HEADER    TRANSFERASE                             16-DEC-03   1UU8              
TITLE     STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN COMPLEX WITH BIM-1           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3-PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE-1;             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN, RESIDUES 51-360;                            
COMPND   5 SYNONYM: HPDK1;                                                      
COMPND   6 EC: 2.7.1.37;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1;                                
SOURCE  10 OTHER_DETAILS: BACULOVIRUS INFECTED                                  
KEYWDS    PROTEIN KINASE, PKB, PDK1, INHIBITOR, LY333531, BISINDOLYL MALEIMIDE, 
KEYWDS   2 BIM-1, DIABETES, CANCER, TRANSFERASE, SERINE/THREONINE-PROTEIN       
KEYWDS   3 KINASE                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.KOMANDER,G.S.KULAR,A.W.SCHUTTELKOPF,M.DEAK,K.R.PRAKASH,J.BAIN,      
AUTHOR   2 M.ELLIOT,M.GARRIDO-FRANCO,A.P.KOZIKOWSKI,D.R.ALESSI,D.M.F.VAN AALTEN 
REVDAT   4   13-DEC-23 1UU8    1       REMARK                                   
REVDAT   3   24-APR-19 1UU8    1       SOURCE REMARK LINK                       
REVDAT   2   24-FEB-09 1UU8    1       VERSN                                    
REVDAT   1   04-MAR-04 1UU8    0                                                
JRNL        AUTH   D.KOMANDER,G.S.KULAR,A.W.SCHUTTELKOPF,M.DEAK,K.R.PRAKASH,    
JRNL        AUTH 2 J.BAIN,M.ELLIOT,M.GARRIDO-FRANCO,A.P.KOZIKOWSKI,D.R.ALESSI,  
JRNL        AUTH 3 D.M.F.VAN AALTEN                                             
JRNL        TITL   INTERACTIONS OF LY333531 AND OTHER BISINDOLYL MALEIMIDE      
JRNL        TITL 2 INHIBITORS WITH PDK1                                         
JRNL        REF    STRUCTURE                     V.  12   215 2004              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   14962382                                                     
JRNL        DOI    10.1016/J.STR.2004.01.005                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.32                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 13551                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 547                             
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2221                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 88                                      
REMARK   3   SOLVENT ATOMS            : 47                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.19000                                              
REMARK   3    B22 (A**2) : 3.19000                                              
REMARK   3    B33 (A**2) : -6.37000                                             
REMARK   3    B12 (A**2) : -0.59000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.159         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.152         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.122         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.062         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: SOME SIDECHAINS REFINED WITH OCCUPANCY    
REMARK   3  = 0.00 DUE TO DISORDER. SOME RESIDUES MODELED AS ALANINE DUE TO     
REMARK   3  DISORDER.                                                           
REMARK   4                                                                      
REMARK   4 1UU8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-03.                  
REMARK 100 THE DEPOSITION ID IS D_1290014228.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13556                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1H1W                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 M AMMONIUM SULPHATE, 0.1 M TRIS      
REMARK 280  -HCL PH 7.50                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       32.01067            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       16.00533            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       16.00533            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       32.01067            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
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: PQS                                                   
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2035  LIES ON A SPECIAL POSITION.                          
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    51                                                      
REMARK 465     ASP A    52                                                      
REMARK 465     GLY A    53                                                      
REMARK 465     THR A    54                                                      
REMARK 465     ALA A    55                                                      
REMARK 465     ALA A    56                                                      
REMARK 465     GLU A    57                                                      
REMARK 465     PRO A    58                                                      
REMARK 465     ARG A    59                                                      
REMARK 465     PRO A    60                                                      
REMARK 465     GLY A    61                                                      
REMARK 465     ALA A    62                                                      
REMARK 465     GLY A    63                                                      
REMARK 465     SER A    64                                                      
REMARK 465     LEU A    65                                                      
REMARK 465     GLN A    66                                                      
REMARK 465     HIS A    67                                                      
REMARK 465     ALA A    68                                                      
REMARK 465     GLN A    69                                                      
REMARK 465     PRO A    70                                                      
REMARK 465     PRO A    71                                                      
REMARK 465     PRO A   232                                                      
REMARK 465     GLU A   233                                                      
REMARK 465     SER A   234                                                      
REMARK 465     LYS A   235                                                      
REMARK 465     GLN A   236                                                      
REMARK 465     ALA A   237                                                      
REMARK 465     ARG A   238                                                      
REMARK 465     ALA A   239                                                      
REMARK 465     THR A   359                                                      
REMARK 465     ALA A   360                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A  73    CG   CD   OE1  NE2                                  
REMARK 470     ARG A  75    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 116    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 120    CG   CD   CE   NZ                                   
REMARK 470     LYS A 169    CG   CD   CE   NZ                                   
REMARK 470     GLU A 215    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 228    CG   CD   CE   NZ                                   
REMARK 470     LYS A 257    CG   CD   CE   NZ                                   
REMARK 470     GLU A 303    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 304    CG   CD   CE   NZ                                   
REMARK 470     LYS A 323    CG   CD   CE   NZ                                   
REMARK 470     GLU A 328    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 357    CG   CD   CE   NZ                                   
REMARK 470     LEU A 358    CA   C    O    CB   CG   CD1  CD2                   
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A   78   NE   CZ   NH1  NH2                                  
REMARK 480     LYS A  163   CD   CE   NZ                                        
REMARK 480     LYS A  173   CD   CE   NZ                                        
REMARK 480     LYS A  199   CE   NZ                                             
REMARK 480     GLU A  256   CD   OE1  OE2                                       
REMARK 480     SER A  258   OG                                                  
REMARK 480     GLU A  343   CD   OE1  OE2                                       
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 151     -159.21   -117.92                                   
REMARK 500    ASP A 205       46.73   -165.17                                   
REMARK 500    ASP A 223       71.98     63.01                                   
REMARK 500    LYS A 257       66.75     60.75                                   
REMARK 500    SER A 258      122.07    179.61                                   
REMARK 500    ASN A 349       51.05   -164.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 185         0.06    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1365                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1366                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1367                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BI1 A1368                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1358                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1359                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1360                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1361                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1362                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1363                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1364                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1H1W   RELATED DB: PDB                                   
REMARK 900 HIGH RESOLUTION CRYSTAL STRUCTURE OF THE HUMAN PDK1 CATALYTIC DOMAIN 
REMARK 900 RELATED ID: 1OKY   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN COMPLEX WITH STAUROSPORINE  
REMARK 900 RELATED ID: 1OKZ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN COMPLEX WITH UCN-01         
REMARK 900 RELATED ID: 1UU3   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN COMPLEX WITH LY333531       
REMARK 900 RELATED ID: 1UU7   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN COMPLEX WITH BIM-2          
REMARK 900 RELATED ID: 1UU9   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN COMPLEX WITH BIM-3          
REMARK 900 RELATED ID: 1UVR   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN COMPLEX WITH BIM-8          
DBREF  1UU8 A   51   360  UNP    O15530   PDPK_HUMAN      51    360             
SEQRES   1 A  310  MET ASP GLY THR ALA ALA GLU PRO ARG PRO GLY ALA GLY          
SEQRES   2 A  310  SER LEU GLN HIS ALA GLN PRO PRO PRO GLN PRO ARG LYS          
SEQRES   3 A  310  LYS ARG PRO GLU ASP PHE LYS PHE GLY LYS ILE LEU GLY          
SEQRES   4 A  310  GLU GLY SER PHE SER THR VAL VAL LEU ALA ARG GLU LEU          
SEQRES   5 A  310  ALA THR SER ARG GLU TYR ALA ILE LYS ILE LEU GLU LYS          
SEQRES   6 A  310  ARG HIS ILE ILE LYS GLU ASN LYS VAL PRO TYR VAL THR          
SEQRES   7 A  310  ARG GLU ARG ASP VAL MET SER ARG LEU ASP HIS PRO PHE          
SEQRES   8 A  310  PHE VAL LYS LEU TYR PHE THR PHE GLN ASP ASP GLU LYS          
SEQRES   9 A  310  LEU TYR PHE GLY LEU SER TYR ALA LYS ASN GLY GLU LEU          
SEQRES  10 A  310  LEU LYS TYR ILE ARG LYS ILE GLY SER PHE ASP GLU THR          
SEQRES  11 A  310  CYS THR ARG PHE TYR THR ALA GLU ILE VAL SER ALA LEU          
SEQRES  12 A  310  GLU TYR LEU HIS GLY LYS GLY ILE ILE HIS ARG ASP LEU          
SEQRES  13 A  310  LYS PRO GLU ASN ILE LEU LEU ASN GLU ASP MET HIS ILE          
SEQRES  14 A  310  GLN ILE THR ASP PHE GLY THR ALA LYS VAL LEU SER PRO          
SEQRES  15 A  310  GLU SER LYS GLN ALA ARG ALA ASN SEP PHE VAL GLY THR          
SEQRES  16 A  310  ALA GLN TYR VAL SER PRO GLU LEU LEU THR GLU LYS SER          
SEQRES  17 A  310  ALA CYS LYS SER SER ASP LEU TRP ALA LEU GLY CYS ILE          
SEQRES  18 A  310  ILE TYR GLN LEU VAL ALA GLY LEU PRO PRO PHE ARG ALA          
SEQRES  19 A  310  GLY ASN GLU TYR LEU ILE PHE GLN LYS ILE ILE LYS LEU          
SEQRES  20 A  310  GLU TYR ASP PHE PRO GLU LYS PHE PHE PRO LYS ALA ARG          
SEQRES  21 A  310  ASP LEU VAL GLU LYS LEU LEU VAL LEU ASP ALA THR LYS          
SEQRES  22 A  310  ARG LEU GLY CYS GLU GLU MET GLU GLY TYR GLY PRO LEU          
SEQRES  23 A  310  LYS ALA HIS PRO PHE PHE GLU SER VAL THR TRP GLU ASN          
SEQRES  24 A  310  LEU HIS GLN GLN THR PRO PRO LYS LEU THR ALA                  
MODRES 1UU8 SEP A  241  SER  PHOSPHOSERINE                                      
HET    SEP  A 241      10                                                       
HET    GOL  A1358       6                                                       
HET    GOL  A1359       6                                                       
HET    GOL  A1360       6                                                       
HET    GOL  A1361       6                                                       
HET    GOL  A1362       6                                                       
HET    GOL  A1363       6                                                       
HET    GOL  A1364       6                                                       
HET    SO4  A1365       5                                                       
HET    SO4  A1366       5                                                       
HET    SO4  A1367       5                                                       
HET    BI1  A1368      31                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     BI1 3-{1-[3-(DIMETHYLAMINO)PROPYL]-1H-INDOL-3-YL}-4-(1H-             
HETNAM   2 BI1  INDOL-3-YL)-1H-PYRROLE-2,5-DIONE                                
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     BI1 RBT205 INHIBITOR                                                 
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   2  GOL    7(C3 H8 O3)                                                  
FORMUL   9  SO4    3(O4 S 2-)                                                   
FORMUL  12  BI1    C25 H24 N4 O2                                                
FORMUL  13  HOH   *47(H2 O)                                                     
HELIX    1   1 ARG A   78  GLU A   80  5                                   3    
HELIX    2   2 LYS A  115  GLU A  121  1                                   7    
HELIX    3   3 LYS A  123  SER A  135  1                                  13    
HELIX    4   4 GLU A  166  GLY A  175  1                                  10    
HELIX    5   5 ASP A  178  LYS A  199  1                                  22    
HELIX    6   6 THR A  245  VAL A  249  5                                   5    
HELIX    7   7 CYS A  260  GLY A  278  1                                  19    
HELIX    8   8 ASN A  286  LEU A  297  1                                  12    
HELIX    9   9 PHE A  306  LEU A  317  1                                  12    
HELIX   10  10 ASP A  320  ARG A  324  5                                   5    
HELIX   11  11 CYS A  327  GLU A  331  5                                   5    
HELIX   12  12 GLY A  332  HIS A  339  1                                   8    
HELIX   13  13 PRO A  340  GLU A  343  5                                   4    
HELIX   14  14 THR A  346  GLN A  353  5                                   8    
SHEET    1  AA 5 PHE A  82  GLU A  90  0                                        
SHEET    2  AA 5 SER A  94  GLU A 101 -1  O  VAL A  96   N  LEU A  88           
SHEET    3  AA 5 GLU A 107  GLU A 114 -1  O  TYR A 108   N  ALA A  99           
SHEET    4  AA 5 LYS A 154  LEU A 159 -1  O  LEU A 155   N  LEU A 113           
SHEET    5  AA 5 LEU A 145  GLN A 150 -1  N  TYR A 146   O  GLY A 158           
SHEET    1  AB 2 ILE A 201  ILE A 202  0                                        
SHEET    2  AB 2 LYS A 228  VAL A 229 -1  O  LYS A 228   N  ILE A 202           
SHEET    1  AC 2 ILE A 211  LEU A 213  0                                        
SHEET    2  AC 2 ILE A 219  ILE A 221 -1  O  GLN A 220   N  LEU A 212           
LINK         C   ASN A 240                 N   SEP A 241     1555   1555  1.33  
LINK         C   SEP A 241                 N   PHE A 242     1555   1555  1.33  
SITE     1 AC1  4 TYR A 146  SER A 160  GLN A 220  GOL A1363                    
SITE     1 AC2  4 ARG A 106  PRO A 140  HIS A 351  GOL A1363                    
SITE     1 AC3  5 GLY A  91  SER A  92  PHE A  93  SER A  94                    
SITE     2 AC3  5 GOL A1360                                                     
SITE     1 AC4 14 LEU A  88  GLY A  89  ALA A 109  VAL A 143                    
SITE     2 AC4 14 LEU A 159  SER A 160  TYR A 161  ALA A 162                    
SITE     3 AC4 14 GLU A 166  GLU A 209  LEU A 212  THR A 222                    
SITE     4 AC4 14 ASP A 223  GOL A1360                                          
SITE     1 AC5  7 LYS A  76  ARG A 131  THR A 148  PHE A 149                    
SITE     2 AC5  7 GLN A 150  LEU A 155  HOH A2010                               
SITE     1 AC6  6 PRO A  79  LYS A 154  TYR A 156  GLU A 328                    
SITE     2 AC6  6 GLU A 331  GLY A 332                                          
SITE     1 AC7  5 SER A  94  VAL A  96  LYS A 111  SO4 A1367                    
SITE     2 AC7  5 BI1 A1368                                                     
SITE     1 AC8  5 LEU A 297  TYR A 299  PHE A 301  ARG A 310                    
SITE     2 AC8  5 HOH A2034                                                     
SITE     1 AC9  5 LYS A  83  PHE A  84  GLU A 194  GLY A 334                    
SITE     2 AC9  5 LYS A 337                                                     
SITE     1 BC1  7 ARG A 106  GLU A 107  TYR A 108  SER A 160                    
SITE     2 BC1  7 TYR A 161  SO4 A1365  SO4 A1366                               
SITE     1 BC2  9 ALA A 103  THR A 104  SER A 105  HIS A 139                    
SITE     2 BC2  9 SER A 191  TRP A 347  ASN A 349  LEU A 350                    
SITE     3 BC2  9 HIS A 351                                                     
CRYST1  122.397  122.397   48.016  90.00  90.00 120.00 P 32 2 1      6          
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      0.008170  0.004717  0.000000        0.00000                         
SCALE2      0.000000  0.009434  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020826        0.00000                         
ATOM      1  N   PRO A  72      37.557  52.250  26.441  1.00 82.68           N  
ATOM      2  CA  PRO A  72      37.781  52.451  27.901  1.00 83.02           C  
ATOM      3  C   PRO A  72      37.983  53.944  28.207  1.00 82.82           C  
ATOM      4  O   PRO A  72      39.099  54.456  28.094  1.00 84.86           O  
ATOM      5  CB  PRO A  72      39.028  51.651  28.282  1.00 82.70           C  
ATOM      6  CG  PRO A  72      39.115  50.632  27.138  1.00 83.78           C  
ATOM      7  CD  PRO A  72      38.618  51.393  25.884  1.00 83.51           C  
ATOM      8  N   GLN A  73      36.908  54.628  28.601  1.00 81.14           N  
ATOM      9  CA  GLN A  73      36.944  56.062  28.903  1.00 78.75           C  
ATOM     10  C   GLN A  73      37.223  56.349  30.381  1.00 77.78           C  
ATOM     11  O   GLN A  73      37.158  55.448  31.216  1.00 78.46           O  
ATOM     12  CB  GLN A  73      35.620  56.711  28.481  1.00 77.88           C  
ATOM     13  N   PRO A  74      37.547  57.614  30.722  1.00 76.40           N  
ATOM     14  CA  PRO A  74      37.833  57.998  32.111  1.00 75.17           C  
ATOM     15  C   PRO A  74      36.664  57.685  33.052  1.00 73.79           C  
ATOM     16  O   PRO A  74      35.509  57.703  32.622  1.00 74.50           O  
ATOM     17  CB  PRO A  74      38.089  59.505  32.009  1.00 74.83           C  
ATOM     18  CG  PRO A  74      38.665  59.665  30.641  1.00 75.57           C  
ATOM     19  CD  PRO A  74      37.784  58.751  29.810  1.00 76.61           C  
ATOM     20  N   ARG A  75      36.967  57.397  34.323  1.00 71.00           N  
ATOM     21  CA  ARG A  75      35.933  57.111  35.328  1.00 67.42           C  
ATOM     22  C   ARG A  75      34.858  58.190  35.204  1.00 64.43           C  
ATOM     23  O   ARG A  75      35.173  59.338  34.910  1.00 64.39           O  
ATOM     24  CB  ARG A  75      36.541  57.142  36.732  1.00 67.09           C  
ATOM     25  N   LYS A  76      33.595  57.832  35.401  1.00 60.51           N  
ATOM     26  CA  LYS A  76      32.521  58.817  35.303  1.00 56.72           C  
ATOM     27  C   LYS A  76      32.858  59.885  36.336  1.00 54.76           C  
ATOM     28  O   LYS A  76      33.346  59.556  37.413  1.00 56.24           O  
ATOM     29  CB  LYS A  76      31.187  58.162  35.649  1.00 56.00           C  
ATOM     30  CG  LYS A  76      29.975  58.797  35.009  1.00 57.14           C  
ATOM     31  CD  LYS A  76      30.001  58.662  33.484  1.00 57.44           C  
ATOM     32  CE  LYS A  76      28.667  59.077  32.865  1.00 58.90           C  
ATOM     33  NZ  LYS A  76      28.795  59.288  31.398  1.00 60.22           N  
ATOM     34  N   LYS A  77      32.637  61.157  36.032  1.00 51.39           N  
ATOM     35  CA  LYS A  77      32.960  62.174  37.027  1.00 48.40           C  
ATOM     36  C   LYS A  77      31.763  62.400  37.946  1.00 47.37           C  
ATOM     37  O   LYS A  77      30.661  61.923  37.681  1.00 46.18           O  
ATOM     38  CB  LYS A  77      33.375  63.483  36.362  1.00 46.27           C  
ATOM     39  CG  LYS A  77      34.543  63.344  35.404  1.00 43.96           C  
ATOM     40  CD  LYS A  77      34.987  64.698  34.898  1.00 43.84           C  
ATOM     41  CE  LYS A  77      35.931  64.585  33.717  1.00 42.34           C  
ATOM     42  NZ  LYS A  77      37.166  63.872  34.078  1.00 39.08           N  
ATOM     43  N   ARG A  78      31.982  63.104  39.046  1.00 45.20           N  
ATOM     44  CA  ARG A  78      30.894  63.356  39.963  1.00 43.86           C  
ATOM     45  C   ARG A  78      31.028  64.746  40.596  1.00 42.02           C  
ATOM     46  O   ARG A  78      32.117  65.296  40.685  1.00 41.43           O  
ATOM     47  CB  ARG A  78      30.821  62.228  41.005  1.00 45.23           C  
ATOM     48  CG  ARG A  78      32.043  62.058  41.878  1.00 47.61           C  
ATOM     49  CD  ARG A  78      31.804  60.958  42.930  1.00 49.78           C  
ATOM     50  NE  ARG A  78      32.788  60.986  44.009  0.00 49.46           N  
ATOM     51  CZ  ARG A  78      34.103  60.897  43.835  0.00 49.76           C  
ATOM     52  NH1 ARG A  78      34.610  60.773  42.617  0.00 49.78           N  
ATOM     53  NH2 ARG A  78      34.913  60.934  44.884  0.00 49.78           N  
ATOM     54  N   PRO A  79      29.909  65.317  41.058  1.00 40.84           N  
ATOM     55  CA  PRO A  79      29.882  66.650  41.670  1.00 41.55           C  
ATOM     56  C   PRO A  79      31.070  66.985  42.568  1.00 42.54           C  
ATOM     57  O   PRO A  79      31.681  68.036  42.430  1.00 43.38           O  
ATOM     58  CB  PRO A  79      28.558  66.657  42.446  1.00 40.07           C  
ATOM     59  CG  PRO A  79      27.742  65.646  41.764  1.00 39.20           C  
ATOM     60  CD  PRO A  79      28.712  64.553  41.443  1.00 38.25           C  
ATOM     61  N   GLU A  80      31.389  66.092  43.493  1.00 43.72           N  
ATOM     62  CA  GLU A  80      32.478  66.328  44.416  1.00 46.40           C  
ATOM     63  C   GLU A  80      33.815  66.491  43.716  1.00 46.28           C  
ATOM     64  O   GLU A  80      34.782  66.930  44.336  1.00 47.90           O  
ATOM     65  CB  GLU A  80      32.558  65.210  45.456  1.00 48.86           C  
ATOM     66  CG  GLU A  80      32.261  63.821  44.927  1.00 56.74           C  
ATOM     67  CD  GLU A  80      30.762  63.502  44.884  1.00 61.06           C  
ATOM     68  OE1 GLU A  80      30.006  64.236  44.214  1.00 62.81           O  
ATOM     69  OE2 GLU A  80      30.338  62.507  45.519  1.00 63.09           O  
ATOM     70  N   ASP A  81      33.887  66.151  42.431  1.00 44.55           N  
ATOM     71  CA  ASP A  81      35.149  66.306  41.709  1.00 43.37           C  
ATOM     72  C   ASP A  81      35.348  67.775  41.385  1.00 42.22           C  
ATOM     73  O   ASP A  81      36.425  68.190  40.956  1.00 39.75           O  
ATOM     74  CB  ASP A  81      35.149  65.501  40.406  1.00 43.92           C  
ATOM     75  CG  ASP A  81      35.179  64.009  40.644  1.00 44.54           C  
ATOM     76  OD1 ASP A  81      35.968  63.571  41.504  1.00 47.56           O  
ATOM     77  OD2 ASP A  81      34.429  63.268  39.979  1.00 46.49           O  
ATOM     78  N   PHE A  82      34.299  68.558  41.623  1.00 39.95           N  
ATOM     79  CA  PHE A  82      34.334  69.975  41.323  1.00 39.80           C  
ATOM     80  C   PHE A  82      34.172  70.932  42.501  1.00 40.20           C  
ATOM     81  O   PHE A  82      33.833  70.562  43.618  1.00 42.44           O  
ATOM     82  CB  PHE A  82      33.260  70.295  40.282  1.00 37.18           C  
ATOM     83  CG  PHE A  82      33.404  69.517  39.009  1.00 34.70           C  
ATOM     84  CD1 PHE A  82      34.173  70.008  37.958  1.00 33.34           C  
ATOM     85  CD2 PHE A  82      32.801  68.273  38.870  1.00 33.70           C  
ATOM     86  CE1 PHE A  82      34.347  69.268  36.783  1.00 31.78           C  
ATOM     87  CE2 PHE A  82      32.969  67.530  37.705  1.00 33.31           C  
ATOM     88  CZ  PHE A  82      33.748  68.030  36.660  1.00 31.40           C  
ATOM     89  N   LYS A  83      34.447  72.185  42.211  1.00 39.60           N  
ATOM     90  CA  LYS A  83      34.325  73.254  43.148  1.00 38.07           C  
ATOM     91  C   LYS A  83      33.487  74.189  42.321  1.00 38.45           C  
ATOM     92  O   LYS A  83      34.001  74.842  41.414  1.00 39.49           O  
ATOM     93  CB  LYS A  83      35.684  73.863  43.415  1.00 39.92           C  
ATOM     94  CG  LYS A  83      35.668  75.125  44.280  1.00 44.13           C  
ATOM     95  CD  LYS A  83      37.051  75.355  44.875  1.00 47.41           C  
ATOM     96  CE  LYS A  83      37.193  76.721  45.471  1.00 51.16           C  
ATOM     97  NZ  LYS A  83      36.974  77.770  44.426  1.00 56.13           N  
ATOM     98  N   PHE A  84      32.188  74.229  42.590  1.00 36.91           N  
ATOM     99  CA  PHE A  84      31.322  75.092  41.815  1.00 36.88           C  
ATOM    100  C   PHE A  84      31.468  76.531  42.260  1.00 38.15           C  
ATOM    101  O   PHE A  84      31.670  76.808  43.434  1.00 38.85           O  
ATOM    102  CB  PHE A  84      29.870  74.644  41.954  1.00 36.82           C  
ATOM    103  CG  PHE A  84      29.608  73.298  41.376  1.00 34.69           C  
ATOM    104  CD1 PHE A  84      30.022  72.156  42.031  1.00 35.51           C  
