  
ATOM   5191  C   PRO B 338     -22.681  12.548  81.816  1.00120.37           C  
ANISOU 5191  C   PRO B 338    10312  23101  12322   2920   1182   1291       C  
ATOM   5192  O   PRO B 338     -21.583  12.700  82.372  1.00121.27           O  
ANISOU 5192  O   PRO B 338    10359  23319  12399   2942   1165   1210       O  
ATOM   5193  CB  PRO B 338     -24.077  10.504  82.322  1.00151.38           C  
ANISOU 5193  CB  PRO B 338    14486  27079  15955   3077   1138   1350       C  
ATOM   5194  CG  PRO B 338     -25.554  10.335  82.211  1.00149.70           C  
ANISOU 5194  CG  PRO B 338    14331  26739  15811   3040   1161   1384       C  
ATOM   5195  CD  PRO B 338     -26.036  11.606  81.605  1.00146.08           C  
ANISOU 5195  CD  PRO B 338    13772  26127  15604   2900   1204   1389       C  
ATOM   5196  N   PHE B 339     -22.886  12.857  80.534  1.00117.32           N  
ANISOU 5196  N   PHE B 339     9922  22635  12021   2889   1209   1411       N  
ATOM   5197  CA  PHE B 339     -21.826  13.472  79.746  1.00135.32           C  
ANISOU 5197  CA  PHE B 339    12109  24934  14374   2868   1232   1459       C  
ATOM   5198  C   PHE B 339     -21.431  14.820  80.328  1.00123.92           C  
ANISOU 5198  C   PHE B 339    10491  23415  13180   2741   1267   1339       C  
ATOM   5199  O   PHE B 339     -20.242  15.120  80.472  1.00128.41           O  
ANISOU 5199  O   PHE B 339    10967  24058  13764   2745   1268   1294       O  
ATOM   5200  CB  PHE B 339     -22.266  13.627  78.291  1.00149.18           C  
ANISOU 5200  CB  PHE B 339    13890  26608  16183   2862   1260   1613       C  
ATOM   5201  CG  PHE B 339     -21.331  14.465  77.472  1.00137.74           C  
ANISOU 5201  CG  PHE B 339    12328  25147  14858   2824   1302   1670       C  
ATOM   5202  CD1 PHE B 339     -20.084  13.983  77.118  1.00128.74           C  
ANISOU 5202  CD1 PHE B 339    11193  24152  13571   2914   1286   1717       C  
ATOM   5203  CD2 PHE B 339     -21.693  15.738  77.065  1.00135.93           C  
ANISOU 5203  CD2 PHE B 339    11985  24762  14900   2700   1361   1679       C  
ATOM   5204  CE1 PHE B 339     -19.214  14.754  76.373  1.00149.14           C  
ANISOU 5204  CE1 PHE B 339    13665  26724  16278   2879   1334   1774       C  
ATOM   5205  CE2 PHE B 339     -20.830  16.512  76.315  1.00132.68           C  
ANISOU 5205  CE2 PHE B 339    11463  24335  14616   2668   1410   1739       C  
ATOM   5206  CZ  PHE B 339     -19.589  16.018  75.967  1.00151.00           C  
ANISOU 5206  CZ  PHE B 339    13784  26798  16790   2756   1399   1788       C  
ATOM   5207  N   PHE B 340     -22.421  15.643  80.684  1.00119.40           N  
ANISOU 5207  N   PHE B 340     9865  22691  12809   2631   1295   1280       N  
ATOM   5208  CA  PHE B 340     -22.124  16.942  81.280  1.00104.56           C  
ANISOU 5208  CA  PHE B 340     7815  20729  11185   2513   1325   1156       C  
ATOM   5209  C   PHE B 340     -21.428  16.786  82.626  1.00109.02           C  
ANISOU 5209  C   PHE B 340     8338  21411  11673   2547   1286    998       C  
ATOM   5210  O   PHE B 340     -20.517  17.553  82.951  1.00106.51           O  
ANISOU 5210  O   PHE B 340     7876  21103  11490   2501   1296    908       O  
ATOM   5211  CB  PHE B 340     -23.407  17.759  81.431  1.00120.90           C  
ANISOU 5211  CB  PHE B 340     9851  22620  13467   2402   1354   1124       C  
ATOM   5212  CG  PHE B 340     -23.665  18.700  80.288  1.00123.54           C  
ANISOU 5212  CG  PHE B 340    10114  22810  14017   2318   1409   1220       C  
ATOM   5213  CD1 PHE B 340     -24.239  18.245  79.113  1.00120.63           C  
ANISOU 5213  CD1 PHE B 340     9846  22415  13571   2361   1418   1376       C  
ATOM   5214  CD2 PHE B 340     -23.337  20.041  80.392  1.00117.81           C  
ANISOU 5214  CD2 PHE B 340     9215  21974  13573   2205   1450   1152       C  
ATOM   5215  CE1 PHE B 340     -24.479  19.109  78.062  1.00110.13           C  
ANISOU 5215  CE1 PHE B 340     8455  20966  12425   2299   1468   1468       C  
ATOM   5216  CE2 PHE B 340     -23.575  20.911  79.343  1.00112.93           C  
ANISOU 5216  CE2 PHE B 340     8530  21223  13153   2136   1506   1246       C  
ATOM   5217  CZ  PHE B 340     -24.147  20.444  78.177  1.00106.09           C  
ANISOU 5217  CZ  PHE B 340     7774  20345  12190   2186   1516   1408       C  
ATOM   5218  N   ILE B 341     -21.845  15.799  83.421  1.00122.90           N  
ANISOU 5218  N   ILE B 341    10216  23261  13219   2634   1244    962       N  
ATOM   5219  CA  ILE B 341     -21.248  15.591  84.738  1.00131.17           C  
ANISOU 5219  CA  ILE B 341    11237  24437  14166   2688   1203    813       C  
ATOM   5220  C   ILE B 341     -19.778  15.211  84.601  1.00124.67           C  
ANISOU 5220  C   ILE B 341    10387  23771  13210   2768   1177    811       C  
ATOM   5221  O   ILE B 341     -18.901  15.805  85.243  1.00124.79           O  
ANISOU 5221  O   ILE B 341    10274  23836  13305   2748   1168    683       O  
ATOM   5222  CB  ILE B 341     -22.038  14.524  85.519  1.00133.46           C  
ANISOU 5222  CB  ILE B 341    11672  24792  14243   2780   1171    801       C  
ATOM   5223  CG1 ILE B 341     -23.448  15.027  85.838  1.00110.65           C  
ANISOU 5223  CG1 ILE B 341     8784  21750  11508   2691   1201    776       C  
ATOM   5224  CG2 ILE B 341     -21.303  14.138  86.794  1.00119.41           C  
ANISOU 5224  CG2 ILE B 341     9885  23179  12306   2871   1124    667       C  
ATOM   5225  CD1 ILE B 341     -24.343  13.978  86.460  1.00105.90           C  
ANISOU 5225  CD1 ILE B 341     8324  21189  10726   2774   1185    789       C  
ATOM   5226  N   THR B 342     -19.487  14.222  83.752  1.00123.38           N  
ANISOU 5226  N   THR B 342    10339  23690  12849   2865   1163    947       N  
ATOM   5227  CA  THR B 342     -18.101  13.811  83.547  1.00104.62           C  
ANISOU 5227  CA  THR B 342     7946  21469  10337   2949   1137    956       C  
ATOM   5228  C   THR B 342     -17.281  14.930  82.913  1.00104.65           C  
ANISOU 5228  C   THR B 342     7781  21408  10573   2853   1184    957       C  
ATOM   5229  O   THR B 342     -16.100  15.109  83.240  1.00128.25           O  
ANISOU 5229  O   THR B 342    10674  24497  13559   2873   1171    878       O  
ATOM   5230  CB  THR B 342     -18.047  12.546  82.690  1.00105.99           C  
ANISOU 5230  CB  THR B 342     8279  21731  10261   3075   1111   1111       C  
ATOM   5231  OG1 THR B 342     -18.899  12.702  81.549  1.00113.04           O  
ANISOU 5231  OG1 THR B 342     9213  22491  11247   3027   1148   1249       O  
ATOM   5232  CG2 THR B 342     -18.504  11.337  83.494  1.00105.69           C  
ANISOU 5232  CG2 THR B 342     8387  21790   9979   3196   1058   1092       C  
ATOM   5233  N   ASN B 343     -17.891  15.697  82.004  1.00105.00           N  
ANISOU 5233  N   ASN B 343     7782  21285  10827   2752   1240   1046       N  
ATOM   5234  CA  ASN B 343     -17.184  16.803  81.371  1.00 98.64           C  
ANISOU 5234  CA  ASN B 343     6811  20400  10268   2659   1295   1061       C  
ATOM   5235  C   ASN B 343     -16.825  17.885  82.382  1.00108.42           C  
ANISOU 5235  C   ASN B 343     7869  21588  11739   2563   1303    879       C  
ATOM   5236  O   ASN B 343     -15.707  18.403  82.363  1.00123.03           O  
ANISOU 5236  O   ASN B 343     9577  23469  13699   2540   1319    830       O  
ATOM   5237  CB  ASN B 343     -18.030  17.384  80.239  1.00105.32           C  
ANISOU 5237  CB  ASN B 343     7659  21078  11280   2582   1353   1195       C  
ATOM   5238  CG  ASN B 343     -17.253  18.348  79.367  1.00 91.26           C  
ANISOU 5238  CG  ASN B 343     5728  19229   9717   2513   1418   1254       C  
ATOM   5239  OD1 ASN B 343     -16.029  18.264  79.268  1.00 92.30           O  
ANISOU 5239  OD1 ASN B 343     5794  19464   9813   2551   1420   1248       O  
ATOM   5240  ND2 ASN B 343     -17.961  19.272  78.730  1.00104.74           N  
ANISOU 5240  ND2 ASN B 343     7378  20763  11655   2415   1476   1313       N  
ATOM   5241  N   ILE B 344     -17.752  18.235  83.276  1.00111.47           N  
ANISOU 5241  N   ILE B 344     8251  21897  12206   2511   1291    774       N  
ATOM   5242  CA  ILE B 344     -17.459  19.237  84.297  1.00113.66           C  
ANISOU 5242  CA  ILE B 344     8359  22132  12695   2434   1287    591       C  
ATOM   5243  C   ILE B 344     -16.405  18.716  85.267  1.00113.67           C  
ANISOU 5243  C   ILE B 344     8340  22327  12522   2530   1228    461       C  
ATOM   5244  O   ILE B 344     -15.519  19.467  85.709  1.00132.46           O  
ANISOU 5244  O   ILE B 344    10548  24716  15064   2489   1226    338       O  
ATOM   5245  CB  ILE B 344     -18.750  19.656  85.023  1.00120.06           C  
ANISOU 5245  CB  ILE B 344     9184  22829  13605   2373   1284    516       C  
ATOM   5246  CG1 ILE B 344     -19.688  20.392  84.062  1.00112.47           C  
ANISOU 5246  CG1 ILE B 344     8206  21665  12862   2265   1344    627       C  
ATOM   5247  CG2 ILE B 344     -18.433  20.529  86.228  1.00121.42           C  
ANISOU 5247  CG2 ILE B 344     9198  22992  13945   2324   1262    314       C  
ATOM   5248  CD1 ILE B 344     -19.085  21.640  83.450  1.00113.21           C  
ANISOU 5248  CD1 ILE B 344     8111  21634  13270   2157   1402    633       C  
ATOM   5249  N   MET B 345     -16.491  17.430  85.624  1.00110.61           N  
ANISOU 5249  N   MET B 345     8122  22097  11808   2664   1177    481       N  
ATOM   5250  CA  MET B 345     -15.413  16.784  86.364  1.00126.38           C  
ANISOU 5250  CA  MET B 345    10122  24299  13597   2780   1119    384       C  
ATOM   5251  C   MET B 345     -14.068  17.076  85.712  1.00143.98           C  
ANISOU 5251  C   MET B 345    12233  26575  15899   2772   1137    405       C  
ATOM   5252  O   MET B 345     -13.221  17.770  86.282  1.00149.26           O  
ANISOU 5252  O   MET B 345    12735  27268  16708   2739   1128    263       O  
ATOM   5253  CB  MET B 345     -15.656  15.273  86.436  1.00123.28           C  
ANISOU 5253  CB  MET B 345     9942  24052  12847   2931   1074    464       C  
ATOM   5254  CG  MET B 345     -16.744  14.841  87.401  1.00122.69           C  
ANISOU 5254  CG  MET B 345     9972  23980  12664   2970   1047    410       C  
ATOM   5255  SD  MET B 345     -17.265  13.140  87.098  1.00116.26           S  
ANISOU 5255  SD  MET B 345     9402  23263  11508   3121   1016    561       S  
ATOM   5256  CE  MET B 345     -15.683  12.322  86.918  1.00116.60           C  
ANISOU 5256  CE  MET B 345     9463  23523  11314   3259    967    572       C  
ATOM   5257  N   ALA B 346     -13.891  16.612  84.472  1.00140.16           N  
ANISOU 5257  N   ALA B 346    11821  26091  15340   2798   1166    584       N  
ATOM   5258  CA  ALA B 346     -12.631  16.830  83.767  1.00120.36           C  
ANISOU 5258  CA  ALA B 346     9209  23633  12889   2799   1192    624       C  
ATOM   5259  C   ALA B 346     -12.291  18.309  83.622  1.00136.48           C  
