HEADER    SIGNALING PROTEIN                       17-NOV-19   6TGN              
TITLE     CRYO-EM STRUCTURE OF ATNBR1-PB1 FILAMENT (L-TYPE)                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN NBR1 HOMOLOG;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ATNBR1,AT4G24690;                                           
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: NBR1, AT4G24690, F22K18.110;                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    AUTOPHAGY, HELICAL FILAMENT, SIGNALING PROTEIN                        
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    A.J.JAKOBI,C.SACHSE                                                   
REVDAT   1   12-FEB-20 6TGN    0                                                
JRNL        AUTH   A.J.JAKOBI,S.T.HUBER,S.A.MORTENSEN,S.W.SCHULTZ,A.PALARA,     
JRNL        AUTH 2 T.KUHM,B.K.SHRESTHA,T.LAMARK,W.J.H.HAGEN,M.WILMANNS,         
JRNL        AUTH 3 T.JOHANSEN,A.BRECH,C.SACHSE                                  
JRNL        TITL   STRUCTURAL BASIS OF P62/SQSTM1 HELICAL FILAMENTS AND THEIR   
JRNL        TITL 2 ROLE IN CELLULAR CARGO UPTAKE.                               
JRNL        REF    NAT COMMUN                    V.  11   440 2020              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   31974402                                                     
JRNL        DOI    10.1038/S41467-020-14343-8                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : SPRING, SERIALEM, CTFFIND, PHENIX,        
REMARK   3                            SPRING, SPRING, SPRING, SPRING, PHENIX    
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : FLEXIBLE FIT                        
REMARK   3   REFINEMENT TARGET            : CORRELATION COEFFICIENT             
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.900                          
REMARK   3   NUMBER OF PARTICLES               : 25387                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6TGN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-NOV-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292102747.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : HELICAL                           
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : FILAMENT                          
REMARK 245   PARTICLE TYPE                  : HELICAL                           
REMARK 245   NAME OF SAMPLE                 : ATNBR1-PB1 (L-TYPE)               
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : HELICAL FILAMENT OF ATNBR 1-PB1   
REMARK 245  DOMAIN (1-95)                                                       
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : FEI FALCON II (4K X 4K)        
REMARK 245   MINIMUM DEFOCUS (NM)              : 500.00                         
REMARK 245   MAXIMUM DEFOCUS (NM)              : 4500.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 14.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 59000                          
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 5770 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     VAL A    93                                                      
REMARK 465     SER A    94                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TYR A  58   CB  -  CG  -  CD2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  32       44.46    -98.28                                   
REMARK 500    ARG A  81       66.53     60.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-10499   RELATED DB: EMDB                             
REMARK 900 CRYO-EM STRUCTURE OF ATNBR1-PB1 FILAMENT (L-TYPE)                    
DBREF  6TGN A    1    94  UNP    Q9SB64   NBR1_ARATH       1     94             
SEQRES   1 A   94  MET GLU SER THR ALA ASN ALA LEU VAL VAL LYS VAL SER          
SEQRES   2 A   94  TYR GLY GLY VAL LEU ARG ARG PHE ARG VAL PRO VAL LYS          
SEQRES   3 A   94  ALA ASN GLY GLN LEU ASP LEU GLU MET ALA GLY LEU LYS          
SEQRES   4 A   94  GLU LYS ILE ALA ALA LEU PHE ASN LEU SER ALA ASP ALA          
SEQRES   5 A   94  GLU LEU SER LEU THR TYR SER ASP GLU ASP GLY ASP VAL          
SEQRES   6 A   94  VAL ALA LEU VAL ASP ASP ASN ASP LEU PHE ASP VAL THR          
SEQRES   7 A   94  ASN GLN ARG LEU LYS PHE LEU LYS ILE ASN VAL ASN ALA          
SEQRES   8 A   94  GLY VAL SER                                                  
HELIX    1 AA1 GLU A   34  PHE A   46  1                                  13    
HELIX    2 AA2 PHE A   75  ARG A   81  1                                   7    
SHEET    1 AA1 3 VAL A  17  LEU A  18  0                                        
SHEET    2 AA1 3 LEU A   8  TYR A  14 -1  N  TYR A  14   O  VAL A  17           
SHEET    3 AA1 3 PHE A  21  VAL A  23 -1  O  VAL A  23   N  LEU A   8           
SHEET    1 AA2 4 VAL A  17  LEU A  18  0                                        
SHEET    2 AA2 4 LEU A   8  TYR A  14 -1  N  TYR A  14   O  VAL A  17           
SHEET    3 AA2 4 LEU A  85  ALA A  91  1  O  LEU A  85   N  LYS A  11           
SHEET    4 AA2 4 LEU A  54  THR A  57 -1  N  THR A  57   O  ASN A  88           
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  N   ALA A   5      29.111  83.477  98.229  1.00120.76           N  
ATOM      2  CA  ALA A   5      28.573  84.868  98.405  1.00165.81           C  
ATOM      3  C   ALA A   5      29.141  85.807  97.333  1.00226.89           C  
ATOM      4  O   ALA A   5      29.225  87.012  97.563  1.00268.33           O  
ATOM      5  CB  ALA A   5      28.878  85.364  99.810  1.00 97.40           C  
ATOM      6  N   ASN A   6      29.496  85.270  96.155  1.00242.55           N  
ATOM      7  CA  ASN A   6      30.416  85.936  95.239  1.00199.75           C  
ATOM      8  C   ASN A   6      29.815  86.052  93.841  1.00132.64           C  
ATOM      9  O   ASN A   6      28.840  85.402  93.539  1.00123.08           O  
ATOM     10  CB  ASN A   6      31.755  85.193  95.204  1.00293.07           C  
ATOM     11  CG  ASN A   6      31.620  83.713  94.896  1.00366.36           C  
ATOM     12  OD1 ASN A   6      30.520  83.208  94.671  1.00397.40           O  
ATOM     13  ND2 ASN A   6      32.737  83.003  94.890  1.00413.63           N  
ATOM     14  N   ALA A   7      30.422  86.877  92.997  1.00133.28           N  
ATOM     15  CA  ALA A   7      29.859  87.178  91.700  1.00127.13           C  
ATOM     16  C   ALA A   7      30.688  86.532  90.598  1.00129.59           C  
ATOM     17  O   ALA A   7      31.861  86.184  90.781  1.00136.94           O  
ATOM     18  CB  ALA A   7      29.847  88.681  91.524  1.00158.13           C  
ATOM     19  N   LEU A   8      30.070  86.466  89.412  1.00118.87           N  
ATOM     20  CA  LEU A   8      30.804  86.069  88.223  1.00 97.03           C  
ATOM     21  C   LEU A   8      31.206  87.294  87.414  1.00 78.11           C  
ATOM     22  O   LEU A   8      30.336  88.094  87.046  1.00 77.46           O  
ATOM     23  CB  LEU A   8      29.923  85.175  87.363  1.00104.46           C  
ATOM     24  CG  LEU A   8      30.632  84.638  86.132  1.00137.82           C  
ATOM     25  CD1 LEU A   8      31.898  83.860  86.520  1.00170.69           C  
ATOM     26  CD2 LEU A   8      29.652  83.731  85.422  1.00176.08           C  
ATOM     27  N   VAL A   9      32.502  87.409  87.123  1.00 61.42           N  
ATOM     28  CA  VAL A   9      32.938  88.535  86.317  1.00 54.02           C  
ATOM     29  C   VAL A   9      32.681  88.154  84.879  1.00 51.21           C  
