HEADER    SIGNALING PROTEIN                       04-SEP-18   6AKY              
TITLE     THE CRYSTAL STRUCTURE OF HUMAN CHEMOKINE RECEPTOR CCR5 IN COMPLEX WITH
TITLE    2 COMPOUND 34                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C-C CHEMOKINE RECEPTOR TYPE 5,RUBREDOXIN,C-C CHEMOKINE     
COMPND   3 RECEPTOR TYPE 5;                                                     
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: CCR5,CHEMR13,HIV-1 FUSION CORECEPTOR,RD;                    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: CHIMERA PROTEIN OF C-C CHEMOKINE RECEPTOR TYPE 5 AND  
COMPND   9 RUBREDOXIN. RUBREDOXIN WAS INSERTED INTO CCR5 BETWEEN RESIDUE 223 AND
COMPND  10 227.                                                                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, CLOSTRIDIUM PASTEURIANUM;         
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 1501;                                          
SOURCE   5 GENE: CCR5, CMKBR5;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    G PROTEIN-COUPLED RECEPTOR CHEMOKINE RECEPTOR CCR5 ANTAGONIST COMPLEX 
KEYWDS   2 STRUCTURE, SIGNALING PROTEIN                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHU,Q.ZHAO,B.WU                                                     
REVDAT   2   21-NOV-18 6AKY    1       JRNL                                     
REVDAT   1   24-OCT-18 6AKY    0                                                
JRNL        AUTH   P.PENG,H.CHEN,Y.ZHU,Z.WANG,J.LI,R.H.LUO,J.WANG,L.CHEN,       
JRNL        AUTH 2 L.M.YANG,H.JIANG,X.XIE,B.WU,Y.T.ZHENG,H.LIU                  
JRNL        TITL   STRUCTURE-BASED DESIGN OF 1-HETEROARYL-1,3-PROPANEDIAMINE    
JRNL        TITL 2 DERIVATIVES AS A NOVEL SERIES OF CC-CHEMOKINE RECEPTOR 5     
JRNL        TITL 3 ANTAGONISTS.                                                 
JRNL        REF    J. MED. CHEM.                 V.  61  9621 2018              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   30234300                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.8B01077                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.56                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 12401                          
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)  : 0.275                          
REMARK   3   R VALUE            (WORKING SET)  : 0.275                          
REMARK   3   FREE R VALUE                      : 0.283                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.150                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 639                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 6                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.07                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 95.59                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2863                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2789                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2700                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2781                   
REMARK   3   BIN FREE R VALUE                        : 0.2919                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.69                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 163                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2657                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 49                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 82.94                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 82.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.54370                                              
REMARK   3    B22 (A**2) : 2.90720                                              
REMARK   3    B33 (A**2) : -3.45090                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.540               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 1.059               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.370               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 1.016               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.373               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.905                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2779   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3796   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 887    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 48     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 402    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2779   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 375    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 3218   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.00                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.05                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.89                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6AKY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-SEP-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300008970.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12438                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4MBS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400, HEPES, AMMONIUM ACETATE,         
REMARK 280  LIPIDIC CUBIC PHASE, TEMPERATURE 293K                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
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  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.74150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.28450            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.74150            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       68.28450            
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     TYR A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     ILE A     9                                                      
REMARK 465     TYR A    10                                                      
REMARK 465     ASP A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     ASN A    13                                                      
REMARK 465     TYR A    14                                                      
REMARK 465     TYR A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     GLU A    18                                                      
REMARK 465     PRO A    19                                                      
REMARK 465     LEU A   309                                                      
REMARK 465     VAL A   310                                                      
REMARK 465     PHE A   311                                                      
REMARK 465     PHE A   312                                                      
REMARK 465     GLN A   313                                                      
REMARK 465     LYS A   314                                                      
REMARK 465     HIS A   315                                                      
REMARK 465     ILE A   316                                                      
REMARK 465     ALA A   317                                                      
REMARK 465     LYS A   318                                                      
REMARK 465     ARG A   319                                                      
REMARK 465     GLY A   320                                                      
REMARK 465     ARG A   321                                                      
REMARK 465     PRO A   322                                                      
REMARK 465     LEU A   323                                                      
REMARK 465     GLU A   324                                                      
REMARK 465     VAL A   325                                                      
REMARK 465     LEU A   326                                                      
REMARK 465     PHE A   327                                                      
REMARK 465     GLN A   328                                                      
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  21    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  22    CG   CD   CE   NZ                                   
REMARK 470     TYR A  58    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A  59    CD   CE   NZ                                        
REMARK 470     LYS A 138    CG   CD   CE   NZ                                   
REMARK 470     HIS A 175    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 191    CD   CE   NZ                                        
REMARK 470     ARG A 223    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1002    CG   CD   CE   NZ                                   
REMARK 470     LYS A1031    CG   CD   CE   NZ                                   
REMARK 470     GLN A1048    CG   CD   OE1  NE2                                  
REMARK 470     GLU A1053    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 227    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 232    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 233    CG   OD1  OD2                                       
REMARK 470     ARG A 235    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 262    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 263    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 266    CG   CD1  CD2                                       
REMARK 470     PHE A 304    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TYR A 307    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 308    CG   CD1  CD2                                       
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    TYR A  58      -58.39   -122.43                                   
REMARK 500    LEU A  61       72.51     30.31                                   
REMARK 500    ALA A  92     -101.51   -130.40                                   
REMARK 500    VAL A 130      -71.61    -70.07                                   
REMARK 500    ARG A 140       51.30   -154.12                                   
REMARK 500    LEU A 203      -66.58   -127.56                                   
REMARK 500    ASP A1019       75.14   -155.32                                   
REMARK 500    PRO A1040        1.88    -69.05                                   
REMARK 500    GLN A1048       35.28    -86.91                                   
REMARK 500    PHE A 260       51.79   -104.19                                   
REMARK 500    PHE A 263       -9.79     61.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLC A 2002                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1006   SG                                                     
REMARK 620 2 CYS A1009   SG   94.4                                              
REMARK 620 3 CYS A1039   SG  109.1 102.3                                        
REMARK 620 4 CYS A1042   SG  110.4 126.0 112.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue A4X A 2003                
DBREF  6AKY A    2   223  UNP    P51681   CCR5_HUMAN       2    223             
DBREF  6AKY A 1001  1054  UNP    P00268   RUBR_CLOPA       1     54             
DBREF  6AKY A  227   319  UNP    P51681   CCR5_HUMAN     227    319             
SEQADV 6AKY GLY A   -1  UNP  P51681              EXPRESSION TAG                 
SEQADV 6AKY ALA A    0  UNP  P51681              EXPRESSION TAG                 
SEQADV 6AKY PRO A    1  UNP  P51681              EXPRESSION TAG                 
SEQADV 6AKY TYR A   58  UNP  P51681    CYS    58 ENGINEERED MUTATION            
SEQADV 6AKY ASN A  163  UNP  P51681    GLY   163 ENGINEERED MUTATION            
SEQADV 6AKY ASP A  233  UNP  P51681    ALA   233 ENGINEERED MUTATION            
SEQADV 6AKY GLU A  303  UNP  P51681    LYS   303 ENGINEERED MUTATION            
SEQADV 6AKY GLY A  320  UNP  P51681              EXPRESSION TAG                 
SEQADV 6AKY ARG A  321  UNP  P51681              EXPRESSION TAG                 
SEQADV 6AKY PRO A  322  UNP  P51681              EXPRESSION TAG                 
SEQADV 6AKY LEU A  323  UNP  P51681              EXPRESSION TAG                 
SEQADV 6AKY GLU A  324  UNP  P51681              EXPRESSION TAG                 
SEQADV 6AKY VAL A  325  UNP  P51681              EXPRESSION TAG                 
SEQADV 6AKY LEU A  326  UNP  P51681              EXPRESSION TAG                 
SEQADV 6AKY PHE A  327  UNP  P51681              EXPRESSION TAG                 
SEQADV 6AKY GLN A  328  UNP  P51681              EXPRESSION TAG                 