ANISOU 5259  C   ALA B 346    11022  25519  15317   2650   1252    564       C  
ATOM   5260  O   ALA B 346     -11.112  18.652  83.483  1.00152.92           O  
ANISOU 5260  O   ALA B 346    12965  27648  17488   2643   1267    528       O  
ATOM   5261  CB  ALA B 346     -12.678  16.167  82.389  1.00 94.54           C  
ANISOU 5261  CB  ALA B 346     6060  20372   9488   2851   1218    840       C  
ATOM   5262  N   VAL B 347     -13.293  19.189  83.641  1.00128.83           N  
ANISOU 5262  N   VAL B 347    10004  24362  14585   2534   1289    555       N  
ATOM   5263  CA  VAL B 347     -13.038  20.622  83.521  1.00130.29           C  
ANISOU 5263  CA  VAL B 347     9966  24381  15155   2394   1347    499       C  
ATOM   5264  C   VAL B 347     -12.351  21.154  84.772  1.00134.92           C  
ANISOU 5264  C   VAL B 347    10394  25017  15854   2378   1303    278       C  
ATOM   5265  O   VAL B 347     -11.344  21.865  84.688  1.00143.62           O  
ANISOU 5265  O   VAL B 347    11305  26097  17166   2327   1329    222       O  
ATOM   5266  CB  VAL B 347     -14.348  21.377  83.233  1.00142.32           C  
ANISOU 5266  CB  VAL B 347    11492  25696  16886   2285   1391    546       C  
ATOM   5267  CG1 VAL B 347     -14.222  22.838  83.636  1.00143.67           C  
ANISOU 5267  CG1 VAL B 347    11434  25709  17447   2150   1425    423       C  
ATOM   5268  CG2 VAL B 347     -14.698  21.271  81.763  1.00135.35           C  
ANISOU 5268  CG2 VAL B 347    10685  24739  16001   2276   1452    761       C  
ATOM   5269  N   ILE B 348     -12.877  20.820  85.950  1.00140.78           N  
ANISOU 5269  N   ILE B 348    11205  25828  16458   2427   1237    147       N  
ATOM   5270  CA  ILE B 348     -12.305  21.365  87.181  1.00148.12           C  
ANISOU 5270  CA  ILE B 348    11983  26808  17486   2422   1187    -74       C  
ATOM   5271  C   ILE B 348     -11.059  20.587  87.590  1.00170.17           C  
ANISOU 5271  C   ILE B 348    14782  29829  20046   2546   1131   -147       C  
ATOM   5272  O   ILE B 348      -9.979  21.163  87.763  1.00169.28           O  
ANISOU 5272  O   ILE B 348    14486  29739  20096   2520   1128   -247       O  
ATOM   5273  CB  ILE B 348     -13.353  21.397  88.308  1.00151.89           C  
ANISOU 5273  CB  ILE B 348    12522  27277  17912   2432   1140   -192       C  
ATOM   5274  CG1 ILE B 348     -14.408  22.462  88.006  1.00161.12           C  
ANISOU 5274  CG1 ILE B 348    13626  28207  19387   2290   1194   -158       C  
ATOM   5275  CG2 ILE B 348     -12.678  21.673  89.648  1.00127.15           C  
ANISOU 5275  CG2 ILE B 348     9272  24261  14780   2477   1068   -426       C  
ATOM   5276  CD1 ILE B 348     -15.283  22.817  89.191  1.00136.56           C  
ANISOU 5276  CD1 ILE B 348    10512  25069  16305   2280   1151   -305       C  
ATOM   5277  N   CYS B 349     -11.184  19.270  87.757  1.00235.15           N  
ANISOU 5277  N   CYS B 349    18696  41581  29071   5720   1454  -2085       N  
ATOM   5278  CA  CYS B 349     -10.020  18.425  88.030  1.00237.85           C  
ANISOU 5278  CA  CYS B 349    18960  42100  29313   5937   1181  -1861       C  
ATOM   5279  C   CYS B 349      -9.366  18.033  86.704  1.00236.75           C  
ANISOU 5279  C   CYS B 349    18676  41605  29673   5963   1218  -1695       C  
ATOM   5280  O   CYS B 349      -9.375  16.879  86.274  1.00249.10           O  
ANISOU 5280  O   CYS B 349    20368  43014  31266   6095   1292  -1283       O  
ATOM   5281  CB  CYS B 349     -10.409  17.205  88.860  1.00242.26           C  
ANISOU 5281  CB  CYS B 349    19802  42854  29393   6121   1174  -1470       C  
ATOM   5282  SG  CYS B 349     -11.790  16.208  88.247  1.00241.43           S  
ANISOU 5282  SG  CYS B 349    20036  42410  29286   6113   1568  -1044       S  
ATOM   5283  N   LYS B 350      -8.787  19.045  86.051  1.00199.36           N  
ANISOU 5283  N   LYS B 350    13666  36741  25342   5830   1167  -2033       N  
ATOM   5284  CA  LYS B 350      -8.157  18.847  84.751  1.00192.92           C  
ANISOU 5284  CA  LYS B 350    12687  35578  25036   5827   1206  -1933       C  
ATOM   5285  C   LYS B 350      -6.900  17.992  84.843  1.00201.39           C  
ANISOU 5285  C   LYS B 350    13650  36785  26086   6043    936  -1708       C  
ATOM   5286  O   LYS B 350      -6.439  17.476  83.818  1.00194.99           O  
ANISOU 5286  O   LYS B 350    12763  35691  25632   6087    979  -1506       O  
ATOM   5287  CB  LYS B 350      -7.830  20.203  84.118  1.00188.27           C  
ANISOU 5287  CB  LYS B 350    11830  34846  24858   5628   1204  -2379       C  
ATOM   5288  CG  LYS B 350      -7.674  20.174  82.605  1.00184.12           C  
ANISOU 5288  CG  LYS B 350    11197  33863  24897   5554   1371  -2305       C  
ATOM   5289  CD  LYS B 350      -7.555  21.581  82.041  1.00182.49           C  
ANISOU 5289  CD  LYS B 350    10764  33513  25062   5336   1405  -2760       C  
ATOM   5290  CE  LYS B 350      -7.519  21.568  80.522  1.00178.17           C  
ANISOU 5290  CE  LYS B 350    10133  32492  25070   5251   1599  -2686       C  
ATOM   5291  NZ  LYS B 350      -7.465  22.946  79.961  1.00176.49           N  
ANISOU 5291  NZ  LYS B 350     9850  32004  25205   4976   1635  -3083       N  
ATOM   5292  N   GLU B 351      -6.339  17.831  86.042  1.00218.89           N  
ANISOU 5292  N   GLU B 351    15857  39423  27889   6179    658  -1737       N  
ATOM   5293  CA  GLU B 351      -5.163  17.002  86.256  1.00226.18           C  
ANISOU 5293  CA  GLU B 351    16688  40510  28739   6395    386  -1525       C  
ATOM   5294  C   GLU B 351      -5.375  15.894  87.278  1.00232.81           C  
ANISOU 5294  C   GLU B 351    17779  41623  29056   6596    306  -1187       C  
ATOM   5295  O   GLU B 351      -4.648  14.895  87.237  1.00242.21           O  
ANISOU 5295  O   GLU B 351    18969  42851  30209   6790    164   -884       O  
ATOM   5296  CB  GLU B 351      -3.973  17.873  86.700  1.00226.37           C  
ANISOU 5296  CB  GLU B 351    16407  40803  28801   6391     61  -1903       C  
ATOM   5297  CG  GLU B 351      -2.622  17.166  86.735  1.00231.10           C  
ANISOU 5297  CG  GLU B 351    16852  41532  29423   6595   -228  -1738       C  
ATOM   5298  CD  GLU B 351      -2.120  16.776  85.359  1.00238.50           C  
ANISOU 5298  CD  GLU B 351    17665  42086  30869   6601   -145  -1568       C  
ATOM   5299  OE1 GLU B 351      -2.546  17.403  84.366  1.00241.94           O  
ANISOU 5299  OE1 GLU B 351    18039  42184  31705   6418     76  -1709       O  
ATOM   5300  OE2 GLU B 351      -1.297  15.840  85.269  1.00237.63           O  
ANISOU 5300  OE2 GLU B 351    17520  42011  30756   6790   -303  -1292       O  
ATOM   5301  N   SER B 352      -6.361  16.022  88.168  1.00229.30           N  
ANISOU 5301  N   SER B 352    17551  41359  28211   6556    400  -1223       N  
ATOM   5302  CA  SER B 352      -6.572  15.076  89.257  1.00229.86           C  
ANISOU 5302  CA  SER B 352    17860  41725  27750   6737    312   -944       C  
ATOM   5303  C   SER B 352      -7.769  14.161  89.014  1.00224.09           C  
ANISOU 5303  C   SER B 352    17456  40785  26902   6753    618   -564       C  
ATOM   5304  O   SER B 352      -8.447  13.755  89.961  1.00225.67           O  
ANISOU 5304  O   SER B 352    17897  41201  26645   6810    648   -439       O  
ATOM   5305  CB  SER B 352      -6.740  15.819  90.580  1.00228.53           C  
ANISOU 5305  CB  SER B 352    17708  41962  27161   6701    165  -1251       C  
ATOM   5306  OG  SER B 352      -7.772  16.785  90.505  1.00227.45           O  
ANISOU 5306  OG  SER B 352    17620  41724  27078   6481    389  -1525       O  
ATOM   5307  N   CYS B 353      -8.038  13.823  87.756  1.00210.84           N  
ANISOU 5307  N   CYS B 353    15789  38689  25631   6703    847   -377       N  
ATOM   5308  CA  CYS B 353      -9.138  12.932  87.421  1.00222.70           C  
ANISOU 5308  CA  CYS B 353    17588  39965  27062   6718   1143     -9       C  
ATOM   5309  C   CYS B 353      -8.741  12.064  86.235  1.00221.96           C  
ANISOU 5309  C   CYS B 353    17465  39527  27342   6798   1223    324       C  
ATOM   5310  O   CYS B 353      -8.167  12.554  85.259  1.00207.76           O  
ANISOU 5310  O   CYS B 353    15433  37494  26011   6719   1219    177       O  
ATOM   5311  CB  CYS B 353     -10.419  13.725  87.129  1.00229.45           C  
ANISOU 5311  CB  CYS B 353    18543  40627  28012   6491   1450   -207       C  
ATOM   5312  SG  CYS B 353     -11.270  14.283  88.634  1.00205.82           S  
ANISOU 5312  SG  CYS B 353    15722  38028  24453   6435   1434   -431       S  
ATOM   5313  N   ASN B 354      -9.056  10.775  86.334  1.00263.02           N  
ANISOU 5313  N   ASN B 354    22906  44699  32329   6955   1296    771       N  
ATOM   5314  CA  ASN B 354      -8.557   9.777  85.400  1.00255.59           C  
ANISOU 5314  CA  ASN B 354    21953  43498  31662   7076   1321   1130       C  
ATOM   5315  C   ASN B 354      -9.181   9.949  84.015  1.00247.87           C  
ANISOU 5315  C   ASN B 354    20970  42041  31168   6922   1637   1166       C  
ATOM   5316  O   ASN B 354     -10.271  10.504  83.853  1.00236.87           O  
ANISOU 5316  O   ASN B 354    19684  40507  29808   6751   1888   1033       O  
ATOM   5317  CB  ASN B 354      -8.838   8.372  85.937  1.00262.93           C  
ANISOU 5317  CB  ASN B 354    23165  44532  32202   7277   1331   1594       C  
ATOM   5318  CG  ASN B 354      -8.186   7.286  85.105  1.00248.35           C  
ANISOU 5318  CG  ASN B 354    21300  42470  30594   7430   1310   1972       C  
ATOM   5319  OD1 ASN B 354      -8.830   6.669  84.257  1.00258.73           O  
ANISOU 5319  OD1 ASN B 354    22757  43450  32098   7412   1572   2251       O  
ATOM   5320  ND2 ASN B 354      -6.901   7.049  85.342  1.00234.26           N  
ANISOU 5320  ND2 ASN B 354    19334  40874  28799   7584    997   1981       N  
ATOM   5321  N   GLU B 355      -8.454   9.467  82.999  1.00221.11           N  
ANISOU 5321  N   GLU B 355    17452  38400  28161   6986   1617   1344       N  
ATOM   5322  CA  GLU B 355      -8.929   9.489  81.620  1.00211.18           C  
ANISOU 5322  CA  GLU B 355    16187  36674  27378   6866   1901   1424       C  
ATOM   5323  C   GLU B 355      -8.590   8.198  80.880  1.00196.67           C  
ANISOU 5323  C   GLU B 355    14418  34614  25694   7025   1940   1881       C  
ATOM   5324  O   GLU B 355      -8.444   8.206  79.653  1.00181.92           O  
ANISOU 5324  O   GLU B 355    12444  32382  24293   6964   2069   1929       O  
ATOM   5325  CB  GLU B 355      -8.358  10.685  80.855  1.00200.98           C  
ANISOU 5325  CB  GLU B 355    14584  35225  26554   6702   1862   1028       C  
ATOM   5326  CG  GLU B 355      -9.196  11.947  80.954  1.00209.18           C  
ANISOU 5326  CG  GLU B 355    15610  36239  27630   6472   2013    633       C  
ATOM   5327  CD  GLU B 355      -8.657  13.069  80.089  1.00195.53           C  
ANISOU 5327  CD  GLU B 355    13586  34314  26391   6309   1997    270       C  
ATOM   5328  OE1 GLU B 355      -7.420  13.223  80.016  1.00177.88           O  