ATOM     30  O   VAL A   9      33.243  87.166  84.378  1.00 65.78           O  
ATOM     31  CB  VAL A   9      34.425  88.897  86.485  1.00 63.35           C  
ATOM     32  CG1 VAL A   9      34.830  90.095  85.630  1.00 53.82           C  
ATOM     33  CG2 VAL A   9      34.790  89.126  87.933  1.00101.12           C  
ATOM     34  N   VAL A  10      31.875  88.996  84.222  1.00 48.36           N  
ATOM     35  CA  VAL A  10      31.558  88.785  82.833  1.00 53.63           C  
ATOM     36  C   VAL A  10      32.230  89.881  82.036  1.00 47.57           C  
ATOM     37  O   VAL A  10      32.029  91.051  82.330  1.00 48.93           O  
ATOM     38  CB  VAL A  10      30.031  88.784  82.662  1.00 63.79           C  
ATOM     39  CG1 VAL A  10      29.614  88.828  81.200  1.00 68.84           C  
ATOM     40  CG2 VAL A  10      29.462  87.537  83.322  1.00 91.51           C  
ATOM     41  N   LYS A  11      32.966  89.461  81.006  1.00 40.81           N  
ATOM     42  CA  LYS A  11      33.511  90.428  80.086  1.00 42.39           C  
ATOM     43  C   LYS A  11      32.803  90.269  78.747  1.00 38.04           C  
ATOM     44  O   LYS A  11      32.918  89.183  78.204  1.00 44.03           O  
ATOM     45  CB  LYS A  11      35.000  90.123  79.922  1.00 48.10           C  
ATOM     46  CG  LYS A  11      35.752  89.906  81.218  1.00 66.26           C  
ATOM     47  CD  LYS A  11      37.258  90.292  81.289  1.00 79.25           C  
ATOM     48  CE  LYS A  11      37.733  90.495  82.734  1.00 78.68           C  
ATOM     49  NZ  LYS A  11      38.826  91.485  82.900  1.00 53.94           N  
ATOM     50  N   VAL A  12      32.194  91.335  78.194  1.00 35.47           N  
ATOM     51  CA  VAL A  12      31.696  91.315  76.818  1.00 35.21           C  
ATOM     52  C   VAL A  12      32.477  92.253  75.901  1.00 40.80           C  
ATOM     53  O   VAL A  12      33.170  93.148  76.395  1.00 54.96           O  
ATOM     54  CB  VAL A  12      30.230  91.705  76.767  1.00 32.35           C  
ATOM     55  CG1 VAL A  12      29.438  90.683  77.543  1.00 34.88           C  
ATOM     56  CG2 VAL A  12      30.112  93.038  77.448  1.00 32.32           C  
ATOM     57  N   SER A  13      32.376  92.059  74.570  1.00 43.05           N  
ATOM     58  CA  SER A  13      33.202  92.826  73.639  1.00 56.50           C  
ATOM     59  C   SER A  13      32.548  92.892  72.275  1.00 79.69           C  
ATOM     60  O   SER A  13      32.432  91.887  71.592  1.00 97.68           O  
ATOM     61  CB  SER A  13      34.575  92.273  73.446  1.00 52.26           C  
ATOM     62  OG  SER A  13      34.513  90.966  72.906  1.00 67.38           O  
ATOM     63  N   TYR A  14      32.143  94.098  71.873  1.00105.79           N  
ATOM     64  CA  TYR A  14      31.514  94.357  70.588  1.00103.20           C  
ATOM     65  C   TYR A  14      32.139  95.614  70.011  1.00107.56           C  
ATOM     66  O   TYR A  14      32.318  96.610  70.725  1.00125.70           O  
ATOM     67  CB  TYR A  14      29.999  94.557  70.706  1.00 88.22           C  
ATOM     68  CG  TYR A  14      29.367  95.015  69.426  1.00 74.41           C  
ATOM     69  CD1 TYR A  14      29.324  94.128  68.351  1.00104.44           C  
ATOM     70  CD2 TYR A  14      28.900  96.310  69.253  1.00 67.50           C  
ATOM     71  CE1 TYR A  14      28.807  94.497  67.116  1.00129.73           C  
ATOM     72  CE2 TYR A  14      28.399  96.687  68.013  1.00111.07           C  
ATOM     73  CZ  TYR A  14      28.343  95.786  66.938  1.00130.68           C  
ATOM     74  OH  TYR A  14      27.883  96.059  65.673  1.00 99.05           O  
ATOM     75  N   GLY A  15      32.452  95.513  68.718  1.00113.04           N  
ATOM     76  CA  GLY A  15      33.151  96.564  68.001  1.00123.85           C  
ATOM     77  C   GLY A  15      34.538  96.773  68.582  1.00 97.89           C  
ATOM     78  O   GLY A  15      35.030  97.909  68.607  1.00 78.18           O  
ATOM     79  N   GLY A  16      35.119  95.640  69.011  1.00 90.71           N  
ATOM     80  CA  GLY A  16      36.508  95.545  69.414  1.00123.86           C  
ATOM     81  C   GLY A  16      36.828  96.410  70.628  1.00124.15           C  
ATOM     82  O   GLY A  16      37.995  96.748  70.879  1.00166.99           O  
ATOM     83  N   VAL A  17      35.799  96.683  71.434  1.00 89.04           N  
ATOM     84  CA  VAL A  17      36.030  97.280  72.739  1.00 89.17           C  
ATOM     85  C   VAL A  17      35.546  96.327  73.821  1.00 76.75           C  
ATOM     86  O   VAL A  17      34.357  96.088  73.950  1.00 81.47           O  
ATOM     87  CB  VAL A  17      35.302  98.615  72.871  1.00105.14           C  
ATOM     88  CG1 VAL A  17      35.597  99.206  74.248  1.00129.24           C  
ATOM     89  CG2 VAL A  17      35.673  99.547  71.727  1.00123.87           C  
ATOM     90  N   LEU A  18      36.481  95.786  74.591  1.00 69.55           N  
ATOM     91  CA  LEU A  18      36.114  94.891  75.668  1.00 68.67           C  
ATOM     92  C   LEU A  18      35.585  95.731  76.810  1.00 56.84           C  
ATOM     93  O   LEU A  18      36.082  96.832  77.066  1.00 71.18           O  
ATOM     94  CB  LEU A  18      37.383  94.136  76.081  1.00109.28           C  
ATOM     95  CG  LEU A  18      37.246  93.071  77.174  1.00149.30           C  
ATOM     96  CD1 LEU A  18      36.278  91.965  76.783  1.00158.27           C  
ATOM     97  CD2 LEU A  18      38.609  92.490  77.529  1.00198.46           C  
ATOM     98  N   ARG A  19      34.621  95.171  77.534  1.00 51.66           N  
ATOM     99  CA  ARG A  19      34.140  95.856  78.716  1.00 60.27           C  
ATOM    100  C   ARG A  19      34.085  94.859  79.846  1.00 72.49           C  
ATOM    101  O   ARG A  19      34.576  93.755  79.716  1.00 75.32           O  
ATOM    102  CB  ARG A  19      32.768  96.447  78.449  1.00 58.80           C  
ATOM    103  CG  ARG A  19      32.763  97.381  77.254  1.00 70.73           C  
ATOM    104  CD  ARG A  19      31.938  98.675  77.418  1.00 86.47           C  
ATOM    105  NE  ARG A  19      32.172  99.148  78.790  1.00100.65           N  
ATOM    106  CZ  ARG A  19      31.532 100.168  79.387  1.00112.84           C  
ATOM    107  NH1 ARG A  19      30.641 100.881  78.701  1.00103.87           N  
ATOM    108  NH2 ARG A  19      31.865 100.501  80.627  1.00104.61           N  
ATOM    109  N   ARG A  20      33.570  95.255  81.002  1.00 72.78           N  
ATOM    110  CA  ARG A  20      33.432  94.235  82.032  1.00 70.29           C  
ATOM    111  C   ARG A  20      32.509  94.774  83.104  1.00 68.18           C  
ATOM    112  O   ARG A  20      32.617  95.951  83.493  1.00 66.87           O  
ATOM    113  CB  ARG A  20      34.767  93.713  82.620  1.00 75.35           C  
ATOM    114  CG  ARG A  20      35.351  94.583  83.704  1.00100.78           C  
ATOM    115  CD  ARG A  20      35.101  93.899  85.027  1.00106.50           C  
ATOM    116  NE  ARG A  20      36.122  94.056  86.065  1.00101.27           N  
ATOM    117  CZ  ARG A  20      37.266  93.374  86.132  1.00 98.78           C  
ATOM    118  NH1 ARG A  20      38.106  93.590  87.142  1.00 85.88           N  
ATOM    119  NH2 ARG A  20      37.562  92.527  85.154  1.00 81.66           N  
ATOM    120  N   PHE A  21      31.668  93.861  83.588  1.00 77.22           N  
ATOM    121  CA  PHE A  21      30.776  94.104  84.718  1.00 96.46           C  