SEQRES   1 A  381  GLY ALA PRO ASP TYR GLN VAL SER SER PRO ILE TYR ASP          
SEQRES   2 A  381  ILE ASN TYR TYR THR SER GLU PRO CYS GLN LYS ILE ASN          
SEQRES   3 A  381  VAL LYS GLN ILE ALA ALA ARG LEU LEU PRO PRO LEU TYR          
SEQRES   4 A  381  SER LEU VAL PHE ILE PHE GLY PHE VAL GLY ASN MET LEU          
SEQRES   5 A  381  VAL ILE LEU ILE LEU ILE ASN TYR LYS ARG LEU LYS SER          
SEQRES   6 A  381  MET THR ASP ILE TYR LEU LEU ASN LEU ALA ILE SER ASP          
SEQRES   7 A  381  LEU PHE PHE LEU LEU THR VAL PRO PHE TRP ALA HIS TYR          
SEQRES   8 A  381  ALA ALA ALA GLN TRP ASP PHE GLY ASN THR MET CYS GLN          
SEQRES   9 A  381  LEU LEU THR GLY LEU TYR PHE ILE GLY PHE PHE SER GLY          
SEQRES  10 A  381  ILE PHE PHE ILE ILE LEU LEU THR ILE ASP ARG TYR LEU          
SEQRES  11 A  381  ALA VAL VAL HIS ALA VAL PHE ALA LEU LYS ALA ARG THR          
SEQRES  12 A  381  VAL THR PHE GLY VAL VAL THR SER VAL ILE THR TRP VAL          
SEQRES  13 A  381  VAL ALA VAL PHE ALA SER LEU PRO ASN ILE ILE PHE THR          
SEQRES  14 A  381  ARG SER GLN LYS GLU GLY LEU HIS TYR THR CYS SER SER          
SEQRES  15 A  381  HIS PHE PRO TYR SER GLN TYR GLN PHE TRP LYS ASN PHE          
SEQRES  16 A  381  GLN THR LEU LYS ILE VAL ILE LEU GLY LEU VAL LEU PRO          
SEQRES  17 A  381  LEU LEU VAL MET VAL ILE CYS TYR SER GLY ILE LEU LYS          
SEQRES  18 A  381  THR LEU LEU ARG MET LYS LYS TYR THR CYS THR VAL CYS          
SEQRES  19 A  381  GLY TYR ILE TYR ASN PRO GLU ASP GLY ASP PRO ASP ASN          
SEQRES  20 A  381  GLY VAL ASN PRO GLY THR ASP PHE LYS ASP ILE PRO ASP          
SEQRES  21 A  381  ASP TRP VAL CYS PRO LEU CYS GLY VAL GLY LYS ASP GLN          
SEQRES  22 A  381  PHE GLU GLU VAL GLU GLU GLU LYS LYS ARG HIS ARG ASP          
SEQRES  23 A  381  VAL ARG LEU ILE PHE THR ILE MET ILE VAL TYR PHE LEU          
SEQRES  24 A  381  PHE TRP ALA PRO TYR ASN ILE VAL LEU LEU LEU ASN THR          
SEQRES  25 A  381  PHE GLN GLU PHE PHE GLY LEU ASN ASN CYS SER SER SER          
SEQRES  26 A  381  ASN ARG LEU ASP GLN ALA MET GLN VAL THR GLU THR LEU          
SEQRES  27 A  381  GLY MET THR HIS CYS CYS ILE ASN PRO ILE ILE TYR ALA          
SEQRES  28 A  381  PHE VAL GLY GLU GLU PHE ARG ASN TYR LEU LEU VAL PHE          
SEQRES  29 A  381  PHE GLN LYS HIS ILE ALA LYS ARG GLY ARG PRO LEU GLU          
SEQRES  30 A  381  VAL LEU PHE GLN                                              
HET     ZN  A2001       1                                                       
HET    OLC  A2002      12                                                       
HET    A4X  A2003      36                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     A4X 4,4-DIFLUORO-N-[(1S)-3-{(3-EXO)-3-[3-METHYL-5-(PROPAN-           
HETNAM   2 A4X  2-YL)-4H-1,2,4-TRIAZOL-4-YL]-8-AZABICYCLO[3.2.1]OCTAN-          
HETNAM   3 A4X  8-YL}-1-(THIOPHEN-3-YL)PROPYL]CYCLOHEXANE-1-                    
HETNAM   4 A4X  CARBOXAMIDE                                                     
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  OLC    C21 H40 O4                                                   
FORMUL   4  A4X    C27 H39 F2 N5 O S                                            
HELIX    1 AA1 VAL A   25  TYR A   58  1                                  34    
HELIX    2 AA2 SER A   63  ALA A   92  1                                  30    
HELIX    3 AA3 PHE A   96  VAL A  131  1                                  36    
HELIX    4 AA4 HIS A  132  ALA A  139  1                                   8    
HELIX    5 AA5 THR A  141  PHE A  166  1                                  26    
HELIX    6 AA6 PRO A  183  SER A  185  5                                   3    
HELIX    7 AA7 GLN A  186  LEU A  203  1                                  18    
HELIX    8 AA8 LEU A  203  MET A 1001  1                                  22    
HELIX    9 AA9 GLY A 1045  ASP A 1047  5                                   3    
HELIX   10 AB1 HIS A  231  PHE A  260  1                                  30    
HELIX   11 AB2 ASN A  268  HIS A  289  1                                  22    
HELIX   12 AB3 ILE A  292  VAL A  300  1                                   9    
HELIX   13 AB4 GLY A  301  LEU A  308  1                                   8    
SHEET    1 AA1 2 THR A 167  GLU A 172  0                                        
SHEET    2 AA1 2 HIS A 175  SER A 180 -1  O  HIS A 175   N  GLU A 172           
SHEET    1 AA2 3 ILE A1012  TYR A1013  0                                        
SHEET    2 AA2 3 TYR A1004  CYS A1006 -1  N  TYR A1004   O  TYR A1013           
SHEET    3 AA2 3 PHE A1049  GLU A1051 -1  O  GLU A1050   N  THR A1005           
SSBOND   1 CYS A   20    CYS A  269                          1555   1555  2.03  
SSBOND   2 CYS A  101    CYS A  178                          1555   1555  2.05  
LINK         SG  CYS A1006                ZN    ZN A2001     1555   1555  2.69  
LINK         SG  CYS A1009                ZN    ZN A2001     1555   1555  2.76  
LINK         SG  CYS A1039                ZN    ZN A2001     1555   1555  2.37  
LINK         SG  CYS A1042                ZN    ZN A2001     1555   1555  2.36  
SITE     1 AC1  4 CYS A1006  CYS A1009  CYS A1039  CYS A1042                    
SITE     1 AC2  2 PRO A 250  ILE A 253                                          
SITE     1 AC3 12 TYR A  37  TYR A  89  TYR A 108  PHE A 109                    
SITE     2 AC3 12 PHE A 112  PHE A 182  LYS A 191  THR A 195                    
SITE     3 AC3 12 ILE A 198  TYR A 251  THR A 259  GLU A 283                    
CRYST1   35.585  101.483  136.569  90.00  90.00  90.00 P 2 21 21     4          
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      0.028102  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009854  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007322        0.00000                         
ATOM      1  N   CYS A  20      -9.345  11.199  -0.971  1.00115.98           N  
ATOM      2  CA  CYS A  20      -9.684  11.482   0.420  1.00115.81           C  
ATOM      3  C   CYS A  20      -9.657  12.984   0.747  1.00120.11           C  
ATOM      4  O   CYS A  20      -8.924  13.751   0.112  1.00119.97           O  
ATOM      5  CB  CYS A  20      -8.784  10.689   1.364  1.00116.15           C  
ATOM      6  SG  CYS A  20      -9.210  10.857   3.120  1.00119.85           S  
ATOM      7  N   GLN A  21     -10.465  13.389   1.752  1.00116.45           N  
ATOM      8  CA  GLN A  21     -10.586  14.760   2.259  1.00115.96           C  
ATOM      9  C   GLN A  21     -11.119  14.784   3.706  1.00118.50           C  
ATOM     10  O   GLN A  21     -12.023  14.014   4.049  1.00118.07           O  
ATOM     11  CB  GLN A  21     -11.485  15.608   1.343  1.00117.36           C  
ATOM     12  N   LYS A  22     -10.554  15.681   4.545  1.00113.52           N  
ATOM     13  CA  LYS A  22     -10.943  15.866   5.947  1.00112.38           C  
ATOM     14  C   LYS A  22     -12.299  16.597   6.088  1.00113.77           C  
ATOM     15  O   LYS A  22     -12.789  17.193   5.125  1.00112.70           O  
ATOM     16  CB  LYS A  22      -9.828  16.577   6.734  1.00114.78           C  
ATOM     17  N   ILE A  23     -12.902  16.529   7.294  1.00109.08           N  
ATOM     18  CA  ILE A  23     -14.204  17.125   7.633  1.00108.20           C  
ATOM     19  C   ILE A  23     -14.055  18.532   8.268  1.00110.25           C  
ATOM     20  O   ILE A  23     -13.080  18.794   8.979  1.00109.89           O  
ATOM     21  CB  ILE A  23     -15.052  16.130   8.507  1.00111.41           C  
ATOM     22  CG1 ILE A  23     -16.516  16.610   8.699  1.00111.63           C  
ATOM     23  CG2 ILE A  23     -14.381  15.791   9.856  1.00112.44           C  
ATOM     24  CD1 ILE A  23     -17.575  15.515   8.648  1.00117.03           C  
ATOM     25  N   ASN A  24     -15.023  19.430   7.981  1.00105.13           N  
ATOM     26  CA  ASN A  24     -15.091  20.793   8.513  1.00104.23           C  
ATOM     27  C   ASN A  24     -15.958  20.781   9.772  1.00105.79           C  
ATOM     28  O   ASN A  24     -17.178  20.593   9.692  1.00105.85           O  
ATOM     29  CB  ASN A  24     -15.655  21.765   7.457  1.00106.99           C  
ATOM     30  CG  ASN A  24     -15.889  23.178   7.954  1.00135.59           C  
ATOM     31  OD1 ASN A  24     -14.986  24.027   7.943  1.00132.58           O  
ATOM     32  ND2 ASN A  24     -17.117  23.470   8.374  1.00125.57           N  
ATOM     33  N   VAL A  25     -15.318  20.971  10.931  1.00100.15           N  
ATOM     34  CA  VAL A  25     -15.985  20.981  12.238  1.00 99.00           C  
ATOM     35  C   VAL A  25     -16.099  22.403  12.821  1.00101.08           C  
ATOM     36  O   VAL A  25     -16.726  22.577  13.871  1.00101.23           O  
ATOM     37  CB  VAL A  25     -15.371  19.975  13.256  1.00102.58           C  
ATOM     38  CG1 VAL A  25     -15.709  18.535  12.884  1.00102.35           C  
ATOM     39  CG2 VAL A  25     -13.863  20.165  13.409  1.00102.38           C  
ATOM     40  N   LYS A  26     -15.503  23.411  12.132  1.00 95.43           N  
ATOM     41  CA  LYS A  26     -15.505  24.834  12.515  1.00 94.26           C  
ATOM     42  C   LYS A  26     -16.924  25.360  12.784  1.00 94.83           C  
ATOM     43  O   LYS A  26     -17.140  26.013  13.803  1.00 94.36           O  
ATOM     44  CB  LYS A  26     -14.807  25.701  11.441  1.00 97.27           C  
ATOM     45  CG  LYS A  26     -13.294  25.546  11.390  1.00115.49           C  
ATOM     46  CD  LYS A  26     -12.573  26.787  11.901  1.00125.29           C  
ATOM     47  CE  LYS A  26     -11.076  26.697  11.708  1.00136.07           C  
ATOM     48  NZ  LYS A  26     -10.685  26.841  10.277  1.00145.57           N  
ATOM     49  N   GLN A  27     -17.883  25.047  11.887  1.00 88.78           N  
ATOM     50  CA  GLN A  27     -19.284  25.447  12.008  1.00 87.48           C  
ATOM     51  C   GLN A  27     -19.922  24.921  13.311  1.00 87.05           C  
ATOM     52  O   GLN A  27     -20.629  25.668  13.989  1.00 86.94           O  
ATOM     53  CB  GLN A  27     -20.075  24.988  10.763  1.00 89.13           C  
ATOM     54  CG  GLN A  27     -21.569  25.380  10.744  1.00104.45           C  
ATOM     55  CD  GLN A  27     -21.841  26.864  10.592  1.00121.62           C  
ATOM     56  OE1 GLN A  27     -20.969  27.663  10.218  1.00115.49           O  
ATOM     57  NE2 GLN A  27     -23.084  27.259  10.853  1.00112.45           N  
ATOM     58  N   ILE A  28     -19.652  23.657  13.666  1.00 79.62           N  
ATOM     59  CA  ILE A  28     -20.173  23.042  14.889  1.00 77.91           C  
ATOM     60  C   ILE A  28     -19.453  23.618  16.127  1.00 78.51           C  
ATOM     61  O   ILE A  28     -20.127  24.133  17.024  1.00 78.22           O  
ATOM     62  CB  ILE A  28     -20.126  21.478  14.832  1.00 80.74           C  
ATOM     63  CG1 ILE A  28     -20.811  20.926  13.562  1.00 80.80           C  
ATOM     64  CG2 ILE A  28     -20.723  20.833  16.096  1.00 81.00           C  
ATOM     65  CD1 ILE A  28     -19.865  20.434  12.509  1.00 88.08           C  
ATOM     66  N   ALA A  29     -18.092  23.553  16.149  1.00 71.50           N  
ATOM     67  CA  ALA A  29     -17.233  24.004  17.254  1.00 69.42           C  
ATOM     68  C   ALA A  29     -17.394  25.481  17.638  1.00 68.92           C  
ATOM     69  O   ALA A  29     -17.292  25.796  18.819  1.00 67.98           O  
ATOM     70  CB  ALA A  29     -15.776  23.684  16.960  1.00 70.05           C  
ATOM     71  N   ALA A  30     -17.676  26.371  16.665  1.00 62.85           N  
ATOM     72  CA  ALA A  30     -17.888  27.803  16.916  1.00 62.26           C  
ATOM     73  C   ALA A  30     -19.206  28.093  17.643  1.00 65.85           C  
ATOM     74  O   ALA A  30     -19.402  29.193  18.163  1.00 64.77           O  
ATOM     75  CB  ALA A  30     -17.837  28.577  15.614  1.00 62.96           C  
ATOM     76  N   ARG A  31     -20.115  27.112  17.650  1.00 62.99           N  
ATOM     77  CA  ARG A  31     -21.411  27.196  18.323  1.00 62.80           C  
ATOM     78  C   ARG A  31     -21.392  26.445  19.667  1.00 63.24           C  
ATOM     79  O   ARG A  31     -21.911  26.942  20.658  1.00 61.77           O  
ATOM     80  CB  ARG A  31     -22.528  26.622  17.427  1.00 64.52           C  
ATOM     81  CG  ARG A  31     -22.864  27.469  16.215  1.00 74.92           C  
ATOM     82  CD  ARG A  31     -24.125  26.981  15.527  1.00 86.94           C  
ATOM     83  NE  ARG A  31     -24.302  27.642  14.235  1.00104.29           N  
ATOM     84  CZ  ARG A  31     -24.940  28.796  14.061  1.00121.46           C  
ATOM     85  NH1 ARG A  31     -25.497  29.419  15.091  1.00111.30           N  