ANISOU 5328  OE1 GLU B 355    11105  32177  24305   6375   1740    163       O  
ATOM   5329  OE2 GLU B 355      -9.471  13.790  79.475  1.00208.43           O  
ANISOU 5329  OE2 GLU B 355    15236  35694  28265   6115   2241     90       O  
ATOM   5330  N   ASP B 356      -8.458   7.083  81.601  1.00191.77           N  
ANISOU 5330  N   ASP B 356    13973  34202  24687   7230   1831   2219       N  
ATOM   5331  CA  ASP B 356      -8.169   5.809  80.947  1.00180.72           C  
ANISOU 5331  CA  ASP B 356    12655  32602  23407   7390   1870   2668       C  
ATOM   5332  C   ASP B 356      -9.424   5.218  80.312  1.00177.19           C  
ANISOU 5332  C   ASP B 356    12472  31830  23024   7332   2236   2955       C  
ATOM   5333  O   ASP B 356      -9.478   5.007  79.096  1.00173.58           O  
ANISOU 5333  O   ASP B 356    11974  30990  22990   7287   2408   3086       O  
ATOM   5334  CB  ASP B 356      -7.555   4.826  81.948  1.00184.71           C  
ANISOU 5334  CB  ASP B 356    13256  33450  23475   7634   1615   2926       C  
ATOM   5335  CG  ASP B 356      -6.108   5.144  82.262  1.00187.63           C  
ANISOU 5335  CG  ASP B 356    13342  34062  23887   7727   1251   2734       C  
ATOM   5336  OD1 ASP B 356      -5.842   6.227  82.820  1.00189.46           O  
ANISOU 5336  OD1 ASP B 356    13411  34515  24060   7632   1106   2327       O  
ATOM   5337  OD2 ASP B 356      -5.236   4.304  81.952  1.00188.12           O  
ANISOU 5337  OD2 ASP B 356    13344  34094  24039   7897   1108   2990       O  
ATOM   5338  N   VAL B 357     -10.441   4.941  81.127  1.00180.05           N  
ANISOU 5338  N   VAL B 357    13107  32338  22966   7334   2357   3055       N  
ATOM   5339  CA  VAL B 357     -11.724   4.464  80.623  1.00175.05           C  
ANISOU 5339  CA  VAL B 357    12731  31419  22359   7265   2712   3294       C  
ATOM   5340  C   VAL B 357     -12.724   5.601  80.428  1.00172.89           C  
ANISOU 5340  C   VAL B 357    12461  31019  22210   7021   2939   2957       C  
ATOM   5341  O   VAL B 357     -13.656   5.458  79.622  1.00169.27           O  
ANISOU 5341  O   VAL B 357    12131  30225  21960   6921   3247   3080       O  
ATOM   5342  CB  VAL B 357     -12.310   3.382  81.559  1.00177.20           C  
ANISOU 5342  CB  VAL B 357    13322  31896  22108   7414   2738   3640       C  
ATOM   5343  CG1 VAL B 357     -13.495   2.679  80.912  1.00176.40           C  
ANISOU 5343  CG1 VAL B 357    13483  31472  22071   7373   3095   3955       C  
ATOM   5344  CG2 VAL B 357     -11.238   2.372  81.949  1.00180.02           C  
ANISOU 5344  CG2 VAL B 357    13665  32448  22288   7661   2466   3921       C  
ATOM   5345  N   ILE B 358     -12.544   6.732  81.120  1.00168.63           N  
ANISOU 5345  N   ILE B 358    11042  28547  24481   3741    793   4735       N  
ATOM   5346  CA  ILE B 358     -13.486   7.845  81.017  1.00178.13           C  
ANISOU 5346  CA  ILE B 358    12313  29631  25738   3555    881   4689       C  
ATOM   5347  C   ILE B 358     -13.497   8.428  79.609  1.00168.80           C  
ANISOU 5347  C   ILE B 358    11175  28215  24746   3428   1146   4694       C  
ATOM   5348  O   ILE B 358     -14.549   8.858  79.116  1.00174.62           O  
ANISOU 5348  O   ILE B 358    12130  28722  25494   3372   1288   4721       O  
ATOM   5349  CB  ILE B 358     -13.159   8.916  82.079  1.00188.50           C  
ANISOU 5349  CB  ILE B 358    13331  31207  27083   3350    705   4552       C  
ATOM   5350  CG1 ILE B 358     -13.253   8.311  83.481  1.00184.74           C  
ANISOU 5350  CG1 ILE B 358    12849  30948  26396   3488    439   4555       C  
ATOM   5351  CG2 ILE B 358     -14.082  10.123  81.947  1.00191.34           C  
ANISOU 5351  CG2 ILE B 358    13769  31428  27505   3131    806   4490       C  
ATOM   5352  CD1 ILE B 358     -13.145   9.321  84.605  1.00181.17           C  
ANISOU 5352  CD1 ILE B 358    12174  30733  25931   3290    251   4421       C  
ATOM   5353  N   GLY B 359     -12.343   8.450  78.940  1.00153.06           N  
ANISOU 5353  N   GLY B 359     8984  26268  22903   3382   1217   4667       N  
ATOM   5354  CA  GLY B 359     -12.295   8.981  77.586  1.00143.72           C  
ANISOU 5354  CA  GLY B 359     7848  24863  21896   3264   1472   4671       C  
ATOM   5355  C   GLY B 359     -13.192   8.226  76.624  1.00143.82           C  
ANISOU 5355  C   GLY B 359     8241  24565  21838   3423   1645   4805       C  
ATOM   5356  O   GLY B 359     -13.903   8.831  75.817  1.00155.06           O  
ANISOU 5356  O   GLY B 359     9827  25753  23336   3322   1826   4816       O  
ATOM   5357  N   ALA B 360     -13.170   6.893  76.693  1.00141.05           N  
ANISOU 5357  N   ALA B 360     8045  24206  21342   3667   1590   4907       N  
ATOM   5358  CA  ALA B 360     -14.092   6.101  75.886  1.00144.25           C  
ANISOU 5358  CA  ALA B 360     8830  24325  21653   3818   1731   5034       C  
ATOM   5359  C   ALA B 360     -15.532   6.293  76.345  1.00168.77           C  
ANISOU 5359  C   ALA B 360    12184  27304  24637   3826   1707   5054       C  
ATOM   5360  O   ALA B 360     -16.452   6.349  75.520  1.00165.64           O  
ANISOU 5360  O   ALA B 360    12057  26633  24244   3826   1870   5112       O  
ATOM   5361  CB  ALA B 360     -13.701   4.624  75.937  1.00137.69           C  
ANISOU 5361  CB  ALA B 360     8099  23529  20688   4063   1669   5131       C  
ATOM   5362  N   LEU B 361     -15.748   6.392  77.660  1.00169.91           N  
ANISOU 5362  N   LEU B 361    12242  27645  24671   3833   1504   5006       N  
ATOM   5363  CA  LEU B 361     -17.100   6.571  78.181  1.00139.74           C  
ANISOU 5363  CA  LEU B 361     8644  23719  20733   3844   1474   5021       C  
ATOM   5364  C   LEU B 361     -17.670   7.934  77.805  1.00143.47           C  
ANISOU 5364  C   LEU B 361     9094  24070  21349   3618   1598   4954       C  
ATOM   5365  O   LEU B 361     -18.873   8.058  77.556  1.00154.19           O  
ANISOU 5365  O   LEU B 361    10714  25207  22663   3627   1686   4995       O  
ATOM   5366  CB  LEU B 361     -17.112   6.382  79.698  1.00134.12           C  
ANISOU 5366  CB  LEU B 361     7829  23261  19869   3901   1224   4982       C  
ATOM   5367  CG  LEU B 361     -16.996   4.938  80.192  1.00134.30           C  
ANISOU 5367  CG  LEU B 361     7986  23343  19697   4150   1105   5065       C  
ATOM   5368  CD1 LEU B 361     -17.114   4.874  81.707  1.00135.37           C  
ANISOU 5368  CD1 LEU B 361     8040  23714  19680   4191    862   5021       C  
ATOM   5369  CD2 LEU B 361     -18.050   4.063  79.531  1.00131.24           C  
ANISOU 5369  CD2 LEU B 361     8002  22663  19199   4301   1236   5182       C  
ATOM   5370  N   LEU B 362     -16.829   8.970  77.768  1.00135.40           N  
ANISOU 5370  N   LEU B 362     7764  23184  20497   3406   1608   4849       N  
ATOM   5371  CA  LEU B 362     -17.315  10.302  77.415  1.00148.86           C  
ANISOU 5371  CA  LEU B 362     9443  24773  22344   3171   1733   4779       C  
ATOM   5372  C   LEU B 362     -17.853  10.341  75.988  1.00156.89           C  
ANISOU 5372  C   LEU B 362    10713  25453  23445   3168   1985   4846       C  
ATOM   5373  O   LEU B 362     -18.911  10.929  75.728  1.00163.20           O  
ANISOU 5373  O   LEU B 362    11736  26026  24246   3079   2077   4829       O  
ATOM   5374  CB  LEU B 362     -16.199  11.330  77.598  1.00136.19           C  
ANISOU 5374  CB  LEU B 362     7505  23352  20891   2924   1694   4629       C  
ATOM   5375  CG  LEU B 362     -16.158  12.060  78.941  1.00137.70           C  
ANISOU 5375  CG  LEU B 362     7615  23710  20994   2747   1471   4455       C  
ATOM   5376  CD1 LEU B 362     -14.766  12.597  79.220  1.00141.15           C  
ANISOU 5376  CD1 LEU B 362     7655  24415  21560   2594   1388   4348       C  
ATOM   5377  CD2 LEU B 362     -17.169  13.192  78.944  1.00137.20           C  
ANISOU 5377  CD2 LEU B 362     7807  23401  20922   2514   1531   4327       C  
ATOM   5378  N   ASN B 363     -17.142   9.717  75.049  1.00173.53           N  
ANISOU 5378  N   ASN B 363    12839  27492  25602   3250   2087   4901       N  
ATOM   5379  CA  ASN B 363     -17.589   9.741  73.661  1.00172.83           C  
ANISOU 5379  CA  ASN B 363    12991  27090  25588   3246   2320   4966       C  
ATOM   5380  C   ASN B 363     -18.873   8.943  73.474  1.00192.82           C  
ANISOU 5380  C   ASN B 363    15907  29394  27962   3423   2350   5077       C  
ATOM   5381  O   ASN B 363     -19.785   9.383  72.762  1.00190.11           O  
ANISOU 5381  O   ASN B 363    15781  28791  27660   3367   2498   5100       O  
ATOM   5382  CB  ASN B 363     -16.483   9.225  72.746  1.00172.99           C  
ANISOU 5382  CB  ASN B 363    12932  27108  25689   3295   2414   4999       C  
ATOM   5383  CG  ASN B 363     -15.343  10.209  72.615  1.00180.80           C  
ANISOU 5383  CG  ASN B 363    13579  28243  26872   3079   2450   4884       C  
ATOM   5384  OD1 ASN B 363     -15.314  11.021  71.690  1.00187.56           O  
ANISOU 5384  OD1 ASN B 363    14448  28936  27879   2920   2635   4852       O  
ATOM   5385  ND2 ASN B 363     -14.398  10.149  73.546  1.00180.88           N  
ANISOU 5385  ND2 ASN B 363    13289  28557  26879   3068   2271   4815       N  
ATOM   5386  N   VAL B 364     -18.979   7.774  74.110  1.00174.57           N  
ANISOU 5386  N   VAL B 364    13692  27169  25468   3632   2210   5142       N  
ATOM   5387  CA  VAL B 364     -20.238   7.047  74.025  1.00165.98           C  
ANISOU 5387  CA  VAL B 364    12968  25871  24226   3781   2229   5235       C  
ATOM   5388  C   VAL B 364     -21.342   7.776  74.782  1.00156.50           C  
ANISOU 5388  C   VAL B 364    11832  24643  22989   3704   2176   5187       C  
ATOM   5389  O   VAL B 364     -22.519   7.557  74.500  1.00151.29           O  
ANISOU 5389  O   VAL B 364    11473  23753  22258   3766   2241   5244       O  
ATOM   5390  CB  VAL B 364     -20.089   5.590  74.507  1.00158.63           C  
ANISOU 5390  CB  VAL B 364    12144  25025  23103   4013   2105   5315       C  
ATOM   5391  CG1 VAL B 364     -19.060   4.850  73.659  1.00142.39           C  
ANISOU 5391  CG1 VAL B 364    10046  22968  21087   4091   2180   5371       C  
ATOM   5392  CG2 VAL B 364     -19.726   5.531  75.975  1.00153.11           C  
ANISOU 5392  CG2 VAL B 364    11237  24626  22313   4039   1876   5255       C  
ATOM   5393  N   PHE B 365     -21.001   8.679  75.706  1.00151.21           N  
ANISOU 5393  N   PHE B 365    10885  24193  22373   3558   2065   5082       N  
ATOM   5394  CA  PHE B 365     -22.025   9.543  76.293  1.00148.55           C  
ANISOU 5394  CA  PHE B 365    10662  23775  22007   3424   2032   4998       C  
ATOM   5395  C   PHE B 365     -22.492  10.599  75.295  1.00142.34           C  
ANISOU 5395  C   PHE B 365    10020  22705  21356   3219   2219   4935       C  
ATOM   5396  O   PHE B 365     -23.676  10.964  75.269  1.00141.80           O  
ANISOU 5396  O   PHE B 365    10234  22408  21235   3165   2255   4904       O  