ATOM    122  C   PHE A  21      30.553  92.798  85.459  1.00 81.21           C  
ATOM    123  O   PHE A  21      30.898  91.739  84.955  1.00 79.75           O  
ATOM    124  CB  PHE A  21      29.451  94.752  84.301  1.00112.06           C  
ATOM    125  CG  PHE A  21      28.549  93.898  83.457  1.00106.68           C  
ATOM    126  CD1 PHE A  21      28.703  93.852  82.083  1.00107.57           C  
ATOM    127  CD2 PHE A  21      27.526  93.172  84.040  1.00107.97           C  
ATOM    128  CE1 PHE A  21      27.850  93.066  81.322  1.00126.33           C  
ATOM    129  CE2 PHE A  21      26.670  92.397  83.272  1.00105.18           C  
ATOM    130  CZ  PHE A  21      26.829  92.348  81.912  1.00116.02           C  
ATOM    131  N   ARG A  22      29.984  92.907  86.658  1.00 69.27           N  
ATOM    132  CA  ARG A  22      29.861  91.744  87.517  1.00 76.85           C  
ATOM    133  C   ARG A  22      28.387  91.426  87.755  1.00 93.23           C  
ATOM    134  O   ARG A  22      27.529  92.303  87.668  1.00110.01           O  
ATOM    135  CB  ARG A  22      30.532  92.059  88.842  1.00 80.23           C  
ATOM    136  CG  ARG A  22      31.742  92.972  88.695  1.00100.36           C  
ATOM    137  CD  ARG A  22      32.552  93.061  89.976  1.00147.72           C  
ATOM    138  NE  ARG A  22      32.935  91.787  90.595  1.00176.08           N  
ATOM    139  CZ  ARG A  22      32.393  91.281  91.703  1.00189.91           C  
ATOM    140  NH1 ARG A  22      31.422  91.950  92.304  1.00213.88           N  
ATOM    141  NH2 ARG A  22      32.818  90.126  92.187  1.00189.84           N  
ATOM    142  N   VAL A  23      28.102  90.164  88.071  1.00 78.98           N  
ATOM    143  CA  VAL A  23      26.738  89.706  88.262  1.00 74.33           C  
ATOM    144  C   VAL A  23      26.724  88.855  89.518  1.00 88.96           C  
ATOM    145  O   VAL A  23      27.452  87.856  89.611  1.00107.10           O  
ATOM    146  CB  VAL A  23      26.277  88.839  87.078  1.00 88.58           C  
ATOM    147  CG1 VAL A  23      24.962  88.130  87.374  1.00108.34           C  
ATOM    148  CG2 VAL A  23      26.147  89.640  85.813  1.00117.95           C  
ATOM    149  N   PRO A  24      25.871  89.173  90.516  1.00 88.39           N  
ATOM    150  CA  PRO A  24      25.890  88.405  91.771  1.00 88.75           C  
ATOM    151  C   PRO A  24      25.176  87.056  91.647  1.00 90.68           C  
ATOM    152  O   PRO A  24      24.442  86.833  90.685  1.00 92.94           O  
ATOM    153  CB  PRO A  24      25.161  89.378  92.704  1.00 93.28           C  
ATOM    154  CG  PRO A  24      24.132  90.036  91.776  1.00102.24           C  
ATOM    155  CD  PRO A  24      24.854  90.248  90.464  1.00 77.17           C  
ATOM    156  N   VAL A  25      25.391  86.177  92.623  1.00 82.04           N  
ATOM    157  CA  VAL A  25      24.634  84.934  92.710  1.00 93.96           C  
ATOM    158  C   VAL A  25      23.906  84.898  94.044  1.00103.41           C  
ATOM    159  O   VAL A  25      24.310  85.606  94.977  1.00101.38           O  
ATOM    160  CB  VAL A  25      25.500  83.668  92.551  1.00113.49           C  
ATOM    161  CG1 VAL A  25      26.409  83.749  91.340  1.00147.25           C  
ATOM    162  CG2 VAL A  25      26.280  83.318  93.808  1.00133.64           C  
ATOM    163  N   LYS A  26      22.870  84.047  94.103  1.00123.79           N  
ATOM    164  CA  LYS A  26      22.080  83.828  95.300  1.00130.25           C  
ATOM    165  C   LYS A  26      22.887  83.044  96.329  1.00135.36           C  
ATOM    166  O   LYS A  26      24.055  82.689  96.134  1.00137.62           O  
ATOM    167  CB  LYS A  26      20.823  83.014  95.015  1.00121.00           C  
ATOM    168  CG  LYS A  26      19.816  83.661  94.087  1.00161.28           C  
ATOM    169  CD  LYS A  26      18.935  82.603  93.429  1.00210.08           C  
ATOM    170  CE  LYS A  26      18.330  82.996  92.085  1.00289.38           C  
ATOM    171  NZ  LYS A  26      17.653  81.873  91.379  1.00320.00           N  
ATOM    172  N   ALA A  27      22.218  82.765  97.445  1.00132.58           N  
ATOM    173  CA  ALA A  27      22.758  81.829  98.411  1.00134.89           C  
ATOM    174  C   ALA A  27      22.591  80.408  97.871  1.00119.82           C  
ATOM    175  O   ALA A  27      23.368  79.513  98.209  1.00128.52           O  
ATOM    176  CB  ALA A  27      22.061  82.021  99.736  1.00174.14           C  
ATOM    177  N   ASN A  28      21.569  80.206  97.037  1.00 86.17           N  
ATOM    178  CA  ASN A  28      21.258  78.872  96.554  1.00 76.85           C  
ATOM    179  C   ASN A  28      22.337  78.415  95.587  1.00 77.45           C  
ATOM    180  O   ASN A  28      22.792  77.271  95.691  1.00 84.13           O  
ATOM    181  CB  ASN A  28      19.937  78.877  95.797  1.00110.87           C  
ATOM    182  CG  ASN A  28      19.433  77.479  95.504  1.00143.64           C  
ATOM    183  OD1 ASN A  28      19.984  76.511  96.034  1.00154.04           O  
ATOM    184  ND2 ASN A  28      18.430  77.363  94.638  1.00165.61           N  
ATOM    185  N   GLY A  29      22.684  79.275  94.610  1.00 97.93           N  
ATOM    186  CA  GLY A  29      23.855  79.060  93.769  1.00110.05           C  
ATOM    187  C   GLY A  29      23.645  79.404  92.303  1.00 92.60           C  
ATOM    188  O   GLY A  29      24.594  79.332  91.530  1.00 91.43           O  
ATOM    189  N   GLN A  30      22.431  79.808  91.917  1.00103.26           N  
ATOM    190  CA  GLN A  30      22.212  80.158  90.520  1.00118.58           C  
ATOM    191  C   GLN A  30      22.415  81.651  90.288  1.00145.59           C  
ATOM    192  O   GLN A  30      22.325  82.436  91.213  1.00153.81           O  
ATOM    193  CB  GLN A  30      20.819  79.756  90.068  1.00118.68           C  
ATOM    194  CG  GLN A  30      20.668  78.254  90.006  1.00152.28           C  
ATOM    195  CD  GLN A  30      19.289  77.893  89.512  1.00232.74           C  
ATOM    196  OE1 GLN A  30      18.483  78.753  89.156  1.00268.84           O  
ATOM    197  NE2 GLN A  30      19.021  76.598  89.459  1.00282.91           N  
ATOM    198  N   LEU A  31      22.662  82.031  89.031  1.00144.46           N  
ATOM    199  CA  LEU A  31      22.894  83.414  88.657  1.00138.67           C  
ATOM    200  C   LEU A  31      21.618  84.221  88.836  1.00152.57           C  
ATOM    201  O   LEU A  31      20.527  83.739  88.530  1.00176.68           O  
ATOM    202  CB  LEU A  31      23.280  83.431  87.183  1.00153.35           C  
ATOM    203  CG  LEU A  31      24.614  82.777  86.852  1.00193.79           C  
ATOM    204  CD1 LEU A  31      24.912  82.923  85.372  1.00238.90           C  
ATOM    205  CD2 LEU A  31      25.729  83.400  87.668  1.00233.52           C  
ATOM    206  N   ASP A  32      21.771  85.473  89.263  1.00142.26           N  
ATOM    207  CA  ASP A  32      20.592  86.241  89.615  1.00152.92           C  
ATOM    208  C   ASP A  32      20.158  87.163  88.475  1.00147.81           C  
ATOM    209  O   ASP A  32      19.837  88.323  88.725  1.00159.53           O  
ATOM    210  CB  ASP A  32      20.784  86.959  90.952  1.00157.83           C  
ATOM    211  CG  ASP A  32      19.473  87.308  91.627  1.00185.88           C  
ATOM    212  OD1 ASP A  32      18.403  87.020  91.032  1.00200.14           O  
ATOM    213  OD2 ASP A  32      19.528  87.866  92.736  1.00191.44           O  