ATOM     86  NH2 ARG A  31     -25.032  29.331  12.849  1.00104.85           N  
ATOM     87  N   LEU A  32     -20.781  25.264  19.686  1.00 59.36           N  
ATOM     88  CA  LEU A  32     -20.730  24.363  20.827  1.00 59.74           C  
ATOM     89  C   LEU A  32     -19.636  24.659  21.887  1.00 62.43           C  
ATOM     90  O   LEU A  32     -19.921  24.536  23.080  1.00 61.98           O  
ATOM     91  CB  LEU A  32     -20.587  22.930  20.285  1.00 60.34           C  
ATOM     92  CG  LEU A  32     -20.761  21.790  21.261  1.00 66.62           C  
ATOM     93  CD1 LEU A  32     -22.233  21.591  21.624  1.00 67.32           C  
ATOM     94  CD2 LEU A  32     -20.196  20.518  20.679  1.00 71.23           C  
ATOM     95  N   LEU A  33     -18.396  25.010  21.465  1.00 57.47           N  
ATOM     96  CA  LEU A  33     -17.279  25.221  22.395  1.00 56.23           C  
ATOM     97  C   LEU A  33     -17.345  26.538  23.215  1.00 58.92           C  
ATOM     98  O   LEU A  33     -17.217  26.403  24.446  1.00 58.81           O  
ATOM     99  CB  LEU A  33     -15.898  25.061  21.731  1.00 55.84           C  
ATOM    100  CG  LEU A  33     -15.614  23.734  20.997  1.00 59.87           C  
ATOM    101  CD1 LEU A  33     -14.196  23.702  20.495  1.00 60.22           C  
ATOM    102  CD2 LEU A  33     -15.904  22.495  21.864  1.00 59.03           C  
ATOM    103  N   PRO A  34     -17.551  27.776  22.640  1.00 53.22           N  
ATOM    104  CA  PRO A  34     -17.580  28.989  23.495  1.00 52.74           C  
ATOM    105  C   PRO A  34     -18.542  28.979  24.715  1.00 57.97           C  
ATOM    106  O   PRO A  34     -18.056  29.413  25.762  1.00 57.86           O  
ATOM    107  CB  PRO A  34     -17.900  30.139  22.533  1.00 53.99           C  
ATOM    108  CG  PRO A  34     -18.201  29.526  21.248  1.00 58.54           C  
ATOM    109  CD  PRO A  34     -17.675  28.136  21.214  1.00 54.24           C  
ATOM    110  N   PRO A  35     -19.832  28.517  24.695  1.00 54.26           N  
ATOM    111  CA  PRO A  35     -20.620  28.549  25.942  1.00 53.69           C  
ATOM    112  C   PRO A  35     -20.222  27.429  26.904  1.00 56.45           C  
ATOM    113  O   PRO A  35     -20.313  27.603  28.122  1.00 56.57           O  
ATOM    114  CB  PRO A  35     -22.074  28.399  25.464  1.00 55.58           C  
ATOM    115  CG  PRO A  35     -22.019  28.330  23.971  1.00 60.02           C  
ATOM    116  CD  PRO A  35     -20.635  27.952  23.593  1.00 55.73           C  
ATOM    117  N   LEU A  36     -19.770  26.285  26.360  1.00 51.30           N  
ATOM    118  CA  LEU A  36     -19.320  25.148  27.150  1.00 50.50           C  
ATOM    119  C   LEU A  36     -18.056  25.512  27.926  1.00 53.33           C  
ATOM    120  O   LEU A  36     -18.017  25.314  29.131  1.00 52.47           O  
ATOM    121  CB  LEU A  36     -19.109  23.919  26.241  1.00 50.51           C  
ATOM    122  CG  LEU A  36     -18.302  22.749  26.804  1.00 55.22           C  
ATOM    123  CD1 LEU A  36     -19.033  22.062  27.925  1.00 55.30           C  
ATOM    124  CD2 LEU A  36     -18.006  21.748  25.722  1.00 58.49           C  
ATOM    125  N   TYR A  37     -17.053  26.073  27.236  1.00 50.29           N  
ATOM    126  CA  TYR A  37     -15.777  26.490  27.808  1.00 50.65           C  
ATOM    127  C   TYR A  37     -15.976  27.593  28.850  1.00 56.20           C  
ATOM    128  O   TYR A  37     -15.406  27.498  29.932  1.00 56.25           O  
ATOM    129  CB  TYR A  37     -14.798  26.937  26.692  1.00 52.20           C  
ATOM    130  CG  TYR A  37     -14.142  25.832  25.875  1.00 53.54           C  
ATOM    131  CD1 TYR A  37     -14.680  24.547  25.834  1.00 56.26           C  
ATOM    132  CD2 TYR A  37     -13.000  26.082  25.118  1.00 53.17           C  
ATOM    133  CE1 TYR A  37     -14.072  23.527  25.102  1.00 56.58           C  
ATOM    134  CE2 TYR A  37     -12.397  25.075  24.365  1.00 53.33           C  
ATOM    135  CZ  TYR A  37     -12.927  23.796  24.370  1.00 56.90           C  
ATOM    136  OH  TYR A  37     -12.356  22.795  23.627  1.00 50.55           O  
ATOM    137  N   SER A  38     -16.811  28.612  28.546  1.00 54.32           N  
ATOM    138  CA  SER A  38     -17.108  29.728  29.455  1.00 55.16           C  
ATOM    139  C   SER A  38     -17.660  29.234  30.790  1.00 63.34           C  
ATOM    140  O   SER A  38     -17.218  29.725  31.827  1.00 63.75           O  
ATOM    141  CB  SER A  38     -18.095  30.704  28.823  1.00 57.37           C  
ATOM    142  OG  SER A  38     -17.553  31.316  27.669  1.00 64.33           O  
ATOM    143  N   LEU A  39     -18.602  28.250  30.766  1.00 61.52           N  
ATOM    144  CA  LEU A  39     -19.205  27.669  31.978  1.00 61.97           C  
ATOM    145  C   LEU A  39     -18.224  26.831  32.781  1.00 62.95           C  
ATOM    146  O   LEU A  39     -18.192  26.972  34.001  1.00 61.72           O  
ATOM    147  CB  LEU A  39     -20.491  26.887  31.677  1.00 62.78           C  
ATOM    148  CG  LEU A  39     -21.703  27.757  31.346  1.00 69.17           C  
ATOM    149  CD1 LEU A  39     -22.692  27.006  30.490  1.00 70.26           C  
ATOM    150  CD2 LEU A  39     -22.369  28.307  32.613  1.00 72.49           C  
ATOM    151  N   VAL A  40     -17.388  26.003  32.099  1.00 58.57           N  
ATOM    152  CA  VAL A  40     -16.330  25.201  32.735  1.00 58.37           C  
ATOM    153  C   VAL A  40     -15.357  26.186  33.425  1.00 62.30           C  
ATOM    154  O   VAL A  40     -14.833  25.897  34.508  1.00 61.26           O  
ATOM    155  CB  VAL A  40     -15.603  24.237  31.739  1.00 61.98           C  
ATOM    156  CG1 VAL A  40     -14.423  23.523  32.405  1.00 61.75           C  
ATOM    157  CG2 VAL A  40     -16.570  23.212  31.153  1.00 61.57           C  
ATOM    158  N   PHE A  41     -15.162  27.369  32.799  1.00 59.10           N  
ATOM    159  CA  PHE A  41     -14.330  28.437  33.344  1.00 58.31           C  
ATOM    160  C   PHE A  41     -14.989  29.033  34.600  1.00 63.26           C  
ATOM    161  O   PHE A  41     -14.329  29.075  35.626  1.00 64.90           O  
ATOM    162  CB  PHE A  41     -13.979  29.525  32.294  1.00 58.96           C  
ATOM    163  CG  PHE A  41     -13.311  30.733  32.911  1.00 59.40           C  
ATOM    164  CD1 PHE A  41     -11.955  30.715  33.217  1.00 61.62           C  
ATOM    165  CD2 PHE A  41     -14.052  31.862  33.245  1.00 60.89           C  
ATOM    166  CE1 PHE A  41     -11.347  31.816  33.828  1.00 62.09           C  
ATOM    167  CE2 PHE A  41     -13.443  32.962  33.861  1.00 63.37           C  
ATOM    168  CZ  PHE A  41     -12.095  32.934  34.141  1.00 61.22           C  
ATOM    169  N   ILE A  42     -16.265  29.491  34.522  1.00 57.66           N  
ATOM    170  CA  ILE A  42     -17.004  30.090  35.640  1.00 56.11           C  
ATOM    171  C   ILE A  42     -16.974  29.149  36.841  1.00 59.71           C  
ATOM    172  O   ILE A  42     -16.465  29.516  37.891  1.00 57.28           O  
ATOM    173  CB  ILE A  42     -18.459  30.475  35.226  1.00 58.33           C  
ATOM    174  CG1 ILE A  42     -18.468  31.608  34.189  1.00 58.04           C  
ATOM    175  CG2 ILE A  42     -19.318  30.855  36.445  1.00 58.32           C  
ATOM    176  CD1 ILE A  42     -19.665  31.618  33.273  1.00 65.71           C  
ATOM    177  N   PHE A  43     -17.450  27.916  36.640  1.00 59.03           N  
ATOM    178  CA  PHE A  43     -17.555  26.870  37.648  1.00 59.97           C  
ATOM    179  C   PHE A  43     -16.200  26.346  38.141  1.00 64.80           C  
ATOM    180  O   PHE A  43     -16.096  25.865  39.266  1.00 64.68           O  
ATOM    181  CB  PHE A  43     -18.449  25.748  37.108  1.00 62.31           C  
ATOM    182  CG  PHE A  43     -18.766  24.609  38.045  1.00 64.79           C  
ATOM    183  CD1 PHE A  43     -19.295  24.853  39.311  1.00 68.69           C  
ATOM    184  CD2 PHE A  43     -18.611  23.288  37.634  1.00 67.18           C  
ATOM    185  CE1 PHE A  43     -19.603  23.794  40.171  1.00 70.05           C  
ATOM    186  CE2 PHE A  43     -18.929  22.232  38.486  1.00 70.24           C  
ATOM    187  CZ  PHE A  43     -19.412  22.489  39.752  1.00 68.86           C  
ATOM    188  N   GLY A  44     -15.174  26.479  37.317  1.00 62.48           N  
ATOM    189  CA  GLY A  44     -13.826  26.046  37.659  1.00 62.76           C  
ATOM    190  C   GLY A  44     -13.011  27.077  38.406  1.00 67.93           C  
ATOM    191  O   GLY A  44     -12.296  26.724  39.342  1.00 67.58           O  
ATOM    192  N   PHE A  45     -13.073  28.347  37.962  1.00 65.54           N  
ATOM    193  CA  PHE A  45     -12.355  29.469  38.561  1.00 66.01           C  
ATOM    194  C   PHE A  45     -12.889  29.700  39.952  1.00 72.01           C  
ATOM    195  O   PHE A  45     -12.099  29.819  40.889  1.00 71.79           O  
ATOM    196  CB  PHE A  45     -12.505  30.742  37.706  1.00 67.66           C  
ATOM    197  CG  PHE A  45     -11.670  31.917  38.150  1.00 68.98           C  
ATOM    198  CD1 PHE A  45     -10.300  31.950  37.910  1.00 71.77           C  
ATOM    199  CD2 PHE A  45     -12.258  33.014  38.771  1.00 71.19           C  
ATOM    200  CE1 PHE A  45      -9.531  33.049  38.308  1.00 73.09           C  
ATOM    201  CE2 PHE A  45     -11.488  34.112  39.170  1.00 74.10           C  
ATOM    202  CZ  PHE A  45     -10.130  34.125  38.935  1.00 72.22           C  
ATOM    203  N   VAL A  46     -14.235  29.716  40.087  1.00 69.41           N  
ATOM    204  CA  VAL A  46     -14.944  29.897  41.356  1.00 69.32           C  
ATOM    205  C   VAL A  46     -14.649  28.695  42.265  1.00 74.42           C  
ATOM    206  O   VAL A  46     -14.173  28.895  43.388  1.00 74.99           O  
ATOM    207  CB  VAL A  46     -16.461  30.171  41.144  1.00 72.59           C  
ATOM    208  CG1 VAL A  46     -17.261  29.973  42.429  1.00 72.56           C  
ATOM    209  CG2 VAL A  46     -16.688  31.571  40.577  1.00 72.03           C  
ATOM    210  N   GLY A  47     -14.863  27.482  41.735  1.00 70.13           N  
ATOM    211  CA  GLY A  47     -14.621  26.221  42.429  1.00 69.45           C  
ATOM    212  C   GLY A  47     -13.211  26.077  42.964  1.00 72.64           C  
ATOM    213  O   GLY A  47     -13.033  25.683  44.118  1.00 72.14           O  
ATOM    214  N   ASN A  48     -12.204  26.423  42.141  1.00 69.30           N  
ATOM    215  CA  ASN A  48     -10.794  26.304  42.518  1.00 69.16           C  
ATOM    216  C   ASN A  48     -10.331  27.379  43.461  1.00 72.39           C  
ATOM    217  O   ASN A  48      -9.524  27.089  44.344  1.00 70.32           O  
ATOM    218  CB  ASN A  48      -9.878  26.208  41.300  1.00 69.76           C  
ATOM    219  CG  ASN A  48      -9.815  24.799  40.764  1.00 89.99           C  
ATOM    220  OD1 ASN A  48      -9.021  23.967  41.220  1.00 86.11           O  
ATOM    221  ND2 ASN A  48     -10.695  24.480  39.833  1.00 78.58           N  
ATOM    222  N   MET A  49     -10.829  28.618  43.281  1.00 71.14           N  
ATOM    223  CA  MET A  49     -10.474  29.741  44.150  1.00 71.77           C  
ATOM    224  C   MET A  49     -10.999  29.522  45.551  1.00 74.36           C  
ATOM    225  O   MET A  49     -10.296  29.825  46.519  1.00 73.01           O  
ATOM    226  CB  MET A  49     -10.928  31.081  43.573  1.00 74.75           C  
ATOM    227  CG  MET A  49      -9.896  31.699  42.656  1.00 79.45           C  
ATOM    228  SD  MET A  49      -8.390  32.172  43.544  1.00 84.71           S  
ATOM    229  CE  MET A  49      -8.830  33.840  44.089  1.00 81.52           C  
ATOM    230  N   LEU A  50     -12.202  28.909  45.653  1.00 70.78           N  
ATOM    231  CA  LEU A  50     -12.820  28.535  46.923  1.00 70.59           C  
ATOM    232  C   LEU A  50     -11.891  27.553  47.637  1.00 75.02           C  
ATOM    233  O   LEU A  50     -11.602  27.748  48.814  1.00 75.79           O  
ATOM    234  CB  LEU A  50     -14.211  27.904  46.701  1.00 70.37           C  
ATOM    235  CG  LEU A  50     -15.376  28.868  46.450  1.00 74.46           C  
ATOM    236  CD1 LEU A  50     -16.526  28.155  45.792  1.00 74.39           C  
ATOM    237  CD2 LEU A  50     -15.847  29.518  47.731  1.00 76.65           C  
ATOM    238  N   VAL A  51     -11.360  26.562  46.896  1.00 70.40           N  
ATOM    239  CA  VAL A  51     -10.418  25.560  47.389  1.00 69.81           C  
ATOM    240  C   VAL A  51      -9.110  26.211  47.871  1.00 72.49           C  
ATOM    241  O   VAL A  51      -8.723  25.993  49.022  1.00 71.41           O  
ATOM    242  CB  VAL A  51     -10.195  24.435  46.343  1.00 73.68           C  