ATOM    105  CD2 PHE A  84      28.998  73.168  40.151  1.00 33.21           C  
ATOM    106  CE1 PHE A  84      29.838  70.895  41.467  1.00 35.63           C  
ATOM    107  CE2 PHE A  84      28.810  71.919  39.586  1.00 33.36           C  
ATOM    108  CZ  PHE A  84      29.233  70.783  40.246  1.00 31.84           C  
ATOM    109  N   GLY A  85      31.360  77.448  41.313  1.00 37.91           N  
ATOM    110  CA  GLY A  85      31.479  78.851  41.644  1.00 37.84           C  
ATOM    111  C   GLY A  85      30.246  79.630  41.251  1.00 38.37           C  
ATOM    112  O   GLY A  85      29.118  79.228  41.525  1.00 39.98           O  
ATOM    113  N   LYS A  86      30.449  80.746  40.580  1.00 37.47           N  
ATOM    114  CA  LYS A  86      29.320  81.556  40.209  1.00 37.31           C  
ATOM    115  C   LYS A  86      28.432  80.942  39.145  1.00 37.23           C  
ATOM    116  O   LYS A  86      28.873  80.172  38.293  1.00 35.96           O  
ATOM    117  CB  LYS A  86      29.785  82.925  39.745  1.00 38.62           C  
ATOM    118  CG  LYS A  86      30.508  82.924  38.444  1.00 38.58           C  
ATOM    119  CD  LYS A  86      30.756  84.348  38.002  1.00 40.89           C  
ATOM    120  CE  LYS A  86      31.199  84.375  36.549  1.00 44.44           C  
ATOM    121  NZ  LYS A  86      31.318  85.754  36.008  1.00 50.01           N  
ATOM    122  N   ILE A  87      27.161  81.306  39.235  1.00 36.45           N  
ATOM    123  CA  ILE A  87      26.136  80.865  38.322  1.00 35.93           C  
ATOM    124  C   ILE A  87      26.305  81.783  37.133  1.00 38.32           C  
ATOM    125  O   ILE A  87      26.246  82.999  37.292  1.00 41.12           O  
ATOM    126  CB  ILE A  87      24.765  81.083  38.951  1.00 34.20           C  
ATOM    127  CG1 ILE A  87      24.632  80.184  40.186  1.00 32.34           C  
ATOM    128  CG2 ILE A  87      23.665  80.855  37.930  1.00 33.66           C  
ATOM    129  CD1 ILE A  87      23.331  80.380  40.969  1.00 32.69           C  
ATOM    130  N   LEU A  88      26.547  81.224  35.952  1.00 38.24           N  
ATOM    131  CA  LEU A  88      26.705  82.060  34.782  1.00 39.18           C  
ATOM    132  C   LEU A  88      25.338  82.477  34.264  1.00 40.36           C  
ATOM    133  O   LEU A  88      25.191  83.560  33.724  1.00 41.89           O  
ATOM    134  CB  LEU A  88      27.473  81.326  33.687  1.00 39.17           C  
ATOM    135  CG  LEU A  88      28.930  80.960  33.998  1.00 38.99           C  
ATOM    136  CD1 LEU A  88      29.550  80.167  32.852  1.00 35.64           C  
ATOM    137  CD2 LEU A  88      29.699  82.215  34.238  1.00 36.07           C  
ATOM    138  N   GLY A  89      24.335  81.624  34.443  1.00 41.25           N  
ATOM    139  CA  GLY A  89      22.999  81.938  33.976  1.00 41.82           C  
ATOM    140  C   GLY A  89      21.966  80.906  34.389  1.00 44.71           C  
ATOM    141  O   GLY A  89      22.306  79.768  34.734  1.00 44.40           O  
ATOM    142  N   GLU A  90      20.694  81.306  34.348  1.00 46.75           N  
ATOM    143  CA  GLU A  90      19.582  80.427  34.714  1.00 48.44           C  
ATOM    144  C   GLU A  90      18.486  80.424  33.658  1.00 49.32           C  
ATOM    145  O   GLU A  90      18.070  81.479  33.178  1.00 50.10           O  
ATOM    146  CB  GLU A  90      18.981  80.864  36.045  1.00 46.70           C  
ATOM    147  CG  GLU A  90      20.010  81.493  36.936  1.00 50.37           C  
ATOM    148  CD  GLU A  90      19.518  81.795  38.339  1.00 51.18           C  
ATOM    149  OE1 GLU A  90      20.166  82.641  39.007  1.00 50.62           O  
ATOM    150  OE2 GLU A  90      18.512  81.184  38.775  1.00 50.48           O  
ATOM    151  N   GLY A  91      18.031  79.230  33.294  1.00 49.66           N  
ATOM    152  CA  GLY A  91      16.954  79.102  32.330  1.00 48.23           C  
ATOM    153  C   GLY A  91      15.772  78.466  33.052  1.00 49.53           C  
ATOM    154  O   GLY A  91      15.843  78.144  34.244  1.00 48.97           O  
ATOM    155  N   SER A  92      14.675  78.266  32.341  1.00 50.01           N  
ATOM    156  CA  SER A  92      13.507  77.659  32.956  1.00 50.74           C  
ATOM    157  C   SER A  92      13.768  76.216  33.397  1.00 50.94           C  
ATOM    158  O   SER A  92      13.306  75.786  34.459  1.00 50.48           O  
ATOM    159  CB  SER A  92      12.336  77.717  31.978  1.00 52.20           C  
ATOM    160  OG  SER A  92      12.775  77.494  30.642  1.00 56.19           O  
ATOM    161  N   PHE A  93      14.527  75.479  32.588  1.00 51.04           N  
ATOM    162  CA  PHE A  93      14.830  74.087  32.890  1.00 50.25           C  
ATOM    163  C   PHE A  93      16.261  73.793  33.310  1.00 49.31           C  
ATOM    164  O   PHE A  93      16.613  72.633  33.547  1.00 49.33           O  
ATOM    165  CB  PHE A  93      14.462  73.204  31.697  1.00 51.60           C  
ATOM    166  CG  PHE A  93      13.041  73.359  31.254  1.00 52.82           C  
ATOM    167  CD1 PHE A  93      12.684  74.378  30.370  1.00 52.98           C  
ATOM    168  CD2 PHE A  93      12.049  72.533  31.763  1.00 53.67           C  
ATOM    169  CE1 PHE A  93      11.359  74.581  29.996  1.00 53.18           C  
ATOM    170  CE2 PHE A  93      10.710  72.727  31.396  1.00 55.51           C  
ATOM    171  CZ  PHE A  93      10.370  73.758  30.507  1.00 54.02           C  
ATOM    172  N   SER A  94      17.102  74.815  33.408  1.00 47.26           N  
ATOM    173  CA  SER A  94      18.471  74.543  33.824  1.00 46.32           C  
ATOM    174  C   SER A  94      19.222  75.750  34.352  1.00 45.17           C  
ATOM    175  O   SER A  94      18.737  76.878  34.306  1.00 45.48           O  
ATOM    176  CB  SER A  94      19.261  73.921  32.678  1.00 45.87           C  
ATOM    177  OG  SER A  94      19.492  74.874  31.653  1.00 46.23           O  
ATOM    178  N   THR A  95      20.418  75.489  34.860  1.00 42.42           N  
ATOM    179  CA  THR A  95      21.263  76.532  35.400  1.00 40.35           C  
ATOM    180  C   THR A  95      22.671  76.187  34.965  1.00 39.85           C  
ATOM    181  O   THR A  95      23.095  75.048  35.131  1.00 38.68           O  
ATOM    182  CB  THR A  95      21.204  76.549  36.944  1.00 39.68           C  
ATOM    183  OG1 THR A  95      19.896  76.928  37.372  1.00 43.67           O  
ATOM    184  CG2 THR A  95      22.174  77.520  37.504  1.00 38.68           C  
ATOM    185  N   VAL A  96      23.384  77.158  34.389  1.00 39.12           N  
ATOM    186  CA  VAL A  96      24.769  76.949  33.973  1.00 35.96           C  
ATOM    187  C   VAL A  96      25.652  77.564  35.055  1.00 35.78           C  
ATOM    188  O   VAL A  96      25.504  78.739  35.395  1.00 36.74           O  
ATOM    189  CB  VAL A  96      25.057  77.622  32.621  1.00 34.76           C  
ATOM    190  CG1 VAL A  96      26.500  77.393  32.223  1.00 31.57           C  
ATOM    191  CG2 VAL A  96      24.147  77.058  31.573  1.00 31.35           C  
ATOM    192  N   VAL A  97      26.566  76.777  35.604  1.00 34.18           N  
ATOM    193  CA  VAL A  97      27.426  77.270  36.670  1.00 35.63           C  
ATOM    194  C   VAL A  97      28.892  77.014  36.372  1.00 37.25           C  
ATOM    195  O   VAL A  97      29.258  75.939  35.919  1.00 38.35           O  
ATOM    196  CB  VAL A  97      27.086  76.579  38.011  1.00 36.88           C  
ATOM    197  CG1 VAL A  97      27.921  77.184  39.149  1.00 38.73           C  
ATOM    198  CG2 VAL A  97      25.598  76.707  38.307  1.00 35.18           C  
ATOM    199  N   LEU A  98      29.737  78.002  36.628  1.00 38.14           N  
ATOM    200  CA  LEU A  98      31.166  77.855  36.398  1.00 39.03           C  
ATOM    201  C   LEU A  98      31.740  76.946  37.492  1.00 40.81           C  
ATOM    202  O   LEU A  98      31.553  77.218  38.676  1.00 42.82           O  
ATOM    203  CB  LEU A  98      31.824  79.217  36.480  1.00 41.57           C  
ATOM    204  CG  LEU A  98      33.259  79.312  35.972  1.00 42.89           C  
ATOM    205  CD1 LEU A  98      33.296  78.874  34.501  1.00 41.48           C  
ATOM    206  CD2 LEU A  98      33.750  80.739  36.139  1.00 38.94           C  
ATOM    207  N   ALA A  99      32.439  75.881  37.102  1.00 39.52           N  
ATOM    208  CA  ALA A  99      33.014  74.932  38.051  1.00 39.51           C  
ATOM    209  C   ALA A  99      34.481  74.660  37.735  1.00 41.10           C  
ATOM    210  O   ALA A  99      34.891  74.654  36.566  1.00 42.28           O  
ATOM    211  CB  ALA A  99      32.245  73.637  37.991  1.00 39.35           C  
ATOM    212  N   ARG A 100      35.285  74.423  38.762  1.00 39.81           N  
ATOM    213  CA  ARG A 100      36.690  74.147  38.512  1.00 38.90           C  
ATOM    214  C   ARG A 100      36.944  72.742  38.971  1.00 39.48           C  
ATOM    215  O   ARG A 100      36.657  72.409  40.117  1.00 41.71           O  
ATOM    216  CB  ARG A 100      37.611  75.097  39.273  1.00 36.38           C  
ATOM    217  CG  ARG A 100      39.055  74.995  38.792  1.00 39.45           C  
ATOM    218  CD  ARG A 100      40.008  75.921  39.522  1.00 41.23           C  
ATOM    219  NE  ARG A 100      39.803  77.344  39.209  1.00 44.99           N  
ATOM    220  CZ  ARG A 100      40.278  77.969  38.127  1.00 44.37           C  
ATOM    221  NH1 ARG A 100      40.990  77.312  37.223  1.00 41.88           N  
ATOM    222  NH2 ARG A 100      40.066  79.270  37.970  1.00 43.54           N  
ATOM    223  N   GLU A 101      37.463  71.911  38.072  1.00 38.78           N  
ATOM    224  CA  GLU A 101      37.758  70.527  38.409  1.00 36.69           C  
ATOM    225  C   GLU A 101      38.977  70.465  39.331  1.00 35.97           C  
ATOM    226  O   GLU A 101      40.074  70.847  38.947  1.00 34.71           O  
ATOM    227  CB  GLU A 101      38.012  69.732  37.138  1.00 35.89           C  
ATOM    228  CG  GLU A 101      38.512  68.334  37.401  1.00 36.65           C  
ATOM    229  CD  GLU A 101      38.639  67.512  36.138  1.00 35.38           C  
ATOM    230  OE1 GLU A 101      39.078  68.052  35.111  1.00 37.86           O  
ATOM    231  OE2 GLU A 101      38.315  66.316  36.171  1.00 36.41           O  
ATOM    232  N   LEU A 102      38.775  69.991  40.555  1.00 36.73           N  
ATOM    233  CA  LEU A 102      39.862  69.895  41.532  1.00 37.16           C  
ATOM    234  C   LEU A 102      41.113  69.172  41.026  1.00 37.55           C  
ATOM    235  O   LEU A 102      42.218  69.695  41.126  1.00 39.15           O  
ATOM    236  CB  LEU A 102      39.372  69.194  42.792  1.00 37.23           C  
ATOM    237  CG  LEU A 102      38.111  69.746  43.472  1.00 39.44           C  
ATOM    238  CD1 LEU A 102      37.627  68.775  44.566  1.00 35.42           C  
ATOM    239  CD2 LEU A 102      38.417  71.116  44.056  1.00 38.77           C  
ATOM    240  N   ALA A 103      40.949  67.973  40.482  1.00 38.26           N  
ATOM    241  CA  ALA A 103      42.093  67.204  39.999  1.00 37.72           C  
ATOM    242  C   ALA A 103      42.948  67.843  38.913  1.00 37.41           C  
ATOM    243  O   ALA A 103      44.125  67.541  38.826  1.00 38.15           O  
ATOM    244  CB  ALA A 103      41.635  65.838  39.527  1.00 39.02           C  
ATOM    245  N   THR A 104      42.384  68.734  38.102  1.00 37.54           N  
ATOM    246  CA  THR A 104      43.151  69.339  37.008  1.00 35.87           C  
ATOM    247  C   THR A 104      43.167  70.862  36.920  1.00 36.03           C  
ATOM    248  O   THR A 104      43.896  71.412  36.106  1.00 35.55           O  
ATOM    249  CB  THR A 104      42.633  68.843  35.658  1.00 36.56           C  
ATOM    250  OG1 THR A 104      41.307  69.337  35.479  1.00 38.14           O  
ATOM    251  CG2 THR A 104      42.573  67.308  35.607  1.00 35.85           C  
ATOM    252  N   SER A 105      42.369  71.542  37.742  1.00 36.72           N  
ATOM    253  CA  SER A 105      42.284  73.011  37.711  1.00 36.41           C  
ATOM    254  C   SER A 105      41.544  73.522  36.479  1.00 34.65           C  
ATOM    255  O   SER A 105      41.437  74.730  36.275  1.00 32.05           O  
ATOM    256  CB  SER A 105      43.672  73.646  37.706  1.00 36.91           C  
ATOM    257  OG  SER A 105      44.315  73.439  38.936  1.00 44.46           O  
ATOM    258  N   ARG A 106      41.061  72.605  35.648  1.00 34.03           N  
ATOM    259  CA  ARG A 106      40.350  72.989  34.434  1.00 35.06           C  
ATOM    260  C   ARG A 106      39.039  73.626  34.785  1.00 35.64           C  
ATOM    261  O   ARG A 106      38.309  73.135  35.647  1.00 35.11           O  
ATOM    262  CB  ARG A 106      40.113  71.774  33.552  1.00 36.26           C  
ATOM    263  CG  ARG A 106      41.374  71.271  32.911  1.00 37.25           C  
ATOM    264  CD  ARG A 106      41.163  69.941  32.257  1.00 38.02           C  
ATOM    265  NE  ARG A 106      42.223  69.687  31.288  1.00 38.36           N  
ATOM    266  CZ  ARG A 106      42.454  68.508  30.720  1.00 37.56           C  
ATOM    267  NH1 ARG A 106      41.700  67.451  31.033  1.00 37.46           N  
ATOM    268  NH2 ARG A 106      43.414  68.394  29.816  1.00 32.68           N  
ATOM    269  N   GLU A 107      38.742  74.728  34.115  1.00 37.02           N  
ATOM    270  CA  GLU A 107      37.511  75.457  34.372  1.00 38.51           C  
ATOM    271  C   GLU A 107      36.496  75.099  33.314  1.00 37.84           C  
ATOM    272  O   GLU A 107      36.755  75.292  32.131  1.00 38.11           O  
ATOM    273  CB  GLU A 107      37.784  76.959  34.330  1.00 41.29           C  
ATOM    274  CG  GLU A 107      37.001  77.752  35.344  1.00 47.38           C  
ATOM    275  CD  GLU A 107      37.484  79.202  35.484  1.00 52.03           C  
ATOM    276  OE1 GLU A 107      37.204  79.801  36.556  1.00 54.33           O  
ATOM    277  OE2 GLU A 107      38.126  79.744  34.541  1.00 51.72           O  
ATOM    278  N   TYR A 108      35.342  74.581  33.742  1.00 37.13           N  
ATOM    279  CA  TYR A 108      34.251  74.196  32.829  1.00 34.24           C  
ATOM    280  C   TYR A 108      32.951  74.934  33.144  1.00 33.32           C  
ATOM    281  O   TYR A 108      32.780  75.464  34.235  1.00 32.10           O  
ATOM    282  CB  TYR A 108      33.951  72.721  32.974  1.00 30.84           C  
ATOM    283  CG  TYR A 108      35.036  71.811  32.513  1.00 33.97           C  
ATOM    284  CD1 TYR A 108      35.230  71.578  31.163  1.00 30.98           C  
ATOM    285  CD2 TYR A 108      35.841  71.117  33.436  1.00 34.00           C  
ATOM    286  CE1 TYR A 108      36.190  70.675  30.733  1.00 34.63           C  
ATOM    287  CE2 TYR A 108      36.815  70.205  33.010  1.00 32.42           C  
ATOM    288  CZ  TYR A 108      36.982  69.995  31.652  1.00 34.16           C  
ATOM    289  OH  TYR A 108      37.967  69.149  31.183  1.00 35.55           O  
ATOM    290  N   ALA A 109      32.032  74.951  32.186  1.00 32.15           N  
ATOM    291  CA  ALA A 109      30.720  75.554  32.400  1.00 31.72           C  
ATOM    292  C   ALA A 109      29.823  74.325  32.506  1.00 33.32           C  
ATOM    293  O   ALA A 109      29.596  73.641  31.515  1.00 33.30           O  
ATOM    294  CB  ALA A 109      30.311  76.396  31.206  1.00 29.72           C  
ATOM    295  N   ILE A 110      29.334  74.022  33.701  1.00 33.08           N  
ATOM    296  CA  ILE A 110      28.505  72.849  33.866  1.00 34.39           C  
ATOM    297  C   ILE A 110      27.026  73.198  33.843  1.00 35.06           C  
ATOM    298  O   ILE A 110      26.569  74.019  34.604  1.00 36.33           O  
ATOM    299  CB  ILE A 110      28.892  72.125  35.166  1.00 34.25           C  
ATOM    300  CG1 ILE A 110      30.360  71.721  35.077  1.00 33.20           C  
ATOM    301  CG2 ILE A 110      28.003  70.891  35.394  1.00 34.89           C  
ATOM    302  CD1 ILE A 110      30.799  70.793  36.156  1.00 33.67           C  
ATOM    303  N   LYS A 111      26.277  72.586  32.940  1.00 37.54           N  
ATOM    304  CA  LYS A 111      24.853  72.863  32.825  1.00 38.36           C  
ATOM    305  C   LYS A 111      24.105  71.845  33.664  1.00 38.01           C  
ATOM    306  O   LYS A 111      24.202  70.637  33.431  1.00 40.48           O  
ATOM    307  CB  LYS A 111      24.435  72.783  31.355  1.00 39.25           C  
ATOM    308  CG  LYS A 111      22.943  72.934  31.126  1.00 42.92           C  
ATOM    309  CD  LYS A 111      22.611  72.991  29.653  1.00 43.86           C  
ATOM    310  CE  LYS A 111      21.107  72.981  29.434  1.00 46.96           C  
ATOM    311  NZ  LYS A 111      20.747  73.274  28.010  1.00 48.58           N  
ATOM    312  N   ILE A 112      23.366  72.332  34.650  1.00 37.15           N  
ATOM    313  CA  ILE A 112      22.621  71.469  35.562  1.00 36.05           C  
ATOM    314  C   ILE A 112      21.120  71.490  35.315  1.00 37.26           C  
ATOM    315  O   ILE A 112      20.482  72.544  35.361  1.00 37.72           O  
ATOM    316  CB  ILE A 112      22.886  71.893  37.004  1.00 35.71           C  
ATOM    317  CG1 ILE A 112      24.394  71.830  37.268  1.00 34.80           C  
ATOM    318  CG2 ILE A 112      22.086  71.012  37.965  1.00 34.55           C  
ATOM    319  CD1 ILE A 112      24.869  72.657  38.426  1.00 34.64           C  
ATOM    320  N   LEU A 113      20.564  70.316  35.045  1.00 38.55           N  
ATOM    321  CA  LEU A 113      19.130  70.177  34.799  1.00 39.49           C  
ATOM    322  C   LEU A 113      18.548  69.262  35.844  1.00 40.61           C  
ATOM    323  O   LEU A 113      19.119  68.208  36.142  1.00 40.03           O  
ATOM    324  CB  LEU A 113      18.850  69.581  33.419  1.00 38.78           C  
ATOM    325  CG  LEU A 113      19.569  70.257  32.261  1.00 37.49           C  
ATOM    326  CD1 LEU A 113      20.917  69.588  32.046  1.00 36.11           C  
ATOM    327  CD2 LEU A 113      18.724  70.152  31.032  1.00 35.46           C  
ATOM    328  N   GLU A 114      17.412  69.668  36.404  1.00 42.99           N  
ATOM    329  CA  GLU A 114      16.752  68.871  37.427  1.00 45.97           C  
ATOM    330  C   GLU A 114      15.828  67.833  36.774  1.00 45.00           C  
ATOM    331  O   GLU A 114      14.853  68.189  36.096  1.00 45.50           O  
ATOM    332  CB  GLU A 114      15.953  69.780  38.341  1.00 50.70           C  
ATOM    333  CG  GLU A 114      15.549  69.111  39.636  1.00 59.74           C  
ATOM    334  CD  GLU A 114      14.640  69.985  40.474  1.00 64.77           C  
ATOM    335  OE1 GLU A 114      15.036  71.151  40.765  1.00 67.10           O  
ATOM    336  OE2 GLU A 114      13.537  69.498  40.837  1.00 66.24           O  
ATOM    337  N   LYS A 115      16.133  66.554  36.985  1.00 43.11           N  
ATOM    338  CA  LYS A 115      15.363  65.474  36.388  1.00 41.81           C  
ATOM    339  C   LYS A 115      13.856  65.602  36.571  1.00 42.53           C  
ATOM    340  O   LYS A 115      13.107  65.509  35.593  1.00 43.64           O  
ATOM    341  CB  LYS A 115      15.844  64.118  36.912  1.00 40.35           C  
ATOM    342  CG  LYS A 115      17.316  63.865  36.659  1.00 43.09           C  
ATOM    343  CD  LYS A 115      17.619  62.444  36.232  1.00 42.93           C  
ATOM    344  CE  LYS A 115      18.099  61.571  37.384  1.00 45.98           C  
ATOM    345  NZ  LYS A 115      19.404  62.001  37.947  1.00 46.23           N  
ATOM    346  N   ARG A 116      13.393  65.837  37.798  1.00 41.16           N  
ATOM    347  CA  ARG A 116      11.952  65.935  38.007  1.00 40.73           C  
ATOM    348  C   ARG A 116      11.332  66.997  37.126  1.00 40.11           C  
ATOM    349  O   ARG A 116      10.360  66.744  36.439  1.00 41.02           O  
ATOM    350  CB  ARG A 116      11.626  66.217  39.482  1.00 39.85           C  
ATOM    351  N   HIS A 117      11.899  68.188  37.123  1.00 41.10           N  
ATOM    352  CA  HIS A 117      11.313  69.243  36.317  1.00 43.18           C  
ATOM    353  C   HIS A 117      11.231  68.848  34.861  1.00 42.63           C  
ATOM    354  O   HIS A 117      10.240  69.119  34.190  1.00 43.87           O  
ATOM    355  CB  HIS A 117      12.122  70.529  36.445  1.00 45.69           C  
ATOM    356  CG  HIS A 117      11.399  71.747  35.960  1.00 47.84           C  
ATOM    357  ND1 HIS A 117      10.086  71.717  35.543  1.00 50.17           N  
ATOM    358  CD2 HIS A 117      11.818  73.022  35.781  1.00 49.63           C  
ATOM    359  CE1 HIS A 117       9.729  72.918  35.126  1.00 49.31           C  
ATOM    360  NE2 HIS A 117      10.762  73.729  35.260  1.00 49.68           N  
ATOM    361  N   ILE A 118      12.276  68.195  34.374  1.00 41.84           N  
ATOM    362  CA  ILE A 118      12.331  67.779  32.980  1.00 40.19           C  
ATOM    363  C   ILE A 118      11.264  66.772  32.669  1.00 41.36           C  
ATOM    364  O   ILE A 118      10.619  66.823  31.618  1.00 41.04           O  
ATOM    365  CB  ILE A 118      13.685  67.172  32.666  1.00 40.53           C  
ATOM    366  CG1 ILE A 118      14.719  68.293  32.619  1.00 42.20           C  
ATOM    367  CG2 ILE A 118      13.629  66.399  31.367  1.00 37.84           C  
ATOM    368  CD1 ILE A 118      16.120  67.809  32.690  1.00 46.88           C  
ATOM    369  N   ILE A 119      11.086  65.845  33.597  1.00 41.46           N  
ATOM    370  CA  ILE A 119      10.091  64.809  33.439  1.00 42.11           C  
ATOM    371  C   ILE A 119       8.682  65.397  33.452  1.00 42.69           C  
ATOM    372  O   ILE A 119       7.887  65.113  32.558  1.00 42.13           O  
ATOM    373  CB  ILE A 119      10.268  63.756  34.526  1.00 41.60           C  
ATOM    374  CG1 ILE A 119      11.478  62.891  34.179  1.00 40.37           C  
ATOM    375  CG2 ILE A 119       9.033  62.933  34.650  1.00 41.69           C  
ATOM    376  CD1 ILE A 119      11.727  61.780  35.126  1.00 39.37           C  
ATOM    377  N   LYS A 120       8.380  66.226  34.449  1.00 43.18           N  
ATOM    378  CA  LYS A 120       7.068  66.857  34.529  1.00 44.25           C  
ATOM    379  C   LYS A 120       6.727  67.634  33.256  1.00 46.14           C  
ATOM    380  O   LYS A 120       5.638  67.486  32.718  1.00 49.94           O  
ATOM    381  CB  LYS A 120       6.983  67.794  35.746  1.00 40.88           C  
ATOM    382  N   GLU A 121       7.639  68.451  32.749  1.00 46.21           N  
ATOM    383  CA  GLU A 121       7.310  69.224  31.561  1.00 46.88           C  
ATOM    384  C   GLU A 121       7.573  68.535  30.246  1.00 46.94           C  
ATOM    385  O   GLU A 121       7.635  69.188  29.218  1.00 47.97           O  
ATOM    386  CB  GLU A 121       8.047  70.562  31.584  1.00 50.26           C  
ATOM    387  CG  GLU A 121       7.525  71.522  32.652  1.00 54.40           C  
ATOM    388  CD  GLU A 121       5.991  71.643  32.629  1.00 56.37           C  
ATOM    389  OE1 GLU A 121       5.434  72.267  31.691  1.00 56.80           O  
ATOM    390  OE2 GLU A 121       5.343  71.096  33.549  1.00 57.11           O  
ATOM    391  N   ASN A 122       7.732  67.220  30.280  1.00 47.54           N  
ATOM    392  CA  ASN A 122       8.004  66.417  29.075  1.00 48.14           C  
ATOM    393  C   ASN A 122       9.168  66.903  28.200  1.00 45.81           C  
ATOM    394  O   ASN A 122       9.028  67.021  26.983  1.00 45.01           O  
ATOM    395  CB  ASN A 122       6.730  66.306  28.235  1.00 50.75           C  
ATOM    396  CG  ASN A 122       5.550  65.803  29.054  1.00 55.32           C  
ATOM    397  OD1 ASN A 122       5.063  64.690  28.836  1.00 58.31           O  
ATOM    398  ND2 ASN A 122       5.070  66.626  29.982  1.00 55.85           N  
ATOM    399  N   LYS A 123      10.322  67.141  28.823  1.00 43.03           N  
ATOM    400  CA  LYS A 123      11.483  67.629  28.104  1.00 42.53           C  
ATOM    401  C   LYS A 123      12.556  66.604  27.814  1.00 41.80           C  
ATOM    402  O   LYS A 123      13.555  66.927  27.151  1.00 43.69           O  
ATOM    403  CB  LYS A 123      12.113  68.794  28.859  1.00 44.04           C  
ATOM    404  CG  LYS A 123      11.198  69.993  29.001  1.00 45.82           C  
ATOM    405  CD  LYS A 123      10.790  70.488  27.634  1.00 47.67           C  
ATOM    406  CE  LYS A 123       9.632  71.459  27.711  1.00 47.87           C  
ATOM    407  NZ  LYS A 123       8.964  71.484  26.387  1.00 49.30           N  
ATOM    408  N   VAL A 124      12.368  65.380  28.297  1.00 39.08           N  
ATOM    409  CA  VAL A 124      13.344  64.304  28.078  1.00 35.80           C  
ATOM    410  C   VAL A 124      13.814  64.235  26.620  1.00 36.64           C  
ATOM    411  O   VAL A 124      15.003  64.059  26.350  1.00 35.55           O  
ATOM    412  CB  VAL A 124      12.763  62.923  28.465  1.00 34.62           C  
ATOM    413  CG1 VAL A 124      13.803  61.877  28.352  1.00 33.02           C  
ATOM    414  CG2 VAL A 124      12.208  62.955  29.868  1.00 32.71           C  
ATOM    415  N   PRO A 125      12.888  64.379  25.659  1.00 36.73           N  
ATOM    416  CA  PRO A 125      13.301  64.315  24.253  1.00 37.45           C  
ATOM    417  C   PRO A 125      14.282  65.439  23.921  1.00 40.14           C  
ATOM    418  O   PRO A 125      15.177  65.286  23.085  1.00 40.58           O  
ATOM    419  CB  PRO A 125      11.983  64.465  23.497  1.00 37.01           C  
ATOM    420  CG  PRO A 125      10.976  63.861  24.437  1.00 37.10           C  
ATOM    421  CD  PRO A 125      11.421  64.415  25.782  1.00 36.37           C  
ATOM    422  N   TYR A 126      14.101  66.566  24.595  1.00 41.07           N  
ATOM    423  CA  TYR A 126      14.937  67.731  24.387  1.00 43.06           C  
ATOM    424  C   TYR A 126      16.291  67.559  25.030  1.00 43.22           C  
ATOM    425  O   TYR A 126      17.311  67.848  24.414  1.00 44.45           O  
ATOM    426  CB  TYR A 126      14.238  68.967  24.940  1.00 46.05           C  
ATOM    427  CG  TYR A 126      13.113  69.437  24.056  1.00 49.33           C  
ATOM    428  CD1 TYR A 126      13.357  70.344  23.036  1.00 51.80           C  
ATOM    429  CD2 TYR A 126      11.810  68.947  24.210  1.00 51.75           C  
ATOM    430  CE1 TYR A 126      12.351  70.764  22.181  1.00 53.34           C  
ATOM    431  CE2 TYR A 126      10.780  69.360  23.350  1.00 53.80           C  
ATOM    432  CZ  TYR A 126      11.069  70.278  22.332  1.00 54.79           C  
ATOM    433  OH  TYR A 126      10.102  70.730  21.453  1.00 55.71           O  
ATOM    434  N   VAL A 127      16.314  67.100  26.272  1.00 42.14           N  
ATOM    435  CA  VAL A 127      17.598  66.899  26.932  1.00 40.80           C  
ATOM    436  C   VAL A 127      18.357  65.792  26.231  1.00 40.85           C  
ATOM    437  O   VAL A 127      19.565  65.875  26.053  1.00 40.34           O  
ATOM    438  CB  VAL A 127      17.447  66.499  28.392  1.00 39.58           C  
ATOM    439  CG1 VAL A 127      18.816  66.334  29.000  1.00 37.67           C  
ATOM    440  CG2 VAL A 127      16.643  67.549  29.147  1.00 37.68           C  
ATOM    441  N   THR A 128      17.645  64.746  25.840  1.00 41.97           N  