ATOM   5397  CB  PHE B 365     -21.498  10.203  77.568  1.00148.87           C  
ANISOU 5397  CB  PHE B 365    10501  24059  22005   3265   1826   4835       C  
ATOM   5398  CG  PHE B 365     -21.291   9.246  78.709  1.00139.37           C  
ANISOU 5398  CG  PHE B 365     9219  23104  20632   3457   1620   4882       C  
ATOM   5399  CD1 PHE B 365     -21.893   7.998  78.706  1.00127.72           C  
ANISOU 5399  CD1 PHE B 365     7922  21581  19025   3732   1620   5040       C  
ATOM   5400  CD2 PHE B 365     -20.492   9.595  79.786  1.00130.19           C  
ANISOU 5400  CD2 PHE B 365     7808  22220  19439   3361   1424   4766       C  
ATOM   5401  CE1 PHE B 365     -21.701   7.116  79.753  1.00125.09           C  
ANISOU 5401  CE1 PHE B 365     7551  21454  18522   3900   1429   5071       C  
ATOM   5402  CE2 PHE B 365     -20.297   8.718  80.836  1.00129.40           C  
ANISOU 5402  CE2 PHE B 365     7644  22345  19177   3541   1229   4809       C  
ATOM   5403  CZ  PHE B 365     -20.902   7.477  80.820  1.00127.71           C  
ANISOU 5403  CZ  PHE B 365     7616  22077  18831   3818   1236   4969       C  
ATOM   5404  N   VAL B 366     -21.574  11.110  74.474  1.00122.75           N  
ANISOU 5404  N   VAL B 366     7350  20237  19053   3102   2341   4914       N  
ATOM   5405  CA  VAL B 366     -21.984  11.966  73.359  1.00137.82           C  
ANISOU 5405  CA  VAL B 366     9414  21860  21091   2942   2543   4883       C  
ATOM   5406  C   VAL B 366     -22.927  11.200  72.438  1.00155.51           C  
ANISOU 5406  C   VAL B 366    11951  23840  23295   3130   2684   5041       C  
ATOM   5407  O   VAL B 366     -23.954  11.726  71.981  1.00151.51           O  
ANISOU 5407  O   VAL B 366    11713  23061  22794   3049   2776   5016       O  
ATOM   5408  CB  VAL B 366     -20.756  12.491  72.590  1.00123.60           C  
ANISOU 5408  CB  VAL B 366     7352  20126  19485   2812   2662   4852       C  
ATOM   5409  CG1 VAL B 366     -21.152  13.633  71.672  1.00122.71           C  
ANISOU 5409  CG1 VAL B 366     7389  19737  19497   2591   2841   4776       C  
ATOM   5410  CG2 VAL B 366     -19.675  12.938  73.541  1.00143.58           C  
ANISOU 5410  CG2 VAL B 366     9546  22964  22042   2682   2502   4725       C  
ATOM   5411  N   TRP B 367     -22.591   9.941  72.155  1.00152.58           N  
ANISOU 5411  N   TRP B 367    11614  23509  22849   3355   2676   5166       N  
ATOM   5412  CA  TRP B 367     -23.473   9.104  71.348  1.00149.66           C  
ANISOU 5412  CA  TRP B 367    11610  22867  22388   3508   2766   5279       C  
ATOM   5413  C   TRP B 367     -24.786   8.814  72.068  1.00154.16           C  
ANISOU 5413  C   TRP B 367    12402  23361  22811   3599   2682   5303       C  
ATOM   5414  O   TRP B 367     -25.807   8.598  71.416  1.00153.57           O  
ANISOU 5414  O   TRP B 367    12630  23019  22701   3652   2777   5364       O  
ATOM   5415  CB  TRP B 367     -22.765   7.804  70.959  1.00152.91           C  
ANISOU 5415  CB  TRP B 367    12069  23317  22711   3685   2749   5367       C  
ATOM   5416  CG  TRP B 367     -21.570   8.040  70.085  1.00170.15           C  
ANISOU 5416  CG  TRP B 367    14076  25530  25044   3608   2859   5355       C  
ATOM   5417  CD1 TRP B 367     -20.263   7.836  70.413  1.00166.31           C  
ANISOU 5417  CD1 TRP B 367    13304  25293  24593   3610   2783   5320       C  
ATOM   5418  CD2 TRP B 367     -21.571   8.549  68.745  1.00157.83           C  
ANISOU 5418  CD2 TRP B 367    12611  23736  23620   3514   3068   5373       C  
ATOM   5419  NE1 TRP B 367     -19.451   8.181  69.362  1.00147.52           N  
ANISOU 5419  NE1 TRP B 367    10834  22851  22367   3522   2937   5313       N  
ATOM   5420  CE2 TRP B 367     -20.229   8.622  68.325  1.00145.49           C  
ANISOU 5420  CE2 TRP B 367    10812  22298  22171   3462   3115   5346       C  
ATOM   5421  CE3 TRP B 367     -22.577   8.942  67.858  1.00150.35           C  
ANISOU 5421  CE3 TRP B 367    11932  22485  22710   3473   3219   5409       C  
ATOM   5422  CZ2 TRP B 367     -19.867   9.074  67.058  1.00145.61           C  
ANISOU 5422  CZ2 TRP B 367    10855  22140  22329   3368   3312   5355       C  
ATOM   5423  CZ3 TRP B 367     -22.215   9.393  66.602  1.00140.92           C  
ANISOU 5423  CZ3 TRP B 367    10768  21121  21655   3382   3408   5419       C  
ATOM   5424  CH2 TRP B 367     -20.873   9.452  66.213  1.00143.30           C  
ANISOU 5424  CH2 TRP B 367    10836  21549  22061   3330   3456   5393       C  
ATOM   5425  N   ILE B 368     -24.786   8.823  73.402  1.00146.61           N  
ANISOU 5425  N   ILE B 368    11302  22634  21769   3615   2504   5253       N  
ATOM   5426  CA  ILE B 368     -26.029   8.682  74.158  1.00132.98           C  
ANISOU 5426  CA  ILE B 368     9772  20841  19914   3681   2428   5259       C  
ATOM   5427  C   ILE B 368     -26.902   9.921  73.989  1.00126.64           C  
ANISOU 5427  C   ILE B 368     9154  19802  19162   3448   2487   5130       C  
ATOM   5428  O   ILE B 368     -28.128   9.824  73.881  1.00120.93           O  
ANISOU 5428  O   ILE B 368     8715  18860  18374   3489   2521   5155       O  
ATOM   5429  CB  ILE B 368     -25.721   8.396  75.640  1.00116.14           C  
ANISOU 5429  CB  ILE B 368     7497  18987  17642   3721   2201   5202       C  
ATOM   5430  CG1 ILE B 368     -25.304   6.936  75.827  1.00115.01           C  
ANISOU 5430  CG1 ILE B 368     7402  18948  17350   3950   2116   5300       C  
ATOM   5431  CG2 ILE B 368     -26.915   8.722  76.524  1.00113.27           C  
ANISOU 5431  CG2 ILE B 368     7362  18526  17149   3663   2107   5117       C  
ATOM   5432  CD1 ILE B 368     -24.946   6.585  77.253  1.00117.57           C  
ANISOU 5432  CD1 ILE B 368     7566  19562  17544   4020   1899   5267       C  
ATOM   5433  N   GLY B 369     -26.289  11.104  73.976  1.00129.52           N  
ANISOU 5433  N   GLY B 369     9360  20207  19646   3201   2499   4988       N  
ATOM   5434  CA  GLY B 369     -27.050  12.311  73.676  1.00133.48           C  
ANISOU 5434  CA  GLY B 369    10036  20468  20210   2979   2578   4871       C  
ATOM   5435  C   GLY B 369     -27.629  12.291  72.272  1.00136.64           C  
ANISOU 5435  C   GLY B 369    10651  20566  20697   3013   2783   4964       C  
ATOM   5436  O   GLY B 369     -28.784  12.677  72.048  1.00134.53           O  
ANISOU 5436  O   GLY B 369    10651  20052  20412   2968   2834   4942       O  
ATOM   5437  N   TYR B 370     -26.836  11.830  71.306  1.00128.01           N  
ANISOU 5437  N   TYR B 370     9448  19490  19700   3098   2903   5071       N  
ATOM   5438  CA  TYR B 370     -27.358  11.651  69.954  1.00132.23           C  
ANISOU 5438  CA  TYR B 370    10196  19744  20301   3160   3094   5178       C  
ATOM   5439  C   TYR B 370     -28.474  10.608  69.932  1.00129.20           C  
ANISOU 5439  C   TYR B 370    10074  19229  19785   3386   3083   5307       C  
ATOM   5440  O   TYR B 370     -29.453  10.736  69.186  1.00124.38           O  
ANISOU 5440  O   TYR B 370     9730  18339  19189   3390   3189   5343       O  
ATOM   5441  CB  TYR B 370     -26.222  11.262  69.011  1.00117.87           C  
ANISOU 5441  CB  TYR B 370     8196  17991  18599   3222   3219   5272       C  
ATOM   5442  CG  TYR B 370     -25.098  12.276  68.959  1.00114.35           C  
ANISOU 5442  CG  TYR B 370     7485  17667  18296   2997   3247   5148       C  
ATOM   5443  CD1 TYR B 370     -25.344  13.628  69.160  1.00118.22           C  
ANISOU 5443  CD1 TYR B 370     8006  18069  18843   2732   3246   4980       C  
ATOM   5444  CD2 TYR B 370     -23.791  11.879  68.714  1.00128.93           C  
ANISOU 5444  CD2 TYR B 370     9062  19710  20216   3043   3270   5190       C  
ATOM   5445  CE1 TYR B 370     -24.318  14.556  69.114  1.00126.20           C  
ANISOU 5445  CE1 TYR B 370     8777  19188  19983   2519   3275   4863       C  
ATOM   5446  CE2 TYR B 370     -22.760  12.798  68.665  1.00120.46           C  
ANISOU 5446  CE2 TYR B 370     7727  18755  19286   2838   3304   5080       C  
ATOM   5447  CZ  TYR B 370     -23.028  14.134  68.866  1.00121.83           C  
ANISOU 5447  CZ  TYR B 370     7941  18837  19512   2570   3303   4913       C  
ATOM   5448  OH  TYR B 370     -22.002  15.049  68.821  1.00119.88           O  
ANISOU 5448  OH  TYR B 370     7448  18701  19401   2354   3335   4793       O  
ATOM   5449  N   LEU B 371     -28.351   9.574  70.763  1.00122.51           N  
ANISOU 5449  N   LEU B 371     9163  18580  18806   3573   2950   5372       N  
ATOM   5450  CA  LEU B 371     -29.412   8.586  70.893  1.00118.40           C  
ANISOU 5450  CA  LEU B 371     8953  17921  18113   3740   2900   5447       C  
ATOM   5451  C   LEU B 371     -30.670   9.203  71.485  1.00125.20           C  
ANISOU 5451  C   LEU B 371     9962  18662  18945   3677   2867   5382       C  
ATOM   5452  O   LEU B 371     -31.775   8.777  71.157  1.00117.28           O  
ANISOU 5452  O   LEU B 371     9224  17450  17885   3776   2912   5452       O  
ATOM   5453  CB  LEU B 371     -28.929   7.416  71.749  1.00105.82           C  
ANISOU 5453  CB  LEU B 371     7316  16546  16346   3896   2738   5479       C  
ATOM   5454  CG  LEU B 371     -29.822   6.177  71.804  1.00113.98           C  
ANISOU 5454  CG  LEU B 371     8675  17450  17182   4065   2695   5560       C  
ATOM   5455  CD1 LEU B 371     -30.099   5.659  70.402  1.00112.92           C  
ANISOU 5455  CD1 LEU B 371     8802  17051  17052   4103   2840   5648       C  
ATOM   5456  CD2 LEU B 371     -29.177   5.098  72.658  1.00120.65           C  
ANISOU 5456  CD2 LEU B 371     9446  18527  17869   4199   2546   5582       C  
ATOM   5457  N   SER B 372     -30.524  10.190  72.370  1.00149.88           N  
ANISOU 5457  N   SER B 372    12986  21889  22074   3477   2765   5216       N  
ATOM   5458  CA  SER B 372     -31.688  10.929  72.857  1.00158.59           C  
ANISOU 5458  CA  SER B 372    14295  22828  23133   3354   2729   5108       C  
ATOM   5459  C   SER B 372     -32.349  11.705  71.725  1.00158.82           C  
ANISOU 5459  C   SER B 372    14519  22545  23280   3237   2892   5093       C  
ATOM   5460  O   SER B 372     -33.587  11.740  71.609  1.00164.29           O  
ANISOU 5460  O   SER B 372    15473  23017  23934   3259   2918   5101       O  
ATOM   5461  CB  SER B 372     -31.281  11.880  73.981  1.00159.71           C  
ANISOU 5461  CB  SER B 372    14275  23144  23262   3151   2596   4929       C  
ATOM   5462  OG  SER B 372     -30.436  12.910  73.500  1.00149.54           O  
ANISOU 5462  OG  SER B 372    12822  21872  22124   2943   2665   4837       O  
ATOM   5463  N   SER B 373     -31.527  12.351  70.892  1.00127.58           N  
ANISOU 5463  N   SER B 373    10438  18567  19469   3110   3002   5068       N  
ATOM   5464  CA  SER B 373     -32.038  12.973  69.673  1.00134.09           C  
ANISOU 5464  CA  SER B 373    11447  19094  20406   3023   3170   5076       C  
ATOM   5465  C   SER B 373     -32.805  11.969  68.822  1.00124.74           C  