ATOM    214  N   LEU A  33      20.146  86.645  87.237  1.00130.03           N  
ATOM    215  CA  LEU A  33      19.469  87.287  86.107  1.00109.30           C  
ATOM    216  C   LEU A  33      19.125  86.279  85.027  1.00 88.93           C  
ATOM    217  O   LEU A  33      19.543  85.135  85.089  1.00105.84           O  
ATOM    218  CB  LEU A  33      20.234  88.477  85.499  1.00157.28           C  
ATOM    219  CG  LEU A  33      21.708  88.330  85.100  1.00200.60           C  
ATOM    220  CD1 LEU A  33      21.887  87.786  83.683  1.00213.66           C  
ATOM    221  CD2 LEU A  33      22.391  89.692  85.183  1.00252.08           C  
ATOM    222  N   GLU A  34      18.360  86.730  84.035  1.00 89.14           N  
ATOM    223  CA  GLU A  34      17.988  85.873  82.926  1.00 98.31           C  
ATOM    224  C   GLU A  34      18.234  86.605  81.609  1.00121.07           C  
ATOM    225  O   GLU A  34      18.626  87.772  81.613  1.00121.70           O  
ATOM    226  CB  GLU A  34      16.523  85.499  83.052  1.00113.49           C  
ATOM    227  CG  GLU A  34      15.584  86.668  82.828  1.00167.21           C  
ATOM    228  CD  GLU A  34      15.323  87.474  84.096  1.00225.85           C  
ATOM    229  OE1 GLU A  34      16.038  87.243  85.104  1.00223.59           O  
ATOM    230  OE2 GLU A  34      14.418  88.329  84.077  1.00292.22           O  
ATOM    231  N   MET A  35      17.976  85.922  80.491  1.00124.90           N  
ATOM    232  CA  MET A  35      18.398  86.412  79.184  1.00127.34           C  
ATOM    233  C   MET A  35      17.713  87.735  78.815  1.00101.19           C  
ATOM    234  O   MET A  35      18.322  88.631  78.224  1.00 89.74           O  
ATOM    235  CB  MET A  35      18.123  85.345  78.120  1.00119.66           C  
ATOM    236  CG  MET A  35      19.199  84.291  78.107  1.00 90.29           C  
ATOM    237  SD  MET A  35      20.785  85.059  77.724  1.00110.25           S  
ATOM    238  CE  MET A  35      20.609  85.400  75.971  1.00160.86           C  
ATOM    239  N   ALA A  36      16.425  87.834  79.127  1.00100.10           N  
ATOM    240  CA  ALA A  36      15.740  89.067  78.790  1.00117.04           C  
ATOM    241  C   ALA A  36      16.250  90.180  79.699  1.00116.28           C  
ATOM    242  O   ALA A  36      16.101  91.361  79.363  1.00157.66           O  
ATOM    243  CB  ALA A  36      14.233  88.886  78.899  1.00180.52           C  
ATOM    244  N   GLY A  37      16.720  89.792  80.899  1.00100.87           N  
ATOM    245  CA  GLY A  37      17.398  90.673  81.839  1.00115.12           C  
ATOM    246  C   GLY A  37      18.847  90.921  81.431  1.00101.73           C  
ATOM    247  O   GLY A  37      19.467  91.879  81.893  1.00102.97           O  
ATOM    248  N   LEU A  38      19.373  90.059  80.558  1.00 82.75           N  
ATOM    249  CA  LEU A  38      20.762  90.183  80.179  1.00 82.81           C  
ATOM    250  C   LEU A  38      20.896  90.943  78.865  1.00 74.86           C  
ATOM    251  O   LEU A  38      21.789  91.768  78.704  1.00 68.06           O  
ATOM    252  CB  LEU A  38      21.367  88.780  80.087  1.00115.74           C  
ATOM    253  CG  LEU A  38      22.865  88.758  79.753  1.00175.18           C  
ATOM    254  CD1 LEU A  38      23.705  89.431  80.828  1.00213.10           C  
ATOM    255  CD2 LEU A  38      23.397  87.373  79.393  1.00180.47           C  
ATOM    256  N   LYS A  39      20.040  90.622  77.900  1.00 81.53           N  
ATOM    257  CA  LYS A  39      20.224  91.172  76.571  1.00 88.80           C  
ATOM    258  C   LYS A  39      19.862  92.653  76.559  1.00103.37           C  
ATOM    259  O   LYS A  39      20.321  93.404  75.710  1.00122.43           O  
ATOM    260  CB  LYS A  39      19.357  90.409  75.577  1.00 90.63           C  
ATOM    261  CG  LYS A  39      19.871  89.016  75.280  1.00 83.19           C  
ATOM    262  CD  LYS A  39      18.838  88.200  74.586  1.00107.86           C  
ATOM    263  CE  LYS A  39      18.402  88.835  73.281  1.00162.11           C  
ATOM    264  NZ  LYS A  39      17.122  88.275  72.782  1.00217.05           N  
ATOM    265  N   GLU A  40      18.985  93.083  77.464  1.00 95.29           N  
ATOM    266  CA  GLU A  40      18.676  94.500  77.563  1.00 90.78           C  
ATOM    267  C   GLU A  40      19.717  95.189  78.436  1.00 94.25           C  
ATOM    268  O   GLU A  40      19.801  96.418  78.419  1.00 94.11           O  
ATOM    269  CB  GLU A  40      17.282  94.725  78.111  1.00121.49           C  
ATOM    270  CG  GLU A  40      16.216  94.105  77.242  1.00200.51           C  
ATOM    271  CD  GLU A  40      14.820  94.095  77.836  1.00319.13           C  
ATOM    272  OE1 GLU A  40      14.661  94.479  79.017  1.00358.18           O  
ATOM    273  OE2 GLU A  40      13.889  93.710  77.109  1.00363.26           O  
ATOM    274  N   LYS A  41      20.515  94.410  79.185  1.00 84.93           N  
ATOM    275  CA  LYS A  41      21.646  94.979  79.909  1.00 85.84           C  
ATOM    276  C   LYS A  41      22.853  95.235  78.988  1.00 93.58           C  
ATOM    277  O   LYS A  41      23.554  96.228  79.148  1.00 83.52           O  
ATOM    278  CB  LYS A  41      21.954  94.081  81.097  1.00 84.45           C  
ATOM    279  CG  LYS A  41      23.209  94.433  81.862  1.00106.25           C  
ATOM    280  CD  LYS A  41      23.096  95.779  82.530  1.00135.62           C  
ATOM    281  CE  LYS A  41      24.378  96.184  83.225  1.00195.50           C  
ATOM    282  NZ  LYS A  41      24.454  97.650  83.471  1.00248.61           N  
ATOM    283  N   ILE A  42      23.091  94.350  78.014  1.00 96.74           N  
ATOM    284  CA  ILE A  42      24.131  94.529  77.003  1.00 89.04           C  
ATOM    285  C   ILE A  42      23.799  95.724  76.114  1.00 95.08           C  
ATOM    286  O   ILE A  42      24.685  96.475  75.754  1.00 89.80           O  
ATOM    287  CB  ILE A  42      24.275  93.246  76.177  1.00100.26           C  
ATOM    288  CG1 ILE A  42      24.866  92.143  77.062  1.00132.13           C  
ATOM    289  CG2 ILE A  42      25.011  93.440  74.841  1.00 99.12           C  
ATOM    290  CD1 ILE A  42      24.844  90.738  76.460  1.00173.51           C  
ATOM    291  N   ALA A  43      22.513  95.951  75.831  1.00110.04           N  
ATOM    292  CA  ALA A  43      22.116  97.062  74.979  1.00110.86           C  
ATOM    293  C   ALA A  43      22.298  98.400  75.699  1.00 99.20           C  
ATOM    294  O   ALA A  43      22.227  99.452  75.086  1.00 99.04           O  
ATOM    295  CB  ALA A  43      20.692  96.870  74.516  1.00120.45           C  
ATOM    296  N   ALA A  44      22.484  98.362  77.015  1.00100.95           N  
ATOM    297  CA  ALA A  44      22.782  99.569  77.765  1.00117.86           C  
ATOM    298  C   ALA A  44      24.244  99.960  77.606  1.00 88.58           C  
ATOM    299  O   ALA A  44      24.575 101.141  77.609  1.00 80.26           O  
ATOM    300  CB  ALA A  44      22.438  99.397  79.227  1.00159.81           C  
ATOM    301  N   LEU A  45      25.117  98.964  77.500  1.00 86.30           N  
ATOM    302  CA  LEU A  45      26.542  99.254  77.501  1.00 98.62           C  
ATOM    303  C   LEU A  45      26.946  99.837  76.161  1.00 76.63           C  
ATOM    304  O   LEU A  45      27.807 100.713  76.129  1.00 79.58           O  
ATOM    305  CB  LEU A  45      27.356  97.983  77.780  1.00120.15           C  
ATOM    306  CG  LEU A  45      27.244  97.327  79.161  1.00140.56           C  