ATOM    442  CA  THR A 128      18.292  63.646  25.152  1.00 42.90           C  
ATOM    443  C   THR A 128      18.926  64.220  23.896  1.00 44.92           C  
ATOM    444  O   THR A 128      20.132  64.092  23.711  1.00 45.51           O  
ATOM    445  CB  THR A 128      17.285  62.528  24.766  1.00 41.98           C  
ATOM    446  OG1 THR A 128      16.791  61.899  25.954  1.00 40.33           O  
ATOM    447  CG2 THR A 128      17.947  61.480  23.897  1.00 39.66           C  
ATOM    448  N   ARG A 129      18.116  64.885  23.064  1.00 46.08           N  
ATOM    449  CA  ARG A 129      18.587  65.479  21.811  1.00 45.70           C  
ATOM    450  C   ARG A 129      19.789  66.416  21.964  1.00 46.44           C  
ATOM    451  O   ARG A 129      20.766  66.303  21.225  1.00 46.61           O  
ATOM    452  CB  ARG A 129      17.460  66.233  21.132  1.00 47.64           C  
ATOM    453  CG  ARG A 129      17.580  66.214  19.623  1.00 52.68           C  
ATOM    454  CD  ARG A 129      16.459  66.971  18.930  1.00 54.92           C  
ATOM    455  NE  ARG A 129      15.130  66.552  19.361  1.00 57.02           N  
ATOM    456  CZ  ARG A 129      14.237  67.390  19.885  1.00 60.83           C  
ATOM    457  NH1 ARG A 129      14.554  68.679  20.032  1.00 60.15           N  
ATOM    458  NH2 ARG A 129      13.032  66.949  20.261  1.00 61.31           N  
ATOM    459  N   GLU A 130      19.712  67.341  22.914  1.00 44.85           N  
ATOM    460  CA  GLU A 130      20.794  68.266  23.158  1.00 44.65           C  
ATOM    461  C   GLU A 130      22.098  67.514  23.396  1.00 46.74           C  
ATOM    462  O   GLU A 130      23.171  67.925  22.920  1.00 45.74           O  
ATOM    463  CB  GLU A 130      20.474  69.144  24.371  1.00 44.45           C  
ATOM    464  CG  GLU A 130      21.701  69.780  25.037  1.00 45.14           C  
ATOM    465  CD  GLU A 130      21.348  70.904  26.012  1.00 46.82           C  
ATOM    466  OE1 GLU A 130      20.405  70.721  26.815  1.00 48.88           O  
ATOM    467  OE2 GLU A 130      22.016  71.967  25.980  1.00 45.30           O  
ATOM    468  N   ARG A 131      22.001  66.416  24.146  1.00 47.77           N  
ATOM    469  CA  ARG A 131      23.161  65.594  24.477  1.00 47.20           C  
ATOM    470  C   ARG A 131      23.654  64.810  23.269  1.00 46.24           C  
ATOM    471  O   ARG A 131      24.849  64.728  22.985  1.00 45.20           O  
ATOM    472  CB  ARG A 131      22.807  64.604  25.580  1.00 49.19           C  
ATOM    473  CG  ARG A 131      23.990  63.751  25.970  1.00 52.43           C  
ATOM    474  CD  ARG A 131      23.585  62.659  26.887  1.00 57.04           C  
ATOM    475  NE  ARG A 131      24.745  61.885  27.300  1.00 63.20           N  
ATOM    476  CZ  ARG A 131      24.676  60.765  28.014  1.00 65.64           C  
ATOM    477  NH1 ARG A 131      23.487  60.296  28.387  1.00 66.38           N  
ATOM    478  NH2 ARG A 131      25.791  60.118  28.354  1.00 65.88           N  
ATOM    479  N   ASP A 132      22.709  64.231  22.558  1.00 45.25           N  
ATOM    480  CA  ASP A 132      23.025  63.441  21.403  1.00 46.10           C  
ATOM    481  C   ASP A 132      23.558  64.288  20.233  1.00 45.63           C  
ATOM    482  O   ASP A 132      24.321  63.788  19.411  1.00 47.67           O  
ATOM    483  CB  ASP A 132      21.788  62.608  21.035  1.00 49.05           C  
ATOM    484  CG  ASP A 132      21.511  61.457  22.056  1.00 51.77           C  
ATOM    485  OD1 ASP A 132      21.888  61.562  23.248  1.00 53.28           O  
ATOM    486  OD2 ASP A 132      20.902  60.435  21.670  1.00 54.41           O  
ATOM    487  N   VAL A 133      23.204  65.571  20.162  1.00 43.18           N  
ATOM    488  CA  VAL A 133      23.714  66.420  19.078  1.00 38.42           C  
ATOM    489  C   VAL A 133      25.118  66.868  19.395  1.00 39.21           C  
ATOM    490  O   VAL A 133      26.010  66.754  18.575  1.00 40.43           O  
ATOM    491  CB  VAL A 133      22.894  67.699  18.878  1.00 36.45           C  
ATOM    492  CG1 VAL A 133      23.679  68.678  18.035  1.00 34.45           C  
ATOM    493  CG2 VAL A 133      21.585  67.382  18.207  1.00 33.06           C  
ATOM    494  N   MET A 134      25.314  67.383  20.594  1.00 39.77           N  
ATOM    495  CA  MET A 134      26.619  67.856  20.986  1.00 41.18           C  
ATOM    496  C   MET A 134      27.695  66.798  20.966  1.00 43.06           C  
ATOM    497  O   MET A 134      28.867  67.116  20.785  1.00 44.31           O  
ATOM    498  CB  MET A 134      26.559  68.499  22.364  1.00 40.75           C  
ATOM    499  CG  MET A 134      25.779  69.779  22.342  1.00 44.87           C  
ATOM    500  SD  MET A 134      26.033  70.782  23.801  1.00 51.10           S  
ATOM    501  CE  MET A 134      27.321  71.911  23.195  1.00 51.06           C  
ATOM    502  N   SER A 135      27.318  65.541  21.151  1.00 45.00           N  
ATOM    503  CA  SER A 135      28.312  64.479  21.153  1.00 45.85           C  
ATOM    504  C   SER A 135      28.756  64.199  19.751  1.00 45.18           C  
ATOM    505  O   SER A 135      29.804  63.609  19.539  1.00 46.57           O  
ATOM    506  CB  SER A 135      27.748  63.201  21.762  1.00 48.03           C  
ATOM    507  OG  SER A 135      27.506  63.378  23.145  1.00 52.32           O  
ATOM    508  N   ARG A 136      27.956  64.632  18.793  1.00 45.15           N  
ATOM    509  CA  ARG A 136      28.268  64.418  17.392  1.00 45.49           C  
ATOM    510  C   ARG A 136      29.132  65.528  16.799  1.00 43.84           C  
ATOM    511  O   ARG A 136      29.725  65.363  15.746  1.00 45.02           O  
ATOM    512  CB  ARG A 136      26.975  64.305  16.583  1.00 48.05           C  
ATOM    513  CG  ARG A 136      26.085  63.116  16.937  1.00 52.59           C  
ATOM    514  CD  ARG A 136      24.954  63.007  15.925  1.00 56.62           C  
ATOM    515  NE  ARG A 136      25.496  63.076  14.568  1.00 63.44           N  
ATOM    516  CZ  ARG A 136      24.772  63.023  13.449  1.00 66.36           C  
ATOM    517  NH1 ARG A 136      23.446  62.892  13.518  1.00 68.02           N  
ATOM    518  NH2 ARG A 136      25.375  63.113  12.258  1.00 64.86           N  
ATOM    519  N   LEU A 137      29.218  66.659  17.477  1.00 43.17           N  
ATOM    520  CA  LEU A 137      29.991  67.775  16.963  1.00 41.15           C  
ATOM    521  C   LEU A 137      31.440  67.732  17.373  1.00 41.72           C  
ATOM    522  O   LEU A 137      31.766  67.449  18.524  1.00 43.77           O  
ATOM    523  CB  LEU A 137      29.393  69.102  17.437  1.00 40.46           C  
ATOM    524  CG  LEU A 137      27.909  69.368  17.144  1.00 39.52           C  
ATOM    525  CD1 LEU A 137      27.538  70.730  17.694  1.00 38.72           C  
ATOM    526  CD2 LEU A 137      27.619  69.292  15.660  1.00 39.02           C  
ATOM    527  N   ASP A 138      32.314  68.020  16.416  1.00 40.61           N  
ATOM    528  CA  ASP A 138      33.746  68.057  16.668  1.00 38.46           C  
ATOM    529  C   ASP A 138      34.356  69.134  15.787  1.00 37.17           C  
ATOM    530  O   ASP A 138      35.056  68.827  14.830  1.00 38.35           O  
ATOM    531  CB  ASP A 138      34.373  66.704  16.360  1.00 38.31           C  
ATOM    532  CG  ASP A 138      35.835  66.675  16.682  1.00 39.56           C  
ATOM    533  OD1 ASP A 138      36.206  67.213  17.749  1.00 37.88           O  
ATOM    534  OD2 ASP A 138      36.614  66.121  15.878  1.00 42.32           O  
ATOM    535  N   HIS A 139      34.091  70.394  16.120  1.00 33.90           N  
ATOM    536  CA  HIS A 139      34.575  71.507  15.322  1.00 33.07           C  
ATOM    537  C   HIS A 139      34.841  72.746  16.186  1.00 33.94           C  
ATOM    538  O   HIS A 139      34.058  73.100  17.078  1.00 35.79           O  
ATOM    539  CB  HIS A 139      33.549  71.810  14.231  1.00 33.82           C  
ATOM    540  CG  HIS A 139      33.969  72.882  13.274  1.00 35.57           C  
ATOM    541  ND1 HIS A 139      34.153  74.195  13.659  1.00 34.91           N  
ATOM    542  CD2 HIS A 139      34.230  72.837  11.944  1.00 34.03           C  
ATOM    543  CE1 HIS A 139      34.507  74.912  12.606  1.00 35.80           C  
ATOM    544  NE2 HIS A 139      34.562  74.113  11.554  1.00 35.17           N  
ATOM    545  N   PRO A 140      35.937  73.447  15.906  1.00 31.48           N  
ATOM    546  CA  PRO A 140      36.252  74.619  16.699  1.00 31.94           C  
ATOM    547  C   PRO A 140      35.209  75.703  16.948  1.00 33.11           C  
ATOM    548  O   PRO A 140      35.324  76.413  17.940  1.00 36.09           O  
ATOM    549  CB  PRO A 140      37.524  75.147  16.033  1.00 30.68           C  
ATOM    550  CG  PRO A 140      37.402  74.687  14.642  1.00 31.85           C  
ATOM    551  CD  PRO A 140      36.891  73.292  14.801  1.00 31.28           C  
ATOM    552  N   PHE A 141      34.195  75.857  16.098  1.00 33.38           N  
ATOM    553  CA  PHE A 141      33.211  76.924  16.342  1.00 31.78           C  
ATOM    554  C   PHE A 141      31.991  76.482  17.110  1.00 32.93           C  
ATOM    555  O   PHE A 141      30.942  77.101  17.031  1.00 34.86           O  
ATOM    556  CB  PHE A 141      32.759  77.569  15.034  1.00 29.49           C  
ATOM    557  CG  PHE A 141      33.867  78.259  14.282  1.00 30.48           C  
ATOM    558  CD1 PHE A 141      34.956  78.816  14.968  1.00 31.38           C  
ATOM    559  CD2 PHE A 141      33.818  78.378  12.893  1.00 27.33           C  
ATOM    560  CE1 PHE A 141      35.977  79.480  14.278  1.00 31.68           C  
ATOM    561  CE2 PHE A 141      34.827  79.039  12.193  1.00 29.85           C  
ATOM    562  CZ  PHE A 141      35.915  79.597  12.886  1.00 29.66           C  
ATOM    563  N   PHE A 142      32.126  75.417  17.877  1.00 32.20           N  
ATOM    564  CA  PHE A 142      31.009  74.930  18.641  1.00 31.71           C  
ATOM    565  C   PHE A 142      31.437  74.598  20.035  1.00 33.56           C  
ATOM    566  O   PHE A 142      32.543  74.128  20.258  1.00 35.92           O  
ATOM    567  CB  PHE A 142      30.453  73.693  17.975  1.00 31.29           C  
ATOM    568  CG  PHE A 142      29.736  73.981  16.692  1.00 31.94           C  
ATOM    569  CD1 PHE A 142      28.400  74.382  16.702  1.00 30.62           C  
ATOM    570  CD2 PHE A 142      30.385  73.850  15.475  1.00 29.15           C  
ATOM    571  CE1 PHE A 142      27.716  74.646  15.509  1.00 30.45           C  
ATOM    572  CE2 PHE A 142      29.717  74.112  14.284  1.00 29.61           C  
ATOM    573  CZ  PHE A 142      28.379  74.511  14.293  1.00 29.48           C  
ATOM    574  N   VAL A 143      30.567  74.857  20.992  1.00 35.43           N  
ATOM    575  CA  VAL A 143      30.887  74.529  22.365  1.00 36.20           C  
ATOM    576  C   VAL A 143      31.022  73.022  22.424  1.00 35.02           C  
ATOM    577  O   VAL A 143      30.227  72.295  21.845  1.00 34.54           O  
ATOM    578  CB  VAL A 143      29.776  74.987  23.316  1.00 37.66           C  
ATOM    579  CG1 VAL A 143      29.910  74.290  24.654  1.00 38.62           C  
ATOM    580  CG2 VAL A 143      29.873  76.497  23.507  1.00 38.10           C  
ATOM    581  N   LYS A 144      32.043  72.557  23.121  1.00 34.47           N  
ATOM    582  CA  LYS A 144      32.288  71.143  23.227  1.00 33.76           C  
ATOM    583  C   LYS A 144      31.701  70.564  24.496  1.00 32.73           C  
ATOM    584  O   LYS A 144      31.717  71.208  25.541  1.00 35.25           O  
ATOM    585  CB  LYS A 144      33.787  70.892  23.172  1.00 35.87           C  
ATOM    586  CG  LYS A 144      34.140  69.404  23.189  1.00 44.32           C  
ATOM    587  CD  LYS A 144      35.647  69.165  23.095  1.00 47.57           C  
ATOM    588  CE  LYS A 144      35.995  67.687  23.238  1.00 51.46           C  
ATOM    589  NZ  LYS A 144      37.486  67.501  23.180  1.00 56.21           N  
ATOM    590  N   LEU A 145      31.155  69.360  24.402  1.00 30.23           N  
ATOM    591  CA  LEU A 145      30.596  68.696  25.562  1.00 30.26           C  
ATOM    592  C   LEU A 145      31.694  67.733  25.988  1.00 32.12           C  
ATOM    593  O   LEU A 145      31.977  66.768  25.285  1.00 34.87           O  
ATOM    594  CB  LEU A 145      29.368  67.884  25.197  1.00 29.85           C  
ATOM    595  CG  LEU A 145      28.391  67.426  26.303  1.00 31.60           C  
ATOM    596  CD1 LEU A 145      27.868  66.031  25.952  1.00 27.61           C  
ATOM    597  CD2 LEU A 145      29.048  67.415  27.675  1.00 29.37           C  
ATOM    598  N   TYR A 146      32.312  67.989  27.130  1.00 31.08           N  
ATOM    599  CA  TYR A 146      33.390  67.143  27.588  1.00 31.53           C  
ATOM    600  C   TYR A 146      32.899  65.934  28.346  1.00 32.57           C  
ATOM    601  O   TYR A 146      33.526  64.896  28.294  1.00 33.74           O  
ATOM    602  CB  TYR A 146      34.350  67.931  28.477  1.00 29.68           C  
ATOM    603  CG  TYR A 146      35.157  68.976  27.749  1.00 29.44           C  
ATOM    604  CD1 TYR A 146      34.627  70.227  27.449  1.00 29.46           C  
ATOM    605  CD2 TYR A 146      36.463  68.711  27.359  1.00 30.60           C  
ATOM    606  CE1 TYR A 146      35.390  71.182  26.788  1.00 29.65           C  
ATOM    607  CE2 TYR A 146      37.226  69.651  26.695  1.00 28.13           C  
ATOM    608  CZ  TYR A 146      36.694  70.879  26.416  1.00 30.55           C  
ATOM    609  OH  TYR A 146      37.493  71.805  25.787  1.00 31.51           O  
ATOM    610  N   PHE A 147      31.780  66.042  29.051  1.00 32.14           N  
ATOM    611  CA  PHE A 147      31.318  64.892  29.807  1.00 31.21           C  
ATOM    612  C   PHE A 147      29.935  65.086  30.399  1.00 32.88           C  
ATOM    613  O   PHE A 147      29.403  66.199  30.404  1.00 32.68           O  
ATOM    614  CB  PHE A 147      32.302  64.606  30.937  1.00 29.72           C  
ATOM    615  CG  PHE A 147      32.562  65.786  31.816  1.00 31.56           C  
ATOM    616  CD1 PHE A 147      31.589  66.231  32.714  1.00 32.29           C  
ATOM    617  CD2 PHE A 147      33.745  66.514  31.679  1.00 32.74           C  
ATOM    618  CE1 PHE A 147      31.777  67.393  33.460  1.00 33.04           C  
ATOM    619  CE2 PHE A 147      33.962  67.680  32.413  1.00 33.44           C  
ATOM    620  CZ  PHE A 147      32.975  68.130  33.307  1.00 35.14           C  
ATOM    621  N   THR A 148      29.357  63.996  30.897  1.00 32.68           N  
ATOM    622  CA  THR A 148      28.065  64.061  31.536  1.00 34.06           C  
ATOM    623  C   THR A 148      28.072  63.093  32.708  1.00 36.93           C  
ATOM    624  O   THR A 148      28.878  62.169  32.786  1.00 35.78           O  
ATOM    625  CB  THR A 148      26.915  63.656  30.607  1.00 33.41           C  
ATOM    626  OG1 THR A 148      26.951  62.245  30.390  1.00 38.03           O  
ATOM    627  CG2 THR A 148      27.028  64.345  29.281  1.00 33.55           C  
ATOM    628  N   PHE A 149      27.182  63.347  33.650  1.00 38.97           N  
ATOM    629  CA  PHE A 149      27.029  62.493  34.802  1.00 39.96           C  
ATOM    630  C   PHE A 149      25.788  62.982  35.512  1.00 42.23           C  
ATOM    631  O   PHE A 149      25.213  64.014  35.151  1.00 42.21           O  
ATOM    632  CB  PHE A 149      28.277  62.511  35.696  1.00 37.50           C  
ATOM    633  CG  PHE A 149      28.645  63.856  36.244  1.00 36.97           C  
ATOM    634  CD1 PHE A 149      28.029  64.354  37.389  1.00 37.85           C  
ATOM    635  CD2 PHE A 149      29.651  64.610  35.650  1.00 36.08           C  
ATOM    636  CE1 PHE A 149      28.417  65.586  37.936  1.00 36.24           C  
ATOM    637  CE2 PHE A 149      30.037  65.833  36.187  1.00 35.23           C  
ATOM    638  CZ  PHE A 149      29.419  66.322  37.334  1.00 33.54           C  
ATOM    639  N   GLN A 150      25.327  62.213  36.480  1.00 44.59           N  
ATOM    640  CA  GLN A 150      24.146  62.619  37.193  1.00 47.00           C  
ATOM    641  C   GLN A 150      24.153  62.024  38.559  1.00 47.57           C  
ATOM    642  O   GLN A 150      24.888  61.085  38.828  1.00 47.71           O  
ATOM    643  CB  GLN A 150      22.898  62.178  36.447  1.00 48.69           C  
ATOM    644  CG  GLN A 150      22.900  60.730  36.021  1.00 51.57           C  
ATOM    645  CD  GLN A 150      21.560  60.309  35.436  1.00 53.49           C  
ATOM    646  OE1 GLN A 150      20.563  60.207  36.161  1.00 55.31           O  
ATOM    647  NE2 GLN A 150      21.521  60.079  34.119  1.00 52.94           N  
ATOM    648  N   ASP A 151      23.363  62.617  39.439  1.00 48.72           N  
ATOM    649  CA  ASP A 151      23.234  62.104  40.783  1.00 48.89           C  
ATOM    650  C   ASP A 151      21.763  61.722  40.906  1.00 51.19           C  
ATOM    651  O   ASP A 151      21.072  61.522  39.890  1.00 51.20           O  
ATOM    652  CB  ASP A 151      23.629  63.161  41.824  1.00 47.02           C  
ATOM    653  CG  ASP A 151      22.865  64.442  41.668  1.00 45.90           C  
ATOM    654  OD1 ASP A 151      21.739  64.391  41.138  1.00 47.31           O  
ATOM    655  OD2 ASP A 151      23.379  65.497  42.090  1.00 44.94           O  
ATOM    656  N   ASP A 152      21.274  61.625  42.134  1.00 52.64           N  
ATOM    657  CA  ASP A 152      19.888  61.253  42.336  1.00 53.97           C  
ATOM    658  C   ASP A 152      18.891  62.317  41.880  1.00 52.67           C  
ATOM    659  O   ASP A 152      17.739  62.014  41.598  1.00 51.97           O  
ATOM    660  CB  ASP A 152      19.671  60.917  43.807  1.00 57.97           C  
ATOM    661  CG  ASP A 152      19.959  59.461  44.114  1.00 63.50           C  
ATOM    662  OD1 ASP A 152      18.983  58.682  44.201  1.00 67.02           O  
ATOM    663  OD2 ASP A 152      21.153  59.086  44.249  1.00 66.29           O  
ATOM    664  N   GLU A 153      19.325  63.561  41.760  1.00 51.49           N  
ATOM    665  CA  GLU A 153      18.367  64.570  41.391  1.00 50.69           C  
ATOM    666  C   GLU A 153      18.659  65.384  40.142  1.00 49.63           C  
ATOM    667  O   GLU A 153      17.730  65.857  39.489  1.00 49.79           O  
ATOM    668  CB  GLU A 153      18.149  65.508  42.579  1.00 53.55           C  
ATOM    669  CG  GLU A 153      18.358  64.871  43.961  1.00 58.39           C  
ATOM    670  CD  GLU A 153      19.841  64.781  44.344  1.00 63.29           C  
ATOM    671  OE1 GLU A 153      20.546  65.818  44.258  1.00 67.00           O  
ATOM    672  OE2 GLU A 153      20.314  63.687  44.737  1.00 65.37           O  
ATOM    673  N   LYS A 154      19.928  65.533  39.777  1.00 47.04           N  
ATOM    674  CA  LYS A 154      20.262  66.357  38.621  1.00 43.91           C  
ATOM    675  C   LYS A 154      21.103  65.703  37.541  1.00 42.14           C  
ATOM    676  O   LYS A 154      21.726  64.661  37.751  1.00 41.72           O  
ATOM    677  CB  LYS A 154      20.990  67.619  39.085  1.00 43.87           C  
ATOM    678  CG  LYS A 154      20.213  68.507  40.027  1.00 44.51           C  
ATOM    679  CD  LYS A 154      21.152  69.334  40.936  1.00 44.54           C  
ATOM    680  CE  LYS A 154      20.384  70.393  41.746  1.00 44.31           C  
ATOM    681  NZ  LYS A 154      21.102  70.774  42.999  1.00 46.33           N  
ATOM    682  N   LEU A 155      21.121  66.372  36.394  1.00 39.06           N  
ATOM    683  CA  LEU A 155      21.878  65.970  35.222  1.00 36.76           C  
ATOM    684  C   LEU A 155      22.945  67.034  35.024  1.00 37.40           C  
ATOM    685  O   LEU A 155      22.643  68.240  35.064  1.00 36.61           O  
ATOM    686  CB  LEU A 155      20.985  65.967  33.987  1.00 34.54           C  
ATOM    687  CG  LEU A 155      19.889  64.932  33.844  1.00 32.99           C  
ATOM    688  CD1 LEU A 155      19.053  65.279  32.668  1.00 32.45           C  
ATOM    689  CD2 LEU A 155      20.483  63.566  33.668  1.00 33.56           C  
ATOM    690  N   TYR A 156      24.179  66.603  34.772  1.00 36.76           N  
ATOM    691  CA  TYR A 156      25.274  67.548  34.580  1.00 35.34           C  
ATOM    692  C   TYR A 156      25.951  67.417  33.229  1.00 36.20           C  
ATOM    693  O   TYR A 156      26.275  66.310  32.821  1.00 36.50           O  
ATOM    694  CB  TYR A 156      26.334  67.343  35.648  1.00 36.02           C  
ATOM    695  CG  TYR A 156      25.846  67.433  37.068  1.00 35.84           C  
ATOM    696  CD1 TYR A 156      25.284  66.332  37.702  1.00 37.62           C  
ATOM    697  CD2 TYR A 156      25.963  68.622  37.788  1.00 36.55           C  
ATOM    698  CE1 TYR A 156      24.844  66.409  39.032  1.00 39.04           C  
ATOM    699  CE2 TYR A 156      25.531  68.710  39.108  1.00 38.42           C  
ATOM    700  CZ  TYR A 156      24.974  67.602  39.721  1.00 38.76           C  
ATOM    701  OH  TYR A 156      24.551  67.688  41.020  1.00 39.41           O  
ATOM    702  N   PHE A 157      26.170  68.541  32.541  1.00 36.48           N  
ATOM    703  CA  PHE A 157      26.850  68.550  31.242  1.00 36.54           C  
ATOM    704  C   PHE A 157      28.114  69.401  31.326  1.00 35.84           C  
ATOM    705  O   PHE A 157      28.031  70.593  31.565  1.00 38.22           O  
ATOM    706  CB  PHE A 157      25.957  69.136  30.152  1.00 40.63           C  
ATOM    707  CG  PHE A 157      24.764  68.279  29.791  1.00 44.92           C  
ATOM    708  CD1 PHE A 157      24.588  67.013  30.344  1.00 47.87           C  
ATOM    709  CD2 PHE A 157      23.797  68.761  28.914  1.00 44.83           C  
ATOM    710  CE1 PHE A 157      23.448  66.236  30.029  1.00 49.19           C  
ATOM    711  CE2 PHE A 157      22.670  68.008  28.595  1.00 46.28           C  
ATOM    712  CZ  PHE A 157      22.491  66.747  29.151  1.00 48.02           C  
ATOM    713  N   GLY A 158      29.285  68.810  31.142  1.00 33.11           N  
ATOM    714  CA  GLY A 158      30.499  69.598  31.225  1.00 31.34           C  
ATOM    715  C   GLY A 158      30.741  70.245  29.888  1.00 30.54           C  
ATOM    716  O   GLY A 158      31.020  69.555  28.920  1.00 32.59           O  
ATOM    717  N   LEU A 159      30.655  71.565  29.831  1.00 30.10           N  
ATOM    718  CA  LEU A 159      30.821  72.299  28.585  1.00 30.74           C  
ATOM    719  C   LEU A 159      32.037  73.237  28.538  1.00 32.38           C  
ATOM    720  O   LEU A 159      32.566  73.637  29.570  1.00 32.44           O  
ATOM    721  CB  LEU A 159      29.553  73.119  28.332  1.00 28.11           C  
ATOM    722  CG  LEU A 159      28.233  72.350  28.245  1.00 29.01           C  
ATOM    723  CD1 LEU A 159      27.060  73.321  28.162  1.00 26.54           C  
ATOM    724  CD2 LEU A 159      28.260  71.457  27.013  1.00 30.57           C  
ATOM    725  N   SER A 160      32.480  73.594  27.335  1.00 32.16           N  
ATOM    726  CA  SER A 160      33.577  74.533  27.234  1.00 32.27           C  
ATOM    727  C   SER A 160      33.061  75.800  27.889  1.00 32.70           C  
ATOM    728  O   SER A 160      31.889  76.118  27.811  1.00 32.01           O  
ATOM    729  CB  SER A 160      33.886  74.879  25.792  1.00 31.61           C  
ATOM    730  OG  SER A 160      33.567  73.801  24.961  1.00 37.67           O  
ATOM    731  N   TYR A 161      33.952  76.529  28.531  1.00 34.04           N  
ATOM    732  CA  TYR A 161      33.587  77.774  29.153  1.00 33.71           C  
ATOM    733  C   TYR A 161      34.161  78.872  28.268  1.00 35.62           C  
ATOM    734  O   TYR A 161      35.373  79.112  28.255  1.00 36.75           O  
ATOM    735  CB  TYR A 161      34.183  77.840  30.542  1.00 33.72           C  
ATOM    736  CG  TYR A 161      34.191  79.217  31.117  1.00 34.99           C  
ATOM    737  CD1 TYR A 161      33.050  80.036  31.060  1.00 34.18           C  
ATOM    738  CD2 TYR A 161      35.328  79.706  31.750  1.00 34.96           C  
ATOM    739  CE1 TYR A 161      33.050  81.322  31.632  1.00 34.18           C  
ATOM    740  CE2 TYR A 161      35.340  80.978  32.322  1.00 36.46           C  
ATOM    741  CZ  TYR A 161      34.204  81.785  32.264  1.00 35.71           C  
ATOM    742  OH  TYR A 161      34.260  83.032  32.847  1.00 33.93           O  
ATOM    743  N   ALA A 162      33.280  79.514  27.510  1.00 36.55           N  
ATOM    744  CA  ALA A 162      33.660  80.587  26.617  1.00 37.07           C  
ATOM    745  C   ALA A 162      33.852  81.808  27.490  1.00 38.62           C  
ATOM    746  O   ALA A 162      32.884  82.402  27.919  1.00 39.34           O  
ATOM    747  CB  ALA A 162      32.565  80.824  25.627  1.00 36.68           C  
ATOM    748  N   LYS A 163      35.107  82.175  27.741  1.00 41.21           N  
ATOM    749  CA  LYS A 163      35.445  83.313  28.598  1.00 42.07           C  
ATOM    750  C   LYS A 163      34.950  84.697  28.206  1.00 41.71           C  
ATOM    751  O   LYS A 163      34.773  85.536  29.070  1.00 42.31           O  
ATOM    752  CB  LYS A 163      36.966  83.392  28.804  1.00 42.59           C  
ATOM    753  CG  LYS A 163      37.516  82.362  29.775  1.00 45.40           C  
ATOM    754  CD  LYS A 163      38.858  82.752  30.354  0.00 44.95           C  
ATOM    755  CE  LYS A 163      39.142  81.935  31.607  0.00 45.39           C  
ATOM    756  NZ  LYS A 163      38.973  80.474  31.369  0.00 45.49           N  
ATOM    757  N   ASN A 164      34.718  84.948  26.921  1.00 42.08           N  
ATOM    758  CA  ASN A 164      34.286  86.280  26.504  1.00 40.47           C  
ATOM    759  C   ASN A 164      32.798  86.531  26.308  1.00 40.31           C  
ATOM    760  O   ASN A 164      32.405  87.448  25.597  1.00 40.53           O  
ATOM    761  CB  ASN A 164      35.068  86.704  25.258  1.00 40.81           C  
ATOM    762  CG  ASN A 164      36.482  87.133  25.598  1.00 41.11           C  
ATOM    763  OD1 ASN A 164      36.674  88.006  26.437  1.00 39.73           O  
ATOM    764  ND2 ASN A 164      37.475  86.523  24.959  1.00 42.30           N  
ATOM    765  N   GLY A 165      31.968  85.720  26.950  1.00 40.22           N  
ATOM    766  CA  GLY A 165      30.541  85.920  26.849  1.00 41.53           C  
ATOM    767  C   GLY A 165      29.880  85.617  25.529  1.00 44.19           C  
ATOM    768  O   GLY A 165      30.245  84.675  24.846  1.00 46.94           O  
ATOM    769  N   GLU A 166      28.889  86.424  25.175  1.00 46.23           N  
ATOM    770  CA  GLU A 166      28.141  86.244  23.942  1.00 47.20           C  
ATOM    771  C   GLU A 166      28.287  87.400  22.983  1.00 46.70           C  
ATOM    772  O   GLU A 166      28.632  88.513  23.358  1.00 47.53           O  
ATOM    773  CB  GLU A 166      26.666  86.037  24.254  1.00 49.65           C  
ATOM    774  CG  GLU A 166      26.108  87.009  25.251  1.00 53.89           C  
ATOM    775  CD  GLU A 166      24.788  86.523  25.829  1.00 57.74           C  
ATOM    776  OE1 GLU A 166      24.734  85.377  26.345  1.00 59.94           O  
ATOM    777  OE2 GLU A 166      23.800  87.285  25.771  1.00 61.03           O  
ATOM    778  N   LEU A 167      28.004  87.117  21.728  1.00 45.34           N  