ATOM    243  CG1 VAL A  51      -8.985  23.569  46.677  1.00 73.12           C  
ATOM    244  CG2 VAL A  51     -11.443  23.579  46.195  1.00 73.70           C  
ATOM    245  N   ILE A  52      -8.451  27.017  47.005  1.00 69.48           N  
ATOM    246  CA  ILE A  52      -7.192  27.719  47.315  1.00 70.07           C  
ATOM    247  C   ILE A  52      -7.332  28.552  48.598  1.00 76.47           C  
ATOM    248  O   ILE A  52      -6.482  28.442  49.484  1.00 75.97           O  
ATOM    249  CB  ILE A  52      -6.660  28.554  46.101  1.00 72.86           C  
ATOM    250  CG1 ILE A  52      -6.249  27.638  44.923  1.00 72.55           C  
ATOM    251  CG2 ILE A  52      -5.495  29.492  46.499  1.00 73.14           C  
ATOM    252  CD1 ILE A  52      -6.340  28.264  43.526  1.00 73.50           C  
ATOM    253  N   LEU A  53      -8.427  29.333  48.709  1.00 74.86           N  
ATOM    254  CA  LEU A  53      -8.706  30.169  49.869  1.00 75.69           C  
ATOM    255  C   LEU A  53      -8.950  29.363  51.148  1.00 80.64           C  
ATOM    256  O   LEU A  53      -8.284  29.630  52.146  1.00 80.58           O  
ATOM    257  CB  LEU A  53      -9.855  31.160  49.599  1.00 76.33           C  
ATOM    258  CG  LEU A  53      -9.567  32.306  48.606  1.00 82.02           C  
ATOM    259  CD1 LEU A  53     -10.861  32.855  48.007  1.00 82.37           C  
ATOM    260  CD2 LEU A  53      -8.748  33.431  49.251  1.00 85.15           C  
ATOM    261  N   ILE A  54      -9.854  28.360  51.116  1.00 77.85           N  
ATOM    262  CA  ILE A  54     -10.177  27.513  52.279  1.00 78.30           C  
ATOM    263  C   ILE A  54      -8.927  26.764  52.813  1.00 84.68           C  
ATOM    264  O   ILE A  54      -8.782  26.632  54.021  1.00 83.86           O  
ATOM    265  CB  ILE A  54     -11.387  26.581  51.970  1.00 81.28           C  
ATOM    266  CG1 ILE A  54     -12.694  27.404  51.946  1.00 81.79           C  
ATOM    267  CG2 ILE A  54     -11.508  25.392  52.950  1.00 81.54           C  
ATOM    268  CD1 ILE A  54     -13.866  26.766  51.178  1.00 91.13           C  
ATOM    269  N   LEU A  55      -8.008  26.333  51.929  1.00 84.02           N  
ATOM    270  CA  LEU A  55      -6.776  25.627  52.323  1.00 84.62           C  
ATOM    271  C   LEU A  55      -5.799  26.477  53.128  1.00 88.11           C  
ATOM    272  O   LEU A  55      -5.063  25.938  53.956  1.00 87.22           O  
ATOM    273  CB  LEU A  55      -6.075  25.019  51.100  1.00 85.13           C  
ATOM    274  CG  LEU A  55      -6.653  23.705  50.561  1.00 90.87           C  
ATOM    275  CD1 LEU A  55      -6.179  23.447  49.149  1.00 91.76           C  
ATOM    276  CD2 LEU A  55      -6.267  22.517  51.443  1.00 94.20           C  
ATOM    277  N   ILE A  56      -5.804  27.797  52.889  1.00 85.55           N  
ATOM    278  CA  ILE A  56      -4.937  28.761  53.572  1.00 86.21           C  
ATOM    279  C   ILE A  56      -5.662  29.472  54.743  1.00 91.23           C  
ATOM    280  O   ILE A  56      -5.089  29.601  55.825  1.00 90.65           O  
ATOM    281  CB  ILE A  56      -4.285  29.770  52.572  1.00 89.35           C  
ATOM    282  CG1 ILE A  56      -3.716  29.054  51.319  1.00 89.81           C  
ATOM    283  CG2 ILE A  56      -3.201  30.620  53.262  1.00 89.80           C  
ATOM    284  CD1 ILE A  56      -3.519  29.964  50.079  1.00 97.36           C  
ATOM    285  N   ASN A  57      -6.907  29.931  54.515  1.00 88.61           N  
ATOM    286  CA  ASN A  57      -7.718  30.675  55.486  1.00 88.95           C  
ATOM    287  C   ASN A  57      -8.485  29.812  56.510  1.00 93.44           C  
ATOM    288  O   ASN A  57      -8.917  30.353  57.531  1.00 94.07           O  
ATOM    289  CB  ASN A  57      -8.688  31.630  54.769  1.00 90.35           C  
ATOM    290  CG  ASN A  57      -8.029  32.703  53.920  1.00111.39           C  
ATOM    291  OD1 ASN A  57      -6.845  32.631  53.559  1.00104.54           O  
ATOM    292  ND2 ASN A  57      -8.797  33.720  53.555  1.00102.75           N  
ATOM    293  N   TYR A  58      -8.671  28.503  56.254  1.00 89.00           N  
ATOM    294  CA  TYR A  58      -9.379  27.625  57.190  1.00 88.70           C  
ATOM    295  C   TYR A  58      -8.511  26.442  57.626  1.00 93.80           C  
ATOM    296  O   TYR A  58      -8.248  26.300  58.824  1.00 93.05           O  
ATOM    297  CB  TYR A  58     -10.746  27.179  56.630  1.00 89.59           C  
ATOM    298  N   LYS A  59      -8.042  25.619  56.651  1.00 91.69           N  
ATOM    299  CA  LYS A  59      -7.201  24.427  56.857  1.00 91.85           C  
ATOM    300  C   LYS A  59      -5.814  24.789  57.375  1.00 96.13           C  
ATOM    301  O   LYS A  59      -5.237  24.035  58.159  1.00 95.85           O  
ATOM    302  CB  LYS A  59      -7.095  23.598  55.568  1.00 94.67           C  
ATOM    303  CG  LYS A  59      -6.998  22.096  55.820  1.00110.86           C  
ATOM    304  N   ARG A  60      -5.298  25.952  56.929  1.00 93.01           N  
ATOM    305  CA  ARG A  60      -4.029  26.597  57.307  1.00 92.65           C  
ATOM    306  C   ARG A  60      -2.753  25.775  57.000  1.00 95.27           C  
ATOM    307  O   ARG A  60      -1.798  25.840  57.790  1.00 96.04           O  
ATOM    308  CB  ARG A  60      -4.038  27.049  58.788  1.00 91.97           C  
ATOM    309  CG  ARG A  60      -4.671  28.409  59.013  1.00103.85           C  
ATOM    310  CD  ARG A  60      -4.153  29.013  60.303  1.00118.94           C  
ATOM    311  NE  ARG A  60      -5.077  29.997  60.870  1.00128.80           N  
ATOM    312  CZ  ARG A  60      -4.982  30.495  62.099  1.00143.10           C  
ATOM    313  NH1 ARG A  60      -4.001  30.107  62.907  1.00130.39           N  
ATOM    314  NH2 ARG A  60      -5.867  31.382  62.533  1.00129.57           N  
ATOM    315  N   LEU A  61      -2.712  25.078  55.835  1.00 88.44           N  
ATOM    316  CA  LEU A  61      -1.573  24.277  55.348  1.00 87.09           C  
ATOM    317  C   LEU A  61      -0.711  23.654  56.471  1.00 87.90           C  
ATOM    318  O   LEU A  61       0.407  24.112  56.733  1.00 86.43           O  
ATOM    319  CB  LEU A  61      -0.684  25.075  54.358  1.00 87.21           C  
ATOM    320  CG  LEU A  61      -1.336  25.840  53.191  1.00 91.88           C  
ATOM    321  CD1 LEU A  61      -0.273  26.488  52.322  1.00 92.03           C  
ATOM    322  CD2 LEU A  61      -2.199  24.939  52.323  1.00 93.65           C  
ATOM    323  N   LYS A  62      -1.261  22.626  57.141  1.00 83.45           N  
ATOM    324  CA  LYS A  62      -0.644  21.927  58.276  1.00 82.52           C  
ATOM    325  C   LYS A  62       0.269  20.760  57.877  1.00 85.20           C  
ATOM    326  O   LYS A  62       1.247  20.486  58.574  1.00 85.09           O  
ATOM    327  CB  LYS A  62      -1.730  21.435  59.262  1.00 84.88           C  
ATOM    328  CG  LYS A  62      -2.530  22.547  59.951  1.00100.77           C  
ATOM    329  CD  LYS A  62      -3.549  21.998  60.945  1.00109.54           C  
ATOM    330  CE  LYS A  62      -4.225  23.099  61.723  1.00118.69           C  
ATOM    331  NZ  LYS A  62      -5.049  22.559  62.838  1.00125.24           N  
ATOM    332  N   SER A  63      -0.056  20.069  56.778  1.00 80.63           N  
ATOM    333  CA  SER A  63       0.690  18.895  56.327  1.00 79.66           C  
ATOM    334  C   SER A  63       1.278  19.024  54.922  1.00 82.39           C  
ATOM    335  O   SER A  63       1.207  20.089  54.305  1.00 81.10           O  
ATOM    336  CB  SER A  63      -0.182  17.642  56.439  1.00 82.49           C  
ATOM    337  OG  SER A  63      -1.513  17.860  55.998  1.00 88.94           O  
ATOM    338  N   MET A  64       1.890  17.930  54.438  1.00 79.72           N  
ATOM    339  CA  MET A  64       2.482  17.797  53.103  1.00 79.64           C  
ATOM    340  C   MET A  64       1.362  17.688  52.062  1.00 79.73           C  
ATOM    341  O   MET A  64       1.511  18.195  50.950  1.00 78.63           O  
ATOM    342  CB  MET A  64       3.388  16.560  53.050  1.00 82.55           C  
ATOM    343  CG  MET A  64       4.625  16.772  52.217  1.00 87.20           C  
ATOM    344  SD  MET A  64       5.967  15.608  52.592  1.00 92.47           S  
ATOM    345  CE  MET A  64       5.505  14.209  51.549  1.00 89.12           C  
ATOM    346  N   THR A  65       0.237  17.041  52.440  1.00 74.07           N  
ATOM    347  CA  THR A  65      -0.956  16.871  51.608  1.00 73.22           C  
ATOM    348  C   THR A  65      -1.499  18.236  51.209  1.00 75.24           C  
ATOM    349  O   THR A  65      -1.834  18.435  50.046  1.00 75.06           O  
ATOM    350  CB  THR A  65      -2.048  16.098  52.360  1.00 82.97           C  
ATOM    351  OG1 THR A  65      -2.242  16.699  53.642  1.00 88.71           O  
ATOM    352  CG2 THR A  65      -1.735  14.638  52.521  1.00 79.19           C  
ATOM    353  N   ASP A  66      -1.560  19.174  52.178  1.00 70.58           N  
ATOM    354  CA  ASP A  66      -2.050  20.550  52.023  1.00 70.06           C  
ATOM    355  C   ASP A  66      -1.233  21.354  51.011  1.00 72.40           C  
ATOM    356  O   ASP A  66      -1.810  22.107  50.235  1.00 70.43           O  
ATOM    357  CB  ASP A  66      -2.103  21.261  53.387  1.00 72.00           C  
ATOM    358  CG  ASP A  66      -2.942  20.558  54.445  1.00 84.32           C  
ATOM    359  OD1 ASP A  66      -3.985  19.947  54.079  1.00 85.82           O  
ATOM    360  OD2 ASP A  66      -2.577  20.639  55.638  1.00 88.01           O  
ATOM    361  N   ILE A  67       0.099  21.166  51.005  1.00 70.24           N  
ATOM    362  CA  ILE A  67       1.029  21.788  50.057  1.00 70.63           C  
ATOM    363  C   ILE A  67       0.782  21.216  48.622  1.00 75.54           C  
ATOM    364  O   ILE A  67       0.663  21.998  47.675  1.00 76.36           O  
ATOM    365  CB  ILE A  67       2.500  21.607  50.523  1.00 73.82           C  
ATOM    366  CG1 ILE A  67       2.730  22.096  51.982  1.00 74.57           C  
ATOM    367  CG2 ILE A  67       3.495  22.239  49.542  1.00 74.76           C  
ATOM    368  CD1 ILE A  67       2.482  23.625  52.290  1.00 85.83           C  
ATOM    369  N   TYR A  68       0.677  19.867  48.476  1.00 70.03           N  
ATOM    370  CA  TYR A  68       0.418  19.207  47.191  1.00 69.15           C  
ATOM    371  C   TYR A  68      -0.967  19.529  46.631  1.00 72.55           C  
ATOM    372  O   TYR A  68      -1.074  19.783  45.429  1.00 72.49           O  
ATOM    373  CB  TYR A  68       0.620  17.682  47.273  1.00 70.16           C  
ATOM    374  CG  TYR A  68       2.012  17.219  47.662  1.00 71.58           C  
ATOM    375  CD1 TYR A  68       3.140  17.959  47.313  1.00 73.79           C  
ATOM    376  CD2 TYR A  68       2.205  16.011  48.324  1.00 71.92           C  
ATOM    377  CE1 TYR A  68       4.421  17.536  47.666  1.00 74.78           C  
ATOM    378  CE2 TYR A  68       3.482  15.574  48.675  1.00 72.71           C  
ATOM    379  CZ  TYR A  68       4.587  16.337  48.339  1.00 80.48           C  
ATOM    380  OH  TYR A  68       5.849  15.907  48.678  1.00 81.09           O  
ATOM    381  N   LEU A  69      -2.023  19.525  47.491  1.00 68.04           N  
ATOM    382  CA  LEU A  69      -3.403  19.859  47.099  1.00 67.46           C  
ATOM    383  C   LEU A  69      -3.520  21.319  46.653  1.00 69.83           C  
ATOM    384  O   LEU A  69      -4.346  21.618  45.789  1.00 69.66           O  
ATOM    385  CB  LEU A  69      -4.406  19.600  48.242  1.00 67.76           C  
ATOM    386  CG  LEU A  69      -4.713  18.145  48.603  1.00 73.00           C  
ATOM    387  CD1 LEU A  69      -5.257  18.047  50.014  1.00 73.30           C  
ATOM    388  CD2 LEU A  69      -5.688  17.516  47.630  1.00 75.45           C  
ATOM    389  N   LEU A  70      -2.704  22.225  47.258  1.00 65.06           N  
ATOM    390  CA  LEU A  70      -2.661  23.658  46.938  1.00 64.63           C  
ATOM    391  C   LEU A  70      -2.094  23.850  45.543  1.00 68.91           C  
ATOM    392  O   LEU A  70      -2.677  24.573  44.742  1.00 68.64           O  
ATOM    393  CB  LEU A  70      -1.825  24.448  47.973  1.00 64.39           C  
ATOM    394  CG  LEU A  70      -1.639  25.953  47.721  1.00 68.24           C  
ATOM    395  CD1 LEU A  70      -2.862  26.730  48.108  1.00 68.40           C  
ATOM    396  CD2 LEU A  70      -0.456  26.479  48.465  1.00 70.04           C  
ATOM    397  N   ASN A  71      -0.963  23.189  45.264  1.00 65.71           N  
ATOM    398  CA  ASN A  71      -0.278  23.198  43.978  1.00 65.30           C  
ATOM    399  C   ASN A  71      -1.109  22.504  42.884  1.00 66.79           C  