ANISOU 5465  C   SER B 373    10492  17719  19186   3238   3258   5244       C  
ATOM   5466  O   SER B 373     -33.779  12.330  68.155  1.00110.50           O  
ANISOU 5466  O   SER B 373     8931  15639  17414   3205   3345   5249       O  
ATOM   5467  CB  SER B 373     -30.890  13.576  68.861  1.00124.05           C  
ANISOU 5467  CB  SER B 373     9992  17853  19289   2893   3285   5052       C  
ATOM   5468  OG  SER B 373     -30.083  14.430  69.653  1.00115.80           O  
ANISOU 5468  OG  SER B 373     8712  17007  18278   2700   3200   4901       O  
ATOM   5469  N   ALA B 374     -32.367  10.710  68.826  1.00112.28           N  
ANISOU 5469  N   ALA B 374     8838  16281  17542   3458   3237   5381       N  
ATOM   5470  CA  ALA B 374     -33.059   9.668  68.074  1.00103.71           C  
ANISOU 5470  CA  ALA B 374     7987  15021  16397   3657   3304   5533       C  
ATOM   5471  C   ALA B 374     -34.337   9.198  68.768  1.00107.91           C  
ANISOU 5471  C   ALA B 374     8741  15472  16788   3749   3210   5539       C  
ATOM   5472  O   ALA B 374     -35.314   8.850  68.095  1.00 93.73           O  
ANISOU 5472  O   ALA B 374     7246  13422  14945   3795   3260   5589       O  
ATOM   5473  CB  ALA B 374     -32.125   8.478  67.842  1.00 98.47           C  
ANISOU 5473  CB  ALA B 374     7304  14481  15631   3776   3263   5608       C  
ATOM   5474  N   VAL B 375     -34.342   9.147  70.103  1.00107.90           N  
ANISOU 5474  N   VAL B 375     8618  15677  16702   3763   3064   5480       N  
ATOM   5475  CA  VAL B 375     -35.465   8.543  70.820  1.00 94.97           C  
ANISOU 5475  CA  VAL B 375     7181  13986  14919   3871   2975   5495       C  
ATOM   5476  C   VAL B 375     -36.623   9.506  71.028  1.00104.57           C  
ANISOU 5476  C   VAL B 375     8575  15000  16156   3727   2977   5385       C  
ATOM   5477  O   VAL B 375     -37.748   9.051  71.282  1.00116.81           O  
ANISOU 5477  O   VAL B 375    10331  16429  17622   3821   2953   5418       O  
ATOM   5478  CB  VAL B 375     -35.075   7.979  72.200  1.00 96.22           C  
ANISOU 5478  CB  VAL B 375     7193  14427  14940   3950   2806   5473       C  
ATOM   5479  CG1 VAL B 375     -34.002   6.904  72.073  1.00111.95           C  
ANISOU 5479  CG1 VAL B 375     9123  16578  16835   4045   2758   5532       C  
ATOM   5480  CG2 VAL B 375     -34.653   9.095  73.149  1.00 97.94           C  
ANISOU 5480  CG2 VAL B 375     7236  14795  15183   3741   2707   5301       C  
ATOM   5481  N   ASN B 376     -36.394  10.818  70.956  1.00110.78           N  
ANISOU 5481  N   ASN B 376     9301  15743  17046   3492   3001   5247       N  
ATOM   5482  CA  ASN B 376     -37.536  11.732  71.007  1.00101.37           C  
ANISOU 5482  CA  ASN B 376     8311  14325  15879   3356   3017   5147       C  
ATOM   5483  C   ASN B 376     -38.568  11.416  69.925  1.00 94.46           C  
ANISOU 5483  C   ASN B 376     7702  13154  15036   3449   3133   5247       C  
ATOM   5484  O   ASN B 376     -39.766  11.314  70.253  1.00 92.89           O  
ANISOU 5484  O   ASN B 376     7700  12817  14778   3487   3102   5237       O  
ATOM   5485  CB  ASN B 376     -37.053  13.188  70.934  1.00 98.08           C  
ANISOU 5485  CB  ASN B 376     7794  13894  15580   3091   3047   4994       C  
ATOM   5486  CG  ASN B 376     -36.220  13.591  72.136  1.00111.96           C  
ANISOU 5486  CG  ASN B 376     9315  15929  17296   2980   2914   4873       C  
ATOM   5487  OD1 ASN B 376     -36.322  12.994  73.208  1.00104.43           O  
ANISOU 5487  OD1 ASN B 376     8325  15141  16213   3071   2785   4872       O  
ATOM   5488  ND2 ASN B 376     -35.391  14.615  71.963  1.00114.18           N  
ANISOU 5488  ND2 ASN B 376     9440  16260  17685   2778   2947   4769       N  
ATOM   5489  N   PRO B 377     -38.194  11.221  68.651  1.00 90.74           N  
ANISOU 5489  N   PRO B 377     7252  12573  14652   3493   3263   5347       N  
ATOM   5490  CA  PRO B 377     -39.184  10.731  67.676  1.00 88.57           C  
ANISOU 5490  CA  PRO B 377     7235  12032  14386   3611   3356   5458       C  
ATOM   5491  C   PRO B 377     -39.787   9.387  68.044  1.00 87.34           C  
ANISOU 5491  C   PRO B 377     7239  11893  14054   3786   3275   5538       C  
ATOM   5492  O   PRO B 377     -40.960   9.141  67.738  1.00103.30           O  
ANISOU 5492  O   PRO B 377     9544  13698  16008   3790   3279   5539       O  
ATOM   5493  CB  PRO B 377     -38.377  10.645  66.373  1.00 89.59           C  
ANISOU 5493  CB  PRO B 377     7321  12103  14618   3627   3495   5548       C  
ATOM   5494  CG  PRO B 377     -37.289  11.636  66.544  1.00102.75           C  
ANISOU 5494  CG  PRO B 377     8761  13908  16372   3432   3499   5432       C  
ATOM   5495  CD  PRO B 377     -36.919  11.563  67.992  1.00111.07           C  
ANISOU 5495  CD  PRO B 377     9633  15234  17334   3415   3342   5350       C  
ATOM   5496  N   LEU B 378     -39.022   8.501  68.687  1.00 88.42           N  
ANISOU 5496  N   LEU B 378     7262  12269  14065   3865   3181   5561       N  
ATOM   5497  CA  LEU B 378     -39.582   7.215  69.090  1.00 87.34           C  
ANISOU 5497  CA  LEU B 378     7336  12141  13709   3958   3091   5585       C  
ATOM   5498  C   LEU B 378     -40.674   7.393  70.138  1.00 90.28           C  
ANISOU 5498  C   LEU B 378     7791  12490  14020   3962   3009   5519       C  
ATOM   5499  O   LEU B 378     -41.681   6.681  70.116  1.00 99.03           O  
ANISOU 5499  O   LEU B 378     9165  13470  14993   3980   2990   5512       O  
ATOM   5500  CB  LEU B 378     -38.486   6.290  69.614  1.00100.64           C  
ANISOU 5500  CB  LEU B 378     8867  14090  15282   4044   3010   5619       C  
ATOM   5501  CG  LEU B 378     -38.949   4.843  69.809  1.00 87.78           C  
ANISOU 5501  CG  LEU B 378     7467  12459  13427   4129   2953   5646       C  
ATOM   5502  CD1 LEU B 378     -39.129   4.151  68.463  1.00 86.51           C  
ANISOU 5502  CD1 LEU B 378     7533  12115  13222   4117   3059   5703       C  
ATOM   5503  CD2 LEU B 378     -37.992   4.065  70.699  1.00 89.43           C  
ANISOU 5503  CD2 LEU B 378     7508  12946  13526   4222   2846   5661       C  
ATOM   5504  N   VAL B 379     -40.492   8.333  71.069  1.00 87.65           N  
ANISOU 5504  N   VAL B 379     7225  12291  13786   3930   2968   5459       N  
ATOM   5505  CA  VAL B 379     -41.543   8.625  72.040  1.00 98.71           C  
ANISOU 5505  CA  VAL B 379     8700  13654  15151   3932   2906   5398       C  
ATOM   5506  C   VAL B 379     -42.762   9.222  71.345  1.00 95.33           C  
ANISOU 5506  C   VAL B 379     8506  12913  14802   3864   2989   5374       C  
ATOM   5507  O   VAL B 379     -43.912   8.860  71.652  1.00 83.58           O  
ANISOU 5507  O   VAL B 379     7248  11297  13210   3877   2952   5346       O  
ATOM   5508  CB  VAL B 379     -41.003   9.550  73.146  1.00 88.70           C  
ANISOU 5508  CB  VAL B 379     7250  12572  13878   3763   2806   5243       C  
ATOM   5509  CG1 VAL B 379     -42.141  10.093  73.995  1.00 96.55           C  
ANISOU 5509  CG1 VAL B 379     8393  13467  14826   3679   2750   5130       C  
ATOM   5510  CG2 VAL B 379     -40.011   8.799  74.012  1.00 90.35           C  
ANISOU 5510  CG2 VAL B 379     7255  13092  13982   3863   2697   5272       C  
ATOM   5511  N   TYR B 380     -42.534  10.149  70.403  1.00 99.06           N  
ANISOU 5511  N   TYR B 380     8972  13249  15418   3733   3087   5343       N  
ATOM   5512  CA  TYR B 380     -43.644  10.667  69.603  1.00 83.51           C  
ANISOU 5512  CA  TYR B 380     7230  10972  13527   3683   3169   5335       C  
ATOM   5513  C   TYR B 380     -44.422   9.527  68.961  1.00 93.41           C  
ANISOU 5513  C   TYR B 380     8780  12080  14632   3739   3171   5385       C  
ATOM   5514  O   TYR B 380     -45.658   9.535  68.941  1.00 91.09           O  
ANISOU 5514  O   TYR B 380     8710  11610  14289   3697   3162   5331       O  
ATOM   5515  CB  TYR B 380     -43.138  11.621  68.516  1.00 84.00           C  
ANISOU 5515  CB  TYR B 380     7269  10911  13735   3538   3278   5306       C  
ATOM   5516  CG  TYR B 380     -42.312  12.794  68.996  1.00 85.88           C  
ANISOU 5516  CG  TYR B 380     7325  11275  14031   3321   3252   5158       C  
ATOM   5517  CD1 TYR B 380     -42.427  13.277  70.293  1.00 86.67           C  
ANISOU 5517  CD1 TYR B 380     7354  11506  14070   3223   3140   5027       C  
ATOM   5518  CD2 TYR B 380     -41.417  13.424  68.141  1.00 98.19           C  
ANISOU 5518  CD2 TYR B 380     8786  12816  15704   3211   3344   5147       C  
ATOM   5519  CE1 TYR B 380     -41.667  14.350  70.725  1.00 88.45           C  
ANISOU 5519  CE1 TYR B 380     7415  11844  14346   3019   3115   4889       C  
ATOM   5520  CE2 TYR B 380     -40.654  14.494  68.562  1.00112.11           C  
ANISOU 5520  CE2 TYR B 380    10381  14693  17523   3006   3324   5009       C  
ATOM   5521  CZ  TYR B 380     -40.782  14.954  69.854  1.00110.03           C  
ANISOU 5521  CZ  TYR B 380    10049  14561  17198   2910   3207   4880       C  
ATOM   5522  OH  TYR B 380     -40.021  16.021  70.275  1.00110.28           O  
ANISOU 5522  OH  TYR B 380     9916  14703  17282   2701   3186   4740       O  
ATOM   5523  N   THR B 381     -43.705   8.536  68.427  1.00125.38           N  
ANISOU 5523  N   THR B 381    12842  16215  18580   3782   3179   5447       N  
ATOM   5524  CA  THR B 381     -44.351   7.362  67.849  1.00125.87           C  
ANISOU 5524  CA  THR B 381    13170  16191  18465   3777   3183   5443       C  
ATOM   5525  C   THR B 381     -45.124   6.584  68.907  1.00123.94           C  
ANISOU 5525  C   THR B 381    13024  16018  18048   3814   3082   5385       C  
ATOM   5526  O   THR B 381     -46.266   6.170  68.683  1.00120.23           O  
ANISOU 5526  O   THR B 381    12779  15417  17487   3761   3085   5313       O  
ATOM   5527  CB  THR B 381     -43.303   6.459  67.197  1.00122.48           C  
ANISOU 5527  CB  THR B 381    12697  15869  17971   3826   3216   5522       C  
ATOM   5528  OG1 THR B 381     -42.391   7.252  66.428  1.00134.77           O  
ANISOU 5528  OG1 THR B 381    14103  17399  19703   3805   3305   5579       O  
ATOM   5529  CG2 THR B 381     -43.970   5.432  66.294  1.00120.86           C  
ANISOU 5529  CG2 THR B 381    12747  15551  17623   3790   3261   5496       C  
ATOM   5530  N   LEU B 382     -44.509   6.377  70.071  1.00 95.48           N  
ANISOU 5530  N   LEU B 382     9243  12636  14400   3898   2992   5401       N  
ATOM   5531  CA  LEU B 382     -45.086   5.487  71.073  1.00 99.32           C  
ANISOU 5531  CA  LEU B 382     9822  13207  14708   3948   2903   5360       C  
ATOM   5532  C   LEU B 382     -46.409   6.016  71.606  1.00104.93           C  
ANISOU 5532  C   LEU B 382    10661  13777  15431   3899   2883   5276       C  
ATOM   5533  O   LEU B 382     -47.378   5.258  71.738  1.00103.49           O  
ANISOU 5533  O   LEU B 382    10677  13530  15114   3882   2866   5215       O  
ATOM   5534  CB  LEU B 382     -44.101   5.278  72.224  1.00 82.31           C  