ATOM    779  CA  LEU A 167      28.118  88.103  20.684  1.00 43.85           C  
ATOM    780  C   LEU A 167      27.184  89.295  20.893  1.00 44.55           C  
ATOM    781  O   LEU A 167      27.488  90.429  20.487  1.00 46.11           O  
ATOM    782  CB  LEU A 167      27.838  87.423  19.349  1.00 40.26           C  
ATOM    783  CG  LEU A 167      28.169  88.222  18.102  1.00 37.86           C  
ATOM    784  CD1 LEU A 167      29.522  88.842  18.234  1.00 37.33           C  
ATOM    785  CD2 LEU A 167      28.133  87.302  16.908  1.00 39.37           C  
ATOM    786  N   LEU A 168      26.039  89.042  21.513  1.00 43.33           N  
ATOM    787  CA  LEU A 168      25.091  90.114  21.749  1.00 42.82           C  
ATOM    788  C   LEU A 168      25.699  91.162  22.655  1.00 42.45           C  
ATOM    789  O   LEU A 168      25.464  92.338  22.459  1.00 43.68           O  
ATOM    790  CB  LEU A 168      23.813  89.577  22.376  1.00 41.34           C  
ATOM    791  CG  LEU A 168      22.834  90.659  22.822  1.00 40.70           C  
ATOM    792  CD1 LEU A 168      22.403  91.511  21.657  1.00 37.95           C  
ATOM    793  CD2 LEU A 168      21.640  89.990  23.450  1.00 41.69           C  
ATOM    794  N   LYS A 169      26.482  90.733  23.640  1.00 43.53           N  
ATOM    795  CA  LYS A 169      27.117  91.655  24.573  1.00 45.37           C  
ATOM    796  C   LYS A 169      27.986  92.606  23.788  1.00 47.74           C  
ATOM    797  O   LYS A 169      27.925  93.820  23.987  1.00 49.77           O  
ATOM    798  CB  LYS A 169      27.963  90.907  25.588  1.00 44.56           C  
ATOM    799  N   TYR A 170      28.796  92.062  22.892  1.00 47.70           N  
ATOM    800  CA  TYR A 170      29.648  92.910  22.081  1.00 50.83           C  
ATOM    801  C   TYR A 170      28.858  93.853  21.190  1.00 51.85           C  
ATOM    802  O   TYR A 170      29.162  95.046  21.113  1.00 52.19           O  
ATOM    803  CB  TYR A 170      30.600  92.054  21.253  1.00 53.08           C  
ATOM    804  CG  TYR A 170      31.780  91.686  22.079  1.00 57.70           C  
ATOM    805  CD1 TYR A 170      32.954  92.436  22.017  1.00 59.36           C  
ATOM    806  CD2 TYR A 170      31.675  90.698  23.068  1.00 60.47           C  
ATOM    807  CE1 TYR A 170      33.996  92.222  22.934  1.00 61.26           C  
ATOM    808  CE2 TYR A 170      32.710  90.477  23.990  1.00 61.88           C  
ATOM    809  CZ  TYR A 170      33.862  91.246  23.915  1.00 61.67           C  
ATOM    810  OH  TYR A 170      34.875  91.050  24.823  1.00 64.88           O  
ATOM    811  N   ILE A 171      27.836  93.339  20.518  1.00 51.83           N  
ATOM    812  CA  ILE A 171      27.053  94.212  19.667  1.00 51.27           C  
ATOM    813  C   ILE A 171      26.580  95.427  20.466  1.00 51.64           C  
ATOM    814  O   ILE A 171      26.677  96.539  19.980  1.00 50.30           O  
ATOM    815  CB  ILE A 171      25.842  93.491  19.084  1.00 50.92           C  
ATOM    816  CG1 ILE A 171      26.294  92.236  18.337  1.00 50.57           C  
ATOM    817  CG2 ILE A 171      25.098  94.428  18.149  1.00 49.57           C  
ATOM    818  CD1 ILE A 171      25.149  91.382  17.830  1.00 49.14           C  
ATOM    819  N   ARG A 172      26.077  95.215  21.685  1.00 52.78           N  
ATOM    820  CA  ARG A 172      25.614  96.321  22.533  1.00 55.16           C  
ATOM    821  C   ARG A 172      26.805  97.188  22.926  1.00 56.60           C  
ATOM    822  O   ARG A 172      26.815  98.408  22.741  1.00 56.61           O  
ATOM    823  CB  ARG A 172      24.969  95.811  23.824  1.00 56.81           C  
ATOM    824  CG  ARG A 172      23.689  95.002  23.669  1.00 59.32           C  
ATOM    825  CD  ARG A 172      23.012  94.843  25.043  1.00 62.86           C  
ATOM    826  NE  ARG A 172      21.888  93.884  25.111  1.00 63.57           N  
ATOM    827  CZ  ARG A 172      20.920  93.767  24.194  1.00 64.79           C  
ATOM    828  NH1 ARG A 172      20.936  94.539  23.109  1.00 65.92           N  
ATOM    829  NH2 ARG A 172      19.914  92.932  24.398  1.00 62.55           N  
ATOM    830  N   LYS A 173      27.812  96.534  23.488  1.00 57.97           N  
ATOM    831  CA  LYS A 173      29.027  97.199  23.926  1.00 57.91           C  
ATOM    832  C   LYS A 173      29.643  98.137  22.893  1.00 57.54           C  
ATOM    833  O   LYS A 173      29.912  99.289  23.209  1.00 58.55           O  
ATOM    834  CB  LYS A 173      30.068  96.158  24.348  1.00 59.20           C  
ATOM    835  CG  LYS A 173      31.475  96.716  24.580  1.00 59.19           C  
ATOM    836  CD  LYS A 173      32.460  95.606  24.931  0.00 59.39           C  
ATOM    837  CE  LYS A 173      32.043  94.863  26.193  0.00 59.45           C  
ATOM    838  NZ  LYS A 173      31.943  95.774  27.366  0.00 59.53           N  
ATOM    839  N   ILE A 174      29.883  97.663  21.672  1.00 56.41           N  
ATOM    840  CA  ILE A 174      30.498  98.539  20.687  1.00 55.53           C  
ATOM    841  C   ILE A 174      29.453  99.166  19.786  1.00 56.52           C  
ATOM    842  O   ILE A 174      29.744 100.075  19.017  1.00 57.61           O  
ATOM    843  CB  ILE A 174      31.583  97.810  19.839  1.00 55.59           C  
ATOM    844  CG1 ILE A 174      30.942  96.938  18.774  1.00 56.01           C  
ATOM    845  CG2 ILE A 174      32.474  96.967  20.727  1.00 54.30           C  
ATOM    846  CD1 ILE A 174      30.735  97.665  17.473  1.00 56.83           C  
ATOM    847  N   GLY A 175      28.224  98.683  19.881  1.00 56.29           N  
ATOM    848  CA  GLY A 175      27.164  99.262  19.088  1.00 55.34           C  
ATOM    849  C   GLY A 175      26.963  98.720  17.699  1.00 55.60           C  
ATOM    850  O   GLY A 175      25.995  98.024  17.434  1.00 59.48           O  
ATOM    851  N   SER A 176      27.878  99.027  16.804  1.00 54.47           N  
ATOM    852  CA  SER A 176      27.746  98.604  15.423  1.00 52.97           C  
ATOM    853  C   SER A 176      29.124  98.206  14.906  1.00 52.85           C  
ATOM    854  O   SER A 176      30.080  98.978  15.022  1.00 53.54           O  
ATOM    855  CB  SER A 176      27.176  99.773  14.612  1.00 51.79           C  
ATOM    856  OG  SER A 176      27.324  99.576  13.223  1.00 53.85           O  
ATOM    857  N   PHE A 177      29.221  96.998  14.357  1.00 49.83           N  
ATOM    858  CA  PHE A 177      30.466  96.467  13.825  1.00 46.77           C  
ATOM    859  C   PHE A 177      30.797  97.106  12.496  1.00 47.59           C  
ATOM    860  O   PHE A 177      29.901  97.344  11.691  1.00 48.33           O  
ATOM    861  CB  PHE A 177      30.323  94.969  13.612  1.00 44.78           C  
ATOM    862  CG  PHE A 177      30.421  94.171  14.867  1.00 43.07           C  
ATOM    863  CD1 PHE A 177      30.128  94.747  16.100  1.00 41.57           C  
ATOM    864  CD2 PHE A 177      30.836  92.848  14.825  1.00 41.50           C  
ATOM    865  CE1 PHE A 177      30.251  94.021  17.277  1.00 40.55           C  
ATOM    866  CE2 PHE A 177      30.962  92.116  15.993  1.00 41.70           C  
ATOM    867  CZ  PHE A 177      30.670  92.705  17.227  1.00 40.87           C  
ATOM    868  N   ASP A 178      32.069  97.388  12.238  1.00 46.73           N  
ATOM    869  CA  ASP A 178      32.381  97.968  10.946  1.00 46.01           C  
ATOM    870  C   ASP A 178      32.451  96.830   9.961  1.00 44.14           C  
ATOM    871  O   ASP A 178      32.024  95.728  10.271  1.00 42.84           O  
ATOM    872  CB  ASP A 178      33.683  98.758  10.964  1.00 50.00           C  
ATOM    873  CG  ASP A 178      34.848  97.948  11.451  1.00 55.54           C  
ATOM    874  OD1 ASP A 178      34.708  96.704  11.579  1.00 58.05           O  
ATOM    875  OD2 ASP A 178      35.911  98.571  11.695  1.00 58.39           O  
ATOM    876  N   GLU A 179      33.002  97.070   8.783  1.00 43.03           N  
ATOM    877  CA  GLU A 179      33.013  96.010   7.802  1.00 43.09           C  
ATOM    878  C   GLU A 179      33.991  94.886   8.034  1.00 42.40           C  
ATOM    879  O   GLU A 179      33.682  93.732   7.789  1.00 41.79           O  
ATOM    880  CB  GLU A 179      33.205  96.568   6.412  1.00 42.22           C  
ATOM    881  CG  GLU A 179      32.744  95.583   5.395  1.00 46.49           C  
ATOM    882  CD  GLU A 179      32.621  96.165   4.008  1.00 50.98           C  
ATOM    883  OE1 GLU A 179      32.437  97.398   3.889  1.00 51.87           O  
ATOM    884  OE2 GLU A 179      32.684  95.376   3.034  1.00 53.48           O  
ATOM    885  N   THR A 180      35.173  95.211   8.514  1.00 42.27           N  
ATOM    886  CA  THR A 180      36.161  94.178   8.761  1.00 42.44           C  
ATOM    887  C   THR A 180      35.692  93.153   9.783  1.00 41.52           C  
ATOM    888  O   THR A 180      35.943  91.971   9.599  1.00 42.13           O  
ATOM    889  CB  THR A 180      37.493  94.792   9.227  1.00 42.65           C  
ATOM    890  OG1 THR A 180      37.969  95.676   8.212  1.00 43.93           O  
ATOM    891  CG2 THR A 180      38.530  93.719   9.453  1.00 43.10           C  
ATOM    892  N   CYS A 181      35.025  93.600  10.849  1.00 40.27           N  
ATOM    893  CA  CYS A 181      34.540  92.691  11.885  1.00 42.19           C  
ATOM    894  C   CYS A 181      33.238  92.016  11.461  1.00 41.55           C  
ATOM    895  O   CYS A 181      32.996  90.852  11.766  1.00 41.81           O  
ATOM    896  CB  CYS A 181      34.306  93.432  13.196  1.00 44.23           C  
ATOM    897  SG  CYS A 181      35.762  94.234  13.861  1.00 50.93           S  
ATOM    898  N   THR A 182      32.388  92.761  10.777  1.00 39.78           N  
ATOM    899  CA  THR A 182      31.149  92.193  10.290  1.00 39.11           C  
ATOM    900  C   THR A 182      31.518  91.030   9.353  1.00 38.20           C  
ATOM    901  O   THR A 182      30.966  89.933   9.470  1.00 38.51           O  
ATOM    902  CB  THR A 182      30.334  93.233   9.505  1.00 37.74           C  
ATOM    903  OG1 THR A 182      29.917  94.274  10.386  1.00 38.98           O  
ATOM    904  CG2 THR A 182      29.134  92.594   8.896  1.00 36.65           C  
ATOM    905  N   ARG A 183      32.460  91.271   8.441  1.00 35.31           N  
ATOM    906  CA  ARG A 183      32.884  90.230   7.524  1.00 34.54           C  
ATOM    907  C   ARG A 183      33.549  89.068   8.245  1.00 34.73           C  
ATOM    908  O   ARG A 183      33.297  87.921   7.923  1.00 34.68           O  
ATOM    909  CB  ARG A 183      33.855  90.754   6.478  1.00 33.17           C  
ATOM    910  CG  ARG A 183      34.363  89.627   5.615  1.00 34.21           C  
ATOM    911  CD  ARG A 183      35.279  90.059   4.459  1.00 39.91           C  
ATOM    912  NE  ARG A 183      35.862  91.385   4.616  1.00 42.48           N  
ATOM    913  CZ  ARG A 183      35.393  92.462   3.989  1.00 49.26           C  
ATOM    914  NH1 ARG A 183      34.343  92.362   3.160  1.00 48.99           N  
ATOM    915  NH2 ARG A 183      35.944  93.652   4.210  1.00 51.21           N  
ATOM    916  N   PHE A 184      34.387  89.338   9.230  1.00 34.10           N  
ATOM    917  CA  PHE A 184      35.039  88.223   9.893  1.00 35.74           C  
ATOM    918  C   PHE A 184      34.060  87.338  10.648  1.00 36.58           C  
ATOM    919  O   PHE A 184      34.038  86.116  10.456  1.00 38.14           O  
ATOM    920  CB  PHE A 184      36.107  88.706  10.866  1.00 37.38           C  
ATOM    921  CG  PHE A 184      36.856  87.592  11.532  1.00 36.13           C  
ATOM    922  CD1 PHE A 184      37.891  86.942  10.874  1.00 37.05           C  
ATOM    923  CD2 PHE A 184      36.489  87.155  12.793  1.00 35.79           C  
ATOM    924  CE1 PHE A 184      38.555  85.853  11.468  1.00 37.02           C  
ATOM    925  CE2 PHE A 184      37.138  86.074  13.394  1.00 37.52           C  
ATOM    926  CZ  PHE A 184      38.176  85.422  12.722  1.00 38.86           C  
ATOM    927  N   TYR A 185      33.245  87.950  11.498  1.00 34.44           N  
ATOM    928  CA  TYR A 185      32.290  87.193  12.287  1.00 34.58           C  
ATOM    929  C   TYR A 185      31.193  86.476  11.506  1.00 35.57           C  
ATOM    930  O   TYR A 185      30.795  85.355  11.842  1.00 34.16           O  
ATOM    931  CB  TYR A 185      31.725  88.099  13.372  1.00 34.46           C  
ATOM    932  CG  TYR A 185      32.729  88.226  14.490  1.00 36.38           C  
ATOM    933  CD1 TYR A 185      33.074  87.105  15.257  1.00 36.02           C  
ATOM    934  CD2 TYR A 185      33.460  89.398  14.682  1.00 36.29           C  
ATOM    935  CE1 TYR A 185      34.122  87.143  16.161  1.00 35.19           C  
ATOM    936  CE2 TYR A 185      34.523  89.438  15.598  1.00 36.46           C  
ATOM    937  CZ  TYR A 185      34.844  88.302  16.324  1.00 36.49           C  
ATOM    938  OH  TYR A 185      35.915  88.293  17.187  1.00 39.57           O  
ATOM    939  N   THR A 186      30.713  87.105  10.446  1.00 36.11           N  
ATOM    940  CA  THR A 186      29.695  86.480   9.625  1.00 35.07           C  
ATOM    941  C   THR A 186      30.299  85.223   9.025  1.00 36.11           C  
ATOM    942  O   THR A 186      29.696  84.144   9.076  1.00 37.89           O  
ATOM    943  CB  THR A 186      29.279  87.401   8.518  1.00 35.49           C  
ATOM    944  OG1 THR A 186      28.646  88.554   9.088  1.00 35.65           O  
ATOM    945  CG2 THR A 186      28.337  86.698   7.584  1.00 34.85           C  
ATOM    946  N   ALA A 187      31.497  85.367   8.462  1.00 34.69           N  
ATOM    947  CA  ALA A 187      32.210  84.247   7.866  1.00 32.24           C  
ATOM    948  C   ALA A 187      32.313  83.057   8.837  1.00 33.27           C  
ATOM    949  O   ALA A 187      32.035  81.900   8.471  1.00 34.77           O  
ATOM    950  CB  ALA A 187      33.583  84.687   7.466  1.00 29.87           C  
ATOM    951  N   GLU A 188      32.702  83.321  10.079  1.00 31.03           N  
ATOM    952  CA  GLU A 188      32.838  82.216  11.019  1.00 30.32           C  
ATOM    953  C   GLU A 188      31.496  81.547  11.207  1.00 29.81           C  
ATOM    954  O   GLU A 188      31.414  80.337  11.362  1.00 29.35           O  
ATOM    955  CB  GLU A 188      33.376  82.697  12.382  1.00 31.10           C  
ATOM    956  CG  GLU A 188      34.789  83.303  12.335  1.00 31.20           C  
ATOM    957  CD  GLU A 188      35.541  83.165  13.659  1.00 32.77           C  
ATOM    958  OE1 GLU A 188      34.939  83.431  14.717  1.00 35.39           O  
ATOM    959  OE2 GLU A 188      36.730  82.805  13.652  1.00 30.10           O  
ATOM    960  N   ILE A 189      30.431  82.334  11.181  1.00 29.25           N  
ATOM    961  CA  ILE A 189      29.116  81.761  11.375  1.00 28.79           C  
ATOM    962  C   ILE A 189      28.718  80.952  10.157  1.00 29.62           C  
ATOM    963  O   ILE A 189      28.219  79.842  10.281  1.00 29.15           O  
ATOM    964  CB  ILE A 189      28.075  82.844  11.650  1.00 28.54           C  
ATOM    965  CG1 ILE A 189      28.476  83.639  12.906  1.00 29.58           C  
ATOM    966  CG2 ILE A 189      26.740  82.209  11.864  1.00 27.30           C  
ATOM    967  CD1 ILE A 189      27.673  84.916  13.175  1.00 25.81           C  
ATOM    968  N   VAL A 190      28.955  81.497   8.974  1.00 30.49           N  
ATOM    969  CA  VAL A 190      28.616  80.777   7.760  1.00 29.79           C  
ATOM    970  C   VAL A 190      29.365  79.453   7.779  1.00 32.12           C  
ATOM    971  O   VAL A 190      28.805  78.388   7.528  1.00 30.06           O  
ATOM    972  CB  VAL A 190      29.042  81.563   6.520  1.00 28.81           C  
ATOM    973  CG1 VAL A 190      29.059  80.657   5.333  1.00 28.93           C  
ATOM    974  CG2 VAL A 190      28.081  82.707   6.271  1.00 27.89           C  
ATOM    975  N   SER A 191      30.647  79.547   8.101  1.00 33.07           N  
ATOM    976  CA  SER A 191      31.519  78.392   8.144  1.00 35.06           C  
ATOM    977  C   SER A 191      31.069  77.333   9.156  1.00 34.14           C  
ATOM    978  O   SER A 191      31.213  76.130   8.919  1.00 33.42           O  
ATOM    979  CB  SER A 191      32.935  78.865   8.452  1.00 37.61           C  
ATOM    980  OG  SER A 191      33.875  77.833   8.250  1.00 40.90           O  
ATOM    981  N   ALA A 192      30.503  77.784  10.268  1.00 34.33           N  
ATOM    982  CA  ALA A 192      30.038  76.876  11.309  1.00 34.06           C  
ATOM    983  C   ALA A 192      28.714  76.230  10.965  1.00 35.79           C  
ATOM    984  O   ALA A 192      28.435  75.126  11.430  1.00 38.04           O  
ATOM    985  CB  ALA A 192      29.912  77.600  12.610  1.00 34.28           C  
ATOM    986  N   LEU A 193      27.888  76.905  10.168  1.00 34.39           N  
ATOM    987  CA  LEU A 193      26.607  76.337   9.790  1.00 34.28           C  
ATOM    988  C   LEU A 193      26.813  75.332   8.677  1.00 35.15           C  
ATOM    989  O   LEU A 193      26.139  74.300   8.604  1.00 36.95           O  
ATOM    990  CB  LEU A 193      25.645  77.426   9.315  1.00 35.65           C  
ATOM    991  CG  LEU A 193      25.074  78.396  10.351  1.00 37.64           C  
ATOM    992  CD1 LEU A 193      24.268  79.494   9.653  1.00 35.31           C  
ATOM    993  CD2 LEU A 193      24.211  77.613  11.340  1.00 36.96           C  
ATOM    994  N   GLU A 194      27.730  75.646   7.779  1.00 35.10           N  
ATOM    995  CA  GLU A 194      28.007  74.736   6.694  1.00 35.81           C  
ATOM    996  C   GLU A 194      28.326  73.374   7.278  1.00 35.16           C  
ATOM    997  O   GLU A 194      27.899  72.372   6.742  1.00 34.28           O  
ATOM    998  CB  GLU A 194      29.187  75.229   5.884  1.00 38.92           C  
ATOM    999  CG  GLU A 194      29.839  74.140   5.076  1.00 40.05           C  
ATOM   1000  CD  GLU A 194      30.917  74.674   4.164  1.00 41.30           C  
ATOM   1001  OE1 GLU A 194      31.868  75.328   4.648  1.00 41.73           O  
ATOM   1002  OE2 GLU A 194      30.809  74.423   2.956  1.00 45.10           O  
ATOM   1003  N   TYR A 195      29.083  73.358   8.376  1.00 35.52           N  
ATOM   1004  CA  TYR A 195      29.462  72.124   9.073  1.00 35.82           C  
ATOM   1005  C   TYR A 195      28.259  71.468   9.741  1.00 36.42           C  
ATOM   1006  O   TYR A 195      28.053  70.251   9.671  1.00 36.90           O  
ATOM   1007  CB  TYR A 195      30.468  72.425  10.168  1.00 35.53           C  
ATOM   1008  CG  TYR A 195      30.782  71.248  11.067  1.00 35.04           C  
ATOM   1009  CD1 TYR A 195      31.700  70.270  10.667  1.00 36.57           C  
ATOM   1010  CD2 TYR A 195      30.198  71.123  12.332  1.00 34.57           C  
ATOM   1011  CE1 TYR A 195      32.044  69.190  11.507  1.00 33.63           C  
ATOM   1012  CE2 TYR A 195      30.533  70.041  13.184  1.00 35.40           C  
ATOM   1013  CZ  TYR A 195      31.463  69.084  12.753  1.00 34.92           C  
ATOM   1014  OH  TYR A 195      31.825  68.032  13.551  1.00 37.68           O  
ATOM   1015  N   LEU A 196      27.484  72.292  10.428  1.00 36.07           N  
ATOM   1016  CA  LEU A 196      26.301  71.814  11.123  1.00 34.06           C  
ATOM   1017  C   LEU A 196      25.347  71.212  10.119  1.00 35.35           C  
ATOM   1018  O   LEU A 196      24.904  70.069  10.258  1.00 36.18           O  
ATOM   1019  CB  LEU A 196      25.619  72.972  11.830  1.00 32.08           C  
ATOM   1020  CG  LEU A 196      24.502  72.589  12.782  1.00 31.47           C  
ATOM   1021  CD1 LEU A 196      25.054  71.611  13.802  1.00 32.62           C  
ATOM   1022  CD2 LEU A 196      23.944  73.841  13.450  1.00 27.28           C  
ATOM   1023  N   HIS A 197      25.043  71.987   9.087  1.00 34.37           N  
ATOM   1024  CA  HIS A 197      24.119  71.534   8.075  1.00 34.31           C  
ATOM   1025  C   HIS A 197      24.672  70.374   7.256  1.00 35.69           C  
ATOM   1026  O   HIS A 197      23.935  69.651   6.598  1.00 35.58           O  
ATOM   1027  CB  HIS A 197      23.768  72.706   7.177  1.00 36.16           C  
ATOM   1028  CG  HIS A 197      22.891  73.725   7.831  1.00 36.65           C  
ATOM   1029  ND1 HIS A 197      22.491  74.880   7.194  1.00 36.01           N  
ATOM   1030  CD2 HIS A 197      22.304  73.746   9.055  1.00 35.47           C  
ATOM   1031  CE1 HIS A 197      21.693  75.564   7.995  1.00 37.28           C  
ATOM   1032  NE2 HIS A 197      21.564  74.898   9.130  1.00 34.91           N  
ATOM   1033  N   GLY A 198      25.979  70.187   7.297  1.00 35.55           N  
ATOM   1034  CA  GLY A 198      26.554  69.112   6.526  1.00 34.38           C  
ATOM   1035  C   GLY A 198      26.238  67.827   7.218  1.00 35.21           C  
ATOM   1036  O   GLY A 198      26.172  66.792   6.583  1.00 38.52           O  
ATOM   1037  N   LYS A 199      26.047  67.895   8.530  1.00 35.23           N  
ATOM   1038  CA  LYS A 199      25.734  66.708   9.317  1.00 34.88           C  
ATOM   1039  C   LYS A 199      24.243  66.550   9.457  1.00 34.69           C  
ATOM   1040  O   LYS A 199      23.781  65.861  10.335  1.00 36.62           O  
ATOM   1041  CB  LYS A 199      26.356  66.800  10.719  1.00 34.87           C  
ATOM   1042  CG  LYS A 199      27.835  66.516  10.771  1.00 36.69           C  
ATOM   1043  CD  LYS A 199      28.393  66.734  12.172  1.00 39.35           C  
ATOM   1044  CE  LYS A 199      29.658  65.928  12.417  0.00 38.43           C  
ATOM   1045  NZ  LYS A 199      29.360  64.478  12.572  0.00 38.75           N  
ATOM   1046  N   GLY A 200      23.480  67.211   8.606  1.00 35.78           N  
ATOM   1047  CA  GLY A 200      22.044  67.098   8.696  1.00 33.97           C  
ATOM   1048  C   GLY A 200      21.473  67.567  10.023  1.00 36.29           C  
ATOM   1049  O   GLY A 200      20.515  66.982  10.526  1.00 40.95           O  
ATOM   1050  N   ILE A 201      22.027  68.616  10.607  1.00 34.89           N  
ATOM   1051  CA  ILE A 201      21.497  69.124  11.869  1.00 34.25           C  
ATOM   1052  C   ILE A 201      21.131  70.594  11.706  1.00 35.59           C  
ATOM   1053  O   ILE A 201      21.832  71.342  11.021  1.00 35.92           O  
ATOM   1054  CB  ILE A 201      22.559  69.020  13.016  1.00 35.79           C  
ATOM   1055  CG1 ILE A 201      22.950  67.553  13.267  1.00 34.08           C  
ATOM   1056  CG2 ILE A 201      22.025  69.665  14.289  1.00 33.82           C  
ATOM   1057  CD1 ILE A 201      24.148  67.375  14.196  1.00 32.84           C  
ATOM   1058  N   ILE A 202      20.027  71.018  12.304  1.00 35.38           N  
ATOM   1059  CA  ILE A 202      19.671  72.424  12.247  1.00 35.69           C  
ATOM   1060  C   ILE A 202      19.545  72.875  13.688  1.00 36.11           C  
ATOM   1061  O   ILE A 202      19.062  72.142  14.547  1.00 37.22           O  
ATOM   1062  CB  ILE A 202      18.360  72.683  11.492  1.00 38.38           C  
ATOM   1063  CG1 ILE A 202      17.200  71.978  12.171  1.00 40.75           C  
ATOM   1064  CG2 ILE A 202      18.479  72.194  10.071  1.00 39.18           C  
ATOM   1065  CD1 ILE A 202      15.944  72.039  11.358  1.00 42.91           C  
ATOM   1066  N   HIS A 203      20.009  74.083  13.946  1.00 36.23           N  
ATOM   1067  CA  HIS A 203      20.007  74.653  15.274  1.00 35.62           C  
ATOM   1068  C   HIS A 203      18.596  75.029  15.728  1.00 37.49           C  
ATOM   1069  O   HIS A 203      18.148  74.617  16.806  1.00 37.73           O  
ATOM   1070  CB  HIS A 203      20.930  75.864  15.272  1.00 33.80           C  
ATOM   1071  CG  HIS A 203      21.190  76.420  16.628  1.00 34.25           C  
ATOM   1072  ND1 HIS A 203      20.217  77.055  17.367  1.00 33.96           N  
ATOM   1073  CD2 HIS A 203      22.303  76.410  17.397  1.00 33.57           C  
ATOM   1074  CE1 HIS A 203      20.720  77.413  18.535  1.00 34.61           C  
ATOM   1075  NE2 HIS A 203      21.984  77.032  18.578  1.00 36.32           N  
ATOM   1076  N   ARG A 204      17.903  75.810  14.904  1.00 38.03           N  
ATOM   1077  CA  ARG A 204      16.533  76.240  15.179  1.00 37.62           C  
ATOM   1078  C   ARG A 204      16.345  77.322  16.213  1.00 38.72           C  
ATOM   1079  O   ARG A 204      15.228  77.572  16.648  1.00 39.35           O  
ATOM   1080  CB  ARG A 204      15.666  75.058  15.560  1.00 37.44           C  
ATOM   1081  CG  ARG A 204      15.458  74.133  14.405  1.00 40.07           C  
ATOM   1082  CD  ARG A 204      14.205  73.336  14.598  1.00 38.65           C  
ATOM   1083  NE  ARG A 204      14.249  72.532  15.811  1.00 39.08           N  
ATOM   1084  CZ  ARG A 204      13.196  71.891  16.300  1.00 39.73           C  
ATOM   1085  NH1 ARG A 204      12.026  71.969  15.671  1.00 37.07           N  
ATOM   1086  NH2 ARG A 204      13.318  71.173  17.409  1.00 40.54           N  
ATOM   1087  N   ASP A 205      17.434  77.952  16.624  1.00 37.88           N  
ATOM   1088  CA  ASP A 205      17.339  79.051  17.555  1.00 36.23           C  
ATOM   1089  C   ASP A 205      18.648  79.811  17.573  1.00 35.62           C  
ATOM   1090  O   ASP A 205      19.185  80.153  18.610  1.00 36.31           O  
ATOM   1091  CB  ASP A 205      16.971  78.569  18.937  1.00 36.60           C  
ATOM   1092  CG  ASP A 205      16.641  79.719  19.862  1.00 40.67           C  
ATOM   1093  OD1 ASP A 205      16.240  80.787  19.347  1.00 41.92           O  
ATOM   1094  OD2 ASP A 205      16.777  79.574  21.096  1.00 43.39           O  
ATOM   1095  N   LEU A 206      19.150  80.092  16.385  1.00 34.70           N  
ATOM   1096  CA  LEU A 206      20.398  80.796  16.236  1.00 33.71           C  
ATOM   1097  C   LEU A 206      20.180  82.275  16.545  1.00 34.68           C  
ATOM   1098  O   LEU A 206      19.180  82.854  16.105  1.00 36.18           O  
ATOM   1099  CB  LEU A 206      20.889  80.611  14.803  1.00 31.47           C  
ATOM   1100  CG  LEU A 206      22.287  81.122  14.472  1.00 33.28           C  
ATOM   1101  CD1 LEU A 206      23.300  80.209  15.132  1.00 32.26           C  
ATOM   1102  CD2 LEU A 206      22.498  81.167  12.957  1.00 29.11           C  
ATOM   1103  N   LYS A 207      21.099  82.868  17.312  1.00 34.19           N  
ATOM   1104  CA  LYS A 207      21.055  84.292  17.680  1.00 35.14           C  
ATOM   1105  C   LYS A 207      22.345  84.697  18.375  1.00 35.22           C  
ATOM   1106  O   LYS A 207      23.094  83.842  18.835  1.00 38.51           O  
ATOM   1107  CB  LYS A 207      19.856  84.598  18.578  1.00 35.41           C  
ATOM   1108  CG  LYS A 207      19.674  83.632  19.699  1.00 36.58           C  
ATOM   1109  CD  LYS A 207      18.415  83.916  20.473  1.00 33.99           C  
ATOM   1110  CE  LYS A 207      18.336  82.963  21.649  1.00 34.72           C  
ATOM   1111  NZ  LYS A 207      17.127  83.145  22.490  1.00 37.16           N  
ATOM   1112  N   PRO A 208      22.637  86.006  18.447  1.00 34.58           N  
ATOM   1113  CA  PRO A 208      23.864  86.471  19.094  1.00 33.29           C  
ATOM   1114  C   PRO A 208      24.040  86.013  20.542  1.00 33.90           C  