ATOM    400  O   ASN A  71      -0.986  22.851  41.712  1.00 66.01           O  
ATOM    401  CB  ASN A  71       1.092  22.554  44.126  1.00 66.89           C  
ATOM    402  CG  ASN A  71       2.107  23.440  44.801  1.00 85.18           C  
ATOM    403  OD1 ASN A  71       2.510  24.480  44.272  1.00 77.81           O  
ATOM    404  ND2 ASN A  71       2.561  23.039  45.971  1.00 75.42           N  
ATOM    405  N   LEU A  72      -1.964  21.547  43.277  1.00 62.14           N  
ATOM    406  CA  LEU A  72      -2.865  20.833  42.370  1.00 61.78           C  
ATOM    407  C   LEU A  72      -4.013  21.766  41.933  1.00 66.54           C  
ATOM    408  O   LEU A  72      -4.489  21.673  40.802  1.00 65.80           O  
ATOM    409  CB  LEU A  72      -3.397  19.548  43.039  1.00 61.28           C  
ATOM    410  CG  LEU A  72      -4.428  18.734  42.273  1.00 65.07           C  
ATOM    411  CD1 LEU A  72      -3.833  18.166  41.002  1.00 65.81           C  
ATOM    412  CD2 LEU A  72      -5.013  17.637  43.137  1.00 65.62           C  
ATOM    413  N   ALA A  73      -4.431  22.670  42.829  1.00 64.09           N  
ATOM    414  CA  ALA A  73      -5.473  23.663  42.579  1.00 64.26           C  
ATOM    415  C   ALA A  73      -4.912  24.838  41.758  1.00 68.61           C  
ATOM    416  O   ALA A  73      -5.672  25.485  41.037  1.00 68.51           O  
ATOM    417  CB  ALA A  73      -6.041  24.159  43.900  1.00 64.91           C  
ATOM    418  N   ILE A  74      -3.585  25.109  41.874  1.00 64.97           N  
ATOM    419  CA  ILE A  74      -2.866  26.159  41.134  1.00 64.47           C  
ATOM    420  C   ILE A  74      -2.702  25.692  39.686  1.00 70.51           C  
ATOM    421  O   ILE A  74      -2.913  26.486  38.765  1.00 71.39           O  
ATOM    422  CB  ILE A  74      -1.502  26.529  41.794  1.00 66.47           C  
ATOM    423  CG1 ILE A  74      -1.714  27.197  43.165  1.00 66.07           C  
ATOM    424  CG2 ILE A  74      -0.667  27.441  40.890  1.00 66.41           C  
ATOM    425  CD1 ILE A  74      -0.576  26.997  44.124  1.00 72.04           C  
ATOM    426  N   SER A  75      -2.351  24.395  39.494  1.00 66.41           N  
ATOM    427  CA  SER A  75      -2.174  23.762  38.185  1.00 65.61           C  
ATOM    428  C   SER A  75      -3.483  23.772  37.410  1.00 68.69           C  
ATOM    429  O   SER A  75      -3.463  23.900  36.185  1.00 67.64           O  
ATOM    430  CB  SER A  75      -1.648  22.340  38.341  1.00 69.41           C  
ATOM    431  OG  SER A  75      -2.632  21.433  38.812  1.00 80.39           O  
ATOM    432  N   ASP A  76      -4.619  23.665  38.147  1.00 65.25           N  
ATOM    433  CA  ASP A  76      -5.986  23.697  37.622  1.00 64.33           C  
ATOM    434  C   ASP A  76      -6.371  25.113  37.191  1.00 66.12           C  
ATOM    435  O   ASP A  76      -6.928  25.293  36.105  1.00 64.88           O  
ATOM    436  CB  ASP A  76      -6.995  23.105  38.632  1.00 65.85           C  
ATOM    437  CG  ASP A  76      -7.297  21.620  38.449  1.00 74.31           C  
ATOM    438  OD1 ASP A  76      -6.763  21.014  37.489  1.00 74.88           O  
ATOM    439  OD2 ASP A  76      -8.105  21.077  39.231  1.00 79.17           O  
ATOM    440  N   LEU A  77      -6.016  26.115  38.012  1.00 62.69           N  
ATOM    441  CA  LEU A  77      -6.263  27.532  37.732  1.00 62.99           C  
ATOM    442  C   LEU A  77      -5.455  27.998  36.519  1.00 66.73           C  
ATOM    443  O   LEU A  77      -5.948  28.784  35.710  1.00 64.94           O  
ATOM    444  CB  LEU A  77      -5.921  28.379  38.959  1.00 63.39           C  
ATOM    445  CG  LEU A  77      -6.680  29.687  39.061  1.00 68.88           C  
ATOM    446  CD1 LEU A  77      -8.084  29.461  39.625  1.00 69.36           C  
ATOM    447  CD2 LEU A  77      -5.910  30.688  39.897  1.00 72.47           C  
ATOM    448  N   PHE A  78      -4.218  27.489  36.401  1.00 65.16           N  
ATOM    449  CA  PHE A  78      -3.299  27.729  35.295  1.00 66.12           C  
ATOM    450  C   PHE A  78      -3.976  27.232  33.999  1.00 70.28           C  
ATOM    451  O   PHE A  78      -4.034  27.971  33.007  1.00 70.70           O  
ATOM    452  CB  PHE A  78      -1.971  26.981  35.557  1.00 68.50           C  
ATOM    453  CG  PHE A  78      -0.870  27.745  36.268  1.00 70.29           C  
ATOM    454  CD1 PHE A  78      -1.171  28.722  37.216  1.00 73.61           C  
ATOM    455  CD2 PHE A  78       0.470  27.465  36.009  1.00 72.44           C  
ATOM    456  CE1 PHE A  78      -0.150  29.438  37.860  1.00 74.83           C  
ATOM    457  CE2 PHE A  78       1.492  28.175  36.658  1.00 75.59           C  
ATOM    458  CZ  PHE A  78       1.175  29.158  37.581  1.00 73.80           C  
ATOM    459  N   PHE A  79      -4.553  26.007  34.056  1.00 65.27           N  
ATOM    460  CA  PHE A  79      -5.311  25.354  32.988  1.00 64.13           C  
ATOM    461  C   PHE A  79      -6.551  26.189  32.677  1.00 66.87           C  
ATOM    462  O   PHE A  79      -6.852  26.412  31.503  1.00 66.06           O  
ATOM    463  CB  PHE A  79      -5.739  23.942  33.441  1.00 65.45           C  
ATOM    464  CG  PHE A  79      -5.799  22.894  32.364  1.00 66.11           C  
ATOM    465  CD1 PHE A  79      -6.934  22.746  31.577  1.00 68.19           C  
ATOM    466  CD2 PHE A  79      -4.734  22.024  32.161  1.00 68.15           C  
ATOM    467  CE1 PHE A  79      -6.996  21.763  30.589  1.00 68.95           C  
ATOM    468  CE2 PHE A  79      -4.798  21.033  31.180  1.00 70.86           C  
ATOM    469  CZ  PHE A  79      -5.928  20.911  30.400  1.00 68.61           C  
ATOM    470  N   LEU A  80      -7.247  26.670  33.731  1.00 63.26           N  
ATOM    471  CA  LEU A  80      -8.452  27.496  33.617  1.00 63.31           C  
ATOM    472  C   LEU A  80      -8.207  28.867  32.981  1.00 68.57           C  
ATOM    473  O   LEU A  80      -9.089  29.382  32.279  1.00 68.93           O  
ATOM    474  CB  LEU A  80      -9.137  27.668  34.973  1.00 63.08           C  
ATOM    475  CG  LEU A  80     -10.007  26.519  35.410  1.00 67.81           C  
ATOM    476  CD1 LEU A  80      -9.991  26.376  36.902  1.00 68.12           C  
ATOM    477  CD2 LEU A  80     -11.411  26.689  34.919  1.00 71.14           C  
ATOM    478  N   LEU A  81      -7.022  29.458  33.219  1.00 64.24           N  
ATOM    479  CA  LEU A  81      -6.687  30.767  32.658  1.00 63.90           C  
ATOM    480  C   LEU A  81      -6.682  30.766  31.119  1.00 64.13           C  
ATOM    481  O   LEU A  81      -7.034  31.777  30.515  1.00 63.84           O  
ATOM    482  CB  LEU A  81      -5.341  31.269  33.202  1.00 64.62           C  
ATOM    483  CG  LEU A  81      -5.313  31.760  34.658  1.00 70.18           C  
ATOM    484  CD1 LEU A  81      -3.922  31.569  35.256  1.00 70.84           C  
ATOM    485  CD2 LEU A  81      -5.765  33.227  34.773  1.00 72.76           C  
ATOM    486  N   THR A  82      -6.330  29.617  30.503  1.00 57.37           N  
ATOM    487  CA  THR A  82      -6.249  29.410  29.053  1.00 55.37           C  
ATOM    488  C   THR A  82      -7.612  29.169  28.394  1.00 58.19           C  
ATOM    489  O   THR A  82      -7.770  29.399  27.200  1.00 57.58           O  
ATOM    490  CB  THR A  82      -5.291  28.248  28.736  1.00 55.64           C  
ATOM    491  OG1 THR A  82      -5.940  27.005  28.991  1.00 53.54           O  
ATOM    492  CG2 THR A  82      -3.986  28.325  29.513  1.00 53.31           C  
ATOM    493  N   VAL A  83      -8.577  28.674  29.169  1.00 55.01           N  
ATOM    494  CA  VAL A  83      -9.916  28.309  28.721  1.00 54.36           C  
ATOM    495  C   VAL A  83     -10.644  29.449  27.981  1.00 60.30           C  
ATOM    496  O   VAL A  83     -11.103  29.164  26.870  1.00 60.21           O  
ATOM    497  CB  VAL A  83     -10.748  27.722  29.880  1.00 56.89           C  
ATOM    498  CG1 VAL A  83     -12.205  27.523  29.479  1.00 56.50           C  
ATOM    499  CG2 VAL A  83     -10.133  26.416  30.377  1.00 56.18           C  
ATOM    500  N   PRO A  84     -10.753  30.713  28.507  1.00 58.24           N  
ATOM    501  CA  PRO A  84     -11.480  31.767  27.752  1.00 58.05           C  
ATOM    502  C   PRO A  84     -10.864  32.148  26.401  1.00 60.49           C  
ATOM    503  O   PRO A  84     -11.565  32.626  25.508  1.00 59.33           O  
ATOM    504  CB  PRO A  84     -11.511  32.964  28.718  1.00 60.02           C  
ATOM    505  CG  PRO A  84     -11.144  32.430  30.035  1.00 64.62           C  
ATOM    506  CD  PRO A  84     -10.267  31.240  29.800  1.00 60.14           C  
ATOM    507  N   PHE A  85      -9.544  31.940  26.268  1.00 56.98           N  
ATOM    508  CA  PHE A  85      -8.782  32.176  25.051  1.00 56.46           C  
ATOM    509  C   PHE A  85      -9.146  31.128  23.990  1.00 60.19           C  
ATOM    510  O   PHE A  85      -9.315  31.495  22.829  1.00 59.92           O  
ATOM    511  CB  PHE A  85      -7.272  32.212  25.360  1.00 58.04           C  
ATOM    512  CG  PHE A  85      -6.899  33.372  26.255  1.00 59.62           C  
ATOM    513  CD1 PHE A  85      -6.711  34.647  25.730  1.00 62.06           C  
ATOM    514  CD2 PHE A  85      -6.763  33.199  27.629  1.00 62.11           C  
ATOM    515  CE1 PHE A  85      -6.397  35.723  26.559  1.00 63.07           C  
ATOM    516  CE2 PHE A  85      -6.434  34.275  28.459  1.00 64.84           C  
ATOM    517  CZ  PHE A  85      -6.262  35.533  27.918  1.00 62.96           C  
ATOM    518  N   TRP A  86      -9.336  29.849  24.403  1.00 56.47           N  
ATOM    519  CA  TRP A  86      -9.740  28.728  23.539  1.00 55.64           C  
ATOM    520  C   TRP A  86     -11.157  28.912  23.039  1.00 56.83           C  
ATOM    521  O   TRP A  86     -11.435  28.548  21.893  1.00 54.97           O  
ATOM    522  CB  TRP A  86      -9.629  27.361  24.261  1.00 54.42           C  
ATOM    523  CG  TRP A  86      -8.281  27.019  24.827  1.00 55.36           C  
ATOM    524  CD1 TRP A  86      -8.028  26.472  26.051  1.00 58.37           C  
ATOM    525  CD2 TRP A  86      -7.004  27.170  24.180  1.00 55.25           C  
ATOM    526  NE1 TRP A  86      -6.675  26.262  26.207  1.00 57.95           N  
ATOM    527  CE2 TRP A  86      -6.022  26.691  25.080  1.00 59.44           C  
ATOM    528  CE3 TRP A  86      -6.593  27.653  22.922  1.00 56.30           C  
ATOM    529  CZ2 TRP A  86      -4.656  26.703  24.770  1.00 58.66           C  
ATOM    530  CZ3 TRP A  86      -5.243  27.649  22.613  1.00 57.65           C  
ATOM    531  CH2 TRP A  86      -4.291  27.185  23.533  1.00 58.31           C  
ATOM    532  N   ALA A  87     -12.050  29.466  23.906  1.00 53.60           N  
ATOM    533  CA  ALA A  87     -13.460  29.759  23.604  1.00 53.55           C  
ATOM    534  C   ALA A  87     -13.563  30.798  22.508  1.00 57.61           C  
ATOM    535  O   ALA A  87     -14.373  30.609  21.608  1.00 57.36           O  
ATOM    536  CB  ALA A  87     -14.195  30.235  24.854  1.00 54.17           C  
ATOM    537  N   HIS A  88     -12.722  31.864  22.564  1.00 54.98           N  
ATOM    538  CA  HIS A  88     -12.650  32.937  21.568  1.00 55.88           C  
ATOM    539  C   HIS A  88     -12.121  32.408  20.224  1.00 60.56           C  
ATOM    540  O   HIS A  88     -12.712  32.700  19.177  1.00 59.47           O  
ATOM    541  CB  HIS A  88     -11.796  34.120  22.078  1.00 57.05           C  
ATOM    542  CG  HIS A  88     -11.764  35.291  21.142  1.00 60.91           C  
ATOM    543  ND1 HIS A  88     -12.796  36.221  21.109  1.00 63.07           N  
ATOM    544  CD2 HIS A  88     -10.842  35.632  20.212  1.00 63.21           C  
ATOM    545  CE1 HIS A  88     -12.471  37.089  20.163  1.00 62.60           C  
ATOM    546  NE2 HIS A  88     -11.306  36.779  19.591  1.00 63.06           N  
ATOM    547  N   TYR A  89     -11.033  31.608  20.266  1.00 57.91           N  
ATOM    548  CA  TYR A  89     -10.397  30.997  19.093  1.00 58.34           C  
ATOM    549  C   TYR A  89     -11.366  30.046  18.349  1.00 63.31           C  
ATOM    550  O   TYR A  89     -11.468  30.117  17.124  1.00 63.23           O  
ATOM    551  CB  TYR A  89      -9.062  30.338  19.499  1.00 59.69           C  
ATOM    552  CG  TYR A  89      -8.309  29.569  18.430  1.00 62.26           C  
ATOM    553  CD1 TYR A  89      -8.031  30.142  17.188  1.00 64.31           C  
ATOM    554  CD2 TYR A  89      -7.759  28.319  18.705  1.00 63.33           C  
ATOM    555  CE1 TYR A  89      -7.305  29.450  16.216  1.00 64.51           C  
ATOM    556  CE2 TYR A  89      -7.016  27.625  17.747  1.00 64.32           C  
ATOM    557  CZ  TYR A  89      -6.796  28.194  16.504  1.00 70.97           C  