ANISOU 5534  CB  LEU B 382     7435  11328  12512   4047   2806   5391       C  
ATOM   5535  CG  LEU B 382     -42.967   4.276  72.002  1.00 84.87           C  
ANISOU 5535  CG  LEU B 382     7680  11822  12744   4117   2793   5457       C  
ATOM   5536  CD1 LEU B 382     -42.119   4.146  73.259  1.00 86.48           C  
ANISOU 5536  CD1 LEU B 382     7653  12305  12901   4205   2680   5464       C  
ATOM   5537  CD2 LEU B 382     -43.523   2.923  71.586  1.00 88.80           C  
ANISOU 5537  CD2 LEU B 382     8425  12251  13063   4125   2814   5447       C  
ATOM   5538  N   PHE B 383     -46.479   7.311  71.918  1.00105.29           N  
ANISOU 5538  N   PHE B 383    10586  13778  15643   3870   2892   5261       N  
ATOM   5539  CA  PHE B 383     -47.614   7.816  72.688  1.00 91.47           C  
ANISOU 5539  CA  PHE B 383     8921  11930  13902   3844   2861   5188       C  
ATOM   5540  C   PHE B 383     -48.706   8.441  71.824  1.00 85.97           C  
ANISOU 5540  C   PHE B 383     8420  10956  13288   3734   2934   5129       C  
ATOM   5541  O   PHE B 383     -49.863   8.014  71.888  1.00 93.76           O  
ANISOU 5541  O   PHE B 383     9610  11836  14178   3692   2920   5052       O  
ATOM   5542  CB  PHE B 383     -47.112   8.800  73.751  1.00 91.85           C  
ANISOU 5542  CB  PHE B 383     8707  12121  14069   3882   2821   5185       C  
ATOM   5543  CG  PHE B 383     -46.323   8.136  74.840  1.00 86.78           C  
ANISOU 5543  CG  PHE B 383     7898  11766  13310   3981   2722   5209       C  
ATOM   5544  CD1 PHE B 383     -46.965   7.553  75.919  1.00108.92           C  
ANISOU 5544  CD1 PHE B 383    10793  14625  15967   4037   2643   5177       C  
ATOM   5545  CD2 PHE B 383     -44.942   8.066  74.769  1.00 83.86           C  
ANISOU 5545  CD2 PHE B 383     7284  11610  12968   4015   2707   5259       C  
ATOM   5546  CE1 PHE B 383     -46.244   6.928  76.917  1.00114.94           C  
ANISOU 5546  CE1 PHE B 383    11414  15648  16610   4132   2547   5199       C  
ATOM   5547  CE2 PHE B 383     -44.215   7.444  75.765  1.00 85.22           C  
ANISOU 5547  CE2 PHE B 383     7307  12052  13022   4102   2604   5274       C  
ATOM   5548  CZ  PHE B 383     -44.867   6.873  76.839  1.00 84.89           C  
ANISOU 5548  CZ  PHE B 383     7366  12058  12829   4165   2521   5247       C  
ATOM   5549  N   ASN B 384     -48.369   9.444  71.019  1.00 90.20           N  
ANISOU 5549  N   ASN B 384     4561  16514  13198  -1212    978   1548       N  
ATOM   5550  CA  ASN B 384     -49.374  10.124  70.206  1.00 88.79           C  
ANISOU 5550  CA  ASN B 384     4455  16214  13066  -1246    984   1288       C  
ATOM   5551  C   ASN B 384     -49.855   9.184  69.106  1.00 97.21           C  
ANISOU 5551  C   ASN B 384     5607  17001  14328  -1340   1086   1390       C  
ATOM   5552  O   ASN B 384     -49.088   8.825  68.207  1.00111.97           O  
ANISOU 5552  O   ASN B 384     7531  18620  16392  -1321   1106   1445       O  
ATOM   5553  CB  ASN B 384     -48.798  11.411  69.625  1.00 87.25           C  
ANISOU 5553  CB  ASN B 384     4301  15917  12932  -1182    868   1032       C  
ATOM   5554  CG  ASN B 384     -49.873  12.377  69.160  1.00 95.24           C  
ANISOU 5554  CG  ASN B 384     5338  16921  13928  -1189    792    747       C  
ATOM   5555  OD1 ASN B 384     -50.837  11.986  68.500  1.00102.96           O  
ANISOU 5555  OD1 ASN B 384     6357  17775  14988  -1250    863    716       O  
ATOM   5556  ND2 ASN B 384     -49.714  13.649  69.509  1.00 99.19           N  
ANISOU 5556  ND2 ASN B 384     5801  17570  14317  -1119    617    531       N  
ATOM   5557  N   LYS B 385     -51.133   8.792  69.174  1.00 92.68           N  
ANISOU 5557  N   LYS B 385     5033  16493  13688  -1445   1148   1404       N  
ATOM   5558  CA  LYS B 385     -51.664   7.790  68.252  1.00 88.44           C  
ANISOU 5558  CA  LYS B 385     4575  15711  13317  -1559   1234   1544       C  
ATOM   5559  C   LYS B 385     -51.635   8.279  66.807  1.00 98.05           C  
ANISOU 5559  C   LYS B 385     5901  16599  14753  -1531   1230   1337       C  
ATOM   5560  O   LYS B 385     -51.377   7.497  65.882  1.00 96.75           O  
ANISOU 5560  O   LYS B 385     5812  16162  14785  -1564   1281   1467       O  
ATOM   5561  CB  LYS B 385     -53.083   7.400  68.664  1.00109.84           C  
ANISOU 5561  CB  LYS B 385     7254  18606  15875  -1708   1290   1572       C  
ATOM   5562  CG  LYS B 385     -53.157   6.675  70.001  1.00106.83           C  
ANISOU 5562  CG  LYS B 385     6777  18558  15256  -1824   1304   1851       C  
ATOM   5563  CD  LYS B 385     -54.581   6.264  70.338  1.00130.64           C  
ANISOU 5563  CD  LYS B 385     9761  21789  18087  -2025   1367   1875       C  
ATOM   5564  CE  LYS B 385     -54.637   5.513  71.659  1.00143.78           C  
ANISOU 5564  CE  LYS B 385    11340  23815  19474  -2211   1372   2188       C  
ATOM   5565  NZ  LYS B 385     -56.028   5.122  72.023  1.00138.56           N  
ANISOU 5565  NZ  LYS B 385    10644  23420  18582  -2451   1436   2206       N  
ATOM   5566  N   THR B 386     -51.906   9.568  66.592  1.00117.32           N  
ANISOU 5566  N   THR B 386     8342  19071  17163  -1476   1146   1029       N  
ATOM   5567  CA  THR B 386     -51.837  10.118  65.241  1.00122.54           C  
ANISOU 5567  CA  THR B 386     9100  19453  18009  -1493   1111    856       C  
ATOM   5568  C   THR B 386     -50.420  10.026  64.685  1.00115.67           C  
ANISOU 5568  C   THR B 386     8277  18419  17255  -1472   1114    930       C  
ATOM   5569  O   THR B 386     -50.228   9.720  63.501  1.00127.14           O  
ANISOU 5569  O   THR B 386     9820  19609  18880  -1523   1160    933       O  
ATOM   5570  CB  THR B 386     -52.330  11.566  65.237  1.00121.59           C  
ANISOU 5570  CB  THR B 386     8946  19443  17811  -1450    954    545       C  
ATOM   5571  OG1 THR B 386     -53.651  11.624  65.790  1.00130.68           O  
ANISOU 5571  OG1 THR B 386    10019  20799  18834  -1432    951    437       O  
ATOM   5572  CG2 THR B 386     -52.361  12.117  63.819  1.00116.47           C  
ANISOU 5572  CG2 THR B 386     8397  18526  17331  -1526    886    389       C  
ATOM   5573  N   TYR B 387     -49.414  10.276  65.529  1.00109.34           N  
ANISOU 5573  N   TYR B 387     7402  17794  16349  -1395   1066    981       N  
ATOM   5574  CA  TYR B 387     -48.025  10.191  65.085  1.00 84.81           C  
ANISOU 5574  CA  TYR B 387     4299  14601  13324  -1368   1067   1026       C  
ATOM   5575  C   TYR B 387     -47.676   8.785  64.610  1.00 87.29           C  
ANISOU 5575  C   TYR B 387     4615  14760  13791  -1341   1177   1243       C  
ATOM   5576  O   TYR B 387     -47.084   8.609  63.538  1.00100.43           O  
ANISOU 5576  O   TYR B 387     6318  16247  15595  -1350   1214   1204       O  
ATOM   5577  CB  TYR B 387     -47.083  10.617  66.213  1.00 84.17           C  
ANISOU 5577  CB  TYR B 387     4119  14768  13096  -1284    989   1057       C  
ATOM   5578  CG  TYR B 387     -46.633  12.060  66.153  1.00 83.60           C  
ANISOU 5578  CG  TYR B 387     4054  14767  12945  -1322    844    851       C  
ATOM   5579  CD1 TYR B 387     -45.901  12.537  65.073  1.00 88.52           C  
ANISOU 5579  CD1 TYR B 387     4733  15253  13648  -1424    816    757       C  
ATOM   5580  CD2 TYR B 387     -46.914  12.938  67.190  1.00 84.18           C  
ANISOU 5580  CD2 TYR B 387     4068  15076  12839  -1277    717    761       C  
ATOM   5581  CE1 TYR B 387     -45.479  13.854  65.021  1.00 82.71           C  
ANISOU 5581  CE1 TYR B 387     4008  14602  12816  -1522    643    609       C  
ATOM   5582  CE2 TYR B 387     -46.497  14.252  67.148  1.00 83.96           C  
ANISOU 5582  CE2 TYR B 387     4044  15126  12733  -1326    534    591       C  
ATOM   5583  CZ  TYR B 387     -45.781  14.706  66.062  1.00 83.25           C  
ANISOU 5583  CZ  TYR B 387     4022  14888  12723  -1470    486    530       C  
ATOM   5584  OH  TYR B 387     -45.365  16.017  66.024  1.00 83.40           O  
ANISOU 5584  OH  TYR B 387     4053  15001  12635  -1585    261    382       O  
ATOM   5585  N   ARG B 388     -48.029   7.766  65.400  1.00 87.60           N  
ANISOU 5585  N   ARG B 388     4595  14885  13803  -1319   1210   1488       N  
ATOM   5586  CA  ARG B 388     -47.700   6.396  65.015  1.00 87.64           C  
ANISOU 5586  CA  ARG B 388     4624  14705  13970  -1272   1251   1717       C  
ATOM   5587  C   ARG B 388     -48.499   5.953  63.798  1.00102.54           C  
ANISOU 5587  C   ARG B 388     6668  16276  16016  -1349   1313   1680       C  
ATOM   5588  O   ARG B 388     -47.985   5.209  62.955  1.00104.98           O  
ANISOU 5588  O   ARG B 388     7070  16336  16481  -1275   1328   1707       O  
ATOM   5589  CB  ARG B 388     -47.925   5.437  66.184  1.00 89.43           C  
ANISOU 5589  CB  ARG B 388     4852  15038  14091  -1270   1211   1992       C  
ATOM   5590  CG  ARG B 388     -49.012   5.872  67.135  1.00127.33           C  
ANISOU 5590  CG  ARG B 388     9571  20126  18685  -1404   1224   2008       C  
ATOM   5591  CD  ARG B 388     -49.243   4.882  68.266  1.00118.18           C  
ANISOU 5591  CD  ARG B 388     8431  19094  17380  -1472   1183   2309       C  
ATOM   5592  NE  ARG B 388     -50.094   3.772  67.856  1.00122.43           N  
ANISOU 5592  NE  ARG B 388     9132  19406  17979  -1614   1197   2494       N  
ATOM   5593  CZ  ARG B 388     -50.787   3.014  68.694  1.00128.68           C  
ANISOU 5593  CZ  ARG B 388     9964  20327  18601  -1798   1169   2747       C  
ATOM   5594  NH1 ARG B 388     -50.766   3.227  70.000  1.00141.59           N  
ANISOU 5594  NH1 ARG B 388    11477  22333  19986  -1857   1142   2839       N  
ATOM   5595  NH2 ARG B 388     -51.528   2.021  68.209  1.00129.82           N  
ANISOU 5595  NH2 ARG B 388    10284  20233  18809  -1956   1158   2917       N  
ATOM   5596  N   SER B 389     -49.757   6.390  63.683  1.00153.32           N  
ANISOU 5596  N   SER B 389    13124  22725  22406  -1479   1338   1594       N  
ATOM   5597  CA  SER B 389     -50.520   6.072  62.479  1.00156.05           C  
ANISOU 5597  CA  SER B 389    13619  22766  22906  -1557   1385   1538       C  
ATOM   5598  C   SER B 389     -49.862   6.675  61.243  1.00160.89           C  
ANISOU 5598  C   SER B 389    14299  23192  23640  -1538   1392   1333       C  
ATOM   5599  O   SER B 389     -49.718   6.003  60.212  1.00157.88           O  
ANISOU 5599  O   SER B 389    14042  22531  23415  -1524   1434   1347       O  
ATOM   5600  CB  SER B 389     -51.961   6.565  62.619  1.00143.22           C  
ANISOU 5600  CB  SER B 389    11981  21242  21194  -1679   1389   1429       C  
ATOM   5601  OG  SER B 389     -52.011   7.977  62.715  1.00150.34           O  
ANISOU 5601  OG  SER B 389    12860  22277  21986  -1651   1315   1136       O  
ATOM   5602  N   ALA B 390     -49.428   7.936  61.338  1.00127.25           N  
ANISOU 5602  N   ALA B 390     9984  19086  19281  -1552   1332   1138       N  