ATOM   1115  O   PRO A 208      25.163  85.964  21.028  1.00 36.05           O  
ATOM   1116  CB  PRO A 208      23.759  87.985  18.987  1.00 33.98           C  
ATOM   1117  CG  PRO A 208      22.909  88.215  17.796  1.00 31.99           C  
ATOM   1118  CD  PRO A 208      21.849  87.152  17.965  1.00 34.36           C  
ATOM   1119  N   GLU A 209      22.952  85.695  21.240  1.00 34.35           N  
ATOM   1120  CA  GLU A 209      23.058  85.234  22.629  1.00 37.39           C  
ATOM   1121  C   GLU A 209      23.599  83.806  22.674  1.00 38.77           C  
ATOM   1122  O   GLU A 209      24.196  83.393  23.660  1.00 39.11           O  
ATOM   1123  CB  GLU A 209      21.697  85.260  23.338  1.00 38.88           C  
ATOM   1124  CG  GLU A 209      21.061  86.646  23.452  1.00 47.68           C  
ATOM   1125  CD  GLU A 209      20.099  87.008  22.280  1.00 52.05           C  
ATOM   1126  OE1 GLU A 209      20.514  86.999  21.081  1.00 49.18           O  
ATOM   1127  OE2 GLU A 209      18.910  87.309  22.587  1.00 53.76           O  
ATOM   1128  N   ASN A 210      23.372  83.062  21.590  1.00 39.01           N  
ATOM   1129  CA  ASN A 210      23.795  81.674  21.441  1.00 36.13           C  
ATOM   1130  C   ASN A 210      25.121  81.528  20.732  1.00 36.53           C  
ATOM   1131  O   ASN A 210      25.549  80.400  20.452  1.00 37.20           O  
ATOM   1132  CB  ASN A 210      22.764  80.915  20.629  1.00 35.69           C  
ATOM   1133  CG  ASN A 210      21.647  80.441  21.453  1.00 37.71           C  
ATOM   1134  OD1 ASN A 210      21.724  80.445  22.668  1.00 40.03           O  
ATOM   1135  ND2 ASN A 210      20.569  80.033  20.803  1.00 39.59           N  
ATOM   1136  N   ILE A 211      25.752  82.650  20.407  1.00 34.30           N  
ATOM   1137  CA  ILE A 211      27.031  82.611  19.712  1.00 32.61           C  
ATOM   1138  C   ILE A 211      28.074  83.213  20.634  1.00 34.52           C  
ATOM   1139  O   ILE A 211      28.308  84.418  20.638  1.00 35.64           O  
ATOM   1140  CB  ILE A 211      26.962  83.407  18.420  1.00 30.42           C  
ATOM   1141  CG1 ILE A 211      25.818  82.871  17.549  1.00 29.62           C  
ATOM   1142  CG2 ILE A 211      28.288  83.361  17.716  1.00 28.76           C  
ATOM   1143  CD1 ILE A 211      25.590  83.646  16.255  1.00 26.75           C  
ATOM   1144  N   LEU A 212      28.689  82.352  21.429  1.00 33.88           N  
ATOM   1145  CA  LEU A 212      29.689  82.766  22.393  1.00 33.09           C  
ATOM   1146  C   LEU A 212      30.994  83.138  21.739  1.00 33.39           C  
ATOM   1147  O   LEU A 212      31.191  82.889  20.561  1.00 34.87           O  
ATOM   1148  CB  LEU A 212      29.921  81.633  23.391  1.00 30.74           C  
ATOM   1149  CG  LEU A 212      28.627  80.957  23.851  1.00 30.03           C  
ATOM   1150  CD1 LEU A 212      28.892  80.082  25.058  1.00 28.19           C  
ATOM   1151  CD2 LEU A 212      27.593  82.009  24.184  1.00 26.04           C  
ATOM   1152  N   LEU A 213      31.892  83.717  22.526  1.00 34.03           N  
ATOM   1153  CA  LEU A 213      33.214  84.121  22.058  1.00 34.41           C  
ATOM   1154  C   LEU A 213      34.256  83.544  23.020  1.00 35.77           C  
ATOM   1155  O   LEU A 213      34.209  83.798  24.224  1.00 37.43           O  
ATOM   1156  CB  LEU A 213      33.271  85.643  22.027  1.00 32.85           C  
ATOM   1157  CG  LEU A 213      32.416  86.175  20.874  1.00 34.20           C  
ATOM   1158  CD1 LEU A 213      31.915  87.555  21.135  1.00 35.59           C  
ATOM   1159  CD2 LEU A 213      33.248  86.142  19.592  1.00 36.04           C  
ATOM   1160  N   ASN A 214      35.188  82.745  22.526  1.00 36.94           N  
ATOM   1161  CA  ASN A 214      36.160  82.185  23.454  1.00 38.89           C  
ATOM   1162  C   ASN A 214      37.197  83.226  23.855  1.00 37.91           C  
ATOM   1163  O   ASN A 214      37.073  84.400  23.510  1.00 37.61           O  
ATOM   1164  CB  ASN A 214      36.827  80.937  22.870  1.00 40.95           C  
ATOM   1165  CG  ASN A 214      37.548  81.211  21.575  1.00 44.57           C  
ATOM   1166  OD1 ASN A 214      37.576  82.339  21.096  1.00 47.68           O  
ATOM   1167  ND2 ASN A 214      38.146  80.174  21.000  1.00 46.52           N  
ATOM   1168  N   GLU A 215      38.204  82.804  24.605  1.00 38.92           N  
ATOM   1169  CA  GLU A 215      39.247  83.725  25.039  1.00 40.39           C  
ATOM   1170  C   GLU A 215      40.029  84.250  23.850  1.00 41.55           C  
ATOM   1171  O   GLU A 215      40.684  85.279  23.941  1.00 41.78           O  
ATOM   1172  CB  GLU A 215      40.189  83.038  26.008  1.00 39.78           C  
ATOM   1173  N   ASP A 216      39.971  83.535  22.733  1.00 43.58           N  
ATOM   1174  CA  ASP A 216      40.687  83.962  21.540  1.00 45.77           C  
ATOM   1175  C   ASP A 216      39.832  84.841  20.658  1.00 45.13           C  
ATOM   1176  O   ASP A 216      40.264  85.274  19.599  1.00 46.61           O  
ATOM   1177  CB  ASP A 216      41.156  82.753  20.741  1.00 50.42           C  
ATOM   1178  CG  ASP A 216      42.528  82.268  21.183  1.00 55.85           C  
ATOM   1179  OD1 ASP A 216      43.231  83.030  21.888  1.00 56.16           O  
ATOM   1180  OD2 ASP A 216      42.905  81.136  20.811  1.00 59.26           O  
ATOM   1181  N   MET A 217      38.612  85.087  21.106  1.00 43.33           N  
ATOM   1182  CA  MET A 217      37.663  85.904  20.382  1.00 41.58           C  
ATOM   1183  C   MET A 217      37.081  85.243  19.158  1.00 40.30           C  
ATOM   1184  O   MET A 217      36.470  85.904  18.326  1.00 42.47           O  
ATOM   1185  CB  MET A 217      38.272  87.254  20.013  1.00 42.02           C  
ATOM   1186  CG  MET A 217      38.424  88.170  21.207  1.00 40.58           C  
ATOM   1187  SD  MET A 217      36.870  88.388  22.104  1.00 43.44           S  
ATOM   1188  CE  MET A 217      36.083  89.746  21.182  1.00 39.43           C  
ATOM   1189  N   HIS A 218      37.294  83.950  19.011  1.00 37.29           N  
ATOM   1190  CA  HIS A 218      36.657  83.262  17.909  1.00 36.33           C  
ATOM   1191  C   HIS A 218      35.301  82.864  18.493  1.00 36.52           C  
ATOM   1192  O   HIS A 218      35.129  82.838  19.710  1.00 37.03           O  
ATOM   1193  CB  HIS A 218      37.435  82.019  17.505  1.00 35.94           C  
ATOM   1194  CG  HIS A 218      38.669  82.309  16.707  1.00 35.93           C  
ATOM   1195  ND1 HIS A 218      38.629  82.621  15.365  1.00 34.16           N  
ATOM   1196  CD2 HIS A 218      39.975  82.335  17.061  1.00 32.70           C  
ATOM   1197  CE1 HIS A 218      39.861  82.821  14.929  1.00 34.08           C  
ATOM   1198  NE2 HIS A 218      40.693  82.654  15.939  1.00 30.38           N  
ATOM   1199  N   ILE A 219      34.338  82.567  17.630  1.00 36.83           N  
ATOM   1200  CA  ILE A 219      32.999  82.191  18.068  1.00 34.55           C  
ATOM   1201  C   ILE A 219      32.887  80.743  18.514  1.00 35.88           C  
ATOM   1202  O   ILE A 219      33.671  79.885  18.114  1.00 38.12           O  
ATOM   1203  CB  ILE A 219      31.971  82.392  16.951  1.00 30.15           C  
ATOM   1204  CG1 ILE A 219      32.108  81.266  15.927  1.00 28.37           C  
ATOM   1205  CG2 ILE A 219      32.173  83.753  16.303  1.00 27.98           C  
ATOM   1206  CD1 ILE A 219      31.175  81.374  14.704  1.00 25.71           C  
ATOM   1207  N   GLN A 220      31.898  80.482  19.351  1.00 34.95           N  
ATOM   1208  CA  GLN A 220      31.629  79.140  19.805  1.00 34.29           C  
ATOM   1209  C   GLN A 220      30.125  79.076  20.002  1.00 33.78           C  
ATOM   1210  O   GLN A 220      29.585  79.628  20.958  1.00 34.60           O  
ATOM   1211  CB  GLN A 220      32.372  78.832  21.104  1.00 36.36           C  
ATOM   1212  CG  GLN A 220      33.847  78.420  20.918  1.00 36.67           C  
ATOM   1213  CD  GLN A 220      34.440  77.761  22.173  1.00 37.55           C  
ATOM   1214  OE1 GLN A 220      34.641  78.407  23.193  1.00 40.69           O  
ATOM   1215  NE2 GLN A 220      34.711  76.464  22.095  1.00 41.13           N  
ATOM   1216  N   ILE A 221      29.440  78.420  19.078  1.00 32.72           N  
ATOM   1217  CA  ILE A 221      28.003  78.320  19.172  1.00 32.56           C  
ATOM   1218  C   ILE A 221      27.522  77.257  20.163  1.00 33.72           C  
ATOM   1219  O   ILE A 221      28.108  76.165  20.263  1.00 32.07           O  
ATOM   1220  CB  ILE A 221      27.401  78.054  17.797  1.00 30.81           C  
ATOM   1221  CG1 ILE A 221      27.884  79.146  16.832  1.00 31.67           C  
ATOM   1222  CG2 ILE A 221      25.878  78.028  17.900  1.00 31.09           C  
ATOM   1223  CD1 ILE A 221      27.323  79.080  15.400  1.00 30.82           C  
ATOM   1224  N   THR A 222      26.453  77.596  20.896  1.00 33.05           N  
ATOM   1225  CA  THR A 222      25.865  76.693  21.877  1.00 31.62           C  
ATOM   1226  C   THR A 222      24.332  76.654  21.830  1.00 33.56           C  
ATOM   1227  O   THR A 222      23.717  77.105  20.853  1.00 33.20           O  
ATOM   1228  CB  THR A 222      26.302  77.068  23.288  1.00 31.57           C  
ATOM   1229  OG1 THR A 222      25.788  76.099  24.203  1.00 31.30           O  
ATOM   1230  CG2 THR A 222      25.804  78.463  23.669  1.00 29.58           C  
ATOM   1231  N   ASP A 223      23.733  76.093  22.883  1.00 34.18           N  
ATOM   1232  CA  ASP A 223      22.285  75.950  23.033  1.00 35.09           C  
ATOM   1233  C   ASP A 223      21.693  75.058  21.956  1.00 35.24           C  
ATOM   1234  O   ASP A 223      20.988  75.535  21.065  1.00 35.16           O  
ATOM   1235  CB  ASP A 223      21.613  77.320  22.997  1.00 39.41           C  
ATOM   1236  CG  ASP A 223      20.135  77.253  23.353  1.00 44.99           C  
ATOM   1237  OD1 ASP A 223      19.746  76.342  24.131  1.00 47.81           O  
ATOM   1238  OD2 ASP A 223      19.363  78.118  22.875  1.00 47.69           O  
ATOM   1239  N   PHE A 224      21.963  73.759  22.065  1.00 34.34           N  
ATOM   1240  CA  PHE A 224      21.513  72.767  21.093  1.00 34.23           C  
ATOM   1241  C   PHE A 224      20.318  71.956  21.516  1.00 37.01           C  
ATOM   1242  O   PHE A 224      19.894  71.056  20.781  1.00 38.19           O  
ATOM   1243  CB  PHE A 224      22.661  71.814  20.749  1.00 30.85           C  
ATOM   1244  CG  PHE A 224      23.736  72.452  19.917  1.00 28.45           C  
ATOM   1245  CD1 PHE A 224      23.555  72.638  18.552  1.00 30.25           C  
ATOM   1246  CD2 PHE A 224      24.868  72.980  20.507  1.00 26.56           C  
ATOM   1247  CE1 PHE A 224      24.492  73.365  17.797  1.00 29.27           C  
ATOM   1248  CE2 PHE A 224      25.808  73.709  19.752  1.00 27.66           C  
ATOM   1249  CZ  PHE A 224      25.615  73.901  18.411  1.00 26.10           C  
ATOM   1250  N   GLY A 225      19.781  72.269  22.694  1.00 38.32           N  
ATOM   1251  CA  GLY A 225      18.619  71.566  23.205  1.00 40.04           C  
ATOM   1252  C   GLY A 225      17.437  71.657  22.260  1.00 42.21           C  
ATOM   1253  O   GLY A 225      16.641  70.718  22.144  1.00 44.89           O  
ATOM   1254  N   THR A 226      17.308  72.780  21.571  1.00 41.13           N  
ATOM   1255  CA  THR A 226      16.215  72.928  20.626  1.00 42.35           C  
ATOM   1256  C   THR A 226      16.571  72.494  19.186  1.00 42.14           C  
ATOM   1257  O   THR A 226      15.754  72.595  18.271  1.00 40.22           O  
ATOM   1258  CB  THR A 226      15.697  74.378  20.651  1.00 43.10           C  
ATOM   1259  OG1 THR A 226      16.799  75.295  20.697  1.00 44.30           O  
ATOM   1260  CG2 THR A 226      14.834  74.589  21.879  1.00 42.43           C  
ATOM   1261  N   ALA A 227      17.789  71.993  19.003  1.00 42.94           N  
ATOM   1262  CA  ALA A 227      18.268  71.539  17.697  1.00 45.37           C  
ATOM   1263  C   ALA A 227      17.418  70.402  17.112  1.00 47.87           C  
ATOM   1264  O   ALA A 227      16.539  69.861  17.785  1.00 50.08           O  
ATOM   1265  CB  ALA A 227      19.699  71.099  17.810  1.00 44.77           C  
ATOM   1266  N   LYS A 228      17.671  70.039  15.860  1.00 48.52           N  
ATOM   1267  CA  LYS A 228      16.898  68.977  15.224  1.00 49.84           C  
ATOM   1268  C   LYS A 228      17.742  68.247  14.209  1.00 50.68           C  
ATOM   1269  O   LYS A 228      18.434  68.872  13.408  1.00 50.13           O  
ATOM   1270  CB  LYS A 228      15.654  69.551  14.540  1.00 50.05           C  
ATOM   1271  N   VAL A 229      17.691  66.922  14.258  1.00 51.72           N  
ATOM   1272  CA  VAL A 229      18.444  66.107  13.327  1.00 53.62           C  
ATOM   1273  C   VAL A 229      17.478  65.605  12.287  1.00 54.98           C  
ATOM   1274  O   VAL A 229      16.458  65.012  12.618  1.00 53.66           O  
ATOM   1275  CB  VAL A 229      19.091  64.923  14.015  1.00 53.35           C  
ATOM   1276  CG1 VAL A 229      19.964  64.155  13.011  1.00 54.41           C  
ATOM   1277  CG2 VAL A 229      19.919  65.418  15.185  1.00 53.46           C  
ATOM   1278  N   LEU A 230      17.824  65.846  11.029  1.00 56.98           N  
ATOM   1279  CA  LEU A 230      16.985  65.475   9.904  1.00 60.44           C  
ATOM   1280  C   LEU A 230      16.941  64.011   9.513  1.00 63.47           C  
ATOM   1281  O   LEU A 230      17.894  63.263   9.739  1.00 62.41           O  
ATOM   1282  CB  LEU A 230      17.396  66.280   8.682  1.00 58.42           C  
ATOM   1283  CG  LEU A 230      17.355  67.786   8.885  1.00 57.27           C  
ATOM   1284  CD1 LEU A 230      17.953  68.451   7.677  1.00 56.98           C  
ATOM   1285  CD2 LEU A 230      15.935  68.246   9.099  1.00 54.53           C  
ATOM   1286  N   SER A 231      15.817  63.642   8.889  1.00 67.99           N  
ATOM   1287  CA  SER A 231      15.552  62.290   8.388  1.00 71.26           C  
ATOM   1288  C   SER A 231      14.839  62.391   7.028  1.00 72.69           C  
ATOM   1289  O   SER A 231      13.735  61.862   6.833  1.00 75.70           O  
ATOM   1290  CB  SER A 231      14.697  61.508   9.404  1.00 71.48           C  
ATOM   1291  OG  SER A 231      13.753  62.350  10.052  1.00 71.58           O  
ATOM   1292  N   ASN A 240       8.961  69.932  13.998  1.00 84.17           N  
ATOM   1293  CA  ASN A 240       8.007  71.033  13.930  1.00 84.36           C  
ATOM   1294  C   ASN A 240       7.262  71.212  15.254  1.00 83.31           C  
ATOM   1295  O   ASN A 240       6.035  71.316  15.277  1.00 83.28           O  
ATOM   1296  CB  ASN A 240       7.001  70.772  12.806  1.00 86.80           C  
ATOM   1297  CG  ASN A 240       6.296  69.428  12.947  1.00 88.44           C  
ATOM   1298  OD1 ASN A 240       5.731  69.108  14.003  1.00 89.16           O  
ATOM   1299  ND2 ASN A 240       6.322  68.636  11.876  1.00 88.41           N  
HETATM 1300  N   SEP A 241       8.011  71.264  16.352  1.00 81.71           N  
HETATM 1301  CA  SEP A 241       7.421  71.408  17.681  1.00 79.86           C  
HETATM 1302  CB  SEP A 241       7.668  70.137  18.507  1.00 83.25           C  
HETATM 1303  OG  SEP A 241       9.276  70.199  18.661  1.00 84.78           O  
HETATM 1304  C   SEP A 241       7.983  72.584  18.454  1.00 77.23           C  
HETATM 1305  O   SEP A 241       7.606  72.800  19.607  1.00 77.58           O  
HETATM 1306  P   SEP A 241      10.135  69.186  17.972  1.00 86.05           P  
HETATM 1307  O1P SEP A 241      11.522  69.267  18.506  1.00 84.85           O  
HETATM 1308  O2P SEP A 241       9.587  67.824  18.215  1.00 85.75           O  
HETATM 1309  O3P SEP A 241      10.151  69.456  16.508  1.00 85.47           O  
ATOM   1310  N   PHE A 242       8.874  73.341  17.825  1.00 73.06           N  
ATOM   1311  CA  PHE A 242       9.522  74.457  18.502  1.00 69.50           C  
ATOM   1312  C   PHE A 242       9.640  75.733  17.678  1.00 68.43           C  
ATOM   1313  O   PHE A 242       9.580  75.715  16.453  1.00 67.73           O  
ATOM   1314  CB  PHE A 242      10.928  74.016  18.947  1.00 66.93           C  
ATOM   1315  CG  PHE A 242      11.815  75.147  19.416  1.00 64.20           C  
ATOM   1316  CD1 PHE A 242      11.626  75.737  20.656  1.00 63.54           C  
ATOM   1317  CD2 PHE A 242      12.827  75.634  18.603  1.00 62.45           C  
ATOM   1318  CE1 PHE A 242      12.433  76.798  21.077  1.00 62.58           C  
ATOM   1319  CE2 PHE A 242      13.632  76.690  19.016  1.00 62.26           C  
ATOM   1320  CZ  PHE A 242      13.436  77.273  20.253  1.00 61.71           C  
ATOM   1321  N   VAL A 243       9.817  76.845  18.379  1.00 67.06           N  
ATOM   1322  CA  VAL A 243      10.005  78.139  17.745  1.00 64.84           C  
ATOM   1323  C   VAL A 243      11.029  78.940  18.562  1.00 62.98           C  
ATOM   1324  O   VAL A 243      10.818  79.247  19.744  1.00 64.18           O  
ATOM   1325  CB  VAL A 243       8.671  78.922  17.639  1.00 64.63           C  
ATOM   1326  CG1 VAL A 243       8.904  80.279  16.999  1.00 63.71           C  
ATOM   1327  CG2 VAL A 243       7.684  78.132  16.806  1.00 64.62           C  
ATOM   1328  N   GLY A 244      12.147  79.268  17.929  1.00 59.50           N  
ATOM   1329  CA  GLY A 244      13.172  80.026  18.618  1.00 54.17           C  
ATOM   1330  C   GLY A 244      12.699  81.412  18.965  1.00 49.48           C  
ATOM   1331  O   GLY A 244      11.504  81.672  18.994  1.00 50.50           O  
ATOM   1332  N   THR A 245      13.646  82.302  19.217  1.00 45.14           N  
ATOM   1333  CA  THR A 245      13.353  83.673  19.582  1.00 41.45           C  
ATOM   1334  C   THR A 245      12.630  84.426  18.466  1.00 41.16           C  
ATOM   1335  O   THR A 245      13.055  84.435  17.315  1.00 39.95           O  
ATOM   1336  CB  THR A 245      14.665  84.359  19.992  1.00 41.65           C  
ATOM   1337  OG1 THR A 245      15.172  83.684  21.149  1.00 42.04           O  
ATOM   1338  CG2 THR A 245      14.475  85.820  20.314  1.00 37.67           C  
ATOM   1339  N   ALA A 246      11.523  85.060  18.831  1.00 40.50           N  
ATOM   1340  CA  ALA A 246      10.685  85.786  17.887  1.00 40.02           C  
ATOM   1341  C   ALA A 246      11.369  86.623  16.814  1.00 40.12           C  
ATOM   1342  O   ALA A 246      11.011  86.510  15.650  1.00 39.88           O  
ATOM   1343  CB  ALA A 246       9.686  86.652  18.644  1.00 38.23           C  
ATOM   1344  N   GLN A 247      12.336  87.462  17.172  1.00 39.52           N  
ATOM   1345  CA  GLN A 247      12.958  88.314  16.150  1.00 40.53           C  
ATOM   1346  C   GLN A 247      13.805  87.591  15.113  1.00 38.94           C  
ATOM   1347  O   GLN A 247      14.295  88.211  14.170  1.00 39.29           O  
ATOM   1348  CB  GLN A 247      13.815  89.416  16.797  1.00 42.38           C  
ATOM   1349  CG  GLN A 247      13.101  90.255  17.823  1.00 46.25           C  
ATOM   1350  CD  GLN A 247      14.001  91.282  18.454  1.00 49.76           C  
ATOM   1351  OE1 GLN A 247      13.653  92.449  18.534  1.00 54.35           O  
ATOM   1352  NE2 GLN A 247      15.170  90.857  18.903  1.00 53.08           N  
ATOM   1353  N   TYR A 248      13.971  86.285  15.266  1.00 37.23           N  
ATOM   1354  CA  TYR A 248      14.797  85.535  14.324  1.00 36.10           C  
ATOM   1355  C   TYR A 248      14.001  84.444  13.619  1.00 35.50           C  
ATOM   1356  O   TYR A 248      14.519  83.753  12.744  1.00 36.44           O  
ATOM   1357  CB  TYR A 248      16.018  84.940  15.072  1.00 33.93           C  
ATOM   1358  CG  TYR A 248      16.879  86.000  15.755  1.00 32.00           C  
ATOM   1359  CD1 TYR A 248      17.757  86.781  15.020  1.00 34.47           C  
ATOM   1360  CD2 TYR A 248      16.724  86.298  17.121  1.00 34.46           C  
ATOM   1361  CE1 TYR A 248      18.457  87.845  15.609  1.00 34.46           C  
ATOM   1362  CE2 TYR A 248      17.413  87.351  17.727  1.00 30.40           C  
ATOM   1363  CZ  TYR A 248      18.273  88.128  16.958  1.00 34.55           C  
ATOM   1364  OH  TYR A 248      18.894  89.240  17.488  1.00 33.87           O  
ATOM   1365  N   VAL A 249      12.741  84.298  14.008  1.00 34.23           N  
ATOM   1366  CA  VAL A 249      11.854  83.290  13.441  1.00 35.54           C  
ATOM   1367  C   VAL A 249      11.620  83.504  11.948  1.00 36.64           C  
ATOM   1368  O   VAL A 249      11.300  84.617  11.531  1.00 37.16           O  
ATOM   1369  CB  VAL A 249      10.494  83.303  14.161  1.00 35.43           C  
ATOM   1370  CG1 VAL A 249       9.456  82.571  13.336  1.00 39.05           C  
ATOM   1371  CG2 VAL A 249      10.627  82.643  15.501  1.00 39.15           C  
ATOM   1372  N   SER A 250      11.763  82.447  11.144  1.00 37.31           N  
ATOM   1373  CA  SER A 250      11.562  82.580   9.707  1.00 37.78           C  
ATOM   1374  C   SER A 250      10.085  82.594   9.425  1.00 37.93           C  
ATOM   1375  O   SER A 250       9.280  82.178  10.244  1.00 39.98           O  
ATOM   1376  CB  SER A 250      12.216  81.438   8.938  1.00 38.18           C  
ATOM   1377  OG  SER A 250      11.646  80.198   9.281  1.00 39.50           O  
ATOM   1378  N   PRO A 251       9.702  83.095   8.265  1.00 37.44           N  
ATOM   1379  CA  PRO A 251       8.277  83.113   7.987  1.00 39.11           C  
ATOM   1380  C   PRO A 251       7.655  81.750   7.755  1.00 40.72           C  
ATOM   1381  O   PRO A 251       6.497  81.561   8.080  1.00 43.90           O  
ATOM   1382  CB  PRO A 251       8.168  84.045   6.781  1.00 37.62           C  
ATOM   1383  CG  PRO A 251       9.496  84.000   6.156  1.00 37.87           C  
ATOM   1384  CD  PRO A 251      10.442  83.932   7.312  1.00 39.47           C  
ATOM   1385  N   GLU A 252       8.406  80.790   7.214  1.00 41.73           N  
ATOM   1386  CA  GLU A 252       7.846  79.453   6.968  1.00 40.65           C  
ATOM   1387  C   GLU A 252       7.503  78.791   8.277  1.00 42.09           C  
ATOM   1388  O   GLU A 252       6.662  77.898   8.347  1.00 43.09           O  
ATOM   1389  CB  GLU A 252       8.829  78.562   6.210  1.00 38.97           C  
ATOM   1390  CG  GLU A 252      10.155  78.360   6.888  1.00 39.39           C  
ATOM   1391  CD  GLU A 252      11.172  79.411   6.502  1.00 39.50           C  
ATOM   1392  OE1 GLU A 252      10.787  80.435   5.908  1.00 41.45           O  
ATOM   1393  OE2 GLU A 252      12.362  79.217   6.796  1.00 38.92           O  
ATOM   1394  N   LEU A 253       8.171  79.238   9.325  1.00 43.00           N  
ATOM   1395  CA  LEU A 253       7.945  78.699  10.640  1.00 44.89           C  
ATOM   1396  C   LEU A 253       6.594  79.209  11.158  1.00 47.20           C  
ATOM   1397  O   LEU A 253       5.917  78.544  11.950  1.00 47.75           O  
ATOM   1398  CB  LEU A 253       9.078  79.144  11.546  1.00 45.84           C  
ATOM   1399  CG  LEU A 253       9.583  78.088  12.518  1.00 48.51           C  
ATOM   1400  CD1 LEU A 253       9.834  76.792  11.763  1.00 48.32           C  
ATOM   1401  CD2 LEU A 253      10.860  78.587  13.184  1.00 48.61           C  
ATOM   1402  N   LEU A 254       6.200  80.389  10.689  1.00 47.56           N  
ATOM   1403  CA  LEU A 254       4.940  80.988  11.103  1.00 48.42           C  
ATOM   1404  C   LEU A 254       3.765  80.622  10.182  1.00 50.11           C  
ATOM   1405  O   LEU A 254       2.659  81.082  10.398  1.00 50.67           O  
ATOM   1406  CB  LEU A 254       5.079  82.513  11.162  1.00 45.74           C  
ATOM   1407  CG  LEU A 254       6.184  83.152  12.012  1.00 45.46           C  
ATOM   1408  CD1 LEU A 254       6.175  84.650  11.780  1.00 46.42           C  
ATOM   1409  CD2 LEU A 254       5.988  82.857  13.478  1.00 44.07           C  
ATOM   1410  N   THR A 255       3.990  79.795   9.167  1.00 52.04           N  
ATOM   1411  CA  THR A 255       2.903  79.435   8.267  1.00 54.81           C  
ATOM   1412  C   THR A 255       2.713  77.923   8.083  1.00 57.63           C  
ATOM   1413  O   THR A 255       1.586  77.445   7.975  1.00 57.32           O  
ATOM   1414  CB  THR A 255       3.116  80.069   6.878  1.00 54.06           C  
ATOM   1415  OG1 THR A 255       4.180  79.391   6.219  1.00 56.89           O  
ATOM   1416  CG2 THR A 255       3.509  81.534   6.998  1.00 53.23           C  
ATOM   1417  N   GLU A 256       3.812  77.172   8.048  1.00 61.94           N  
ATOM   1418  CA  GLU A 256       3.753  75.719   7.851  1.00 64.81           C  
ATOM   1419  C   GLU A 256       4.016  74.919   9.118  1.00 67.06           C  
ATOM   1420  O   GLU A 256       3.712  73.724   9.166  1.00 68.41           O  
ATOM   1421  CB  GLU A 256       4.771  75.271   6.788  1.00 64.86           C  
ATOM   1422  CG  GLU A 256       4.582  75.889   5.403  1.00 65.76           C  
ATOM   1423  CD  GLU A 256       5.589  75.376   4.395  0.00 65.71           C  
ATOM   1424  OE1 GLU A 256       5.624  74.149   4.160  0.00 65.86           O  
ATOM   1425  OE2 GLU A 256       6.346  76.198   3.838  0.00 65.86           O  
ATOM   1426  N   LYS A 257       4.577  75.563  10.138  1.00 68.98           N  
ATOM   1427  CA  LYS A 257       4.897  74.862  11.383  1.00 71.52           C  
ATOM   1428  C   LYS A 257       5.898  73.742  11.071  1.00 72.72           C  
ATOM   1429  O   LYS A 257       5.567  72.560  11.175  1.00 74.99           O  
ATOM   1430  CB  LYS A 257       3.620  74.264  12.008  1.00 70.70           C  
ATOM   1431  N   SER A 258       7.112  74.116  10.672  1.00 72.90           N  
ATOM   1432  CA  SER A 258       8.164  73.149  10.334  1.00 72.32           C  
ATOM   1433  C   SER A 258       9.445  73.855   9.901  1.00 71.56           C  
ATOM   1434  O   SER A 258       9.438  74.631   8.941  1.00 71.42           O  
ATOM   1435  CB  SER A 258       7.706  72.215   9.208  1.00 72.20           C  
ATOM   1436  OG  SER A 258       6.902  71.162   9.709  0.00 72.35           O  
ATOM   1437  N   ALA A 259      10.546  73.583  10.602  1.00 70.33           N  
ATOM   1438  CA  ALA A 259      11.825  74.217  10.262  1.00 68.58           C  
ATOM   1439  C   ALA A 259      12.795  73.305   9.491  1.00 66.43           C  
ATOM   1440  O   ALA A 259      12.776  72.076   9.611  1.00 65.35           O  
ATOM   1441  CB  ALA A 259      12.509  74.765  11.535  1.00 68.38           C  
ATOM   1442  N   CYS A 260      13.636  73.938   8.686  1.00 63.29           N  
ATOM   1443  CA  CYS A 260      14.628  73.246   7.889  1.00 60.70           C  
ATOM   1444  C   CYS A 260      15.867  74.119   7.876  1.00 56.42           C  
ATOM   1445  O   CYS A 260      15.913  75.133   8.560  1.00 55.83           O  
ATOM   1446  CB  CYS A 260      14.103  73.025   6.468  1.00 64.09           C  
ATOM   1447  SG  CYS A 260      12.916  74.269   5.899  1.00 74.74           S  
ATOM   1448  N   LYS A 261      16.872  73.732   7.105  1.00 53.19           N  
ATOM   1449  CA  LYS A 261      18.107  74.494   7.043  1.00 50.22           C  
ATOM   1450  C   LYS A 261      17.822  75.948   6.788  1.00 48.98           C  
ATOM   1451  O   LYS A 261      18.468  76.822   7.349  1.00 49.97           O  