ATOM    558  OH  TYR A  89      -6.076  27.495  15.565  1.00 71.19           O  
ATOM    559  N   ALA A  90     -12.147  29.245  19.095  1.00 60.51           N  
ATOM    560  CA  ALA A  90     -13.168  28.345  18.537  1.00 60.21           C  
ATOM    561  C   ALA A  90     -14.264  29.110  17.794  1.00 63.35           C  
ATOM    562  O   ALA A  90     -14.681  28.673  16.721  1.00 62.09           O  
ATOM    563  CB  ALA A  90     -13.800  27.529  19.649  1.00 60.83           C  
ATOM    564  N   ALA A  91     -14.709  30.256  18.378  1.00 60.01           N  
ATOM    565  CA  ALA A  91     -15.782  31.140  17.915  1.00 59.76           C  
ATOM    566  C   ALA A  91     -15.386  32.042  16.748  1.00 64.90           C  
ATOM    567  O   ALA A  91     -16.206  32.306  15.875  1.00 64.91           O  
ATOM    568  CB  ALA A  91     -16.264  31.996  19.073  1.00 60.36           C  
ATOM    569  N   ALA A  92     -14.146  32.548  16.756  1.00 61.23           N  
ATOM    570  CA  ALA A  92     -13.621  33.453  15.744  1.00 59.72           C  
ATOM    571  C   ALA A  92     -12.266  32.921  15.272  1.00 64.39           C  
ATOM    572  O   ALA A  92     -12.253  31.944  14.525  1.00 65.37           O  
ATOM    573  CB  ALA A  92     -13.494  34.850  16.330  1.00 60.03           C  
ATOM    574  N   GLN A  93     -11.139  33.502  15.756  1.00 59.41           N  
ATOM    575  CA  GLN A  93      -9.752  33.133  15.421  1.00 58.22           C  
ATOM    576  C   GLN A  93      -8.788  33.609  16.531  1.00 59.20           C  
ATOM    577  O   GLN A  93      -9.256  34.141  17.539  1.00 57.91           O  
ATOM    578  CB  GLN A  93      -9.349  33.748  14.047  1.00 59.53           C  
ATOM    579  CG  GLN A  93      -9.508  35.279  13.944  1.00 65.46           C  
ATOM    580  CD  GLN A  93      -8.692  35.942  12.853  1.00 75.61           C  
ATOM    581  OE1 GLN A  93      -8.426  35.387  11.776  1.00 63.47           O  
ATOM    582  NE2 GLN A  93      -8.330  37.191  13.091  1.00 72.05           N  
ATOM    583  N   TRP A  94      -7.449  33.472  16.320  1.00 54.43           N  
ATOM    584  CA  TRP A  94      -6.435  33.935  17.265  1.00 53.65           C  
ATOM    585  C   TRP A  94      -6.111  35.425  17.118  1.00 60.34           C  
ATOM    586  O   TRP A  94      -5.308  35.817  16.261  1.00 60.61           O  
ATOM    587  CB  TRP A  94      -5.166  33.094  17.189  1.00 51.73           C  
ATOM    588  CG  TRP A  94      -4.364  33.185  18.454  1.00 52.05           C  
ATOM    589  CD1 TRP A  94      -3.230  33.911  18.658  1.00 54.75           C  
ATOM    590  CD2 TRP A  94      -4.683  32.578  19.713  1.00 51.84           C  
ATOM    591  NE1 TRP A  94      -2.811  33.782  19.958  1.00 53.94           N  
ATOM    592  CE2 TRP A  94      -3.674  32.953  20.626  1.00 55.59           C  
ATOM    593  CE3 TRP A  94      -5.694  31.705  20.145  1.00 52.76           C  
ATOM    594  CZ2 TRP A  94      -3.660  32.505  21.954  1.00 54.59           C  
ATOM    595  CZ3 TRP A  94      -5.679  31.267  21.464  1.00 53.94           C  
ATOM    596  CH2 TRP A  94      -4.666  31.655  22.346  1.00 54.37           C  
ATOM    597  N   ASP A  95      -6.727  36.250  17.979  1.00 57.91           N  
ATOM    598  CA  ASP A  95      -6.559  37.704  17.984  1.00 57.98           C  
ATOM    599  C   ASP A  95      -5.612  38.199  19.098  1.00 60.85           C  
ATOM    600  O   ASP A  95      -5.594  39.404  19.385  1.00 61.50           O  
ATOM    601  CB  ASP A  95      -7.939  38.401  18.090  1.00 60.37           C  
ATOM    602  CG  ASP A  95      -8.906  38.107  16.954  1.00 71.59           C  
ATOM    603  OD1 ASP A  95      -8.568  38.417  15.785  1.00 72.99           O  
ATOM    604  OD2 ASP A  95     -10.022  37.619  17.239  1.00 75.54           O  
ATOM    605  N   PHE A  96      -4.802  37.282  19.688  1.00 54.92           N  
ATOM    606  CA  PHE A  96      -3.887  37.558  20.810  1.00 53.43           C  
ATOM    607  C   PHE A  96      -2.367  37.574  20.446  1.00 57.41           C  
ATOM    608  O   PHE A  96      -1.531  37.905  21.294  1.00 55.87           O  
ATOM    609  CB  PHE A  96      -4.161  36.580  21.973  1.00 54.29           C  
ATOM    610  CG  PHE A  96      -5.619  36.293  22.230  1.00 54.98           C  
ATOM    611  CD1 PHE A  96      -6.406  37.186  22.944  1.00 57.67           C  
ATOM    612  CD2 PHE A  96      -6.210  35.124  21.759  1.00 56.49           C  
ATOM    613  CE1 PHE A  96      -7.764  36.919  23.177  1.00 58.23           C  
ATOM    614  CE2 PHE A  96      -7.567  34.862  21.987  1.00 58.82           C  
ATOM    615  CZ  PHE A  96      -8.333  35.758  22.699  1.00 56.71           C  
ATOM    616  N   GLY A  97      -2.034  37.251  19.199  1.00 55.31           N  
ATOM    617  CA  GLY A  97      -0.652  37.240  18.735  1.00 55.64           C  
ATOM    618  C   GLY A  97       0.147  36.012  19.129  1.00 61.34           C  
ATOM    619  O   GLY A  97      -0.391  35.075  19.727  1.00 61.04           O  
ATOM    620  N   ASN A  98       1.451  36.010  18.782  1.00 58.89           N  
ATOM    621  CA  ASN A  98       2.345  34.886  19.039  1.00 58.86           C  
ATOM    622  C   ASN A  98       2.720  34.714  20.503  1.00 64.03           C  
ATOM    623  O   ASN A  98       2.692  33.581  20.999  1.00 63.64           O  
ATOM    624  CB  ASN A  98       3.596  34.953  18.166  1.00 57.01           C  
ATOM    625  CG  ASN A  98       4.386  33.667  18.201  1.00 80.03           C  
ATOM    626  OD1 ASN A  98       3.918  32.620  17.744  1.00 77.02           O  
ATOM    627  ND2 ASN A  98       5.578  33.703  18.791  1.00 68.07           N  
ATOM    628  N   THR A  99       3.104  35.824  21.178  1.00 61.17           N  
ATOM    629  CA  THR A  99       3.515  35.853  22.586  1.00 61.25           C  
ATOM    630  C   THR A  99       2.516  35.080  23.455  1.00 65.08           C  
ATOM    631  O   THR A  99       2.924  34.171  24.181  1.00 63.72           O  
ATOM    632  CB  THR A  99       3.729  37.303  23.059  1.00 72.19           C  
ATOM    633  OG1 THR A  99       4.711  37.945  22.232  1.00 74.65           O  
ATOM    634  CG2 THR A  99       4.128  37.393  24.537  1.00 68.77           C  
ATOM    635  N   MET A 100       1.208  35.409  23.324  1.00 62.06           N  
ATOM    636  CA  MET A 100       0.116  34.767  24.057  1.00 61.81           C  
ATOM    637  C   MET A 100      -0.088  33.334  23.613  1.00 64.18           C  
ATOM    638  O   MET A 100      -0.312  32.484  24.467  1.00 63.94           O  
ATOM    639  CB  MET A 100      -1.196  35.561  23.942  1.00 64.54           C  
ATOM    640  CG  MET A 100      -1.188  36.879  24.704  1.00 68.80           C  
ATOM    641  SD  MET A 100      -1.211  36.690  26.504  1.00 73.62           S  
ATOM    642  CE  MET A 100      -0.405  38.204  26.989  1.00 70.21           C  
ATOM    643  N   CYS A 101       0.019  33.054  22.298  1.00 59.58           N  
ATOM    644  CA  CYS A 101      -0.135  31.711  21.737  1.00 59.59           C  
ATOM    645  C   CYS A 101       0.761  30.666  22.418  1.00 64.86           C  
ATOM    646  O   CYS A 101       0.279  29.595  22.797  1.00 64.30           O  
ATOM    647  CB  CYS A 101       0.066  31.727  20.228  1.00 60.01           C  
ATOM    648  SG  CYS A 101      -0.148  30.114  19.440  1.00 64.20           S  
ATOM    649  N   GLN A 102       2.052  30.998  22.594  1.00 62.07           N  
ATOM    650  CA  GLN A 102       3.045  30.136  23.233  1.00 61.76           C  
ATOM    651  C   GLN A 102       2.844  30.103  24.760  1.00 64.81           C  
ATOM    652  O   GLN A 102       2.938  29.037  25.364  1.00 64.72           O  
ATOM    653  CB  GLN A 102       4.468  30.617  22.896  1.00 63.34           C  
ATOM    654  CG  GLN A 102       4.785  30.726  21.404  1.00 69.67           C  
ATOM    655  CD  GLN A 102       6.257  30.932  21.167  1.00 85.66           C  
ATOM    656  OE1 GLN A 102       6.850  31.926  21.604  1.00 83.55           O  
ATOM    657  NE2 GLN A 102       6.883  30.004  20.460  1.00 75.89           N  
ATOM    658  N   LEU A 103       2.561  31.273  25.370  1.00 60.16           N  
ATOM    659  CA  LEU A 103       2.349  31.463  26.807  1.00 59.26           C  
ATOM    660  C   LEU A 103       1.126  30.707  27.298  1.00 61.25           C  
ATOM    661  O   LEU A 103       1.135  30.217  28.424  1.00 61.49           O  
ATOM    662  CB  LEU A 103       2.187  32.961  27.112  1.00 59.62           C  
ATOM    663  CG  LEU A 103       2.498  33.445  28.530  1.00 64.63           C  
ATOM    664  CD1 LEU A 103       3.109  34.841  28.491  1.00 64.76           C  
ATOM    665  CD2 LEU A 103       1.244  33.451  29.414  1.00 67.24           C  
ATOM    666  N   LEU A 104       0.074  30.618  26.475  1.00 55.41           N  
ATOM    667  CA  LEU A 104      -1.148  29.919  26.867  1.00 53.73           C  
ATOM    668  C   LEU A 104      -1.042  28.406  26.646  1.00 53.34           C  
ATOM    669  O   LEU A 104      -1.454  27.655  27.522  1.00 52.27           O  
ATOM    670  CB  LEU A 104      -2.393  30.540  26.217  1.00 53.65           C  
ATOM    671  CG  LEU A 104      -2.680  31.980  26.677  1.00 58.00           C  
ATOM    672  CD1 LEU A 104      -3.469  32.747  25.647  1.00 58.16           C  
ATOM    673  CD2 LEU A 104      -3.335  32.022  28.064  1.00 59.62           C  
ATOM    674  N   THR A 105      -0.418  27.961  25.535  1.00 48.62           N  
ATOM    675  CA  THR A 105      -0.159  26.545  25.254  1.00 48.09           C  
ATOM    676  C   THR A 105       0.790  26.035  26.350  1.00 53.50           C  
ATOM    677  O   THR A 105       0.643  24.902  26.808  1.00 53.59           O  
ATOM    678  CB  THR A 105       0.361  26.354  23.813  1.00 51.38           C  
ATOM    679  OG1 THR A 105      -0.690  26.639  22.875  1.00 43.63           O  
ATOM    680  CG2 THR A 105       0.924  24.957  23.562  1.00 49.12           C  
ATOM    681  N   GLY A 106       1.682  26.919  26.811  1.00 50.19           N  
ATOM    682  CA  GLY A 106       2.600  26.676  27.920  1.00 49.16           C  
ATOM    683  C   GLY A 106       1.881  26.346  29.214  1.00 51.19           C  
ATOM    684  O   GLY A 106       2.071  25.259  29.747  1.00 51.30           O  
ATOM    685  N   LEU A 107       1.004  27.251  29.704  1.00 47.15           N  
ATOM    686  CA  LEU A 107       0.200  27.079  30.936  1.00 46.14           C  
ATOM    687  C   LEU A 107      -0.718  25.859  30.859  1.00 48.83           C  
ATOM    688  O   LEU A 107      -1.019  25.268  31.894  1.00 47.82           O  
ATOM    689  CB  LEU A 107      -0.638  28.340  31.249  1.00 45.89           C  
ATOM    690  CG  LEU A 107       0.118  29.636  31.542  1.00 50.05           C  
ATOM    691  CD1 LEU A 107      -0.782  30.827  31.377  1.00 51.10           C  
ATOM    692  CD2 LEU A 107       0.721  29.643  32.915  1.00 50.15           C  
ATOM    693  N   TYR A 108      -1.176  25.505  29.635  1.00 45.64           N  
ATOM    694  CA  TYR A 108      -2.013  24.340  29.345  1.00 45.98           C  
ATOM    695  C   TYR A 108      -1.215  23.046  29.611  1.00 49.29           C  
ATOM    696  O   TYR A 108      -1.691  22.175  30.316  1.00 48.36           O  
ATOM    697  CB  TYR A 108      -2.536  24.386  27.884  1.00 47.96           C  
ATOM    698  CG  TYR A 108      -3.617  23.366  27.581  1.00 51.47           C  
ATOM    699  CD1 TYR A 108      -3.291  22.077  27.155  1.00 53.97           C  
ATOM    700  CD2 TYR A 108      -4.963  23.669  27.769  1.00 52.43           C  
ATOM    701  CE1 TYR A 108      -4.282  21.123  26.914  1.00 54.69           C  
ATOM    702  CE2 TYR A 108      -5.961  22.733  27.504  1.00 53.05           C  
ATOM    703  CZ  TYR A 108      -5.616  21.460  27.079  1.00 59.11           C  
ATOM    704  OH  TYR A 108      -6.600  20.538  26.821  1.00 57.75           O  
ATOM    705  N   PHE A 109      -0.011  22.937  29.035  1.00 47.30           N  
ATOM    706  CA  PHE A 109       0.916  21.810  29.162  1.00 47.15           C  
ATOM    707  C   PHE A 109       1.462  21.736  30.580  1.00 51.42           C  
ATOM    708  O   PHE A 109       1.374  20.666  31.198  1.00 51.50           O  
ATOM    709  CB  PHE A 109       2.061  21.924  28.128  1.00 48.76           C  
ATOM    710  CG  PHE A 109       1.815  21.247  26.797  1.00 50.10           C  
ATOM    711  CD1 PHE A 109       2.046  19.883  26.637  1.00 52.72           C  
ATOM    712  CD2 PHE A 109       1.353  21.973  25.699  1.00 51.53           C  
ATOM    713  CE1 PHE A 109       1.823  19.261  25.399  1.00 53.45           C  
ATOM    714  CE2 PHE A 109       1.099  21.344  24.470  1.00 53.75           C  