ATOM   5603  CA  ALA B 390     -48.748   8.572  60.216  1.00120.41           C  
ANISOU 5603  CA  ALA B 390     9180  18090  18480  -1606   1322    969       C  
ATOM   5604  C   ALA B 390     -47.446   7.857  59.879  1.00109.22           C  
ANISOU 5604  C   ALA B 390     7704  16660  17134  -1511   1380   1046       C  
ATOM   5605  O   ALA B 390     -47.137   7.641  58.704  1.00111.56           O  
ANISOU 5605  O   ALA B 390     8081  16776  17531  -1542   1431    967       O  
ATOM   5606  CB  ALA B 390     -48.488  10.046  60.528  1.00117.41           C  
ANISOU 5606  CB  ALA B 390     8773  17883  17953  -1671   1196    782       C  
ATOM   5607  N   PHE B 391     -46.672   7.475  60.898  1.00112.41           N  
ANISOU 5607  N   PHE B 391     7965  17273  17472  -1380   1361   1174       N  
ATOM   5608  CA  PHE B 391     -45.402   6.794  60.647  1.00107.49           C  
ANISOU 5608  CA  PHE B 391     7259  16676  16907  -1238   1385   1202       C  
ATOM   5609  C   PHE B 391     -45.620   5.428  60.004  1.00114.13           C  
ANISOU 5609  C   PHE B 391     8222  17232  17911  -1127   1420   1295       C  
ATOM   5610  O   PHE B 391     -44.878   5.037  59.091  1.00114.46           O  
ANISOU 5610  O   PHE B 391     8252  17201  18036  -1044   1456   1198       O  
ATOM   5611  CB  PHE B 391     -44.613   6.662  61.950  1.00 85.15           C  
ANISOU 5611  CB  PHE B 391     4267  14112  13975  -1104   1320   1318       C  
ATOM   5612  CG  PHE B 391     -44.244   7.981  62.574  1.00 84.70           C  
ANISOU 5612  CG  PHE B 391     4144  14301  13737  -1188   1256   1194       C  
ATOM   5613  CD1 PHE B 391     -44.176   9.133  61.808  1.00 83.46           C  
ANISOU 5613  CD1 PHE B 391     4078  14110  13523  -1355   1235    972       C  
ATOM   5614  CD2 PHE B 391     -43.965   8.069  63.926  1.00 85.74           C  
ANISOU 5614  CD2 PHE B 391     4186  14651  13742  -1106   1185   1292       C  
ATOM   5615  CE1 PHE B 391     -43.840  10.344  62.381  1.00 83.35           C  
ANISOU 5615  CE1 PHE B 391     4062  14254  13352  -1430   1127    867       C  
ATOM   5616  CE2 PHE B 391     -43.626   9.279  64.504  1.00 85.47           C  
ANISOU 5616  CE2 PHE B 391     4153  14781  13543  -1163   1098   1158       C  
ATOM   5617  CZ  PHE B 391     -43.562  10.417  63.730  1.00 84.31           C  
ANISOU 5617  CZ  PHE B 391     4094  14579  13362  -1321   1061    953       C  
ATOM   5618  N   SER B 392     -46.630   4.686  60.468  1.00113.55           N  
ANISOU 5618  N   SER B 392     8264  17014  17865  -1134   1397   1476       N  
ATOM   5619  CA  SER B 392     -46.955   3.404  59.853  1.00 90.89           C  
ANISOU 5619  CA  SER B 392     5564  13826  15145  -1059   1387   1579       C  
ATOM   5620  C   SER B 392     -47.379   3.590  58.404  1.00 90.42           C  
ANISOU 5620  C   SER B 392     5624  13532  15199  -1150   1464   1415       C  
ATOM   5621  O   SER B 392     -47.036   2.776  57.538  1.00 84.66           O  
ANISOU 5621  O   SER B 392     4982  12591  14595  -1035   1466   1385       O  
ATOM   5622  CB  SER B 392     -48.053   2.703  60.652  1.00107.59           C  
ANISOU 5622  CB  SER B 392     7789  15865  17225  -1141   1335   1822       C  
ATOM   5623  OG  SER B 392     -47.645   2.483  61.991  1.00115.89           O  
ANISOU 5623  OG  SER B 392     8754  17130  18149  -1079   1253   1989       O  
ATOM   5624  N   ARG B 393     -48.133   4.655  58.121  1.00 91.22           N  
ANISOU 5624  N   ARG B 393     5744  13661  15253  -1342   1502   1293       N  
ATOM   5625  CA  ARG B 393     -48.424   4.996  56.733  1.00 97.19           C  
ANISOU 5625  CA  ARG B 393     6624  14206  16096  -1449   1553   1121       C  
ATOM   5626  C   ARG B 393     -47.155   5.349  55.963  1.00104.78           C  
ANISOU 5626  C   ARG B 393     7505  15264  17042  -1423   1592    953       C  
ATOM   5627  O   ARG B 393     -47.077   5.113  54.752  1.00115.50           O  
ANISOU 5627  O   ARG B 393     8958  16443  18482  -1449   1643    847       O  
ATOM   5628  CB  ARG B 393     -49.421   6.155  56.680  1.00111.37           C  
ANISOU 5628  CB  ARG B 393     8469  16018  17830  -1638   1526   1001       C  
ATOM   5629  CG  ARG B 393     -50.835   5.785  57.110  1.00106.37           C  
ANISOU 5629  CG  ARG B 393     7898  15306  17213  -1691   1512   1106       C  
ATOM   5630  CD  ARG B 393     -51.566   6.979  57.709  1.00 98.02           C  
ANISOU 5630  CD  ARG B 393     6772  14448  16025  -1780   1446    976       C  
ATOM   5631  NE  ARG B 393     -50.944   8.247  57.346  1.00121.18           N  
ANISOU 5631  NE  ARG B 393     9708  17444  18892  -1834   1377    769       N  
ATOM   5632  CZ  ARG B 393     -51.283   8.977  56.292  1.00130.52           C  
ANISOU 5632  CZ  ARG B 393    11046  18432  20113  -1954   1320    582       C  
ATOM   5633  NH1 ARG B 393     -52.240   8.592  55.464  1.00133.52           N  
ANISOU 5633  NH1 ARG B 393    11572  18545  20613  -2006   1340    554       N  
ATOM   5634  NH2 ARG B 393     -50.643  10.120  56.062  1.00119.84           N  
ANISOU 5634  NH2 ARG B 393     9724  17144  18665  -2045   1218    428       N  
ATOM   5635  N   TYR B 394     -46.160   5.914  56.643  1.00108.82           N  
ANISOU 5635  N   TYR B 394     7828  16087  17431  -1391   1570    924       N  
ATOM   5636  CA  TYR B 394     -44.913   6.349  56.021  1.00100.05           C  
ANISOU 5636  CA  TYR B 394     6588  15169  16257  -1418   1608    763       C  
ATOM   5637  C   TYR B 394     -43.860   5.251  55.932  1.00101.75           C  
ANISOU 5637  C   TYR B 394     6672  15460  16530  -1157   1631    764       C  
ATOM   5638  O   TYR B 394     -42.758   5.522  55.445  1.00111.04           O  
ANISOU 5638  O   TYR B 394     7682  16876  17634  -1163   1676    609       O  
ATOM   5639  CB  TYR B 394     -44.313   7.531  56.791  1.00 93.00           C  
ANISOU 5639  CB  TYR B 394     5549  14596  15190  -1528   1549    721       C  
ATOM   5640  CG  TYR B 394     -45.158   8.784  56.823  1.00 90.18           C  
ANISOU 5640  CG  TYR B 394     5324  14188  14752  -1758   1467    654       C  
ATOM   5641  CD1 TYR B 394     -46.124   9.026  55.856  1.00 87.27           C  
ANISOU 5641  CD1 TYR B 394     5172  13538  14449  -1903   1462    573       C  
ATOM   5642  CD2 TYR B 394     -44.982   9.729  57.826  1.00 82.18           C  
ANISOU 5642  CD2 TYR B 394     4245  13391  13587  -1803   1360    644       C  
ATOM   5643  CE1 TYR B 394     -46.893  10.175  55.890  1.00 92.65           C  
ANISOU 5643  CE1 TYR B 394     5987  14156  15059  -2071   1334    476       C  
ATOM   5644  CE2 TYR B 394     -45.745  10.877  57.868  1.00 79.40           C  
ANISOU 5644  CE2 TYR B 394     4015  12986  13168  -1968   1233    553       C  
ATOM   5645  CZ  TYR B 394     -46.698  11.096  56.899  1.00 89.76           C  
ANISOU 5645  CZ  TYR B 394     5543  14012  14551  -2091   1209    457       C  
ATOM   5646  OH  TYR B 394     -47.459  12.241  56.941  1.00 97.11           O  
ANISOU 5646  OH  TYR B 394     6623  14865  15408  -2211   1031    325       O  
ATOM   5647  N   ILE B 395     -44.152   4.043  56.425  1.00124.41           N  
ANISOU 5647  N   ILE B 395     9610  18154  19508   -937   1575    924       N  
ATOM   5648  CA  ILE B 395     -43.174   2.951  56.383  1.00112.85           C  
ANISOU 5648  CA  ILE B 395     8054  16718  18107   -633   1528    901       C  
ATOM   5649  C   ILE B 395     -42.606   2.792  54.975  1.00129.18           C  
ANISOU 5649  C   ILE B 395    10085  18788  20210   -599   1614    667       C  
ATOM   5650  O   ILE B 395     -41.390   2.865  54.760  1.00144.00           O  
ANISOU 5650  O   ILE B 395    11723  20974  22015   -492   1641    494       O  
ATOM   5651  CB  ILE B 395     -43.806   1.637  56.877  1.00128.13           C  
ANISOU 5651  CB  ILE B 395    10183  18339  20160   -456   1403   1117       C  
ATOM   5652  CG1 ILE B 395     -43.834   1.591  58.406  1.00137.50           C  
ANISOU 5652  CG1 ILE B 395    11326  19653  21264   -424   1299   1330       C  
ATOM   5653  CG2 ILE B 395     -43.046   0.427  56.339  1.00122.50           C  
ANISOU 5653  CG2 ILE B 395     9483  17506  19557   -129   1313   1030       C  
ATOM   5654  CD1 ILE B 395     -44.178   0.217  58.960  1.00133.70           C  
ANISOU 5654  CD1 ILE B 395    11041  18899  20861   -263   1125   1560       C  
ATOM   5655  N   GLN B 396     -43.481   2.579  53.995  1.00130.49           N  
ANISOU 5655  N   GLN B 396    10467  18643  20469   -700   1659    645       N  
ATOM   5656  CA  GLN B 396     -43.076   2.384  52.614  1.00140.44           C  
ANISOU 5656  CA  GLN B 396    11722  19887  21752   -684   1742    426       C  
ATOM   5657  C   GLN B 396     -43.278   3.632  51.770  1.00133.90           C  
ANISOU 5657  C   GLN B 396    10918  19143  20814  -1051   1853    300       C  
ATOM   5658  O   GLN B 396     -43.130   3.570  50.544  1.00118.86           O  
ANISOU 5658  O   GLN B 396     9050  17208  18904  -1115   1932    134       O  
ATOM   5659  CB  GLN B 396     -43.837   1.201  52.010  1.00143.02           C  
ANISOU 5659  CB  GLN B 396    12304  19781  22257   -532   1687    481       C  
ATOM   5660  CG  GLN B 396     -43.078   0.447  50.931  1.00144.07           C  
ANISOU 5660  CG  GLN B 396    12382  19929  22428   -303   1705    250       C  
ATOM   5661  CD  GLN B 396     -43.687  -0.910  50.644  1.00143.28           C  
ANISOU 5661  CD  GLN B 396    12547  19382  22511    -67   1569    332       C  
ATOM   5662  OE1 GLN B 396     -44.261  -1.133  49.578  1.00130.67           O  
ANISOU 5662  OE1 GLN B 396    11131  17533  20986   -133   1611    264       O  
ATOM   5663  NE2 GLN B 396     -43.567  -1.825  51.598  1.00153.33           N  
ANISOU 5663  NE2 GLN B 396    13872  20536  23850    193   1378    490       N  
ATOM   5664  N   CYS B 397     -43.613   4.757  52.402  1.00140.84           N  
ANISOU 5664  N   CYS B 397    11799  20121  21593  -1290   1831    369       N  
ATOM   5665  CA  CYS B 397     -43.972   6.005  51.733  1.00127.45           C  
ANISOU 5665  CA  CYS B 397    10208  18423  19793  -1651   1854    277       C  
ATOM   5666  C   CYS B 397     -45.207   5.843  50.852  1.00119.45           C  
ANISOU 5666  C   CYS B 397     9484  17001  18900  -1755   1857    280       C  
ATOM   5667  O   CYS B 397     -45.406   6.616  49.910  1.00109.99           O  
ANISOU 5667  O   CYS B 397     8413  15743  17636  -2024   1868    165       O  
ATOM   5668  CB  CYS B 397     -42.801   6.582  50.918  1.00131.99           C  
ANISOU 5668  CB  CYS B 397    10619  19336  20197  -1823   1929     81       C  
ATOM   5669  SG  CYS B 397     -42.925   8.361  50.528  1.00165.79           S  
ANISOU 5669  SG  CYS B 397    15024  23698  24270  -2325   1863     15       S  
ATOM   5670  N   GLN B 398     -46.043   4.844  51.133  1.00120.93           N  
ANISOU 5670  N   GLN B 398     9794  16902  19253  -1569   1828    419       N  
ATOM   5671  CA  GLN B 398     -47.338   4.681  50.484  1.00123.81           C  
ANISOU 5671  CA  GLN B 398    10420  16886  19736  -1669   1814    448       C  