ATOM   1452  CB  LYS A 261      19.016  73.930   5.964  1.00 48.18           C  
ATOM   1453  CG  LYS A 261      19.450  72.530   6.305  1.00 51.58           C  
ATOM   1454  CD  LYS A 261      20.349  71.895   5.262  1.00 53.08           C  
ATOM   1455  CE  LYS A 261      20.708  70.471   5.689  1.00 53.30           C  
ATOM   1456  NZ  LYS A 261      21.594  69.762   4.706  1.00 56.88           N  
ATOM   1457  N   SER A 262      16.818  76.189   5.962  1.00 48.10           N  
ATOM   1458  CA  SER A 262      16.406  77.524   5.579  1.00 47.36           C  
ATOM   1459  C   SER A 262      16.197  78.444   6.765  1.00 44.24           C  
ATOM   1460  O   SER A 262      16.585  79.609   6.738  1.00 43.76           O  
ATOM   1461  CB  SER A 262      15.108  77.439   4.776  1.00 51.62           C  
ATOM   1462  OG  SER A 262      14.916  78.617   4.002  1.00 58.23           O  
ATOM   1463  N   SER A 263      15.579  77.921   7.809  1.00 41.52           N  
ATOM   1464  CA  SER A 263      15.310  78.721   8.984  1.00 39.61           C  
ATOM   1465  C   SER A 263      16.582  79.247   9.616  1.00 37.88           C  
ATOM   1466  O   SER A 263      16.589  80.359  10.139  1.00 37.87           O  
ATOM   1467  CB  SER A 263      14.494  77.914   9.976  1.00 41.28           C  
ATOM   1468  OG  SER A 263      13.252  77.581   9.385  1.00 43.96           O  
ATOM   1469  N   ASP A 264      17.660  78.470   9.570  1.00 35.01           N  
ATOM   1470  CA  ASP A 264      18.926  78.961  10.114  1.00 34.76           C  
ATOM   1471  C   ASP A 264      19.529  80.053   9.190  1.00 34.88           C  
ATOM   1472  O   ASP A 264      20.140  81.023   9.663  1.00 34.36           O  
ATOM   1473  CB  ASP A 264      19.935  77.819  10.298  1.00 32.96           C  
ATOM   1474  CG  ASP A 264      19.551  76.869  11.415  1.00 32.53           C  
ATOM   1475  OD1 ASP A 264      18.758  77.256  12.301  1.00 33.65           O  
ATOM   1476  OD2 ASP A 264      20.052  75.734  11.420  1.00 30.34           O  
ATOM   1477  N   LEU A 265      19.353  79.901   7.877  1.00 32.78           N  
ATOM   1478  CA  LEU A 265      19.873  80.890   6.933  1.00 32.53           C  
ATOM   1479  C   LEU A 265      19.108  82.183   7.106  1.00 32.74           C  
ATOM   1480  O   LEU A 265      19.658  83.252   6.952  1.00 34.10           O  
ATOM   1481  CB  LEU A 265      19.747  80.386   5.493  1.00 30.61           C  
ATOM   1482  CG  LEU A 265      20.521  79.086   5.258  1.00 28.48           C  
ATOM   1483  CD1 LEU A 265      20.164  78.457   3.940  1.00 26.67           C  
ATOM   1484  CD2 LEU A 265      22.011  79.413   5.329  1.00 27.42           C  
ATOM   1485  N   TRP A 266      17.828  82.089   7.434  1.00 33.36           N  
ATOM   1486  CA  TRP A 266      17.043  83.292   7.657  1.00 32.63           C  
ATOM   1487  C   TRP A 266      17.618  84.008   8.873  1.00 32.73           C  
ATOM   1488  O   TRP A 266      17.893  85.209   8.833  1.00 33.90           O  
ATOM   1489  CB  TRP A 266      15.589  82.913   7.900  1.00 32.64           C  
ATOM   1490  CG  TRP A 266      14.723  84.049   8.310  1.00 32.45           C  
ATOM   1491  CD1 TRP A 266      14.570  84.553   9.568  1.00 31.99           C  
ATOM   1492  CD2 TRP A 266      13.945  84.879   7.447  1.00 32.17           C  
ATOM   1493  NE1 TRP A 266      13.746  85.660   9.541  1.00 33.04           N  
ATOM   1494  CE2 TRP A 266      13.350  85.882   8.249  1.00 32.22           C  
ATOM   1495  CE3 TRP A 266      13.701  84.882   6.070  1.00 32.94           C  
ATOM   1496  CZ2 TRP A 266      12.528  86.876   7.722  1.00 32.43           C  
ATOM   1497  CZ3 TRP A 266      12.883  85.879   5.541  1.00 35.90           C  
ATOM   1498  CH2 TRP A 266      12.306  86.865   6.372  1.00 33.61           C  
ATOM   1499  N   ALA A 267      17.825  83.257   9.950  1.00 30.90           N  
ATOM   1500  CA  ALA A 267      18.373  83.815  11.180  1.00 28.94           C  
ATOM   1501  C   ALA A 267      19.710  84.486  10.902  1.00 29.99           C  
ATOM   1502  O   ALA A 267      20.000  85.559  11.432  1.00 32.99           O  
ATOM   1503  CB  ALA A 267      18.547  82.732  12.198  1.00 26.96           C  
ATOM   1504  N   LEU A 268      20.533  83.841  10.087  1.00 29.19           N  
ATOM   1505  CA  LEU A 268      21.830  84.393   9.698  1.00 28.63           C  
ATOM   1506  C   LEU A 268      21.612  85.748   9.057  1.00 28.45           C  
ATOM   1507  O   LEU A 268      22.207  86.728   9.457  1.00 30.58           O  
ATOM   1508  CB  LEU A 268      22.514  83.465   8.693  1.00 27.77           C  
ATOM   1509  CG  LEU A 268      23.770  83.916   7.944  1.00 27.90           C  
ATOM   1510  CD1 LEU A 268      24.870  84.298   8.909  1.00 23.51           C  
ATOM   1511  CD2 LEU A 268      24.225  82.773   7.022  1.00 22.95           C  
ATOM   1512  N   GLY A 269      20.757  85.807   8.051  1.00 28.88           N  
ATOM   1513  CA  GLY A 269      20.484  87.086   7.441  1.00 28.83           C  
ATOM   1514  C   GLY A 269      20.175  88.112   8.518  1.00 30.04           C  
ATOM   1515  O   GLY A 269      20.725  89.217   8.506  1.00 30.88           O  
ATOM   1516  N   CYS A 270      19.303  87.755   9.461  1.00 30.50           N  
ATOM   1517  CA  CYS A 270      18.940  88.674  10.547  1.00 30.37           C  
ATOM   1518  C   CYS A 270      20.136  89.145  11.353  1.00 31.07           C  
ATOM   1519  O   CYS A 270      20.240  90.321  11.700  1.00 32.50           O  
ATOM   1520  CB  CYS A 270      17.950  88.011  11.511  1.00 31.21           C  
ATOM   1521  SG  CYS A 270      16.288  87.808  10.874  1.00 34.44           S  
ATOM   1522  N   ILE A 271      21.029  88.209  11.653  1.00 30.30           N  
ATOM   1523  CA  ILE A 271      22.216  88.477  12.444  1.00 29.50           C  
ATOM   1524  C   ILE A 271      23.209  89.350  11.715  1.00 30.08           C  
ATOM   1525  O   ILE A 271      23.802  90.240  12.312  1.00 31.65           O  
ATOM   1526  CB  ILE A 271      22.907  87.167  12.853  1.00 30.54           C  
ATOM   1527  CG1 ILE A 271      21.988  86.370  13.793  1.00 30.11           C  
ATOM   1528  CG2 ILE A 271      24.268  87.469  13.469  1.00 30.32           C  
ATOM   1529  CD1 ILE A 271      22.463  84.988  14.098  1.00 27.16           C  
ATOM   1530  N   ILE A 272      23.407  89.108  10.430  1.00 29.62           N  
ATOM   1531  CA  ILE A 272      24.334  89.938   9.671  1.00 31.03           C  
ATOM   1532  C   ILE A 272      23.816  91.374   9.678  1.00 32.85           C  
ATOM   1533  O   ILE A 272      24.588  92.329   9.742  1.00 34.08           O  
ATOM   1534  CB  ILE A 272      24.411  89.510   8.229  1.00 30.04           C  
ATOM   1535  CG1 ILE A 272      25.038  88.128   8.132  1.00 29.81           C  
ATOM   1536  CG2 ILE A 272      25.182  90.539   7.443  1.00 29.99           C  
ATOM   1537  CD1 ILE A 272      24.932  87.516   6.732  1.00 31.27           C  
ATOM   1538  N   TYR A 273      22.497  91.511   9.615  1.00 32.38           N  
ATOM   1539  CA  TYR A 273      21.872  92.818   9.602  1.00 32.37           C  
ATOM   1540  C   TYR A 273      22.077  93.467  10.937  1.00 33.35           C  
ATOM   1541  O   TYR A 273      22.319  94.658  11.034  1.00 33.63           O  
ATOM   1542  CB  TYR A 273      20.381  92.680   9.320  1.00 31.63           C  
ATOM   1543  CG  TYR A 273      19.631  93.976   9.405  1.00 32.17           C  
ATOM   1544  CD1 TYR A 273      19.382  94.580  10.636  1.00 33.32           C  
ATOM   1545  CD2 TYR A 273      19.175  94.621   8.243  1.00 33.23           C  
ATOM   1546  CE1 TYR A 273      18.699  95.791  10.713  1.00 31.57           C  
ATOM   1547  CE2 TYR A 273      18.495  95.824   8.311  1.00 28.52           C  
ATOM   1548  CZ  TYR A 273      18.257  96.395   9.547  1.00 29.87           C  
ATOM   1549  OH  TYR A 273      17.515  97.538   9.628  1.00 31.31           O  
ATOM   1550  N   GLN A 274      21.979  92.664  11.977  1.00 34.21           N  
ATOM   1551  CA  GLN A 274      22.142  93.168  13.316  1.00 35.11           C  
ATOM   1552  C   GLN A 274      23.569  93.628  13.610  1.00 37.19           C  
ATOM   1553  O   GLN A 274      23.777  94.532  14.420  1.00 38.23           O  
ATOM   1554  CB  GLN A 274      21.732  92.093  14.306  1.00 34.54           C  
ATOM   1555  CG  GLN A 274      21.707  92.578  15.713  1.00 34.94           C  
ATOM   1556  CD  GLN A 274      21.161  91.546  16.638  1.00 37.10           C  
ATOM   1557  OE1 GLN A 274      20.654  90.513  16.199  1.00 36.16           O  
ATOM   1558  NE2 GLN A 274      21.256  91.807  17.939  1.00 40.22           N  
ATOM   1559  N   LEU A 275      24.555  93.008  12.968  1.00 38.74           N  
ATOM   1560  CA  LEU A 275      25.960  93.384  13.187  1.00 38.52           C  
ATOM   1561  C   LEU A 275      26.261  94.756  12.589  1.00 39.29           C  
ATOM   1562  O   LEU A 275      26.972  95.585  13.170  1.00 39.19           O  
ATOM   1563  CB  LEU A 275      26.885  92.356  12.536  1.00 37.48           C  
ATOM   1564  CG  LEU A 275      26.885  90.976  13.171  1.00 34.73           C  
ATOM   1565  CD1 LEU A 275      27.705  90.026  12.355  1.00 34.44           C  
ATOM   1566  CD2 LEU A 275      27.411  91.098  14.576  1.00 36.63           C  
ATOM   1567  N   VAL A 276      25.716  94.981  11.407  1.00 39.43           N  
ATOM   1568  CA  VAL A 276      25.920  96.230  10.712  1.00 40.16           C  
ATOM   1569  C   VAL A 276      25.044  97.345  11.282  1.00 42.10           C  
ATOM   1570  O   VAL A 276      25.541  98.409  11.617  1.00 44.25           O  
ATOM   1571  CB  VAL A 276      25.618  96.024   9.242  1.00 40.61           C  
ATOM   1572  CG1 VAL A 276      25.811  97.298   8.479  1.00 38.98           C  
ATOM   1573  CG2 VAL A 276      26.512  94.913   8.705  1.00 39.84           C  
ATOM   1574  N   ALA A 277      23.746  97.099  11.414  1.00 40.70           N  
ATOM   1575  CA  ALA A 277      22.839  98.109  11.926  1.00 38.74           C  
ATOM   1576  C   ALA A 277      22.867  98.322  13.437  1.00 38.35           C  
ATOM   1577  O   ALA A 277      22.546  99.398  13.912  1.00 39.77           O  
ATOM   1578  CB  ALA A 277      21.419  97.798  11.473  1.00 37.58           C  
ATOM   1579  N   GLY A 278      23.254  97.315  14.200  1.00 38.36           N  
ATOM   1580  CA  GLY A 278      23.285  97.470  15.643  1.00 35.60           C  
ATOM   1581  C   GLY A 278      22.053  96.857  16.272  1.00 37.27           C  
ATOM   1582  O   GLY A 278      22.003  96.658  17.484  1.00 38.87           O  
ATOM   1583  N   LEU A 279      21.044  96.567  15.453  1.00 37.45           N  
ATOM   1584  CA  LEU A 279      19.790  95.967  15.932  1.00 38.83           C  
ATOM   1585  C   LEU A 279      19.219  94.996  14.897  1.00 39.03           C  
ATOM   1586  O   LEU A 279      19.513  95.100  13.709  1.00 41.67           O  
ATOM   1587  CB  LEU A 279      18.743  97.049  16.208  1.00 38.51           C  
ATOM   1588  CG  LEU A 279      18.985  98.172  17.222  1.00 38.44           C  
ATOM   1589  CD1 LEU A 279      17.842  99.140  17.097  1.00 37.48           C  
ATOM   1590  CD2 LEU A 279      19.071  97.648  18.645  1.00 37.43           C  
ATOM   1591  N   PRO A 280      18.389  94.042  15.332  1.00 39.08           N  
ATOM   1592  CA  PRO A 280      17.814  93.085  14.383  1.00 39.92           C  
ATOM   1593  C   PRO A 280      16.817  93.777  13.449  1.00 39.60           C  
ATOM   1594  O   PRO A 280      16.267  94.811  13.783  1.00 41.43           O  
ATOM   1595  CB  PRO A 280      17.194  92.031  15.295  1.00 41.17           C  
ATOM   1596  CG  PRO A 280      16.840  92.803  16.526  1.00 40.29           C  
ATOM   1597  CD  PRO A 280      18.005  93.722  16.715  1.00 40.13           C  
ATOM   1598  N   PRO A 281      16.565  93.201  12.273  1.00 38.10           N  
ATOM   1599  CA  PRO A 281      15.655  93.750  11.266  1.00 38.07           C  
ATOM   1600  C   PRO A 281      14.191  93.956  11.643  1.00 37.10           C  
ATOM   1601  O   PRO A 281      13.596  94.966  11.308  1.00 36.73           O  
ATOM   1602  CB  PRO A 281      15.776  92.764  10.098  1.00 38.02           C  
ATOM   1603  CG  PRO A 281      16.875  91.808  10.502  1.00 39.32           C  
ATOM   1604  CD  PRO A 281      16.850  91.795  11.978  1.00 38.44           C  
ATOM   1605  N   PHE A 282      13.598  92.977  12.299  1.00 36.85           N  
ATOM   1606  CA  PHE A 282      12.203  93.081  12.659  1.00 37.96           C  
ATOM   1607  C   PHE A 282      12.011  93.397  14.148  1.00 38.77           C  
ATOM   1608  O   PHE A 282      12.389  92.627  15.021  1.00 41.39           O  
ATOM   1609  CB  PHE A 282      11.511  91.785  12.236  1.00 35.55           C  
ATOM   1610  CG  PHE A 282      11.749  91.426  10.782  1.00 34.78           C  
ATOM   1611  CD1 PHE A 282      11.008  92.026   9.765  1.00 36.02           C  
ATOM   1612  CD2 PHE A 282      12.751  90.516  10.426  1.00 33.19           C  
ATOM   1613  CE1 PHE A 282      11.265  91.723   8.410  1.00 32.73           C  
ATOM   1614  CE2 PHE A 282      13.018  90.210   9.094  1.00 29.74           C  
ATOM   1615  CZ  PHE A 282      12.281  90.809   8.082  1.00 32.98           C  
ATOM   1616  N   ARG A 283      11.432  94.554  14.433  1.00 40.57           N  
ATOM   1617  CA  ARG A 283      11.224  94.977  15.816  1.00 41.96           C  
ATOM   1618  C   ARG A 283       9.836  95.574  16.024  1.00 42.12           C  
ATOM   1619  O   ARG A 283       9.300  96.258  15.145  1.00 41.96           O  
ATOM   1620  CB  ARG A 283      12.280  96.011  16.186  1.00 43.58           C  
ATOM   1621  CG  ARG A 283      13.691  95.612  15.792  1.00 44.30           C  
ATOM   1622  CD  ARG A 283      14.673  96.650  16.263  1.00 46.63           C  
ATOM   1623  NE  ARG A 283      14.506  97.915  15.557  1.00 49.93           N  
ATOM   1624  CZ  ARG A 283      14.956  98.146  14.327  1.00 53.45           C  
ATOM   1625  NH1 ARG A 283      15.615  97.198  13.666  1.00 52.94           N  
ATOM   1626  NH2 ARG A 283      14.718  99.315  13.739  1.00 54.82           N  
ATOM   1627  N   ALA A 284       9.245  95.319  17.184  1.00 42.27           N  
ATOM   1628  CA  ALA A 284       7.919  95.851  17.462  1.00 42.09           C  
ATOM   1629  C   ALA A 284       7.579  95.702  18.942  1.00 43.30           C  
ATOM   1630  O   ALA A 284       8.354  95.116  19.704  1.00 44.11           O  
ATOM   1631  CB  ALA A 284       6.894  95.137  16.594  1.00 42.98           C  
ATOM   1632  N   GLY A 285       6.423  96.221  19.348  1.00 42.42           N  
ATOM   1633  CA  GLY A 285       6.034  96.158  20.749  1.00 42.25           C  
ATOM   1634  C   GLY A 285       5.771  94.790  21.350  1.00 43.42           C  
ATOM   1635  O   GLY A 285       5.952  94.590  22.543  1.00 45.65           O  
ATOM   1636  N   ASN A 286       5.323  93.832  20.564  1.00 42.08           N  
ATOM   1637  CA  ASN A 286       5.075  92.524  21.141  1.00 42.35           C  
ATOM   1638  C   ASN A 286       5.438  91.465  20.119  1.00 42.69           C  
ATOM   1639  O   ASN A 286       5.891  91.783  19.026  1.00 44.48           O  
ATOM   1640  CB  ASN A 286       3.605  92.406  21.544  1.00 42.47           C  
ATOM   1641  CG  ASN A 286       2.672  92.638  20.385  1.00 43.50           C  
ATOM   1642  OD1 ASN A 286       2.644  91.857  19.429  1.00 45.95           O  
ATOM   1643  ND2 ASN A 286       1.908  93.720  20.448  1.00 43.79           N  
ATOM   1644  N   GLU A 287       5.227  90.204  20.447  1.00 42.36           N  
ATOM   1645  CA  GLU A 287       5.580  89.183  19.502  1.00 41.62           C  
ATOM   1646  C   GLU A 287       4.694  89.182  18.298  1.00 40.47           C  
ATOM   1647  O   GLU A 287       5.183  89.091  17.169  1.00 41.44           O  
ATOM   1648  CB  GLU A 287       5.596  87.819  20.175  1.00 43.68           C  
ATOM   1649  CG  GLU A 287       7.006  87.461  20.573  1.00 52.01           C  
ATOM   1650  CD  GLU A 287       7.116  86.323  21.584  1.00 56.58           C  
ATOM   1651  OE1 GLU A 287       6.378  85.313  21.438  1.00 57.77           O  
ATOM   1652  OE2 GLU A 287       7.968  86.444  22.510  1.00 56.86           O  
ATOM   1653  N   TYR A 288       3.394  89.314  18.519  1.00 38.27           N  
ATOM   1654  CA  TYR A 288       2.452  89.280  17.406  1.00 36.32           C  
ATOM   1655  C   TYR A 288       2.819  90.302  16.342  1.00 34.88           C  
ATOM   1656  O   TYR A 288       2.776  89.999  15.160  1.00 35.72           O  
ATOM   1657  CB  TYR A 288       1.008  89.493  17.902  1.00 35.19           C  
ATOM   1658  CG  TYR A 288      -0.013  89.642  16.794  1.00 34.62           C  
ATOM   1659  CD1 TYR A 288      -0.676  88.528  16.236  1.00 33.93           C  
ATOM   1660  CD2 TYR A 288      -0.258  90.896  16.240  1.00 33.76           C  
ATOM   1661  CE1 TYR A 288      -1.554  88.678  15.129  1.00 31.95           C  
ATOM   1662  CE2 TYR A 288      -1.110  91.057  15.161  1.00 33.90           C  
ATOM   1663  CZ  TYR A 288      -1.749  89.955  14.604  1.00 35.62           C  
ATOM   1664  OH  TYR A 288      -2.524  90.194  13.488  1.00 40.33           O  
ATOM   1665  N   LEU A 289       3.192  91.507  16.759  1.00 34.29           N  
ATOM   1666  CA  LEU A 289       3.565  92.556  15.814  1.00 34.28           C  
ATOM   1667  C   LEU A 289       4.852  92.223  15.085  1.00 35.02           C  
ATOM   1668  O   LEU A 289       5.054  92.636  13.950  1.00 36.58           O  
ATOM   1669  CB  LEU A 289       3.721  93.887  16.539  1.00 33.03           C  
ATOM   1670  CG  LEU A 289       2.393  94.382  17.113  1.00 34.61           C  
ATOM   1671  CD1 LEU A 289       2.625  95.558  18.059  1.00 29.46           C  
ATOM   1672  CD2 LEU A 289       1.441  94.736  15.938  1.00 31.79           C  
ATOM   1673  N   ILE A 290       5.734  91.485  15.745  1.00 35.88           N  
ATOM   1674  CA  ILE A 290       6.985  91.082  15.128  1.00 35.61           C  
ATOM   1675  C   ILE A 290       6.665  90.052  14.052  1.00 36.44           C  
ATOM   1676  O   ILE A 290       7.121  90.172  12.915  1.00 36.81           O  
ATOM   1677  CB  ILE A 290       7.951  90.505  16.181  1.00 36.32           C  
ATOM   1678  CG1 ILE A 290       8.447  91.641  17.074  1.00 35.92           C  
ATOM   1679  CG2 ILE A 290       9.126  89.838  15.516  1.00 34.46           C  
ATOM   1680  CD1 ILE A 290       9.182  91.177  18.260  1.00 36.40           C  
ATOM   1681  N   PHE A 291       5.856  89.058  14.403  1.00 36.90           N  
ATOM   1682  CA  PHE A 291       5.468  88.032  13.450  1.00 38.09           C  
ATOM   1683  C   PHE A 291       4.785  88.652  12.248  1.00 38.94           C  
ATOM   1684  O   PHE A 291       4.923  88.193  11.120  1.00 39.80           O  
ATOM   1685  CB  PHE A 291       4.515  87.043  14.101  1.00 38.88           C  
ATOM   1686  CG  PHE A 291       5.126  86.261  15.231  1.00 41.18           C  
ATOM   1687  CD1 PHE A 291       6.512  86.181  15.375  1.00 39.08           C  
ATOM   1688  CD2 PHE A 291       4.311  85.562  16.134  1.00 40.85           C  
ATOM   1689  CE1 PHE A 291       7.071  85.424  16.395  1.00 40.58           C  
ATOM   1690  CE2 PHE A 291       4.868  84.790  17.167  1.00 41.00           C  
ATOM   1691  CZ  PHE A 291       6.242  84.722  17.300  1.00 39.66           C  
ATOM   1692  N   GLN A 292       4.036  89.709  12.498  1.00 40.28           N  
ATOM   1693  CA  GLN A 292       3.308  90.389  11.441  1.00 40.71           C  
ATOM   1694  C   GLN A 292       4.311  90.953  10.438  1.00 40.15           C  
ATOM   1695  O   GLN A 292       4.135  90.820   9.233  1.00 40.87           O  
ATOM   1696  CB  GLN A 292       2.452  91.503  12.072  1.00 42.99           C  
ATOM   1697  CG  GLN A 292       1.355  92.095  11.206  1.00 46.04           C  
ATOM   1698  CD  GLN A 292       0.196  92.679  12.045  1.00 47.82           C  
ATOM   1699  OE1 GLN A 292       0.335  93.730  12.683  1.00 49.20           O  
ATOM   1700  NE2 GLN A 292      -0.946  91.978  12.055  1.00 46.93           N  
ATOM   1701  N   LYS A 293       5.377  91.566  10.940  1.00 38.10           N  
ATOM   1702  CA  LYS A 293       6.373  92.155  10.065  1.00 38.60           C  
ATOM   1703  C   LYS A 293       7.134  91.110   9.259  1.00 38.81           C  
ATOM   1704  O   LYS A 293       7.385  91.255   8.053  1.00 37.92           O  
ATOM   1705  CB  LYS A 293       7.354  92.991  10.892  1.00 41.05           C  
ATOM   1706  CG  LYS A 293       6.741  94.275  11.405  1.00 40.20           C  
ATOM   1707  CD  LYS A 293       7.713  95.156  12.131  1.00 39.16           C  
ATOM   1708  CE  LYS A 293       7.081  96.510  12.327  1.00 40.24           C  
ATOM   1709  NZ  LYS A 293       7.732  97.269  13.416  1.00 42.59           N  
ATOM   1710  N   ILE A 294       7.506  90.049   9.945  1.00 37.97           N  
ATOM   1711  CA  ILE A 294       8.248  88.983   9.322  1.00 38.55           C  
ATOM   1712  C   ILE A 294       7.558  88.449   8.084  1.00 39.02           C  
ATOM   1713  O   ILE A 294       8.160  88.398   7.026  1.00 38.61           O  
ATOM   1714  CB  ILE A 294       8.481  87.845  10.334  1.00 37.68           C  
ATOM   1715  CG1 ILE A 294       9.465  88.322  11.409  1.00 34.60           C  
ATOM   1716  CG2 ILE A 294       8.975  86.611   9.632  1.00 36.82           C  
ATOM   1717  CD1 ILE A 294       9.472  87.467  12.634  1.00 32.59           C  
ATOM   1718  N   ILE A 295       6.291  88.077   8.197  1.00 40.52           N  
ATOM   1719  CA  ILE A 295       5.606  87.504   7.040  1.00 43.72           C  
ATOM   1720  C   ILE A 295       5.307  88.488   5.926  1.00 44.21           C  
ATOM   1721  O   ILE A 295       5.003  88.076   4.815  1.00 44.87           O  
ATOM   1722  CB  ILE A 295       4.299  86.811   7.438  1.00 44.38           C  
ATOM   1723  CG1 ILE A 295       3.235  87.849   7.767  1.00 46.12           C  
ATOM   1724  CG2 ILE A 295       4.539  85.933   8.657  1.00 45.50           C  
ATOM   1725  CD1 ILE A 295       1.897  87.242   8.093  1.00 49.44           C  
ATOM   1726  N   LYS A 296       5.389  89.781   6.218  1.00 43.79           N  
ATOM   1727  CA  LYS A 296       5.135  90.789   5.201  1.00 43.49           C  
ATOM   1728  C   LYS A 296       6.474  91.309   4.749  1.00 42.52           C  
ATOM   1729  O   LYS A 296       6.543  92.137   3.853  1.00 41.76           O  
ATOM   1730  CB  LYS A 296       4.312  91.947   5.772  1.00 45.00           C  
ATOM   1731  CG  LYS A 296       3.023  91.508   6.442  1.00 48.80           C  
ATOM   1732  CD  LYS A 296       2.331  92.655   7.167  1.00 52.58           C  
ATOM   1733  CE  LYS A 296       1.555  93.538   6.204  1.00 55.27           C  
ATOM   1734  NZ  LYS A 296       1.026  94.757   6.884  1.00 58.23           N  
ATOM   1735  N   LEU A 297       7.532  90.794   5.380  1.00 42.52           N  
ATOM   1736  CA  LEU A 297       8.927  91.178   5.118  1.00 40.17           C  
ATOM   1737  C   LEU A 297       9.054  92.680   5.287  1.00 39.61           C  
ATOM   1738  O   LEU A 297       9.600  93.371   4.450  1.00 39.44           O  
ATOM   1739  CB  LEU A 297       9.375  90.749   3.711  1.00 39.34           C  
ATOM   1740  CG  LEU A 297      10.893  90.811   3.408  1.00 39.70           C  
ATOM   1741  CD1 LEU A 297      11.706  89.949   4.382  1.00 37.25           C  
ATOM   1742  CD2 LEU A 297      11.138  90.327   1.993  1.00 37.09           C  
ATOM   1743  N   GLU A 298       8.571  93.169   6.416  1.00 41.07           N  
ATOM   1744  CA  GLU A 298       8.575  94.591   6.693  1.00 43.23           C  
ATOM   1745  C   GLU A 298       9.779  95.147   7.453  1.00 42.89           C  
ATOM   1746  O   GLU A 298       9.745  95.254   8.668  1.00 44.14           O  
ATOM   1747  CB  GLU A 298       7.291  94.921   7.448  1.00 45.92           C  
ATOM   1748  CG  GLU A 298       7.037  96.384   7.681  1.00 48.59           C  
ATOM   1749  CD  GLU A 298       5.599  96.625   8.076  1.00 51.12           C  
ATOM   1750  OE1 GLU A 298       4.713  96.338   7.236  1.00 51.14           O  
ATOM   1751  OE2 GLU A 298       5.354  97.083   9.219  1.00 51.90           O  
ATOM   1752  N   TYR A 299      10.838  95.518   6.745  1.00 41.71           N  
ATOM   1753  CA  TYR A 299      12.001  96.083   7.413  1.00 42.27           C  
ATOM   1754  C   TYR A 299      12.751  96.890   6.372  1.00 45.41           C  
ATOM   1755  O   TYR A 299      12.416  96.831   5.200  1.00 49.22           O  
ATOM   1756  CB  TYR A 299      12.921  94.983   7.958  1.00 38.73           C  
ATOM   1757  CG  TYR A 299      13.795  94.328   6.893  1.00 37.07           C  
ATOM   1758  CD1 TYR A 299      13.257  93.439   5.979  1.00 35.60           C  
ATOM   1759  CD2 TYR A 299      15.148  94.648   6.772  1.00 35.44           C  
ATOM   1760  CE1 TYR A 299      14.028  92.888   4.971  1.00 35.50           C  
ATOM   1761  CE2 TYR A 299      15.929  94.100   5.767  1.00 33.88           C  
ATOM   1762  CZ  TYR A 299      15.359  93.221   4.867  1.00 34.29           C  
ATOM   1763  OH  TYR A 299      16.097  92.671   3.848  1.00 32.48           O  
ATOM   1764  N   ASP A 300      13.756  97.652   6.782  1.00 47.14           N  
ATOM   1765  CA  ASP A 300      14.541  98.410   5.817  1.00 49.17           C  
ATOM   1766  C   ASP A 300      15.941  98.654   6.340  1.00 47.48           C  
ATOM   1767  O   ASP A 300      16.180  98.589   7.544  1.00 46.30           O  
ATOM   1768  CB  ASP A 300      13.865  99.735   5.501  1.00 54.55           C  
ATOM   1769  CG  ASP A 300      13.017 100.230   6.641  1.00 59.10           C  
ATOM   1770  OD1 ASP A 300      13.549 100.336   7.771  1.00 60.73           O  
ATOM   1771  OD2 ASP A 300      11.816 100.509   6.396  1.00 63.15           O  
ATOM   1772  N   PHE A 301      16.862  98.940   5.431  1.00 45.69           N  
ATOM   1773  CA  PHE A 301      18.245  99.173   5.815  1.00 47.57           C  
ATOM   1774  C   PHE A 301      18.583 100.643   6.052  1.00 48.70           C  
ATOM   1775  O   PHE A 301      18.029 101.539   5.418  1.00 47.58           O  
ATOM   1776  CB  PHE A 301      19.208  98.650   4.742  1.00 45.99           C  
ATOM   1777  CG  PHE A 301      18.880  97.286   4.228  1.00 44.84           C  
ATOM   1778  CD1 PHE A 301      17.891  97.109   3.287  1.00 44.68           C  
ATOM   1779  CD2 PHE A 301      19.578  96.178   4.673  1.00 44.47           C  
ATOM   1780  CE1 PHE A 301      17.604  95.845   2.796  1.00 45.92           C  
ATOM   1781  CE2 PHE A 301      19.293  94.916   4.185  1.00 44.34           C  
ATOM   1782  CZ  PHE A 301      18.302  94.751   3.244  1.00 44.57           C  
ATOM   1783  N   PRO A 302      19.509 100.907   6.978  1.00 49.77           N  
ATOM   1784  CA  PRO A 302      19.900 102.287   7.253  1.00 50.65           C  
ATOM   1785  C   PRO A 302      20.592 102.832   6.007  1.00 53.47           C  
ATOM   1786  O   PRO A 302      21.016 102.066   5.135  1.00 53.02           O  
ATOM   1787  CB  PRO A 302      20.856 102.142   8.420  1.00 50.52           C  
ATOM   1788  CG  PRO A 302      20.328 100.959   9.135  1.00 50.19           C  