ATOM    307  CD1 LEU A  45      27.939  95.965  79.170  1.00 97.43           C  
ATOM    308  CD2 LEU A  45      27.901  98.231  80.198  1.00156.53           C  
ATOM    309  N   PHE A  46      26.358  99.306  75.079  1.00 70.23           N  
ATOM    310  CA  PHE A  46      26.882  99.565  73.754  1.00 87.67           C  
ATOM    311  C   PHE A  46      26.090 100.587  72.948  1.00102.11           C  
ATOM    312  O   PHE A  46      26.461 100.874  71.811  1.00 98.05           O  
ATOM    313  CB  PHE A  46      27.088  98.259  73.001  1.00104.76           C  
ATOM    314  CG  PHE A  46      28.266  97.473  73.514  1.00109.55           C  
ATOM    315  CD1 PHE A  46      29.555  97.745  73.082  1.00 91.88           C  
ATOM    316  CD2 PHE A  46      28.087  96.541  74.522  1.00102.76           C  
ATOM    317  CE1 PHE A  46      30.607  97.007  73.583  1.00 61.34           C  
ATOM    318  CE2 PHE A  46      29.155  95.829  75.032  1.00 73.30           C  
ATOM    319  CZ  PHE A  46      30.393  96.047  74.542  1.00 56.00           C  
ATOM    320  N   ASN A  47      25.012 101.118  73.531  1.00143.30           N  
ATOM    321  CA  ASN A  47      24.061 102.004  72.859  1.00154.43           C  
ATOM    322  C   ASN A  47      23.534 101.393  71.566  1.00113.83           C  
ATOM    323  O   ASN A  47      23.379 102.072  70.554  1.00101.64           O  
ATOM    324  CB  ASN A  47      24.621 103.407  72.622  1.00220.20           C  
ATOM    325  CG  ASN A  47      24.676 104.224  73.891  1.00301.27           C  
ATOM    326  OD1 ASN A  47      23.736 104.215  74.686  1.00333.90           O  
ATOM    327  ND2 ASN A  47      25.767 104.948  74.087  1.00342.52           N  
ATOM    328  N   LEU A  48      23.230 100.102  71.626  1.00 99.16           N  
ATOM    329  CA  LEU A  48      22.618  99.434  70.500  1.00101.87           C  
ATOM    330  C   LEU A  48      21.114  99.620  70.593  1.00125.43           C  
ATOM    331  O   LEU A  48      20.546  99.709  71.684  1.00123.32           O  
ATOM    332  CB  LEU A  48      22.964  97.950  70.586  1.00142.35           C  
ATOM    333  CG  LEU A  48      24.428  97.612  70.327  1.00203.86           C  
ATOM    334  CD1 LEU A  48      24.662  96.119  70.537  1.00221.46           C  
ATOM    335  CD2 LEU A  48      24.797  98.008  68.905  1.00238.83           C  
ATOM    336  N   SER A  49      20.472  99.656  69.426  1.00176.54           N  
ATOM    337  CA  SER A  49      19.019  99.607  69.371  1.00238.65           C  
ATOM    338  C   SER A  49      18.549  98.219  69.796  1.00241.33           C  
ATOM    339  O   SER A  49      19.018  97.216  69.269  1.00237.66           O  
ATOM    340  CB  SER A  49      18.513  99.978  68.004  1.00304.31           C  
ATOM    341  OG  SER A  49      18.847 101.324  67.689  1.00345.59           O  
ATOM    342  N   ALA A  50      17.622  98.181  70.758  1.00269.95           N  
ATOM    343  CA  ALA A  50      17.267  96.952  71.451  1.00317.78           C  
ATOM    344  C   ALA A  50      16.496  95.995  70.542  1.00326.60           C  
ATOM    345  O   ALA A  50      16.426  94.797  70.820  1.00351.98           O  
ATOM    346  CB  ALA A  50      16.499  97.273  72.712  1.00384.27           C  
ATOM    347  N   ASP A  51      15.932  96.524  69.455  1.00377.92           N  
ATOM    348  CA  ASP A  51      15.148  95.709  68.542  1.00433.94           C  
ATOM    349  C   ASP A  51      16.055  94.851  67.659  1.00356.74           C  
ATOM    350  O   ASP A  51      15.583  93.921  67.006  1.00390.75           O  
ATOM    351  CB  ASP A  51      14.204  96.587  67.719  1.00440.00           C  
ATOM    352  CG  ASP A  51      14.910  97.690  66.947  1.00440.00           C  
ATOM    353  OD1 ASP A  51      16.131  97.868  67.148  1.00440.00           O  
ATOM    354  OD2 ASP A  51      14.230  98.376  66.161  1.00440.00           O  
ATOM    355  N   ALA A  52      17.348  95.192  67.612  1.00229.04           N  
ATOM    356  CA  ALA A  52      18.298  94.427  66.822  1.00224.16           C  
ATOM    357  C   ALA A  52      18.496  93.044  67.432  1.00227.20           C  
ATOM    358  O   ALA A  52      18.321  92.839  68.633  1.00235.28           O  
ATOM    359  CB  ALA A  52      19.600  95.176  66.696  1.00255.36           C  
ATOM    360  N   GLU A  53      18.873  92.101  66.571  1.00239.41           N  
ATOM    361  CA  GLU A  53      19.150  90.734  66.977  1.00226.08           C  
ATOM    362  C   GLU A  53      20.547  90.631  67.581  1.00157.87           C  
ATOM    363  O   GLU A  53      21.494  91.224  67.078  1.00138.05           O  
ATOM    364  CB  GLU A  53      19.006  89.807  65.775  1.00317.72           C  
ATOM    365  CG  GLU A  53      17.563  89.654  65.324  1.00440.00           C  
ATOM    366  CD  GLU A  53      17.274  88.540  64.331  1.00440.00           C  
ATOM    367  OE1 GLU A  53      18.184  88.178  63.553  1.00440.00           O  
ATOM    368  OE2 GLU A  53      16.126  88.034  64.327  1.00440.00           O  
ATOM    369  N   LEU A  54      20.663  89.849  68.655  1.00101.15           N  
ATOM    370  CA  LEU A  54      21.956  89.567  69.232  1.00 83.21           C  
ATOM    371  C   LEU A  54      22.255  88.086  69.092  1.00124.58           C  
ATOM    372  O   LEU A  54      21.392  87.254  69.379  1.00145.43           O  
ATOM    373  CB  LEU A  54      21.873  89.910  70.700  1.00 70.68           C  
ATOM    374  CG  LEU A  54      21.806  91.394  70.941  1.00 79.54           C  
ATOM    375  CD1 LEU A  54      22.069  91.673  72.406  1.00122.75           C  
ATOM    376  CD2 LEU A  54      22.858  92.097  70.113  1.00102.38           C  
ATOM    377  N   SER A  55      23.493  87.793  68.679  1.00135.85           N  
ATOM    378  CA  SER A  55      23.980  86.429  68.615  1.00132.53           C  
ATOM    379  C   SER A  55      25.145  86.264  69.596  1.00111.72           C  
ATOM    380  O   SER A  55      26.296  86.613  69.293  1.00 87.60           O  
ATOM    381  CB  SER A  55      24.336  86.071  67.197  1.00159.03           C  
ATOM    382  OG  SER A  55      24.731  84.714  67.137  1.00232.85           O  
ATOM    383  N   LEU A  56      24.817  85.717  70.766  1.00 76.79           N  
ATOM    384  CA  LEU A  56      25.735  85.747  71.872  1.00 72.98           C  
ATOM    385  C   LEU A  56      26.355  84.370  71.999  1.00 73.04           C  
ATOM    386  O   LEU A  56      25.639  83.422  72.225  1.00 89.39           O  
ATOM    387  CB  LEU A  56      24.910  86.034  73.124  1.00 82.05           C  
ATOM    388  CG  LEU A  56      24.269  87.405  73.237  1.00 98.99           C  
ATOM    389  CD1 LEU A  56      23.493  87.434  74.545  1.00119.35           C  
ATOM    390  CD2 LEU A  56      25.346  88.486  73.244  1.00 89.80           C  
ATOM    391  N   THR A  57      27.680  84.298  71.995  1.00 67.40           N  
ATOM    392  CA  THR A  57      28.379  83.037  72.116  1.00 60.45           C  
ATOM    393  C   THR A  57      29.524  83.122  73.132  1.00 51.33           C  
ATOM    394  O   THR A  57      30.498  83.860  72.931  1.00 48.81           O  
ATOM    395  CB  THR A  57      28.938  82.733  70.726  1.00 87.08           C  
ATOM    396  OG1 THR A  57      29.857  83.761  70.322  1.00 90.65           O  
ATOM    397  CG2 THR A  57      27.824  82.659  69.700  1.00 81.22           C  
ATOM    398  N   TYR A  58      29.449  82.282  74.171  1.00 43.47           N  