ATOM    715  CZ  PHE A 109       1.341  19.994  24.325  1.00 51.63           C  
ATOM    716  N   ILE A 110       2.004  22.876  31.107  1.00 47.36           N  
ATOM    717  CA  ILE A 110       2.525  22.994  32.483  1.00 47.17           C  
ATOM    718  C   ILE A 110       1.416  22.648  33.471  1.00 53.61           C  
ATOM    719  O   ILE A 110       1.678  21.959  34.444  1.00 54.37           O  
ATOM    720  CB  ILE A 110       3.185  24.366  32.784  1.00 49.35           C  
ATOM    721  CG1 ILE A 110       4.465  24.587  31.931  1.00 49.34           C  
ATOM    722  CG2 ILE A 110       3.496  24.515  34.277  1.00 48.37           C  
ATOM    723  CD1 ILE A 110       4.749  26.108  31.536  1.00 50.85           C  
ATOM    724  N   GLY A 111       0.193  23.085  33.174  1.00 51.05           N  
ATOM    725  CA  GLY A 111      -1.000  22.785  33.957  1.00 50.83           C  
ATOM    726  C   GLY A 111      -1.399  21.325  33.838  1.00 54.26           C  
ATOM    727  O   GLY A 111      -1.846  20.740  34.825  1.00 55.02           O  
ATOM    728  N   PHE A 112      -1.214  20.708  32.647  1.00 49.96           N  
ATOM    729  CA  PHE A 112      -1.505  19.290  32.450  1.00 50.24           C  
ATOM    730  C   PHE A 112      -0.500  18.407  33.235  1.00 56.33           C  
ATOM    731  O   PHE A 112      -0.936  17.606  34.071  1.00 56.02           O  
ATOM    732  CB  PHE A 112      -1.587  18.887  30.951  1.00 51.90           C  
ATOM    733  CG  PHE A 112      -1.766  17.394  30.715  1.00 53.42           C  
ATOM    734  CD1 PHE A 112      -3.036  16.818  30.705  1.00 55.68           C  
ATOM    735  CD2 PHE A 112      -0.661  16.555  30.544  1.00 54.60           C  
ATOM    736  CE1 PHE A 112      -3.194  15.430  30.542  1.00 55.51           C  
ATOM    737  CE2 PHE A 112      -0.826  15.171  30.365  1.00 56.14           C  
ATOM    738  CZ  PHE A 112      -2.091  14.621  30.361  1.00 53.81           C  
ATOM    739  N   PHE A 113       0.829  18.561  32.980  1.00 53.37           N  
ATOM    740  CA  PHE A 113       1.875  17.746  33.624  1.00 53.17           C  
ATOM    741  C   PHE A 113       1.925  17.877  35.147  1.00 58.52           C  
ATOM    742  O   PHE A 113       1.809  16.864  35.833  1.00 57.66           O  
ATOM    743  CB  PHE A 113       3.256  17.999  33.007  1.00 54.74           C  
ATOM    744  CG  PHE A 113       3.422  17.439  31.615  1.00 56.13           C  
ATOM    745  CD1 PHE A 113       3.269  16.078  31.370  1.00 59.37           C  
ATOM    746  CD2 PHE A 113       3.777  18.265  30.556  1.00 57.77           C  
ATOM    747  CE1 PHE A 113       3.421  15.563  30.080  1.00 60.20           C  
ATOM    748  CE2 PHE A 113       3.941  17.747  29.270  1.00 60.46           C  
ATOM    749  CZ  PHE A 113       3.760  16.402  29.040  1.00 58.52           C  
ATOM    750  N   SER A 114       2.058  19.109  35.680  1.00 57.22           N  
ATOM    751  CA  SER A 114       2.093  19.350  37.129  1.00 57.79           C  
ATOM    752  C   SER A 114       0.837  18.830  37.832  1.00 63.07           C  
ATOM    753  O   SER A 114       0.938  18.329  38.950  1.00 63.15           O  
ATOM    754  CB  SER A 114       2.348  20.821  37.455  1.00 61.55           C  
ATOM    755  OG  SER A 114       1.279  21.658  37.048  1.00 70.67           O  
ATOM    756  N   GLY A 115      -0.306  18.892  37.144  1.00 59.96           N  
ATOM    757  CA  GLY A 115      -1.576  18.377  37.637  1.00 60.03           C  
ATOM    758  C   GLY A 115      -1.480  16.907  37.996  1.00 64.71           C  
ATOM    759  O   GLY A 115      -1.762  16.530  39.131  1.00 65.57           O  
ATOM    760  N   ILE A 116      -1.011  16.077  37.066  1.00 61.26           N  
ATOM    761  CA  ILE A 116      -0.866  14.640  37.323  1.00 61.53           C  
ATOM    762  C   ILE A 116       0.322  14.377  38.261  1.00 66.24           C  
ATOM    763  O   ILE A 116       0.205  13.534  39.149  1.00 65.54           O  
ATOM    764  CB  ILE A 116      -0.861  13.759  36.021  1.00 64.42           C  
ATOM    765  CG1 ILE A 116      -0.924  12.248  36.336  1.00 65.51           C  
ATOM    766  CG2 ILE A 116       0.274  14.078  35.061  1.00 63.34           C  
ATOM    767  CD1 ILE A 116      -2.090  11.789  37.319  1.00 75.20           C  
ATOM    768  N   PHE A 117       1.417  15.150  38.106  1.00 63.68           N  
ATOM    769  CA  PHE A 117       2.618  15.068  38.934  1.00 64.10           C  
ATOM    770  C   PHE A 117       2.302  15.232  40.433  1.00 67.61           C  
ATOM    771  O   PHE A 117       2.836  14.469  41.238  1.00 67.26           O  
ATOM    772  CB  PHE A 117       3.661  16.106  38.495  1.00 66.44           C  
ATOM    773  CG  PHE A 117       4.430  15.864  37.215  1.00 68.56           C  
ATOM    774  CD1 PHE A 117       4.357  14.641  36.557  1.00 72.15           C  
ATOM    775  CD2 PHE A 117       5.250  16.850  36.682  1.00 71.36           C  
ATOM    776  CE1 PHE A 117       5.072  14.418  35.376  1.00 73.37           C  
ATOM    777  CE2 PHE A 117       5.976  16.620  35.505  1.00 74.44           C  
ATOM    778  CZ  PHE A 117       5.874  15.410  34.856  1.00 72.47           C  
ATOM    779  N   PHE A 118       1.408  16.193  40.795  1.00 63.33           N  
ATOM    780  CA  PHE A 118       0.963  16.437  42.175  1.00 62.29           C  
ATOM    781  C   PHE A 118      -0.037  15.375  42.677  1.00 66.43           C  
ATOM    782  O   PHE A 118      -0.091  15.152  43.881  1.00 66.17           O  
ATOM    783  CB  PHE A 118       0.435  17.873  42.374  1.00 63.57           C  
ATOM    784  CG  PHE A 118       1.541  18.910  42.416  1.00 64.98           C  
ATOM    785  CD1 PHE A 118       2.503  18.891  43.423  1.00 67.82           C  
ATOM    786  CD2 PHE A 118       1.620  19.907  41.450  1.00 67.17           C  
ATOM    787  CE1 PHE A 118       3.542  19.826  43.443  1.00 68.43           C  
ATOM    788  CE2 PHE A 118       2.669  20.833  41.462  1.00 69.91           C  
ATOM    789  CZ  PHE A 118       3.617  20.793  42.467  1.00 67.81           C  
ATOM    790  N   ILE A 119      -0.781  14.688  41.768  1.00 63.33           N  
ATOM    791  CA  ILE A 119      -1.715  13.601  42.121  1.00 63.90           C  
ATOM    792  C   ILE A 119      -0.902  12.362  42.526  1.00 69.76           C  
ATOM    793  O   ILE A 119      -1.266  11.667  43.477  1.00 69.10           O  
ATOM    794  CB  ILE A 119      -2.752  13.312  40.989  1.00 67.15           C  
ATOM    795  CG1 ILE A 119      -3.803  14.444  40.902  1.00 67.66           C  
ATOM    796  CG2 ILE A 119      -3.444  11.945  41.164  1.00 67.37           C  
ATOM    797  CD1 ILE A 119      -4.589  14.542  39.544  1.00 74.78           C  
ATOM    798  N   ILE A 120       0.198  12.103  41.788  1.00 68.31           N  
ATOM    799  CA  ILE A 120       1.153  11.014  42.020  1.00 68.64           C  
ATOM    800  C   ILE A 120       1.858  11.261  43.373  1.00 74.04           C  
ATOM    801  O   ILE A 120       2.032  10.324  44.155  1.00 73.91           O  
ATOM    802  CB  ILE A 120       2.153  10.924  40.827  1.00 71.50           C  
ATOM    803  CG1 ILE A 120       1.447  10.461  39.542  1.00 71.75           C  
ATOM    804  CG2 ILE A 120       3.358  10.024  41.141  1.00 72.07           C  
ATOM    805  CD1 ILE A 120       2.078  10.964  38.270  1.00 78.94           C  
ATOM    806  N   LEU A 121       2.231  12.534  43.649  1.00 70.93           N  
ATOM    807  CA  LEU A 121       2.873  12.953  44.897  1.00 70.79           C  
ATOM    808  C   LEU A 121       1.897  12.856  46.073  1.00 77.62           C  
ATOM    809  O   LEU A 121       2.338  12.690  47.206  1.00 77.09           O  
ATOM    810  CB  LEU A 121       3.451  14.365  44.776  1.00 70.41           C  
ATOM    811  CG  LEU A 121       4.787  14.487  44.060  1.00 74.60           C  
ATOM    812  CD1 LEU A 121       4.917  15.832  43.414  1.00 74.37           C  
ATOM    813  CD2 LEU A 121       5.961  14.255  45.011  1.00 77.45           C  
ATOM    814  N   LEU A 122       0.578  12.951  45.800  1.00 76.70           N  
ATOM    815  CA  LEU A 122      -0.481  12.794  46.793  1.00 77.89           C  
ATOM    816  C   LEU A 122      -0.740  11.297  47.025  1.00 84.52           C  
ATOM    817  O   LEU A 122      -1.213  10.910  48.090  1.00 85.27           O  
ATOM    818  CB  LEU A 122      -1.774  13.498  46.342  1.00 78.20           C  
ATOM    819  CG  LEU A 122      -1.896  14.998  46.670  1.00 83.64           C  
ATOM    820  CD1 LEU A 122      -2.875  15.689  45.737  1.00 83.69           C  
ATOM    821  CD2 LEU A 122      -2.293  15.240  48.137  1.00 87.11           C  
ATOM    822  N   THR A 123      -0.427  10.461  46.026  1.00 81.67           N  
ATOM    823  CA  THR A 123      -0.582   9.009  46.091  1.00 81.60           C  
ATOM    824  C   THR A 123       0.587   8.405  46.888  1.00 86.95           C  
ATOM    825  O   THR A 123       0.353   7.663  47.843  1.00 86.51           O  
ATOM    826  CB  THR A 123      -0.709   8.438  44.674  1.00 84.29           C  
ATOM    827  OG1 THR A 123      -1.814   9.069  44.027  1.00 82.15           O  
ATOM    828  CG2 THR A 123      -0.881   6.927  44.662  1.00 81.24           C  
ATOM    829  N   ILE A 124       1.840   8.729  46.490  1.00 84.40           N  
ATOM    830  CA  ILE A 124       3.072   8.254  47.128  1.00 84.76           C  
ATOM    831  C   ILE A 124       3.075   8.682  48.598  1.00 90.56           C  
ATOM    832  O   ILE A 124       3.483   7.905  49.459  1.00 90.49           O  
ATOM    833  CB  ILE A 124       4.335   8.709  46.329  1.00 87.74           C  
ATOM    834  CG1 ILE A 124       4.392   8.022  44.937  1.00 87.91           C  
ATOM    835  CG2 ILE A 124       5.639   8.455  47.110  1.00 88.45           C  
ATOM    836  CD1 ILE A 124       5.350   8.662  43.915  1.00 93.63           C  
ATOM    837  N   ASP A 125       2.559   9.896  48.867  1.00 88.34           N  
ATOM    838  CA  ASP A 125       2.395  10.512  50.178  1.00 88.50           C  
ATOM    839  C   ASP A 125       1.559   9.605  51.104  1.00 92.75           C  
ATOM    840  O   ASP A 125       2.005   9.288  52.206  1.00 92.19           O  
ATOM    841  CB  ASP A 125       1.731  11.877  49.980  1.00 90.44           C  
ATOM    842  CG  ASP A 125       1.375  12.626  51.242  1.00 99.70           C  
ATOM    843  OD1 ASP A 125       0.246  12.416  51.756  1.00105.68           O  
ATOM    844  OD2 ASP A 125       2.195  13.486  51.678  1.00100.09           O  
ATOM    845  N   ARG A 126       0.378   9.153  50.632  1.00 90.22           N  
ATOM    846  CA  ARG A 126      -0.515   8.243  51.360  1.00 90.64           C  
ATOM    847  C   ARG A 126       0.120   6.861  51.533  1.00 97.23           C  
ATOM    848  O   ARG A 126      -0.165   6.181  52.517  1.00 97.39           O  
ATOM    849  CB  ARG A 126      -1.878   8.113  50.654  1.00 89.76           C  
ATOM    850  CG  ARG A 126      -2.747   9.365  50.660  1.00 96.78           C  
ATOM    851  CD  ARG A 126      -3.318   9.687  52.025  1.00103.32           C  
ATOM    852  NE  ARG A 126      -2.497  10.665  52.738  1.00108.95           N  
ATOM    853  CZ  ARG A 126      -2.369  10.711  54.059  1.00122.35           C  
ATOM    854  NH1 ARG A 126      -3.002   9.833  54.827  1.00113.84           N  
ATOM    855  NH2 ARG A 126      -1.611  11.638  54.624  1.00106.06           N  
ATOM    856  N   TYR A 127       0.977   6.450  50.574  1.00 94.89           N  
ATOM    857  CA  TYR A 127       1.711   5.188  50.635  1.00 95.10           C  
ATOM    858  C   TYR A 127       2.786   5.300  51.715  1.00 99.89           C  
ATOM    859  O   TYR A 127       3.056   4.319  52.402  1.00 99.43           O  
ATOM    860  CB  TYR A 127       2.315   4.830  49.261  1.00 96.29           C  
ATOM    861  CG  TYR A 127       3.165   3.576  49.266  1.00 98.11           C  
ATOM    862  CD1 TYR A 127       2.582   2.314  49.243  1.00100.15           C  
ATOM    863  CD2 TYR A 127       4.556   3.652  49.292  1.00 98.92           C  
ATOM    864  CE1 TYR A 127       3.358   1.156  49.243  1.00101.51           C  
ATOM    865  CE2 TYR A 127       5.344   2.501  49.303  1.00 99.85           C  
ATOM    866  CZ  TYR A 127       4.741   1.255  49.275  1.00107.95           C  
ATOM    867  OH  TYR A 127       5.509   0.117  49.274  1.00109.66           O  
ATOM    868  N   LEU A 128       3.380   6.498  51.870  1.00 97.43           N  
ATOM    869  CA  LEU A 128       4.399   6.764  52.881  1.00 98.05           C  
ATOM    870  C   LEU A 128       3.782   6.936  54.273  1.00103.91           C  
ATOM    871  O   LEU A 128       4.442   6.629  55.263  1.00103.66           O  