ATOM   1789  CD  PRO A 302      20.002  99.999   8.023  1.00 49.48           C  
ATOM   1790  N   GLU A 303      20.731 104.152   5.938  1.00 56.00           N  
ATOM   1791  CA  GLU A 303      21.343 104.806   4.782  1.00 56.13           C  
ATOM   1792  C   GLU A 303      22.758 104.350   4.390  1.00 56.04           C  
ATOM   1793  O   GLU A 303      23.030 104.128   3.203  1.00 55.56           O  
ATOM   1794  CB  GLU A 303      21.323 106.321   4.989  1.00 55.87           C  
ATOM   1795  N   LYS A 304      23.652 104.196   5.366  1.00 55.76           N  
ATOM   1796  CA  LYS A 304      25.034 103.817   5.044  1.00 55.98           C  
ATOM   1797  C   LYS A 304      25.440 102.350   5.297  1.00 54.88           C  
ATOM   1798  O   LYS A 304      26.594 102.046   5.650  1.00 55.11           O  
ATOM   1799  CB  LYS A 304      26.004 104.770   5.761  1.00 56.94           C  
ATOM   1800  N   PHE A 305      24.483 101.453   5.083  1.00 50.88           N  
ATOM   1801  CA  PHE A 305      24.673 100.018   5.251  1.00 46.26           C  
ATOM   1802  C   PHE A 305      25.581  99.515   4.121  1.00 43.43           C  
ATOM   1803  O   PHE A 305      25.256  99.682   2.944  1.00 42.28           O  
ATOM   1804  CB  PHE A 305      23.296  99.358   5.175  1.00 46.05           C  
ATOM   1805  CG  PHE A 305      23.239  97.959   5.716  1.00 45.71           C  
ATOM   1806  CD1 PHE A 305      23.873  96.915   5.060  1.00 46.16           C  
ATOM   1807  CD2 PHE A 305      22.487  97.674   6.850  1.00 43.81           C  
ATOM   1808  CE1 PHE A 305      23.749  95.607   5.527  1.00 45.73           C  
ATOM   1809  CE2 PHE A 305      22.359  96.368   7.317  1.00 43.47           C  
ATOM   1810  CZ  PHE A 305      22.989  95.336   6.655  1.00 43.86           C  
ATOM   1811  N   PHE A 306      26.713  98.907   4.479  1.00 40.41           N  
ATOM   1812  CA  PHE A 306      27.657  98.402   3.489  1.00 36.97           C  
ATOM   1813  C   PHE A 306      26.838  97.743   2.411  1.00 38.23           C  
ATOM   1814  O   PHE A 306      26.063  96.852   2.694  1.00 39.90           O  
ATOM   1815  CB  PHE A 306      28.613  97.400   4.116  1.00 35.07           C  
ATOM   1816  CG  PHE A 306      29.159  97.838   5.438  1.00 34.45           C  
ATOM   1817  CD1 PHE A 306      29.750  99.078   5.583  1.00 33.45           C  
ATOM   1818  CD2 PHE A 306      29.016  97.033   6.563  1.00 34.73           C  
ATOM   1819  CE1 PHE A 306      30.180  99.518   6.827  1.00 33.39           C  
ATOM   1820  CE2 PHE A 306      29.445  97.461   7.826  1.00 35.42           C  
ATOM   1821  CZ  PHE A 306      30.024  98.707   7.956  1.00 35.66           C  
ATOM   1822  N   PRO A 307      26.975  98.203   1.156  1.00 39.14           N  
ATOM   1823  CA  PRO A 307      26.259  97.696  -0.021  1.00 39.26           C  
ATOM   1824  C   PRO A 307      26.388  96.197  -0.287  1.00 40.89           C  
ATOM   1825  O   PRO A 307      25.411  95.538  -0.626  1.00 41.77           O  
ATOM   1826  CB  PRO A 307      26.845  98.524  -1.163  1.00 36.15           C  
ATOM   1827  CG  PRO A 307      27.165  99.779  -0.530  1.00 37.08           C  
ATOM   1828  CD  PRO A 307      27.808  99.353   0.773  1.00 38.46           C  
ATOM   1829  N   LYS A 308      27.588  95.651  -0.163  1.00 41.40           N  
ATOM   1830  CA  LYS A 308      27.716  94.236  -0.421  1.00 41.83           C  
ATOM   1831  C   LYS A 308      27.036  93.475   0.707  1.00 40.79           C  
ATOM   1832  O   LYS A 308      26.451  92.433   0.474  1.00 43.32           O  
ATOM   1833  CB  LYS A 308      29.189  93.854  -0.598  1.00 42.78           C  
ATOM   1834  CG  LYS A 308      29.773  94.430  -1.892  1.00 43.92           C  
ATOM   1835  CD  LYS A 308      31.242  94.071  -2.118  1.00 46.81           C  
ATOM   1836  CE  LYS A 308      31.816  94.802  -3.343  1.00 46.14           C  
ATOM   1837  NZ  LYS A 308      33.225  94.400  -3.668  1.00 47.27           N  
ATOM   1838  N   ALA A 309      27.076  94.005   1.923  1.00 38.81           N  
ATOM   1839  CA  ALA A 309      26.402  93.339   3.036  1.00 39.00           C  
ATOM   1840  C   ALA A 309      24.905  93.372   2.777  1.00 38.51           C  
ATOM   1841  O   ALA A 309      24.230  92.366   2.903  1.00 40.82           O  
ATOM   1842  CB  ALA A 309      26.720  94.027   4.360  1.00 37.20           C  
ATOM   1843  N   ARG A 310      24.385  94.532   2.404  1.00 39.25           N  
ATOM   1844  CA  ARG A 310      22.963  94.673   2.121  1.00 39.66           C  
ATOM   1845  C   ARG A 310      22.520  93.651   1.075  1.00 39.39           C  
ATOM   1846  O   ARG A 310      21.518  92.940   1.234  1.00 38.32           O  
ATOM   1847  CB  ARG A 310      22.673  96.086   1.616  1.00 41.91           C  
ATOM   1848  CG  ARG A 310      21.279  96.225   1.047  1.00 46.74           C  
ATOM   1849  CD  ARG A 310      20.914  97.642   0.662  1.00 47.87           C  
ATOM   1850  NE  ARG A 310      19.597  97.670   0.026  1.00 50.40           N  
ATOM   1851  CZ  ARG A 310      18.677  98.604   0.251  1.00 49.89           C  
ATOM   1852  NH1 ARG A 310      18.921  99.594   1.105  1.00 49.14           N  
ATOM   1853  NH2 ARG A 310      17.518  98.550  -0.381  1.00 46.51           N  
ATOM   1854  N   ASP A 311      23.277  93.577  -0.005  1.00 39.19           N  
ATOM   1855  CA  ASP A 311      22.937  92.650  -1.049  1.00 39.24           C  
ATOM   1856  C   ASP A 311      22.841  91.248  -0.484  1.00 40.33           C  
ATOM   1857  O   ASP A 311      21.868  90.538  -0.757  1.00 41.94           O  
ATOM   1858  CB  ASP A 311      23.963  92.687  -2.161  1.00 38.74           C  
ATOM   1859  CG  ASP A 311      23.597  91.760  -3.282  1.00 42.32           C  
ATOM   1860  OD1 ASP A 311      24.047  90.596  -3.254  1.00 45.29           O  
ATOM   1861  OD2 ASP A 311      22.830  92.180  -4.179  1.00 44.10           O  
ATOM   1862  N   LEU A 312      23.842  90.850   0.305  1.00 37.88           N  
ATOM   1863  CA  LEU A 312      23.849  89.529   0.939  1.00 35.83           C  
ATOM   1864  C   LEU A 312      22.581  89.288   1.760  1.00 34.04           C  
ATOM   1865  O   LEU A 312      21.895  88.295   1.571  1.00 35.34           O  
ATOM   1866  CB  LEU A 312      25.058  89.394   1.852  1.00 35.58           C  
ATOM   1867  CG  LEU A 312      25.128  88.099   2.653  1.00 35.72           C  
ATOM   1868  CD1 LEU A 312      24.903  86.912   1.725  1.00 35.99           C  
ATOM   1869  CD2 LEU A 312      26.485  87.993   3.327  1.00 34.02           C  
ATOM   1870  N   VAL A 313      22.277  90.203   2.674  1.00 33.41           N  
ATOM   1871  CA  VAL A 313      21.079  90.115   3.511  1.00 33.04           C  
ATOM   1872  C   VAL A 313      19.812  90.006   2.655  1.00 34.77           C  
ATOM   1873  O   VAL A 313      18.837  89.330   3.012  1.00 33.95           O  
ATOM   1874  CB  VAL A 313      20.947  91.370   4.397  1.00 32.02           C  
ATOM   1875  CG1 VAL A 313      19.646  91.332   5.188  1.00 30.38           C  
ATOM   1876  CG2 VAL A 313      22.147  91.487   5.318  1.00 29.69           C  
ATOM   1877  N   GLU A 314      19.813  90.681   1.520  1.00 35.98           N  
ATOM   1878  CA  GLU A 314      18.635  90.617   0.680  1.00 39.31           C  
ATOM   1879  C   GLU A 314      18.451  89.252   0.044  1.00 39.26           C  
ATOM   1880  O   GLU A 314      17.350  88.900  -0.393  1.00 41.79           O  
ATOM   1881  CB  GLU A 314      18.701  91.675  -0.404  1.00 40.76           C  
ATOM   1882  CG  GLU A 314      18.695  93.076   0.130  1.00 45.52           C  
ATOM   1883  CD  GLU A 314      18.528  94.072  -0.979  1.00 49.22           C  
ATOM   1884  OE1 GLU A 314      19.246  93.932  -2.000  1.00 51.76           O  
ATOM   1885  OE2 GLU A 314      17.685  94.985  -0.835  1.00 51.86           O  
ATOM   1886  N   LYS A 315      19.522  88.477  -0.001  1.00 37.37           N  
ATOM   1887  CA  LYS A 315      19.447  87.170  -0.598  1.00 35.19           C  
ATOM   1888  C   LYS A 315      19.216  86.102   0.446  1.00 36.51           C  
ATOM   1889  O   LYS A 315      19.061  84.934   0.112  1.00 39.25           O  
ATOM   1890  CB  LYS A 315      20.721  86.897  -1.387  1.00 34.45           C  
ATOM   1891  CG  LYS A 315      20.904  87.850  -2.559  1.00 34.90           C  
ATOM   1892  CD  LYS A 315      22.185  87.548  -3.299  1.00 36.57           C  
ATOM   1893  CE  LYS A 315      22.519  88.617  -4.353  1.00 38.28           C  
ATOM   1894  NZ  LYS A 315      21.956  88.303  -5.674  1.00 39.78           N  
ATOM   1895  N   LEU A 316      19.212  86.484   1.716  1.00 35.90           N  
ATOM   1896  CA  LEU A 316      18.962  85.519   2.777  1.00 34.84           C  
ATOM   1897  C   LEU A 316      17.557  85.731   3.315  1.00 36.56           C  
ATOM   1898  O   LEU A 316      16.828  84.765   3.532  1.00 36.64           O  
ATOM   1899  CB  LEU A 316      19.950  85.689   3.912  1.00 33.90           C  
ATOM   1900  CG  LEU A 316      21.402  85.383   3.619  1.00 31.16           C  
ATOM   1901  CD1 LEU A 316      22.185  85.828   4.796  1.00 30.38           C  
ATOM   1902  CD2 LEU A 316      21.609  83.920   3.371  1.00 28.62           C  
ATOM   1903  N   LEU A 317      17.191  86.994   3.540  1.00 35.36           N  
ATOM   1904  CA  LEU A 317      15.860  87.324   4.023  1.00 36.27           C  
ATOM   1905  C   LEU A 317      14.911  87.332   2.836  1.00 36.70           C  
ATOM   1906  O   LEU A 317      14.530  88.383   2.327  1.00 37.88           O  
ATOM   1907  CB  LEU A 317      15.871  88.691   4.703  1.00 34.48           C  
ATOM   1908  CG  LEU A 317      16.834  88.708   5.885  1.00 36.03           C  
ATOM   1909  CD1 LEU A 317      16.652  89.965   6.723  1.00 34.28           C  
ATOM   1910  CD2 LEU A 317      16.588  87.472   6.715  1.00 32.44           C  
ATOM   1911  N   VAL A 318      14.547  86.138   2.391  1.00 37.94           N  
ATOM   1912  CA  VAL A 318      13.659  85.936   1.247  1.00 36.07           C  
ATOM   1913  C   VAL A 318      12.507  85.080   1.747  1.00 37.57           C  
ATOM   1914  O   VAL A 318      12.729  84.011   2.319  1.00 38.45           O  
ATOM   1915  CB  VAL A 318      14.407  85.175   0.128  1.00 37.17           C  
ATOM   1916  CG1 VAL A 318      13.502  85.000  -1.074  1.00 35.86           C  
ATOM   1917  CG2 VAL A 318      15.704  85.917  -0.249  1.00 34.00           C  
ATOM   1918  N   LEU A 319      11.277  85.528   1.548  1.00 39.25           N  
ATOM   1919  CA  LEU A 319      10.138  84.756   2.043  1.00 41.35           C  
ATOM   1920  C   LEU A 319      10.109  83.334   1.509  1.00 41.99           C  
ATOM   1921  O   LEU A 319       9.829  82.402   2.253  1.00 43.32           O  
ATOM   1922  CB  LEU A 319       8.823  85.467   1.726  1.00 42.07           C  
ATOM   1923  CG  LEU A 319       8.623  86.751   2.536  1.00 42.31           C  
ATOM   1924  CD1 LEU A 319       7.327  87.459   2.128  1.00 40.65           C  
ATOM   1925  CD2 LEU A 319       8.613  86.396   4.007  1.00 38.93           C  
ATOM   1926  N   ASP A 320      10.405  83.167   0.226  1.00 42.48           N  
ATOM   1927  CA  ASP A 320      10.434  81.843  -0.377  1.00 42.15           C  
ATOM   1928  C   ASP A 320      11.690  81.112   0.116  1.00 42.37           C  
ATOM   1929  O   ASP A 320      12.792  81.320  -0.391  1.00 41.95           O  
ATOM   1930  CB  ASP A 320      10.466  81.975  -1.892  1.00 42.41           C  
ATOM   1931  CG  ASP A 320      10.496  80.641  -2.583  1.00 45.98           C  
ATOM   1932  OD1 ASP A 320      10.660  79.615  -1.886  1.00 47.30           O  
ATOM   1933  OD2 ASP A 320      10.362  80.613  -3.827  1.00 49.95           O  
ATOM   1934  N   ALA A 321      11.512  80.253   1.110  1.00 43.29           N  
ATOM   1935  CA  ALA A 321      12.618  79.502   1.703  1.00 44.65           C  
ATOM   1936  C   ALA A 321      13.540  78.844   0.717  1.00 47.07           C  
ATOM   1937  O   ALA A 321      14.745  78.865   0.896  1.00 52.03           O  
ATOM   1938  CB  ALA A 321      12.086  78.451   2.628  1.00 42.94           C  
ATOM   1939  N   THR A 322      12.977  78.251  -0.326  1.00 47.78           N  
ATOM   1940  CA  THR A 322      13.772  77.539  -1.319  1.00 47.57           C  
ATOM   1941  C   THR A 322      14.618  78.420  -2.208  1.00 46.92           C  
ATOM   1942  O   THR A 322      15.277  77.915  -3.102  1.00 48.57           O  
ATOM   1943  CB  THR A 322      12.881  76.702  -2.229  1.00 47.26           C  
ATOM   1944  OG1 THR A 322      12.146  77.571  -3.097  1.00 47.68           O  
ATOM   1945  CG2 THR A 322      11.909  75.884  -1.398  1.00 46.50           C  
ATOM   1946  N   LYS A 323      14.600  79.727  -1.979  1.00 45.40           N  
ATOM   1947  CA  LYS A 323      15.395  80.631  -2.802  1.00 44.46           C  
ATOM   1948  C   LYS A 323      16.396  81.415  -1.969  1.00 44.78           C  
ATOM   1949  O   LYS A 323      16.784  82.505  -2.356  1.00 45.94           O  
ATOM   1950  CB  LYS A 323      14.495  81.584  -3.564  1.00 42.86           C  
ATOM   1951  N   ARG A 324      16.804  80.867  -0.822  1.00 43.51           N  
ATOM   1952  CA  ARG A 324      17.781  81.528   0.036  1.00 41.04           C  
ATOM   1953  C   ARG A 324      19.190  81.025  -0.224  1.00 41.96           C  
ATOM   1954  O   ARG A 324      19.442  79.821  -0.290  1.00 42.70           O  
ATOM   1955  CB  ARG A 324      17.461  81.307   1.507  1.00 38.35           C  
ATOM   1956  CG  ARG A 324      16.324  82.124   1.987  1.00 37.78           C  
ATOM   1957  CD  ARG A 324      15.871  81.723   3.366  1.00 34.71           C  
ATOM   1958  NE  ARG A 324      14.544  82.274   3.596  1.00 34.63           N  
ATOM   1959  CZ  ARG A 324      13.698  81.826   4.508  1.00 37.86           C  
ATOM   1960  NH1 ARG A 324      14.043  80.818   5.302  1.00 37.26           N  
ATOM   1961  NH2 ARG A 324      12.479  82.340   4.573  1.00 37.57           N  
ATOM   1962  N   LEU A 325      20.112  81.966  -0.352  1.00 42.37           N  
ATOM   1963  CA  LEU A 325      21.503  81.645  -0.596  1.00 42.52           C  
ATOM   1964  C   LEU A 325      21.902  80.636   0.471  1.00 42.40           C  
ATOM   1965  O   LEU A 325      21.637  80.857   1.646  1.00 42.97           O  
ATOM   1966  CB  LEU A 325      22.342  82.930  -0.495  1.00 42.64           C  
ATOM   1967  CG  LEU A 325      23.600  83.041  -1.356  1.00 43.63           C  
ATOM   1968  CD1 LEU A 325      23.237  82.781  -2.797  1.00 44.77           C  
ATOM   1969  CD2 LEU A 325      24.242  84.407  -1.200  1.00 40.87           C  
ATOM   1970  N   GLY A 326      22.508  79.525   0.053  1.00 42.50           N  
ATOM   1971  CA  GLY A 326      22.930  78.491   0.983  1.00 41.58           C  
ATOM   1972  C   GLY A 326      22.063  77.237   0.945  1.00 43.27           C  
ATOM   1973  O   GLY A 326      22.515  76.136   1.304  1.00 43.46           O  
ATOM   1974  N   CYS A 327      20.813  77.380   0.516  1.00 41.74           N  
ATOM   1975  CA  CYS A 327      19.943  76.222   0.471  1.00 42.17           C  
ATOM   1976  C   CYS A 327      20.335  75.347  -0.709  1.00 42.76           C  
ATOM   1977  O   CYS A 327      20.858  75.843  -1.709  1.00 42.42           O  
ATOM   1978  CB ACYS A 327      18.457  76.628   0.463  0.50 43.29           C  
ATOM   1979  CB BCYS A 327      18.488  76.671   0.264  0.50 38.86           C  
ATOM   1980  SG ACYS A 327      17.899  77.537  -0.954  0.50 50.19           S  
ATOM   1981  SG BCYS A 327      17.485  76.887   1.739  0.50 31.82           S  
ATOM   1982  N   GLU A 328      20.103  74.041  -0.577  1.00 44.03           N  
ATOM   1983  CA  GLU A 328      20.420  73.066  -1.632  1.00 44.24           C  
ATOM   1984  C   GLU A 328      19.788  73.474  -2.952  1.00 43.81           C  
ATOM   1985  O   GLU A 328      20.358  73.298  -4.022  1.00 42.73           O  
ATOM   1986  CB  GLU A 328      19.923  71.676  -1.230  1.00 43.93           C  
ATOM   1987  N   GLU A 329      18.597  74.036  -2.850  1.00 44.95           N  
ATOM   1988  CA  GLU A 329      17.854  74.487  -4.007  1.00 46.39           C  
ATOM   1989  C   GLU A 329      18.646  75.578  -4.712  1.00 45.91           C  
ATOM   1990  O   GLU A 329      18.515  75.773  -5.919  1.00 44.77           O  
ATOM   1991  CB  GLU A 329      16.491  75.025  -3.552  1.00 51.11           C  
ATOM   1992  CG  GLU A 329      15.573  73.977  -2.845  1.00 58.72           C  
ATOM   1993  CD  GLU A 329      16.157  73.415  -1.523  1.00 63.66           C  
ATOM   1994  OE1 GLU A 329      16.313  74.180  -0.532  1.00 65.39           O  
ATOM   1995  OE2 GLU A 329      16.462  72.195  -1.479  1.00 65.94           O  
ATOM   1996  N   MET A 330      19.462  76.309  -3.954  1.00 44.76           N  
ATOM   1997  CA  MET A 330      20.273  77.374  -4.542  1.00 43.25           C  
ATOM   1998  C   MET A 330      21.709  76.893  -4.708  1.00 42.64           C  
ATOM   1999  O   MET A 330      22.624  77.680  -4.908  1.00 41.77           O  
ATOM   2000  CB  MET A 330      20.222  78.638  -3.680  1.00 42.02           C  
ATOM   2001  CG  MET A 330      18.873  79.328  -3.695  1.00 43.29           C  
ATOM   2002  SD  MET A 330      18.581  80.103  -5.306  1.00 45.64           S  
ATOM   2003  CE  MET A 330      19.509  81.570  -5.116  1.00 43.66           C  
ATOM   2004  N   GLU A 331      21.880  75.581  -4.626  1.00 41.42           N  
ATOM   2005  CA  GLU A 331      23.173  74.935  -4.792  1.00 41.50           C  
ATOM   2006  C   GLU A 331      24.139  75.002  -3.607  1.00 41.16           C  
ATOM   2007  O   GLU A 331      25.355  74.912  -3.779  1.00 41.35           O  
ATOM   2008  CB  GLU A 331      23.849  75.432  -6.075  1.00 40.56           C  
ATOM   2009  CG  GLU A 331      22.889  75.536  -7.259  1.00 40.44           C  
ATOM   2010  CD  GLU A 331      22.055  74.271  -7.519  1.00 42.08           C  
ATOM   2011  OE1 GLU A 331      21.164  74.314  -8.406  1.00 41.33           O  
ATOM   2012  OE2 GLU A 331      22.280  73.236  -6.855  1.00 43.24           O  
ATOM   2013  N   GLY A 332      23.592  75.169  -2.406  1.00 40.42           N  
ATOM   2014  CA  GLY A 332      24.408  75.131  -1.205  1.00 37.00           C  
ATOM   2015  C   GLY A 332      25.329  76.253  -0.804  1.00 36.50           C  
ATOM   2016  O   GLY A 332      25.170  77.402  -1.222  1.00 35.72           O  
ATOM   2017  N   TYR A 333      26.311  75.893   0.018  1.00 35.33           N  
ATOM   2018  CA  TYR A 333      27.274  76.841   0.545  1.00 35.15           C  
ATOM   2019  C   TYR A 333      28.296  77.361  -0.444  1.00 37.34           C  
ATOM   2020  O   TYR A 333      28.941  78.385  -0.187  1.00 38.98           O  
ATOM   2021  CB  TYR A 333      27.962  76.234   1.763  1.00 34.24           C  
ATOM   2022  CG  TYR A 333      27.061  76.234   2.965  1.00 36.60           C  
ATOM   2023  CD1 TYR A 333      27.031  77.322   3.837  1.00 36.41           C  
ATOM   2024  CD2 TYR A 333      26.130  75.217   3.157  1.00 37.43           C  
ATOM   2025  CE1 TYR A 333      26.090  77.406   4.865  1.00 37.12           C  
ATOM   2026  CE2 TYR A 333      25.173  75.293   4.179  1.00 38.77           C  
ATOM   2027  CZ  TYR A 333      25.159  76.392   5.028  1.00 39.02           C  
ATOM   2028  OH  TYR A 333      24.202  76.479   6.020  1.00 39.59           O  
ATOM   2029  N   GLY A 334      28.462  76.674  -1.571  1.00 37.18           N  
ATOM   2030  CA  GLY A 334      29.415  77.155  -2.557  1.00 37.69           C  
ATOM   2031  C   GLY A 334      29.086  78.592  -2.944  1.00 37.47           C  
ATOM   2032  O   GLY A 334      29.889  79.501  -2.749  1.00 41.32           O  
ATOM   2033  N   PRO A 335      27.903  78.828  -3.511  1.00 35.47           N  
ATOM   2034  CA  PRO A 335      27.457  80.152  -3.923  1.00 34.57           C  
ATOM   2035  C   PRO A 335      27.490  81.152  -2.779  1.00 35.28           C  
ATOM   2036  O   PRO A 335      27.938  82.271  -2.945  1.00 38.17           O  
ATOM   2037  CB  PRO A 335      26.041  79.880  -4.399  1.00 32.61           C  
ATOM   2038  CG  PRO A 335      26.207  78.598  -5.060  1.00 32.41           C  
ATOM   2039  CD  PRO A 335      27.009  77.803  -4.068  1.00 34.43           C  
ATOM   2040  N   LEU A 336      27.005  80.742  -1.617  1.00 34.34           N  
ATOM   2041  CA  LEU A 336      26.967  81.616  -0.457  1.00 33.77           C  
ATOM   2042  C   LEU A 336      28.343  82.114  -0.054  1.00 34.80           C  
ATOM   2043  O   LEU A 336      28.543  83.315   0.140  1.00 37.63           O  
ATOM   2044  CB  LEU A 336      26.303  80.888   0.719  1.00 30.87           C  
ATOM   2045  CG  LEU A 336      26.263  81.573   2.081  1.00 29.27           C  
ATOM   2046  CD1 LEU A 336      25.679  82.944   1.965  1.00 25.27           C  
ATOM   2047  CD2 LEU A 336      25.409  80.737   3.034  1.00 29.05           C  
ATOM   2048  N   LYS A 337      29.299  81.203   0.071  1.00 33.09           N  
ATOM   2049  CA  LYS A 337      30.636  81.611   0.455  1.00 32.92           C  
ATOM   2050  C   LYS A 337      31.304  82.449  -0.625  1.00 33.99           C  
ATOM   2051  O   LYS A 337      32.248  83.199  -0.349  1.00 35.50           O  
ATOM   2052  CB  LYS A 337      31.465  80.380   0.789  1.00 31.85           C  
ATOM   2053  CG  LYS A 337      30.943  79.691   2.037  1.00 34.58           C  
ATOM   2054  CD  LYS A 337      31.414  78.259   2.171  1.00 35.95           C  
ATOM   2055  CE  LYS A 337      32.879  78.182   2.557  1.00 35.55           C  
ATOM   2056  NZ  LYS A 337      33.316  76.766   2.514  1.00 35.25           N  
ATOM   2057  N   ALA A 338      30.788  82.342  -1.848  1.00 33.69           N  
ATOM   2058  CA  ALA A 338      31.318  83.076  -2.982  1.00 33.44           C  
ATOM   2059  C   ALA A 338      30.784  84.500  -3.098  1.00 35.34           C  
ATOM   2060  O   ALA A 338      31.298  85.282  -3.891  1.00 37.56           O  
ATOM   2061  CB  ALA A 338      31.035  82.317  -4.256  1.00 31.75           C  
ATOM   2062  N   HIS A 339      29.770  84.853  -2.312  1.00 35.37           N  
ATOM   2063  CA  HIS A 339      29.217  86.199  -2.384  1.00 35.72           C  
ATOM   2064  C   HIS A 339      30.287  87.279  -2.322  1.00 36.47           C  
ATOM   2065  O   HIS A 339      31.239  87.186  -1.555  1.00 38.75           O  
ATOM   2066  CB  HIS A 339      28.199  86.418  -1.276  1.00 35.70           C  
ATOM   2067  CG  HIS A 339      27.435  87.698  -1.410  1.00 37.05           C  
ATOM   2068  ND1 HIS A 339      27.931  88.911  -0.980  1.00 37.37           N  
ATOM   2069  CD2 HIS A 339      26.222  87.959  -1.951  1.00 37.04           C  
ATOM   2070  CE1 HIS A 339      27.053  89.860  -1.247  1.00 36.95           C  
ATOM   2071  NE2 HIS A 339      26.007  89.311  -1.837  1.00 37.04           N  
ATOM   2072  N   PRO A 340      30.131  88.340  -3.121  1.00 37.52           N  
ATOM   2073  CA  PRO A 340      31.110  89.434  -3.148  1.00 37.59           C  
ATOM   2074  C   PRO A 340      31.471  89.959  -1.785  1.00 37.79           C  
ATOM   2075  O   PRO A 340      32.619  90.350  -1.536  1.00 38.77           O  
ATOM   2076  CB  PRO A 340      30.433  90.492  -4.018  1.00 38.54           C  
ATOM   2077  CG  PRO A 340      29.647  89.647  -5.004  1.00 37.05           C  
ATOM   2078  CD  PRO A 340      29.046  88.578  -4.093  1.00 37.17           C  
ATOM   2079  N   PHE A 341      30.503  89.951  -0.884  1.00 37.53           N  
ATOM   2080  CA  PHE A 341      30.778  90.455   0.455  1.00 37.40           C  
ATOM   2081  C   PHE A 341      31.960  89.742   1.109  1.00 37.21           C  
ATOM   2082  O   PHE A 341      32.680  90.322   1.918  1.00 36.73           O  
ATOM   2083  CB  PHE A 341      29.545  90.323   1.349  1.00 35.43           C  
ATOM   2084  CG  PHE A 341      29.756  90.876   2.724  1.00 35.46           C  
ATOM   2085  CD1 PHE A 341      30.209  92.183   2.894  1.00 33.19           C  
ATOM   2086  CD2 PHE A 341      29.531  90.091   3.857  1.00 35.63           C  
ATOM   2087  CE1 PHE A 341      30.437  92.703   4.165  1.00 33.58           C  
ATOM   2088  CE2 PHE A 341      29.756  90.607   5.141  1.00 34.58           C  
ATOM   2089  CZ  PHE A 341      30.210  91.917   5.291  1.00 33.58           C  
ATOM   2090  N   PHE A 342      32.166  88.487   0.725  1.00 37.70           N  
ATOM   2091  CA  PHE A 342      33.219  87.678   1.301  1.00 38.17           C  
ATOM   2092  C   PHE A 342      34.447  87.591   0.408  1.00 41.02           C  
ATOM   2093  O   PHE A 342      35.312  86.736   0.640  1.00 41.48           O  
ATOM   2094  CB  PHE A 342      32.711  86.255   1.546  1.00 34.90           C  
ATOM   2095  CG  PHE A 342      31.505  86.167   2.434  1.00 31.99           C  
ATOM   2096  CD1 PHE A 342      31.528  86.687   3.716  1.00 31.40           C  
ATOM   2097  CD2 PHE A 342      30.372  85.489   2.010  1.00 30.22           C  
ATOM   2098  CE1 PHE A 342      30.443  86.526   4.570  1.00 31.67           C  
ATOM   2099  CE2 PHE A 342      29.293  85.326   2.850  1.00 31.38           C  
ATOM   2100  CZ  PHE A 342      29.325  85.843   4.142  1.00 29.17           C  
ATOM   2101  N   GLU A 343      34.526  88.452  -0.607  1.00 42.41           N  
ATOM   2102  CA  GLU A 343      35.667  88.441  -1.534  1.00 42.97           C  
ATOM   2103  C   GLU A 343      37.014  88.160  -0.873  1.00 42.70           C  
ATOM   2104  O   GLU A 343      37.695  87.189  -1.218  1.00 43.32           O  
ATOM   2105  CB  GLU A 343      35.787  89.774  -2.274  1.00 43.62           C  
ATOM   2106  CG  GLU A 343      35.922  89.639  -3.791  1.00 45.83           C  
ATOM   2107  CD  GLU A 343      34.597  89.818  -4.508  0.00 45.35           C  
ATOM   2108  OE1 GLU A 343      34.018  90.921  -4.418  0.00 45.62           O  
ATOM   2109  OE2 GLU A 343      34.134  88.859  -5.160  0.00 45.62           O  
ATOM   2110  N   SER A 344      37.400  88.993   0.087  1.00 41.39           N  
ATOM   2111  CA  SER A 344      38.701  88.815   0.726  1.00 41.82           C  
ATOM   2112  C   SER A 344      38.841  87.698   1.769  1.00 43.28           C  
ATOM   2113  O   SER A 344      39.925  87.521   2.325  1.00 43.57           O  
ATOM   2114  CB  SER A 344      39.141  90.125   1.370  1.00 40.94           C  
ATOM   2115  OG  SER A 344      38.303  90.450   2.459  1.00 44.65           O  
ATOM   2116  N   VAL A 345      37.771  86.948   2.037  1.00 42.19           N  
ATOM   2117  CA  VAL A 345      37.813  85.882   3.036  1.00 41.33           C  
ATOM   2118  C   VAL A 345      38.527  84.591   2.603  1.00 40.85           C  
ATOM   2119  O   VAL A 345      38.337  84.121   1.487  1.00 42.69           O  
ATOM   2120  CB  VAL A 345      36.369  85.492   3.469  1.00 42.30           C  
ATOM   2121  CG1 VAL A 345      36.408  84.330   4.447  1.00 39.86           C  
ATOM   2122  CG2 VAL A 345      35.653  86.679   4.088  1.00 40.37           C  
ATOM   2123  N   THR A 346      39.346  84.023   3.486  1.00 40.00           N  
ATOM   2124  CA  THR A 346      40.005  82.733   3.215  1.00 42.02           C  