ATOM    399  CA  TYR A  58      30.429  82.294  75.241  1.00 41.48           C  
ATOM    400  C   TYR A  58      31.553  81.333  74.928  1.00 41.53           C  
ATOM    401  O   TYR A  58      31.648  80.866  73.830  1.00 41.22           O  
ATOM    402  CB  TYR A  58      29.805  82.116  76.634  1.00 41.57           C  
ATOM    403  CG  TYR A  58      29.302  80.731  76.968  1.00 54.55           C  
ATOM    404  CD1 TYR A  58      28.017  80.380  76.611  1.00 82.65           C  
ATOM    405  CD2 TYR A  58      30.060  79.743  77.594  1.00 51.45           C  
ATOM    406  CE1 TYR A  58      27.478  79.122  76.839  1.00 75.53           C  
ATOM    407  CE2 TYR A  58      29.556  78.472  77.827  1.00 59.41           C  
ATOM    408  CZ  TYR A  58      28.262  78.158  77.431  1.00 74.46           C  
ATOM    409  OH  TYR A  58      27.691  76.937  77.636  1.00 75.82           O  
ATOM    410  N   SER A  59      32.402  81.073  75.915  1.00 49.39           N  
ATOM    411  CA  SER A  59      33.507  80.121  75.822  1.00 84.49           C  
ATOM    412  C   SER A  59      33.338  78.951  76.803  1.00 64.77           C  
ATOM    413  O   SER A  59      33.031  79.142  77.978  1.00 61.13           O  
ATOM    414  CB  SER A  59      34.854  80.787  75.998  1.00 95.83           C  
ATOM    415  OG  SER A  59      35.055  81.778  75.008  1.00109.80           O  
ATOM    416  N   ASP A  60      33.547  77.737  76.313  1.00 61.96           N  
ATOM    417  CA  ASP A  60      33.329  76.578  77.137  1.00 72.22           C  
ATOM    418  C   ASP A  60      34.541  76.445  78.039  1.00 77.81           C  
ATOM    419  O   ASP A  60      35.453  77.251  77.933  1.00 75.18           O  
ATOM    420  CB  ASP A  60      33.081  75.310  76.301  1.00132.71           C  
ATOM    421  CG  ASP A  60      32.842  74.054  77.151  1.00166.50           C  
ATOM    422  OD1 ASP A  60      32.846  74.175  78.377  1.00195.03           O  
ATOM    423  OD2 ASP A  60      32.613  72.957  76.585  1.00122.77           O  
ATOM    424  N   GLU A  61      34.578  75.375  78.857  1.00103.14           N  
ATOM    425  CA  GLU A  61      35.750  75.114  79.676  1.00121.85           C  
ATOM    426  C   GLU A  61      36.906  74.632  78.785  1.00167.33           C  
ATOM    427  O   GLU A  61      38.051  75.059  78.958  1.00205.53           O  
ATOM    428  CB  GLU A  61      35.414  74.162  80.815  1.00 96.98           C  
ATOM    429  CG  GLU A  61      35.064  72.803  80.267  1.00150.31           C  
ATOM    430  CD  GLU A  61      34.735  71.709  81.257  1.00242.51           C  
ATOM    431  OE1 GLU A  61      35.051  71.861  82.439  1.00272.07           O  
ATOM    432  OE2 GLU A  61      34.149  70.702  80.828  1.00307.36           O  
ATOM    433  N   ASP A  62      36.605  73.756  77.814  1.00152.26           N  
ATOM    434  CA  ASP A  62      37.617  73.143  76.964  1.00120.65           C  
ATOM    435  C   ASP A  62      37.574  73.727  75.547  1.00 95.27           C  
ATOM    436  O   ASP A  62      37.832  73.029  74.568  1.00 93.40           O  
ATOM    437  CB  ASP A  62      37.442  71.624  76.990  1.00157.81           C  
ATOM    438  CG  ASP A  62      36.096  71.172  76.437  1.00228.64           C  
ATOM    439  OD1 ASP A  62      35.263  72.029  76.129  1.00271.04           O  
ATOM    440  OD2 ASP A  62      35.911  69.951  76.300  1.00242.29           O  
ATOM    441  N   GLY A  63      37.170  74.988  75.437  1.00 94.69           N  
ATOM    442  CA  GLY A  63      37.561  75.889  74.366  1.00146.26           C  
ATOM    443  C   GLY A  63      36.635  75.912  73.151  1.00162.89           C  
ATOM    444  O   GLY A  63      36.990  76.489  72.121  1.00205.05           O  
ATOM    445  N   ASP A  64      35.436  75.341  73.259  1.00128.45           N  
ATOM    446  CA  ASP A  64      34.502  75.439  72.152  1.00110.97           C  
ATOM    447  C   ASP A  64      33.855  76.820  72.113  1.00 90.12           C  
ATOM    448  O   ASP A  64      33.911  77.556  73.080  1.00 96.38           O  
ATOM    449  CB  ASP A  64      33.476  74.315  72.240  1.00169.29           C  
ATOM    450  CG  ASP A  64      34.051  72.945  71.910  1.00229.90           C  
ATOM    451  OD1 ASP A  64      35.169  72.891  71.349  1.00224.21           O  
ATOM    452  OD2 ASP A  64      33.369  71.934  72.210  1.00286.93           O  
ATOM    453  N   VAL A  65      33.254  77.175  70.979  1.00 95.29           N  
ATOM    454  CA  VAL A  65      32.487  78.408  70.868  1.00100.06           C  
ATOM    455  C   VAL A  65      30.988  78.097  70.914  1.00 77.76           C  
ATOM    456  O   VAL A  65      30.337  77.879  69.893  1.00 92.91           O  
ATOM    457  CB  VAL A  65      32.871  79.177  69.591  1.00142.13           C  
ATOM    458  CG1 VAL A  65      32.034  80.438  69.422  1.00177.15           C  
ATOM    459  CG2 VAL A  65      34.365  79.482  69.554  1.00155.02           C  
ATOM    460  N   VAL A  66      30.448  78.047  72.126  1.00 51.53           N  
ATOM    461  CA  VAL A  66      29.091  77.591  72.372  1.00 46.35           C  
ATOM    462  C   VAL A  66      28.121  78.738  72.085  1.00 59.10           C  
ATOM    463  O   VAL A  66      28.517  79.892  72.197  1.00 72.09           O  
ATOM    464  CB  VAL A  66      29.030  77.216  73.859  1.00 42.92           C  
ATOM    465  CG1 VAL A  66      27.745  76.520  74.260  1.00 43.91           C  
ATOM    466  CG2 VAL A  66      30.156  76.279  74.142  1.00 44.89           C  
ATOM    467  N   ALA A  67      26.847  78.428  71.818  1.00 70.87           N  
ATOM    468  CA  ALA A  67      25.785  79.431  71.709  1.00 65.15           C  
ATOM    469  C   ALA A  67      24.976  79.619  73.004  1.00 61.45           C  
ATOM    470  O   ALA A  67      24.850  78.714  73.801  1.00 50.68           O  
ATOM    471  CB  ALA A  67      24.875  79.067  70.568  1.00 65.06           C  
ATOM    472  N   LEU A  68      24.427  80.819  73.200  1.00 71.03           N  
ATOM    473  CA  LEU A  68      23.465  81.129  74.249  1.00 67.81           C  
ATOM    474  C   LEU A  68      22.098  81.409  73.639  1.00 98.09           C  
ATOM    475  O   LEU A  68      21.952  82.276  72.778  1.00 98.99           O  
ATOM    476  CB  LEU A  68      23.890  82.418  74.917  1.00 50.88           C  
ATOM    477  CG  LEU A  68      25.048  82.237  75.852  1.00 63.13           C  
ATOM    478  CD1 LEU A  68      25.478  83.617  76.346  1.00 59.11           C  
ATOM    479  CD2 LEU A  68      24.568  81.302  76.974  1.00 97.43           C  
ATOM    480  N   VAL A  69      21.077  80.746  74.179  1.00139.62           N  
ATOM    481  CA  VAL A  69      19.750  80.824  73.588  1.00162.66           C  
ATOM    482  C   VAL A  69      18.699  80.964  74.675  1.00131.64           C  
ATOM    483  O   VAL A  69      17.615  81.465  74.409  1.00156.98           O  
ATOM    484  CB  VAL A  69      19.426  79.625  72.664  1.00222.14           C  
ATOM    485  CG1 VAL A  69      20.179  79.688  71.346  1.00288.45           C  
ATOM    486  CG2 VAL A  69      19.589  78.259  73.320  1.00201.32           C  
ATOM    487  N   ASP A  70      19.000  80.486  75.886  1.00123.11           N  
ATOM    488  CA  ASP A  70      17.928  80.260  76.842  1.00149.19           C  
ATOM    489  C   ASP A  70      18.472  80.342  78.252  1.00146.93           C  
ATOM    490  O   ASP A  70      19.686  80.465  78.439  1.00143.98           O  