ATOM   5672  C   GLN B 398     -48.387   5.329  51.377  1.00119.67           C  
ANISOU 5672  C   GLN B 398     9952  16324  19195  -1780   1735    551       C  
ATOM   5673  O   GLN B 398     -48.862   4.718  52.339  1.00104.46           O  
ANISOU 5673  O   GLN B 398     8002  14375  17313  -1657   1699    723       O  
ATOM   5674  CB  GLN B 398     -47.645   3.206  50.249  1.00113.09           C  
ANISOU 5674  CB  GLN B 398     9168  15254  18548  -1435   1806    540       C  
ATOM   5675  CG  GLN B 398     -46.931   2.582  49.057  1.00106.04           C  
ANISOU 5675  CG  GLN B 398     8281  14322  17688  -1321   1866    375       C  
ATOM   5676  CD  GLN B 398     -47.136   1.080  48.954  1.00105.49           C  
ANISOU 5676  CD  GLN B 398     8334  13965  17781  -1039   1794    460       C  
ATOM   5677  OE1 GLN B 398     -46.999   0.353  49.936  1.00110.42           O  
ANISOU 5677  OE1 GLN B 398     8925  14584  18445   -838   1693    615       O  
ATOM   5678  NE2 GLN B 398     -47.466   0.611  47.756  1.00 83.61           N  
ANISOU 5678  NE2 GLN B 398     5737  10934  15097  -1033   1815    363       N  
ATOM   5679  N   TYR B 399     -48.750   6.574  51.058  1.00119.05           N  
ANISOU 5679  N   TYR B 399     9954  16251  19031  -2019   1686    434       N  
ATOM   5680  CA  TYR B 399     -49.636   7.361  51.908  1.00121.17           C  
ANISOU 5680  CA  TYR B 399    10240  16548  19251  -2091   1582    457       C  
ATOM   5681  C   TYR B 399     -50.733   7.960  51.031  1.00111.79           C  
ANISOU 5681  C   TYR B 399     9285  15083  18108  -2266   1506    337       C  
ATOM   5682  O   TYR B 399     -50.596   9.046  50.468  1.00126.58           O  
ANISOU 5682  O   TYR B 399    11267  16940  19889  -2461   1414    188       O  
ATOM   5683  CB  TYR B 399     -48.856   8.415  52.695  1.00153.02           C  
ANISOU 5683  CB  TYR B 399    14129  20903  23111  -2150   1513    410       C  
ATOM   5684  CG  TYR B 399     -48.117   9.432  51.841  1.00150.40           C  
ANISOU 5684  CG  TYR B 399    13857  20633  22654  -2386   1470    252       C  
ATOM   5685  CD1 TYR B 399     -48.570  10.738  51.755  1.00154.86           C  
ANISOU 5685  CD1 TYR B 399    14576  21143  23122  -2592   1294    136       C  
ATOM   5686  CD2 TYR B 399     -46.971   9.091  51.133  1.00132.24           C  
ANISOU 5686  CD2 TYR B 399    11466  18468  20313  -2414   1580    208       C  
ATOM   5687  CE1 TYR B 399     -47.926  11.672  50.988  1.00131.65           C  
ANISOU 5687  CE1 TYR B 399    11742  18239  20041  -2867   1212     23       C  
ATOM   5688  CE2 TYR B 399     -46.306  10.022  50.357  1.00129.88           C  
ANISOU 5688  CE2 TYR B 399    11215  18277  19855  -2700   1543     81       C  
ATOM   5689  CZ  TYR B 399     -46.791  11.315  50.289  1.00129.74           C  
ANISOU 5689  CZ  TYR B 399    11396  18163  19736  -2951   1351     10       C  
ATOM   5690  OH  TYR B 399     -46.150  12.263  49.527  1.00133.26           O  
ANISOU 5690  OH  TYR B 399    11943  18693  19998  -3296   1270    -87       O  
ATOM   5691  N   LYS B 400     -51.835   7.230  50.902  1.00108.32           N  
ANISOU 5691  N   LYS B 400     8941  14412  17803  -2212   1520    407       N  
ATOM   5692  CA  LYS B 400     -53.111   7.817  50.529  1.00 94.98           C  
ANISOU 5692  CA  LYS B 400     7411  12525  16150  -2325   1415    300       C  
ATOM   5693  C   LYS B 400     -54.031   7.814  51.742  1.00111.25           C  
ANISOU 5693  C   LYS B 400     9344  14741  18184  -2248   1370    365       C  
ATOM   5694  O   LYS B 400     -53.654   7.372  52.831  1.00123.28           O  
ANISOU 5694  O   LYS B 400    10687  16502  19652  -2139   1421    513       O  
ATOM   5695  CB  LYS B 400     -53.727   7.065  49.349  1.00 79.48           C  
ANISOU 5695  CB  LYS B 400     5643  10213  14344  -2358   1461    300       C  
ATOM   5696  CG  LYS B 400     -53.644   7.823  48.019  1.00 71.45           C  
ANISOU 5696  CG  LYS B 400     4843   8992  13312  -2546   1398    117       C  
ATOM   5697  CD  LYS B 400     -54.152   7.011  46.837  1.00 71.15           C  
ANISOU 5697  CD  LYS B 400     4997   8615  13423  -2565   1452    119       C  
ATOM   5698  CE  LYS B 400     -53.174   5.913  46.449  1.00 77.11           C  
ANISOU 5698  CE  LYS B 400     5696   9387  14217  -2444   1602    199       C  
ATOM   5699  NZ  LYS B 400     -53.305   5.530  45.015  1.00 72.16           N  
ANISOU 5699  NZ  LYS B 400     5280   8471  13668  -2514   1635    118       N  
ATOM   5700  N   GLU B 401     -55.232   8.353  51.549  1.00109.34           N  
ANISOU 5700  N   GLU B 401     9189  14391  17963  -2309   1262    233       N  
ATOM   5701  CA  GLU B 401     -56.285   8.380  52.565  1.00109.38           C  
ANISOU 5701  CA  GLU B 401     9048  14590  17922  -2254   1222    240       C  
ATOM   5702  C   GLU B 401     -55.818   8.906  53.923  1.00104.97           C  
ANISOU 5702  C   GLU B 401     8275  14413  17194  -2173   1191    253       C  
ATOM   5703  O   GLU B 401     -55.615   8.131  54.863  1.00 96.83           O  
ANISOU 5703  O   GLU B 401     7082  13587  16121  -2108   1291    455       O  
ATOM   5704  CB  GLU B 401     -56.901   6.985  52.745  1.00112.46           C  
ANISOU 5704  CB  GLU B 401     9399  14929  18402  -2238   1343    462       C  
ATOM   5705  CG  GLU B 401     -57.731   6.519  51.558  1.00125.77           C  
ANISOU 5705  CG  GLU B 401    11282  16259  20246  -2317   1342    430       C  
ATOM   5706  CD  GLU B 401     -58.315   5.134  51.756  1.00142.70           C  
ANISOU 5706  CD  GLU B 401    13419  18339  22464  -2336   1425    672       C  
ATOM   5707  OE1 GLU B 401     -57.840   4.418  52.660  1.00151.86           O  
ANISOU 5707  OE1 GLU B 401    14468  19667  23563  -2288   1482    888       O  
ATOM   5708  OE2 GLU B 401     -59.251   4.761  51.015  1.00146.72           O  
ANISOU 5708  OE2 GLU B 401    14056  18615  23077  -2413   1407    653       O  
TER    5709      GLU B 401                                                      
HETATM 5710  C1  A1L A1201     -18.487  11.586  33.186  1.00 78.15           C  
HETATM 5711  C2  A1L A1201     -20.558  12.805  33.734  1.00 90.85           C  
HETATM 5712  C3  A1L A1201     -17.455  12.702  33.190  1.00 92.08           C  
HETATM 5713  C4  A1L A1201     -19.122  11.562  31.802  1.00 80.20           C  
HETATM 5714  C5  A1L A1201     -18.037  11.232  30.781  1.00 76.95           C  
HETATM 5715  C6  A1L A1201     -16.368  12.345  32.185  1.00100.32           C  
HETATM 5716  N1  A1L A1201     -19.941  12.038  36.438  1.00 75.10           N  
HETATM 5717  N2  A1L A1201     -16.935  12.212  30.832  1.00 90.54           N  
HETATM 5718  O1  A1L A1201     -17.679  16.277  40.473  1.00 76.45           O  
HETATM 5719  C7  A1L A1201     -21.899  12.205  34.100  1.00 82.04           C  
HETATM 5720  C8  A1L A1201     -19.607  11.687  37.800  1.00 74.24           C  
HETATM 5721  C9  A1L A1201     -18.145  15.164  39.826  1.00 69.80           C  
HETATM 5722  C10 A1L A1201     -24.364  11.108  34.791  1.00 93.97           C  
HETATM 5723  C11 A1L A1201     -19.093  12.913  38.512  1.00 75.47           C  
HETATM 5724  C12 A1L A1201     -17.092  16.180  41.768  1.00 67.25           C  
HETATM 5725  C13 A1L A1201     -22.670  12.789  35.101  1.00 81.92           C  
HETATM 5726  C14 A1L A1201     -22.363  11.067  33.447  1.00 71.90           C  
HETATM 5727  C15 A1L A1201     -17.290  14.100  39.570  1.00 72.25           C  
HETATM 5728  N   A1L A1201     -19.478  11.940  34.199  1.00 82.61           N  
HETATM 5729  C   A1L A1201     -19.299  11.466  35.428  1.00 71.20           C  
HETATM 5730  O   A1L A1201     -18.537  10.535  35.629  1.00 70.37           O  
HETATM 5731  C16 A1L A1201     -19.474  15.105  39.422  1.00 73.35           C  
HETATM 5732  C17 A1L A1201     -23.595  10.522  33.790  1.00 77.45           C  
HETATM 5733  C18 A1L A1201     -23.901  12.243  35.446  1.00 90.03           C  
HETATM 5734  C19 A1L A1201     -17.763  12.972  38.911  1.00 74.85           C  
HETATM 5735  C20 A1L A1201     -19.949  13.979  38.762  1.00 73.76           C  
HETATM 5736  C21 A1L A1201     -15.856  11.764  29.940  1.00 92.53           C  
HETATM 5737  C22 A1L A1201     -18.162  15.852  42.803  1.00 59.47           C  
HETATM 5738  C23 A1L A1201     -19.374  16.763  42.653  1.00 82.26           C  
HETATM 5739  C24 A1L A1201     -17.586  15.951  44.209  1.00 64.91           C  
HETATM 5740  F   A1L A1201     -25.555  10.577  35.124  1.00 94.68           F  
HETATM 5741  C1  A1L B1201     -20.687  19.952  73.521  1.00128.04           C  
HETATM 5742  C2  A1L B1201     -22.756  21.124  72.948  1.00119.19           C  
HETATM 5743  C3  A1L B1201     -20.116  20.355  72.168  1.00121.63           C  
HETATM 5744  C4  A1L B1201     -21.429  18.636  73.344  1.00122.94           C  
HETATM 5745  C5  A1L B1201     -20.441  17.577  72.869  1.00114.87           C  
HETATM 5746  C6  A1L B1201     -19.142  19.277  71.705  1.00125.31           C  
HETATM 5747  N1  A1L B1201     -22.042  22.840  75.164  1.00113.06           N  
HETATM 5748  N2  A1L B1201     -19.829  17.979  71.591  1.00120.61           N  
HETATM 5749  O1  A1L B1201     -19.525  28.569  75.100  1.00142.11           O  
HETATM 5750  C7  A1L B1201     -24.071  21.263  73.688  1.00129.62           C  
HETATM 5751  C8  A1L B1201     -21.891  23.600  76.386  1.00117.25           C  
HETATM 5752  C9  A1L B1201     -20.095  27.361  75.405  1.00129.69           C  
HETATM 5753  C10 A1L B1201     -26.477  21.545  75.057  1.00115.46           C  
HETATM 5754  C11 A1L B1201     -21.263  24.926  76.044  1.00123.11           C  
HETATM 5755  C12 A1L B1201     -20.235  29.765  75.421  1.00138.00           C  
HETATM 5756  C13 A1L B1201     -24.753  22.477  73.661  1.00126.54           C  
HETATM 5757  C14 A1L B1201     -24.590  20.193  74.409  1.00128.41           C  
HETATM 5758  C15 A1L B1201     -19.399  26.435  76.173  1.00128.79           C  
HETATM 5759  N   A1L B1201     -21.663  20.967  73.903  1.00122.22           N  
HETATM 5760  C   A1L B1201     -21.473  21.648  75.030  1.00119.27           C  
HETATM 5761  O   A1L B1201     -20.778  21.193  75.924  1.00119.02           O  
HETATM 5762  C16 A1L B1201     -21.379  27.066  74.958  1.00126.27           C  
HETATM 5763  C17 A1L B1201     -25.795  20.334  75.089  1.00119.20           C  
HETATM 5764  C18 A1L B1201     -25.956  22.618  74.344  1.00111.36           C  
HETATM 5765  C19 A1L B1201     -19.982  25.217  76.493  1.00121.30           C  
HETATM 5766  C20 A1L B1201     -21.962  25.846  75.273  1.00124.61           C  
HETATM 5767  C21 A1L B1201     -18.850  16.957  71.200  1.00118.70           C  
HETATM 5768  C22 A1L B1201     -19.362  30.991  75.179  1.00134.70           C  
HETATM 5769  C23 A1L B1201     -20.036  31.956  74.211  1.00113.81           C  
HETATM 5770  C24 A1L B1201     -19.028  31.686  76.493  1.00135.31           C  
HETATM 5771  F   A1L B1201     -27.642  21.679  75.717  1.00117.94           F  
END