ATOM   2125  C   THR A 346      39.273  81.742   4.121  1.00 41.95           C  
ATOM   2126  O   THR A 346      39.522  81.689   5.316  1.00 41.34           O  
ATOM   2127  CB  THR A 346      41.498  82.743   3.581  1.00 42.38           C  
ATOM   2128  OG1 THR A 346      42.226  83.489   2.593  1.00 45.36           O  
ATOM   2129  CG2 THR A 346      42.036  81.341   3.615  1.00 40.13           C  
ATOM   2130  N   TRP A 347      38.355  80.971   3.545  1.00 42.89           N  
ATOM   2131  CA  TRP A 347      37.523  80.049   4.326  1.00 43.53           C  
ATOM   2132  C   TRP A 347      38.185  78.817   4.910  1.00 43.04           C  
ATOM   2133  O   TRP A 347      37.777  78.310   5.948  1.00 41.63           O  
ATOM   2134  CB  TRP A 347      36.334  79.578   3.492  1.00 41.14           C  
ATOM   2135  CG  TRP A 347      35.499  80.654   2.970  1.00 37.89           C  
ATOM   2136  CD1 TRP A 347      35.672  81.331   1.799  1.00 38.54           C  
ATOM   2137  CD2 TRP A 347      34.321  81.184   3.579  1.00 36.99           C  
ATOM   2138  NE1 TRP A 347      34.661  82.255   1.636  1.00 38.07           N  
ATOM   2139  CE2 TRP A 347      33.818  82.182   2.715  1.00 36.91           C  
ATOM   2140  CE3 TRP A 347      33.638  80.912   4.772  1.00 36.31           C  
ATOM   2141  CZ2 TRP A 347      32.663  82.907   3.008  1.00 33.74           C  
ATOM   2142  CZ3 TRP A 347      32.496  81.627   5.060  1.00 34.71           C  
ATOM   2143  CH2 TRP A 347      32.018  82.615   4.179  1.00 35.44           C  
ATOM   2144  N   GLU A 348      39.202  78.339   4.226  1.00 44.97           N  
ATOM   2145  CA  GLU A 348      39.887  77.137   4.639  1.00 47.67           C  
ATOM   2146  C   GLU A 348      40.456  77.083   6.067  1.00 47.33           C  
ATOM   2147  O   GLU A 348      40.777  75.998   6.555  1.00 47.23           O  
ATOM   2148  CB  GLU A 348      40.963  76.831   3.604  1.00 50.73           C  
ATOM   2149  CG  GLU A 348      40.396  76.737   2.138  1.00 57.05           C  
ATOM   2150  CD  GLU A 348      39.956  78.088   1.520  1.00 58.78           C  
ATOM   2151  OE1 GLU A 348      40.681  79.088   1.706  1.00 60.59           O  
ATOM   2152  OE2 GLU A 348      38.902  78.152   0.828  1.00 60.05           O  
ATOM   2153  N   ASN A 349      40.530  78.212   6.771  1.00 46.52           N  
ATOM   2154  CA  ASN A 349      41.112  78.180   8.119  1.00 44.88           C  
ATOM   2155  C   ASN A 349      40.797  79.417   8.937  1.00 44.94           C  
ATOM   2156  O   ASN A 349      41.701  80.039   9.509  1.00 45.06           O  
ATOM   2157  CB  ASN A 349      42.621  78.077   8.005  1.00 43.37           C  
ATOM   2158  CG  ASN A 349      43.220  79.320   7.375  1.00 45.06           C  
ATOM   2159  OD1 ASN A 349      42.598  79.943   6.523  1.00 43.64           O  
ATOM   2160  ND2 ASN A 349      44.423  79.693   7.797  1.00 46.29           N  
ATOM   2161  N   LEU A 350      39.528  79.781   9.011  1.00 42.76           N  
ATOM   2162  CA  LEU A 350      39.186  80.961   9.769  1.00 40.39           C  
ATOM   2163  C   LEU A 350      39.631  80.817  11.208  1.00 41.91           C  
ATOM   2164  O   LEU A 350      40.019  81.798  11.849  1.00 42.37           O  
ATOM   2165  CB  LEU A 350      37.683  81.195   9.719  1.00 37.41           C  
ATOM   2166  CG  LEU A 350      37.136  81.496   8.338  1.00 35.37           C  
ATOM   2167  CD1 LEU A 350      35.670  81.223   8.310  1.00 32.37           C  
ATOM   2168  CD2 LEU A 350      37.440  82.932   7.981  1.00 35.19           C  
ATOM   2169  N   HIS A 351      39.577  79.593  11.718  1.00 43.51           N  
ATOM   2170  CA  HIS A 351      39.941  79.336  13.102  1.00 46.04           C  
ATOM   2171  C   HIS A 351      41.360  79.742  13.441  1.00 47.91           C  
ATOM   2172  O   HIS A 351      41.652  80.046  14.598  1.00 49.27           O  
ATOM   2173  CB  HIS A 351      39.780  77.868  13.418  1.00 49.27           C  
ATOM   2174  CG  HIS A 351      40.019  77.540  14.851  1.00 52.83           C  
ATOM   2175  ND1 HIS A 351      40.643  76.378  15.253  1.00 55.06           N  
ATOM   2176  CD2 HIS A 351      39.686  78.205  15.982  1.00 55.55           C  
ATOM   2177  CE1 HIS A 351      40.683  76.341  16.574  1.00 57.10           C  
ATOM   2178  NE2 HIS A 351      40.108  77.437  17.042  1.00 56.91           N  
ATOM   2179  N   GLN A 352      42.239  79.733  12.436  1.00 48.14           N  
ATOM   2180  CA  GLN A 352      43.643  80.088  12.612  1.00 46.86           C  
ATOM   2181  C   GLN A 352      43.966  81.547  12.380  1.00 46.90           C  
ATOM   2182  O   GLN A 352      45.076  81.983  12.653  1.00 48.76           O  
ATOM   2183  CB  GLN A 352      44.525  79.289  11.676  1.00 48.87           C  
ATOM   2184  CG  GLN A 352      45.144  78.077  12.301  1.00 51.39           C  
ATOM   2185  CD  GLN A 352      44.240  76.909  12.233  1.00 51.87           C  
ATOM   2186  OE1 GLN A 352      43.610  76.666  11.196  1.00 52.93           O  
ATOM   2187  NE2 GLN A 352      44.162  76.156  13.324  1.00 49.73           N  
ATOM   2188  N   GLN A 353      43.028  82.309  11.848  1.00 44.69           N  
ATOM   2189  CA  GLN A 353      43.304  83.710  11.625  1.00 42.43           C  
ATOM   2190  C   GLN A 353      43.099  84.469  12.919  1.00 42.54           C  
ATOM   2191  O   GLN A 353      42.483  83.971  13.853  1.00 44.20           O  
ATOM   2192  CB  GLN A 353      42.384  84.244  10.545  1.00 41.04           C  
ATOM   2193  CG  GLN A 353      42.654  83.623   9.224  1.00 40.07           C  
ATOM   2194  CD  GLN A 353      41.507  83.797   8.281  1.00 42.76           C  
ATOM   2195  OE1 GLN A 353      40.993  84.905   8.110  1.00 42.43           O  
ATOM   2196  NE2 GLN A 353      41.091  82.697   7.646  1.00 40.99           N  
ATOM   2197  N   THR A 354      43.619  85.680  12.972  1.00 42.31           N  
ATOM   2198  CA  THR A 354      43.479  86.511  14.147  1.00 43.04           C  
ATOM   2199  C   THR A 354      42.244  87.369  13.982  1.00 43.69           C  
ATOM   2200  O   THR A 354      42.126  88.073  12.984  1.00 43.33           O  
ATOM   2201  CB  THR A 354      44.653  87.452  14.273  1.00 44.71           C  
ATOM   2202  OG1 THR A 354      45.861  86.694  14.327  1.00 47.49           O  
ATOM   2203  CG2 THR A 354      44.520  88.283  15.523  1.00 44.83           C  
ATOM   2204  N   PRO A 355      41.304  87.325  14.951  1.00 44.55           N  
ATOM   2205  CA  PRO A 355      40.106  88.152  14.808  1.00 44.38           C  
ATOM   2206  C   PRO A 355      40.521  89.611  14.854  1.00 46.12           C  
ATOM   2207  O   PRO A 355      41.416  89.981  15.608  1.00 46.15           O  
ATOM   2208  CB  PRO A 355      39.266  87.766  16.022  1.00 41.91           C  
ATOM   2209  CG  PRO A 355      39.686  86.408  16.318  1.00 43.35           C  
ATOM   2210  CD  PRO A 355      41.183  86.456  16.133  1.00 43.32           C  
ATOM   2211  N   PRO A 356      39.875  90.457  14.046  1.00 47.67           N  
ATOM   2212  CA  PRO A 356      40.230  91.874  14.052  1.00 49.79           C  
ATOM   2213  C   PRO A 356      39.818  92.487  15.383  1.00 51.06           C  
ATOM   2214  O   PRO A 356      38.694  92.294  15.826  1.00 52.22           O  
ATOM   2215  CB  PRO A 356      39.437  92.428  12.860  1.00 49.24           C  
ATOM   2216  CG  PRO A 356      38.215  91.545  12.825  1.00 47.90           C  
ATOM   2217  CD  PRO A 356      38.768  90.181  13.108  1.00 47.98           C  
ATOM   2218  N   LYS A 357      40.723  93.201  16.038  1.00 53.34           N  
ATOM   2219  CA  LYS A 357      40.369  93.810  17.316  1.00 57.26           C  
ATOM   2220  C   LYS A 357      39.523  95.049  17.064  1.00 60.19           C  
ATOM   2221  O   LYS A 357      39.297  95.382  15.876  1.00 62.76           O  
ATOM   2222  CB  LYS A 357      41.621  94.186  18.106  1.00 56.86           C  
ATOM   2223  N   LEU A 358      39.100  95.673  18.060  1.00 62.78           N  
TER    2224      LEU A 358                                                      
HETATM 2225  C1  GOL A1358      25.158  60.751  32.087  1.00 63.43           C  
HETATM 2226  O1  GOL A1358      25.268  59.569  32.870  1.00 58.68           O  
HETATM 2227  C2  GOL A1358      23.686  61.050  31.792  1.00 65.04           C  
HETATM 2228  O2  GOL A1358      23.119  59.937  31.090  1.00 65.98           O  
HETATM 2229  C3  GOL A1358      23.582  62.338  30.940  1.00 67.03           C  
HETATM 2230  O3  GOL A1358      22.213  62.661  30.627  1.00 67.56           O  
HETATM 2231  C1  GOL A1359      26.144  70.203  42.829  1.00 72.60           C  
HETATM 2232  O1  GOL A1359      26.896  69.545  43.851  1.00 71.28           O  
HETATM 2233  C2  GOL A1359      24.781  70.569  43.307  1.00 73.33           C  
HETATM 2234  O2  GOL A1359      24.194  71.216  42.230  1.00 73.38           O  
HETATM 2235  C3  GOL A1359      24.868  71.509  44.487  1.00 73.87           C  
HETATM 2236  O3  GOL A1359      23.522  71.809  44.887  1.00 73.76           O  
HETATM 2237  C1  GOL A1360      20.037  76.685  29.469  1.00 80.98           C  
HETATM 2238  O1  GOL A1360      19.931  76.845  28.061  1.00 80.50           O  
HETATM 2239  C2  GOL A1360      20.875  77.803  30.091  1.00 81.19           C  
HETATM 2240  O2  GOL A1360      20.852  77.563  31.522  1.00 81.91           O  
HETATM 2241  C3  GOL A1360      20.286  79.207  29.829  1.00 80.91           C  
HETATM 2242  O3  GOL A1360      21.112  80.187  30.465  1.00 79.57           O  
HETATM 2243  C1  GOL A1361      14.417  95.790   1.810  1.00 58.99           C  
HETATM 2244  O1  GOL A1361      14.799  97.114   1.462  1.00 57.21           O  
HETATM 2245  C2  GOL A1361      12.903  95.725   1.817  1.00 59.35           C  
HETATM 2246  O2  GOL A1361      12.420  96.683   2.759  1.00 60.14           O  
HETATM 2247  C3  GOL A1361      12.457  94.314   2.204  1.00 60.02           C  
HETATM 2248  O3  GOL A1361      11.026  94.225   2.210  1.00 58.66           O  
HETATM 2249  C1  GOL A1362      31.634  72.606  46.155  1.00 64.96           C  
HETATM 2250  O1  GOL A1362      31.103  72.780  44.851  1.00 63.95           O  
HETATM 2251  C2  GOL A1362      31.509  73.924  46.907  1.00 65.98           C  
HETATM 2252  O2  GOL A1362      32.207  74.957  46.223  1.00 65.82           O  
HETATM 2253  C3  GOL A1362      32.079  73.773  48.308  1.00 68.03           C  
HETATM 2254  O3  GOL A1362      31.959  75.029  48.974  1.00 71.92           O  
HETATM 2255  C1  GOL A1363      38.810  72.557  29.631  1.00 50.01           C  
HETATM 2256  O1  GOL A1363      40.228  72.446  29.682  1.00 52.01           O  
HETATM 2257  C2  GOL A1363      38.460  73.930  29.105  1.00 50.11           C  
HETATM 2258  O2  GOL A1363      39.013  74.894  29.988  1.00 51.34           O  
HETATM 2259  C3  GOL A1363      36.949  74.085  29.042  1.00 49.56           C  
HETATM 2260  O3  GOL A1363      36.645  75.388  28.544  1.00 50.35           O  
HETATM 2261  C1  GOL A1364      38.221  76.228  10.470  1.00 38.64           C  
HETATM 2262  O1  GOL A1364      39.268  77.181  10.657  1.00 38.77           O  
HETATM 2263  C2  GOL A1364      37.776  76.241   8.996  1.00 42.78           C  
HETATM 2264  O2  GOL A1364      37.310  77.553   8.589  1.00 44.20           O  
HETATM 2265  C3  GOL A1364      36.656  75.220   8.783  1.00 40.84           C  
HETATM 2266  O3  GOL A1364      35.559  75.564   9.616  1.00 40.07           O  
HETATM 2267  S   SO4 A1365      37.589  75.052  24.784  1.00 60.32           S  
HETATM 2268  O1  SO4 A1365      37.572  75.841  23.540  1.00 62.89           O  
HETATM 2269  O2  SO4 A1365      36.433  74.142  24.794  1.00 59.60           O  
HETATM 2270  O3  SO4 A1365      37.546  75.956  25.949  1.00 60.47           O  
HETATM 2271  O4  SO4 A1365      38.834  74.275  24.849  1.00 62.54           O  
HETATM 2272  S   SO4 A1366      43.684  72.101  28.874  1.00 69.37           S  
HETATM 2273  O1  SO4 A1366      43.707  73.538  29.216  1.00 68.12           O  
HETATM 2274  O2  SO4 A1366      43.676  71.307  30.113  1.00 70.97           O  
HETATM 2275  O3  SO4 A1366      44.880  71.740  28.090  1.00 68.41           O  
HETATM 2276  O4  SO4 A1366      42.453  71.794  28.111  1.00 69.69           O  
HETATM 2277  S   SO4 A1367      16.338  76.109  29.586  1.00 92.09           S  
HETATM 2278  O1  SO4 A1367      15.318  75.104  29.231  1.00 93.40           O  
HETATM 2279  O2  SO4 A1367      17.563  75.791  28.843  1.00 92.50           O  
HETATM 2280  O3  SO4 A1367      16.619  76.042  31.034  1.00 91.13           O  
HETATM 2281  O4  SO4 A1367      15.851  77.455  29.214  1.00 91.64           O  
HETATM 2282  CBD BI1 A1368      21.211  82.732  28.917  1.00 68.53           C  
HETATM 2283  NBC BI1 A1368      22.013  83.172  27.767  1.00 68.16           N  
HETATM 2284  CBE BI1 A1368      21.324  83.321  26.475  1.00 68.44           C  
HETATM 2285  CBB BI1 A1368      23.443  82.811  27.794  1.00 65.34           C  
HETATM 2286  CBA BI1 A1368      24.033  82.473  26.421  1.00 61.14           C  
HETATM 2287  CAY BI1 A1368      23.599  81.101  25.894  1.00 53.65           C  
HETATM 2288  NAH BI1 A1368      24.345  79.975  26.479  1.00 50.74           N  
HETATM 2289  CAW BI1 A1368      25.627  80.029  26.854  1.00 50.91           C  
HETATM 2290  CAE BI1 A1368      23.838  78.750  26.607  1.00 49.51           C  
HETATM 2291  CAF BI1 A1368      22.600  78.179  26.329  1.00 49.09           C  
HETATM 2292  CAA BI1 A1368      22.415  76.816  26.539  1.00 50.27           C  
HETATM 2293  CAB BI1 A1368      23.461  76.036  27.026  1.00 50.31           C  
HETATM 2294  CAC BI1 A1368      24.695  76.618  27.306  1.00 49.26           C  
HETATM 2295  CAD BI1 A1368      24.886  77.979  27.095  1.00 48.06           C  
HETATM 2296  CAG BI1 A1368      25.991  78.806  27.239  1.00 49.01           C  
HETATM 2297  CAI BI1 A1368      27.307  78.540  27.612  1.00 47.54           C  
HETATM 2298  CAT BI1 A1368      28.014  77.401  27.233  1.00 46.36           C  
HETATM 2299  OAZ BI1 A1368      27.604  76.438  26.591  1.00 44.28           O  
HETATM 2300  NAU BI1 A1368      29.257  77.583  27.677  1.00 46.45           N  
HETATM 2301  CAV BI1 A1368      29.433  78.740  28.314  1.00 47.61           C  
HETATM 2302  OAX BI1 A1368      30.481  79.168  28.791  1.00 47.90           O  
HETATM 2303  CAJ BI1 A1368      28.192  79.369  28.292  1.00 48.30           C  
HETATM 2304  CAK BI1 A1368      27.916  80.588  28.910  1.00 49.21           C  
HETATM 2305  CAM BI1 A1368      26.809  81.066  29.592  1.00 47.19           C  
HETATM 2306  CAP BI1 A1368      25.564  80.518  29.890  1.00 47.05           C  
HETATM 2307  CAQ BI1 A1368      24.627  81.267  30.596  1.00 49.31           C  
HETATM 2308  CAR BI1 A1368      24.930  82.562  31.010  1.00 47.76           C  
HETATM 2309  CAS BI1 A1368      26.175  83.110  30.719  1.00 48.79           C  
HETATM 2310  CAN BI1 A1368      27.106  82.355  30.010  1.00 48.17           C  
HETATM 2311  NAO BI1 A1368      28.346  82.594  29.583  1.00 49.87           N  
HETATM 2312  CAL BI1 A1368      28.843  81.543  28.925  1.00 50.14           C  
HETATM 2313  O   HOH A2001      31.254  61.168  30.316  1.00 30.48           O  
HETATM 2314  O   HOH A2002      31.798  61.792  33.497  1.00 40.82           O  
HETATM 2315  O   HOH A2003      38.406  66.622  40.456  1.00 42.36           O  
HETATM 2316  O   HOH A2004      33.554  81.556  40.093  1.00 39.59           O  
HETATM 2317  O   HOH A2005      15.357  71.308  35.349  1.00 44.33           O  
HETATM 2318  O   HOH A2006      38.434  64.928  38.343  1.00 37.12           O  
HETATM 2319  O   HOH A2007      44.545  73.268  34.812  1.00 48.69           O  
HETATM 2320  O   HOH A2008      15.054  62.673  21.139  1.00 41.30           O  
HETATM 2321  O   HOH A2009      17.388  71.752  27.330  1.00 41.48           O  
HETATM 2322  O   HOH A2010      22.942  57.828  29.198  1.00 44.09           O  
HETATM 2323  O   HOH A2011      31.132  67.937  21.958  1.00 40.35           O  
HETATM 2324  O   HOH A2012      33.143  70.685  18.704  1.00 48.51           O  
HETATM 2325  O   HOH A2013      32.365  69.689   6.589  1.00 41.57           O  
HETATM 2326  O   HOH A2014      30.567  70.177   4.871  1.00 42.00           O  
HETATM 2327  O   HOH A2015      30.736  70.191  20.215  1.00 42.45           O  
HETATM 2328  O   HOH A2016      22.894  61.546  44.366  1.00 44.72           O  
HETATM 2329  O   HOH A2017      36.449  97.936   8.114  1.00 42.19           O  
HETATM 2330  O   HOH A2018      38.169  92.401   5.336  1.00 37.73           O  
HETATM 2331  O   HOH A2019      34.704  77.231   5.658  1.00 38.39           O  
HETATM 2332  O   HOH A2020      32.697  74.341   7.478  1.00 42.33           O  
HETATM 2333  O   HOH A2021      30.012  68.614   7.943  1.00 37.38           O  
HETATM 2334  O   HOH A2022      28.134  62.400  12.042  1.00 46.62           O  
HETATM 2335  O   HOH A2023      37.396  80.630  25.991  1.00 36.59           O  
HETATM 2336  O   HOH A2024      18.850  74.857  19.424  1.00 34.80           O  
HETATM 2337  O   HOH A2025      14.605  81.990  16.246  1.00 47.17           O  
HETATM 2338  O   HOH A2026      12.888  88.452  19.979  1.00 45.69           O  
HETATM 2339  O   HOH A2027      11.634  94.364  19.064  1.00 39.56           O  
HETATM 2340  O   HOH A2028      14.561  90.954  14.154  1.00 33.77           O  
HETATM 2341  O   HOH A2029      23.783  71.423   3.504  1.00 35.47           O  
HETATM 2342  O   HOH A2030      16.159  71.382   5.331  1.00 44.80           O  
HETATM 2343  O   HOH A2031      17.679  79.210  13.831  1.00 29.61           O  
HETATM 2344  O   HOH A2032      12.918  86.681  11.756  1.00 38.49           O  
HETATM 2345  O   HOH A2033       5.232  89.757  23.535  1.00 42.04           O  
HETATM 2346  O   HOH A2034      15.451  99.407   3.217  1.00 43.80           O  
HETATM 2347  O   HOH A2035      18.846 105.983   8.003  0.50 36.78           O  
HETATM 2348  O   HOH A2036      20.287  89.660  -8.117  1.00 47.80           O  
HETATM 2349  O   HOH A2037      11.045  87.513  -0.769  1.00 41.35           O  
HETATM 2350  O   HOH A2038      16.536  74.589   2.767  1.00 38.23           O  
HETATM 2351  O   HOH A2039      27.836  74.320  -3.191  1.00 32.29           O  
HETATM 2352  O   HOH A2040      23.388  78.888  -2.559  1.00 28.63           O  
HETATM 2353  O   HOH A2041      26.940  83.987  -5.786  1.00 44.43           O  
HETATM 2354  O   HOH A2042      33.361  85.406  -1.451  1.00 40.47           O  
HETATM 2355  O   HOH A2043      36.279  84.222  -0.682  1.00 40.86           O  
HETATM 2356  O   HOH A2044      39.306  80.477   0.196  1.00 36.81           O  
HETATM 2357  O   HOH A2045      39.012  98.145  18.344  1.00 49.41           O  
HETATM 2358  O   HOH A2046      36.801  96.633  19.518  1.00 51.67           O  
HETATM 2359  O   HOH A2047      41.077  76.011  32.057  1.00 35.42           O  
CONECT 1294 1300                                                                
CONECT 1300 1294 1301                                                           
CONECT 1301 1300 1302 1304                                                      
CONECT 1302 1301 1303                                                           
CONECT 1303 1302 1306                                                           
CONECT 1304 1301 1305 1310                                                      
CONECT 1305 1304                                                                
CONECT 1306 1303 1307 1308 1309                                                 
CONECT 1307 1306                                                                
CONECT 1308 1306                                                                
CONECT 1309 1306                                                                
CONECT 1310 1304                                                                
CONECT 2225 2226 2227                                                           
CONECT 2226 2225                                                                
CONECT 2227 2225 2228 2229                                                      
CONECT 2228 2227                                                                
CONECT 2229 2227 2230                                                           
CONECT 2230 2229                                                                
CONECT 2231 2232 2233                                                           
CONECT 2232 2231                                                                
CONECT 2233 2231 2234 2235                                                      
CONECT 2234 2233                                                                
CONECT 2235 2233 2236                                                           
CONECT 2236 2235                                                                
CONECT 2237 2238 2239                                                           
CONECT 2238 2237                                                                
CONECT 2239 2237 2240 2241                                                      
CONECT 2240 2239                                                                
CONECT 2241 2239 2242                                                           
CONECT 2242 2241                                                                
CONECT 2243 2244 2245                                                           
CONECT 2244 2243                                                                
CONECT 2245 2243 2246 2247                                                      
CONECT 2246 2245                                                                
CONECT 2247 2245 2248                                                           
CONECT 2248 2247                                                                
CONECT 2249 2250 2251                                                           
CONECT 2250 2249                                                                
CONECT 2251 2249 2252 2253                                                      
CONECT 2252 2251                                                                
CONECT 2253 2251 2254                                                           
CONECT 2254 2253                                                                
CONECT 2255 2256 2257                                                           
CONECT 2256 2255                                                                
CONECT 2257 2255 2258 2259                                                      
CONECT 2258 2257                                                                
CONECT 2259 2257 2260                                                           
CONECT 2260 2259                                                                
CONECT 2261 2262 2263                                                           
CONECT 2262 2261                                                                
CONECT 2263 2261 2264 2265                                                      
CONECT 2264 2263                                                                
CONECT 2265 2263 2266                                                           
CONECT 2266 2265                                                                
CONECT 2267 2268 2269 2270 2271                                                 
CONECT 2268 2267                                                                
CONECT 2269 2267                                                                
CONECT 2270 2267                                                                
CONECT 2271 2267                                                                
CONECT 2272 2273 2274 2275 2276                                                 
CONECT 2273 2272                                                                
CONECT 2274 2272                                                                
CONECT 2275 2272                                                                
CONECT 2276 2272                                                                
CONECT 2277 2278 2279 2280 2281                                                 
CONECT 2278 2277                                                                
CONECT 2279 2277                                                                
CONECT 2280 2277                                                                
CONECT 2281 2277                                                                
CONECT 2282 2283                                                                
CONECT 2283 2282 2284 2285                                                      
CONECT 2284 2283                                                                
CONECT 2285 2283 2286                                                           
CONECT 2286 2285 2287                                                           
CONECT 2287 2286 2288                                                           
CONECT 2288 2287 2289 2290                                                      
CONECT 2289 2288 2296                                                           
CONECT 2290 2288 2291 2295                                                      
CONECT 2291 2290 2292                                                           
CONECT 2292 2291 2293                                                           
CONECT 2293 2292 2294                                                           
CONECT 2294 2293 2295                                                           
CONECT 2295 2290 2294 2296                                                      
CONECT 2296 2289 2295 2297                                                      
CONECT 2297 2296 2298 2303                                                      
CONECT 2298 2297 2299 2300                                                      
CONECT 2299 2298                                                                
CONECT 2300 2298 2301                                                           
CONECT 2301 2300 2302 2303                                                      
CONECT 2302 2301                                                                
CONECT 2303 2297 2301 2304                                                      
CONECT 2304 2303 2305 2312                                                      
CONECT 2305 2304 2306 2310                                                      
CONECT 2306 2305 2307                                                           
CONECT 2307 2306 2308                                                           
CONECT 2308 2307 2309                                                           
CONECT 2309 2308 2310                                                           
CONECT 2310 2305 2309 2311                                                      
CONECT 2311 2310 2312                                                           
CONECT 2312 2304 2311                                                           
MASTER      380    0   12   14    9    0   23    6 2356    1  100   24          
END                                                                             