ATOM    491  CB  ASP A  70      17.301  78.881  76.635  1.00207.25           C  
ATOM    492  CG  ASP A  70      18.317  77.747  76.612  1.00260.52           C  
ATOM    493  OD1 ASP A  70      19.534  78.024  76.650  1.00258.57           O  
ATOM    494  OD2 ASP A  70      17.887  76.582  76.551  1.00311.43           O  
ATOM    495  N   ASP A  71      17.545  80.297  79.218  1.00155.64           N  
ATOM    496  CA  ASP A  71      17.931  80.341  80.619  1.00177.12           C  
ATOM    497  C   ASP A  71      18.281  78.952  81.127  1.00148.71           C  
ATOM    498  O   ASP A  71      18.579  78.787  82.311  1.00128.34           O  
ATOM    499  CB  ASP A  71      16.887  81.031  81.491  1.00201.17           C  
ATOM    500  CG  ASP A  71      16.699  82.504  81.157  1.00210.48           C  
ATOM    501  OD1 ASP A  71      17.696  83.182  80.868  1.00161.30           O  
ATOM    502  OD2 ASP A  71      15.541  82.969  81.174  1.00240.79           O  
ATOM    503  N   ASN A  72      18.241  77.968  80.224  1.00116.20           N  
ATOM    504  CA  ASN A  72      18.695  76.634  80.576  1.00138.64           C  
ATOM    505  C   ASN A  72      20.215  76.548  80.519  1.00162.19           C  
ATOM    506  O   ASN A  72      20.829  75.829  81.298  1.00178.09           O  
ATOM    507  CB  ASN A  72      18.054  75.590  79.680  1.00172.20           C  
ATOM    508  CG  ASN A  72      16.551  75.552  79.840  1.00249.83           C  
ATOM    509  OD1 ASN A  72      16.035  75.632  80.953  1.00300.62           O  
ATOM    510  ND2 ASN A  72      15.833  75.410  78.738  1.00287.86           N  
ATOM    511  N   ASP A  73      20.825  77.259  79.568  1.00163.70           N  
ATOM    512  CA  ASP A  73      22.270  77.238  79.399  1.00153.28           C  
ATOM    513  C   ASP A  73      22.963  78.297  80.250  1.00100.81           C  
ATOM    514  O   ASP A  73      24.170  78.254  80.451  1.00 88.26           O  
ATOM    515  CB  ASP A  73      22.661  77.298  77.923  1.00186.18           C  
ATOM    516  CG  ASP A  73      22.346  76.013  77.159  1.00187.90           C  
ATOM    517  OD1 ASP A  73      22.390  74.917  77.777  1.00149.16           O  
ATOM    518  OD2 ASP A  73      22.062  76.106  75.939  1.00188.23           O  
ATOM    519  N   LEU A  74      22.190  79.221  80.793  1.00 98.58           N  
ATOM    520  CA  LEU A  74      22.744  80.132  81.785  1.00120.45           C  
ATOM    521  C   LEU A  74      22.906  79.431  83.135  1.00 89.10           C  
ATOM    522  O   LEU A  74      23.688  79.858  83.982  1.00 82.51           O  
ATOM    523  CB  LEU A  74      21.820  81.346  81.935  1.00175.13           C  
ATOM    524  CG  LEU A  74      22.241  82.593  81.151  1.00178.11           C  
ATOM    525  CD1 LEU A  74      22.105  82.372  79.651  1.00191.79           C  
ATOM    526  CD2 LEU A  74      21.427  83.806  81.579  1.00153.59           C  
ATOM    527  N   PHE A  75      22.137  78.375  83.352  1.00 87.50           N  
ATOM    528  CA  PHE A  75      22.343  77.575  84.531  1.00101.95           C  
ATOM    529  C   PHE A  75      23.672  76.832  84.435  1.00 92.50           C  
ATOM    530  O   PHE A  75      24.332  76.573  85.445  1.00111.51           O  
ATOM    531  CB  PHE A  75      21.188  76.602  84.737  1.00151.43           C  
ATOM    532  CG  PHE A  75      21.441  75.639  85.864  1.00231.47           C  
ATOM    533  CD1 PHE A  75      21.521  76.095  87.173  1.00275.12           C  
ATOM    534  CD2 PHE A  75      21.666  74.294  85.614  1.00286.46           C  
ATOM    535  CE1 PHE A  75      21.766  75.223  88.223  1.00321.78           C  
ATOM    536  CE2 PHE A  75      21.911  73.418  86.663  1.00359.16           C  
ATOM    537  CZ  PHE A  75      21.959  73.883  87.963  1.00373.06           C  
ATOM    538  N   ASP A  76      24.059  76.472  83.214  1.00 77.12           N  
ATOM    539  CA  ASP A  76      25.214  75.630  83.003  1.00 87.11           C  
ATOM    540  C   ASP A  76      26.523  76.378  83.255  1.00 97.98           C  
ATOM    541  O   ASP A  76      27.543  75.757  83.537  1.00122.32           O  
ATOM    542  CB  ASP A  76      25.155  75.039  81.608  1.00104.03           C  
ATOM    543  CG  ASP A  76      26.235  74.010  81.376  1.00135.75           C  
ATOM    544  OD1 ASP A  76      26.131  72.903  81.992  1.00131.12           O  
ATOM    545  OD2 ASP A  76      27.183  74.351  80.604  1.00121.54           O  
ATOM    546  N   VAL A  77      26.503  77.707  83.177  1.00 76.51           N  
ATOM    547  CA  VAL A  77      27.712  78.493  83.375  1.00 63.70           C  
ATOM    548  C   VAL A  77      28.213  78.433  84.807  1.00 62.33           C  
ATOM    549  O   VAL A  77      29.417  78.467  85.010  1.00 68.52           O  
ATOM    550  CB  VAL A  77      27.492  79.945  83.001  1.00 74.15           C  
ATOM    551  CG1 VAL A  77      28.828  80.660  83.125  1.00 95.52           C  
ATOM    552  CG2 VAL A  77      26.933  80.039  81.580  1.00104.50           C  
ATOM    553  N   THR A  78      27.311  78.243  85.764  1.00 72.65           N  
ATOM    554  CA  THR A  78      27.709  78.087  87.149  1.00 84.54           C  
ATOM    555  C   THR A  78      28.405  76.745  87.366  1.00 93.13           C  
ATOM    556  O   THR A  78      29.471  76.706  87.985  1.00106.81           O  
ATOM    557  CB  THR A  78      26.477  78.153  88.046  1.00116.71           C  
ATOM    558  OG1 THR A  78      25.573  77.093  87.717  1.00116.85           O  
ATOM    559  CG2 THR A  78      25.768  79.473  87.874  1.00138.06           C  
ATOM    560  N   ASN A  79      27.821  75.664  86.834  1.00 86.22           N  
ATOM    561  CA  ASN A  79      28.387  74.342  87.035  1.00100.43           C  
ATOM    562  C   ASN A  79      29.610  74.102  86.156  1.00 99.61           C  
ATOM    563  O   ASN A  79      30.337  73.127  86.365  1.00118.62           O  
ATOM    564  CB  ASN A  79      27.343  73.255  86.818  1.00107.08           C  
ATOM    565  CG  ASN A  79      26.354  73.225  87.953  1.00142.70           C  
ATOM    566  OD1 ASN A  79      26.717  73.396  89.115  1.00154.37           O  
ATOM    567  ND2 ASN A  79      25.101  72.999  87.613  1.00184.60           N  
ATOM    568  N   GLN A  80      29.794  74.958  85.150  1.00 87.20           N  
ATOM    569  CA  GLN A  80      30.906  74.776  84.235  1.00 83.13           C  
ATOM    570  C   GLN A  80      32.209  75.102  84.960  1.00 82.81           C  
ATOM    571  O   GLN A  80      33.263  74.631  84.554  1.00 78.98           O  
ATOM    572  CB  GLN A  80      30.674  75.658  83.012  1.00 94.10           C  
ATOM    573  CG  GLN A  80      31.550  75.321  81.843  1.00132.19           C  
ATOM    574  CD  GLN A  80      31.189  74.015  81.181  1.00139.36           C  
ATOM    575  OE1 GLN A  80      30.040  73.757  80.843  1.00103.44           O  
ATOM    576  NE2 GLN A  80      32.195  73.210  80.883  1.00148.87           N  
ATOM    577  N   ARG A  81      32.113  75.973  85.984  1.00116.60           N  
ATOM    578  CA  ARG A  81      33.221  76.391  86.833  1.00164.11           C  
ATOM    579  C   ARG A  81      34.334  77.076  86.018  1.00146.30           C  
ATOM    580  O   ARG A  81      35.442  76.563  85.847  1.00121.07           O  
ATOM    581  CB  ARG A  81      33.657  75.251  87.760  1.00244.30           C  
ATOM    582  CG  ARG A  81      34.554  75.706  88.901  1.00387.63           C  
ATOM    583  CD  ARG A  81      34.791  74.613  89.932  1.00440.00           C  
ATOM    584  NE  ARG A  81      33.613  74.297  90.740  1.00440.00           N  
ATOM    585  CZ  ARG A  81      32.875  73.188  90.658  1.00440.00           C  
ATOM    586  NH1 ARG A  81      33.181  72.219  89.809  1.00440.00           N  
ATOM    587  NH2 ARG A  81      31.839  73.032  91.467  1.00440.00           N  
ATOM    588  N   LEU A  82      33.981  78.239  85.482  1.00129.34           N  
ATOM    589  CA  LEU A  82      34.865  79.044  84.657  1.00107.96           C  
ATOM    590  C   LEU A  82      35.320  80.249  85.469  1.00124.85           C  
ATOM    591  O   LEU A  82      34.524  80.799  86.226  1.00159.25           O  
ATOM    592  CB  LEU A  82      34.083  79.515  83.422  1.00103.68           C  
ATOM    593  CG  LEU A  82      34.967  80.005  82.276  1.00161.52           C  
ATOM    594  CD1 LEU A  82      36.001  78.938  81.891  1.00170.68           C  
ATOM    595  CD2 LEU A  82      34.134  80.363  81.055  1.00198.55           C  
ATOM    596  N   LYS A  83      36.549  80.721  85.218  1.00131.62           N  
ATOM    597  CA  LYS A  83      37.155  81.763  86.042  1.00119.76           C  
ATOM    598  C   LYS A  83      36.578  83.154  85.759  1.00 79.86           C  
ATOM    599  O   LYS A  83      36.424  83.960  86.669  1.00 78.17           O  
ATOM    600  CB  LYS A  83      38.685  81.700  85.971  1.00195.79           C  
ATOM    601  CG  LYS A  83      39.347  82.352  84.759  1.00290.07           C  
ATOM    602  CD  LYS A  83      39.307  81.532  83.476  1.00373.25           C  
ATOM    603  CE  LYS A  83      40.158  80.278  83.515  1.00440.00           C  
ATOM    604  NZ  LYS A  83      40.120  79.545  82.227  1.00440.00           N  
ATOM    605  N   PHE A  84      36.305  83.447  84.494  1.00 63.77           N  
ATOM    606  CA  PHE A  84      35.511  84.600  84.114  1.00 63.16           C  
ATOM    607  C   PHE A  84      34.913  84.315  82.740  1.00 77.43           C  
ATOM    608  O   PHE A  84      35.575  83.740  81.869  1.00 89.60           O  
ATOM    609  CB  PHE A  84      36.335  85.876  84.131  1.00 57.52           C  
ATOM    610  CG  PHE A  84      37.220  86.047  82.930  1.00 63.83           C  
ATOM    611  CD1 PHE A  84      38.418  85.356  82.858  1.00 94.17           C  
ATOM    612  CD2 PHE A  84      36.871  86.877  81.876  1.00 62.41           C  
ATOM    613  CE1 PHE A  84      39.266  85.491  81.773  1.00128.04           C  
ATOM    614  CE2 PHE A  84      37.735  87.033  80.803  1.00 99.75           C  
ATOM    615  CZ  PHE A  84      38.926  86.343  80.752  1.00128.50           C  
ATOM    616  N   LEU A  85      33.624  84.628  82.578  1.00 81.03           N  
ATOM    617  CA  LEU A  85      32.931  84.306  81.349  1.00 69.46           C  
ATOM    618  C   LEU A  85      33.233  85.378  80.288  1.00 84.77           C  
ATOM    619  O   LEU A  85      33.380  86.571  80.626  1.00 98.78           O  
ATOM    620  CB  LEU A  85      31.458  84.240  81.727  1.00 64.19           C  
ATOM    621  CG  LEU A  85      30.583  83.723  80.600  1.00 90.83           C  
ATOM    622  CD1 LEU A  85      30.999  82.312  80.276  1.00115.62           C  
ATOM    623  CD2 LEU A  85      29.101  83.803  80.948  1.00137.66           C  
ATOM    624  N   LYS A  86      33.315  84.975  79.003  1.00 71.95           N  
ATOM    625  CA  LYS A  86      33.467  85.984  77.960  1.00 74.63           C  
ATOM    626  C   LYS A  86      32.433  85.838  76.858  1.00 70.13           C  
ATOM    627  O   LYS A  86      32.439  84.795  76.202  1.00117.59           O  
ATOM    628  CB  LYS A  86      34.812  85.815  77.291  1.00 84.60           C  
ATOM    629  CG  LYS A  86      35.946  85.847  78.302  1.00172.96           C  
ATOM    630  CD  LYS A  86      37.267  85.941  77.585  1.00280.00           C  
ATOM    631  CE  LYS A  86      37.401  87.196  76.746  1.00320.00           C  
ATOM    632  NZ  LYS A  86      37.618  88.417  77.557  1.00366.82           N  
ATOM    633  N   ILE A  87      31.598  86.862  76.622  1.00 53.96           N  
ATOM    634  CA  ILE A  87      30.512  86.735  75.669  1.00 46.48           C  
ATOM    635  C   ILE A  87      30.650  87.660  74.468  1.00 44.03           C  
ATOM    636  O   ILE A  87      30.720  88.861  74.630  1.00 46.63           O  
ATOM    637  CB  ILE A  87      29.225  87.034  76.390  1.00 48.86           C  
ATOM    638  CG1 ILE A  87      29.077  86.105  77.604  1.00 71.22           C  
ATOM    639  CG2 ILE A  87      28.086  86.971  75.365  1.00 50.98           C  
ATOM    640  CD1 ILE A  87      27.896  86.434  78.530  1.00132.88           C  
ATOM    641  N   ASN A  88      30.665  87.109  73.267  1.00 45.56           N  
ATOM    642  CA  ASN A  88      30.846  87.912  72.071  1.00 51.59           C  
ATOM    643  C   ASN A  88      29.504  88.284  71.461  1.00 79.87           C  
ATOM    644  O   ASN A  88      28.558  87.491  71.462  1.00100.44           O  
ATOM    645  CB  ASN A  88      31.482  87.096  70.969  1.00 61.67           C  
ATOM    646  CG  ASN A  88      32.882  86.704  71.356  1.00100.87           C  
ATOM    647  OD1 ASN A  88      33.593  87.525  71.943  1.00128.67           O  
ATOM    648  ND2 ASN A  88      33.273  85.469  71.052  1.00131.37           N  
ATOM    649  N   VAL A  89      29.438  89.507  70.947  1.00 76.84           N  
ATOM    650  CA  VAL A  89      28.207  89.997  70.343  1.00 69.51           C  
ATOM    651  C   VAL A  89      28.391  89.939  68.838  1.00 82.34           C  
ATOM    652  O   VAL A  89      29.403  90.446  68.346  1.00110.34           O  
ATOM    653  CB  VAL A  89      27.850  91.426  70.819  1.00 56.15           C  
ATOM    654  CG1 VAL A  89      26.567  91.892  70.163  1.00 49.62           C  
ATOM    655  CG2 VAL A  89      27.701  91.490  72.348  1.00 57.08           C  
ATOM    656  N   ASN A  90      27.393  89.383  68.144  1.00 77.26           N  
ATOM    657  CA  ASN A  90      27.272  89.583  66.715  1.00 99.79           C  
ATOM    658  C   ASN A  90      25.871  90.038  66.366  1.00126.55           C  
ATOM    659  O   ASN A  90      24.933  89.285  66.576  1.00125.81           O  
ATOM    660  CB  ASN A  90      27.694  88.348  65.947  1.00107.73           C  
ATOM    661  CG  ASN A  90      29.196  88.291  65.799  1.00121.60           C  
ATOM    662  OD1 ASN A  90      29.865  89.314  65.662  1.00117.35           O  
ATOM    663  ND2 ASN A  90      29.734  87.087  65.863  1.00143.04           N  
ATOM    664  N   ALA A  91      25.806  91.247  65.799  1.00172.43           N  
ATOM    665  CA  ALA A  91      24.552  91.878  65.438  1.00219.83           C  
ATOM    666  C   ALA A  91      24.471  92.086  63.933  1.00256.15           C  
ATOM    667  O   ALA A  91      25.487  92.017  63.243  1.00289.45           O  
ATOM    668  CB  ALA A  91      24.364  93.173  66.190  1.00203.91           C  
ATOM    669  N   GLY A  92      23.248  92.366  63.457  1.00270.78           N  
ATOM    670  CA  GLY A  92      22.951  92.701  62.072  1.00328.45           C  
ATOM    671  C   GLY A  92      23.213  91.548  61.113  1.00387.66           C  
ATOM    672  O   GLY A  92      22.483  90.541  61.207  1.00424.25           O  
TER     673      GLY A  92                                                      
MASTER      155    0    0    2    7    0    0    6  672    1    0    8          
END                                                                             