ATOM    872  CB  LEU A 128       5.250   7.997  52.520  1.00 98.14           C  
ATOM    873  CG  LEU A 128       6.268   7.864  51.381  1.00103.04           C  
ATOM    874  CD1 LEU A 128       6.889   9.216  51.066  1.00103.20           C  
ATOM    875  CD2 LEU A 128       7.361   6.830  51.696  1.00105.54           C  
ATOM    876  N   ALA A 129       2.527   7.416  54.355  1.00101.65           N  
ATOM    877  CA  ALA A 129       1.838   7.599  55.629  1.00102.02           C  
ATOM    878  C   ALA A 129       1.347   6.258  56.188  1.00107.51           C  
ATOM    879  O   ALA A 129       1.609   5.972  57.359  1.00107.21           O  
ATOM    880  CB  ALA A 129       0.686   8.576  55.472  1.00102.76           C  
ATOM    881  N   VAL A 130       0.668   5.428  55.346  1.00105.13           N  
ATOM    882  CA  VAL A 130       0.131   4.104  55.708  1.00105.50           C  
ATOM    883  C   VAL A 130       1.290   3.111  55.919  1.00112.98           C  
ATOM    884  O   VAL A 130       1.576   2.747  57.061  1.00112.42           O  
ATOM    885  CB  VAL A 130      -0.948   3.591  54.706  1.00108.59           C  
ATOM    886  CG1 VAL A 130      -1.447   2.203  55.087  1.00108.16           C  
ATOM    887  CG2 VAL A 130      -2.122   4.557  54.611  1.00108.25           C  
ATOM    888  N   VAL A 131       1.960   2.703  54.825  1.00112.69           N  
ATOM    889  CA  VAL A 131       3.120   1.804  54.849  1.00113.92           C  
ATOM    890  C   VAL A 131       4.331   2.675  55.222  1.00121.59           C  
ATOM    891  O   VAL A 131       4.324   3.857  54.891  1.00121.46           O  
ATOM    892  CB  VAL A 131       3.347   1.097  53.484  1.00117.73           C  
ATOM    893  CG1 VAL A 131       4.097  -0.219  53.667  1.00117.63           C  
ATOM    894  CG2 VAL A 131       2.035   0.871  52.734  1.00117.47           C  
ATOM    895  N   HIS A 132       5.369   2.102  55.887  1.00120.70           N  
ATOM    896  CA  HIS A 132       6.596   2.798  56.336  1.00121.63           C  
ATOM    897  C   HIS A 132       6.251   3.962  57.284  1.00127.76           C  
ATOM    898  O   HIS A 132       6.807   5.057  57.150  1.00127.42           O  
ATOM    899  CB  HIS A 132       7.466   3.284  55.147  1.00122.62           C  
ATOM    900  CG  HIS A 132       7.623   2.287  54.041  1.00126.34           C  
ATOM    901  ND1 HIS A 132       6.659   2.138  53.056  1.00128.21           N  
ATOM    902  CD2 HIS A 132       8.641   1.433  53.788  1.00128.44           C  
ATOM    903  CE1 HIS A 132       7.110   1.189  52.253  1.00127.81           C  
ATOM    904  NE2 HIS A 132       8.298   0.734  52.652  1.00128.23           N  
ATOM    905  N   ALA A 133       5.313   3.717  58.233  1.00126.18           N  
ATOM    906  CA  ALA A 133       4.811   4.691  59.216  1.00126.87           C  
ATOM    907  C   ALA A 133       5.915   5.336  60.063  1.00132.97           C  
ATOM    908  O   ALA A 133       5.754   6.473  60.516  1.00132.45           O  
ATOM    909  CB  ALA A 133       3.769   4.042  60.109  1.00127.57           C  
ATOM    910  N   VAL A 134       7.034   4.606  60.264  1.00131.19           N  
ATOM    911  CA  VAL A 134       8.219   5.051  61.009  1.00131.60           C  
ATOM    912  C   VAL A 134       9.002   6.121  60.200  1.00135.81           C  
ATOM    913  O   VAL A 134       9.552   7.058  60.782  1.00135.03           O  
ATOM    914  CB  VAL A 134       9.089   3.840  61.485  1.00135.75           C  
ATOM    915  CG1 VAL A 134       9.649   3.022  60.316  1.00135.52           C  
ATOM    916  CG2 VAL A 134      10.195   4.270  62.447  1.00135.65           C  
ATOM    917  N   PHE A 135       9.014   5.979  58.858  1.00132.94           N  
ATOM    918  CA  PHE A 135       9.665   6.896  57.923  1.00133.03           C  
ATOM    919  C   PHE A 135       8.757   8.082  57.608  1.00136.82           C  
ATOM    920  O   PHE A 135       9.260   9.158  57.274  1.00136.66           O  
ATOM    921  CB  PHE A 135      10.055   6.158  56.633  1.00135.13           C  
ATOM    922  CG  PHE A 135      10.641   7.031  55.548  1.00137.16           C  
ATOM    923  CD1 PHE A 135      11.841   7.708  55.746  1.00140.56           C  
ATOM    924  CD2 PHE A 135      10.000   7.172  54.324  1.00139.80           C  
ATOM    925  CE1 PHE A 135      12.386   8.509  54.738  1.00141.67           C  
ATOM    926  CE2 PHE A 135      10.548   7.973  53.316  1.00142.82           C  
ATOM    927  CZ  PHE A 135      11.735   8.639  53.531  1.00140.93           C  
ATOM    928  N   ALA A 136       7.421   7.881  57.726  1.00132.88           N  
ATOM    929  CA  ALA A 136       6.381   8.889  57.510  1.00132.36           C  
ATOM    930  C   ALA A 136       6.590  10.074  58.438  1.00135.41           C  
ATOM    931  O   ALA A 136       6.852  11.171  57.963  1.00134.96           O  
ATOM    932  CB  ALA A 136       5.004   8.285  57.750  1.00133.08           C  
ATOM    933  N   LEU A 137       6.540   9.830  59.758  1.00131.46           N  
ATOM    934  CA  LEU A 137       6.724  10.831  60.813  1.00131.07           C  
ATOM    935  C   LEU A 137       8.092  11.520  60.737  1.00133.94           C  
ATOM    936  O   LEU A 137       8.192  12.714  61.026  1.00133.49           O  
ATOM    937  CB  LEU A 137       6.510  10.200  62.201  1.00131.29           C  
ATOM    938  CG  LEU A 137       5.173   9.480  62.442  1.00136.31           C  
ATOM    939  CD1 LEU A 137       5.229   8.630  63.694  1.00136.60           C  
ATOM    940  CD2 LEU A 137       4.000  10.459  62.529  1.00138.98           C  
ATOM    941  N   LYS A 138       9.129  10.775  60.307  1.00129.68           N  
ATOM    942  CA  LYS A 138      10.494  11.274  60.145  1.00128.98           C  
ATOM    943  C   LYS A 138      10.623  12.213  58.938  1.00131.21           C  
ATOM    944  O   LYS A 138      11.126  13.327  59.095  1.00130.73           O  
ATOM    945  CB  LYS A 138      11.493  10.104  60.044  1.00131.64           C  
ATOM    946  N   ALA A 139      10.157  11.771  57.744  1.00126.26           N  
ATOM    947  CA  ALA A 139      10.250  12.545  56.502  1.00125.26           C  
ATOM    948  C   ALA A 139       8.893  12.862  55.826  1.00127.45           C  
ATOM    949  O   ALA A 139       8.563  12.275  54.790  1.00126.93           O  
ATOM    950  CB  ALA A 139      11.195  11.854  55.527  1.00125.90           C  
ATOM    951  N   ARG A 140       8.126  13.813  56.422  1.00122.31           N  
ATOM    952  CA  ARG A 140       6.834  14.341  55.953  1.00121.07           C  
ATOM    953  C   ARG A 140       6.596  15.766  56.478  1.00122.25           C  
ATOM    954  O   ARG A 140       5.549  16.071  57.064  1.00121.43           O  
ATOM    955  CB  ARG A 140       5.661  13.396  56.260  1.00121.47           C  
ATOM    956  CG  ARG A 140       5.418  12.356  55.174  1.00131.26           C  
ATOM    957  CD  ARG A 140       4.444  11.291  55.623  1.00140.26           C  
ATOM    958  NE  ARG A 140       3.221  11.334  54.832  1.00148.40           N  
ATOM    959  CZ  ARG A 140       2.134  12.022  55.165  1.00163.88           C  
ATOM    960  NH1 ARG A 140       2.106  12.747  56.275  1.00150.95           N  
ATOM    961  NH2 ARG A 140       1.071  12.000  54.376  1.00151.67           N  
ATOM    962  N   THR A 141       7.601  16.632  56.263  1.00117.15           N  
ATOM    963  CA  THR A 141       7.594  18.029  56.701  1.00116.09           C  
ATOM    964  C   THR A 141       6.952  18.939  55.649  1.00117.95           C  
ATOM    965  O   THR A 141       6.853  18.565  54.473  1.00117.33           O  
ATOM    966  CB  THR A 141       9.023  18.499  57.069  1.00123.73           C  
ATOM    967  OG1 THR A 141       9.859  18.415  55.916  1.00124.17           O  
ATOM    968  CG2 THR A 141       9.634  17.694  58.211  1.00122.07           C  
ATOM    969  N   VAL A 142       6.508  20.131  56.090  1.00113.06           N  
ATOM    970  CA  VAL A 142       5.896  21.163  55.254  1.00112.07           C  
ATOM    971  C   VAL A 142       6.975  21.768  54.331  1.00116.08           C  
ATOM    972  O   VAL A 142       6.734  21.906  53.130  1.00116.34           O  
ATOM    973  CB  VAL A 142       5.159  22.221  56.121  1.00115.09           C  
ATOM    974  CG1 VAL A 142       4.740  23.437  55.302  1.00114.73           C  
ATOM    975  CG2 VAL A 142       3.953  21.605  56.820  1.00114.76           C  
ATOM    976  N   THR A 143       8.172  22.071  54.889  1.00111.37           N  
ATOM    977  CA  THR A 143       9.326  22.653  54.181  1.00110.15           C  
ATOM    978  C   THR A 143       9.821  21.776  53.029  1.00111.59           C  
ATOM    979  O   THR A 143      10.101  22.301  51.950  1.00110.97           O  
ATOM    980  CB  THR A 143      10.444  23.005  55.158  1.00117.22           C  
ATOM    981  OG1 THR A 143      10.800  21.835  55.895  1.00116.41           O  
ATOM    982  CG2 THR A 143      10.053  24.136  56.106  1.00115.23           C  
ATOM    983  N   PHE A 144       9.904  20.446  53.249  1.00106.47           N  
ATOM    984  CA  PHE A 144      10.312  19.477  52.227  1.00105.23           C  
ATOM    985  C   PHE A 144       9.192  19.302  51.195  1.00106.74           C  
ATOM    986  O   PHE A 144       9.477  19.043  50.024  1.00106.47           O  
ATOM    987  CB  PHE A 144      10.710  18.135  52.864  1.00107.14           C  
ATOM    988  CG  PHE A 144      11.041  17.008  51.909  1.00109.19           C  
ATOM    989  CD1 PHE A 144      12.232  17.011  51.187  1.00112.58           C  
ATOM    990  CD2 PHE A 144      10.178  15.927  51.758  1.00111.78           C  
ATOM    991  CE1 PHE A 144      12.543  15.964  50.313  1.00113.65           C  
ATOM    992  CE2 PHE A 144      10.492  14.877  50.887  1.00114.88           C  
ATOM    993  CZ  PHE A 144      11.672  14.901  50.171  1.00113.01           C  
ATOM    994  N   GLY A 145       7.944  19.482  51.638  1.00101.18           N  
ATOM    995  CA  GLY A 145       6.754  19.416  50.798  1.00 99.92           C  
ATOM    996  C   GLY A 145       6.744  20.520  49.764  1.00101.53           C  
ATOM    997  O   GLY A 145       6.335  20.295  48.624  1.00100.99           O  
ATOM    998  N   VAL A 146       7.233  21.714  50.161  1.00 96.63           N  
ATOM    999  CA  VAL A 146       7.366  22.906  49.318  1.00 95.85           C  
ATOM   1000  C   VAL A 146       8.555  22.703  48.365  1.00 98.21           C  
ATOM   1001  O   VAL A 146       8.447  23.021  47.180  1.00 98.22           O  
ATOM   1002  CB  VAL A 146       7.496  24.199  50.177  1.00 99.79           C  
ATOM   1003  CG1 VAL A 146       7.822  25.422  49.322  1.00 99.65           C  
ATOM   1004  CG2 VAL A 146       6.229  24.447  50.991  1.00 99.65           C  
ATOM   1005  N   VAL A 147       9.676  22.153  48.888  1.00 92.65           N  
ATOM   1006  CA  VAL A 147      10.893  21.846  48.130  1.00 90.99           C  
ATOM   1007  C   VAL A 147      10.567  20.888  46.979  1.00 90.68           C  
ATOM   1008  O   VAL A 147      10.908  21.200  45.838  1.00 89.92           O  
ATOM   1009  CB  VAL A 147      12.043  21.365  49.062  1.00 95.03           C  
ATOM   1010  CG1 VAL A 147      13.118  20.575  48.307  1.00 94.85           C  
ATOM   1011  CG2 VAL A 147      12.661  22.546  49.805  1.00 94.76           C  
ATOM   1012  N   THR A 148       9.846  19.775  47.263  1.00 85.00           N  
ATOM   1013  CA  THR A 148       9.422  18.801  46.238  1.00 84.22           C  
ATOM   1014  C   THR A 148       8.469  19.455  45.247  1.00 84.79           C  
ATOM   1015  O   THR A 148       8.497  19.113  44.072  1.00 83.29           O  
ATOM   1016  CB  THR A 148       8.741  17.564  46.848  1.00 96.31           C  
ATOM   1017  OG1 THR A 148       7.687  17.982  47.715  1.00100.07           O  
ATOM   1018  CG2 THR A 148       9.709  16.656  47.581  1.00 95.07           C  
ATOM   1019  N   SER A 149       7.641  20.401  45.726  1.00 80.16           N  
ATOM   1020  CA  SER A 149       6.683  21.136  44.915  1.00 79.40           C  
ATOM   1021  C   SER A 149       7.369  22.092  43.950  1.00 81.59           C  
ATOM   1022  O   SER A 149       6.930  22.211  42.811  1.00 81.58           O  
ATOM   1023  CB  SER A 149       5.684  21.874  45.795  1.00 83.14           C  
ATOM   1024  OG  SER A 149       4.827  20.965  46.469  1.00 91.18           O  
ATOM   1025  N   VAL A 150       8.451  22.748  44.387  1.00 76.87           N  
ATOM   1026  CA  VAL A 150       9.250  23.665  43.559  1.00 76.19           C  
ATOM   1027  C   VAL A 150       9.891  22.874  42.395  1.00 78.93           C  
ATOM   1028  O   VAL A 150       9.812  23.294  41.243  1.00 78.26           O  
ATOM   1029  CB  VAL A 150      10.311  24.421  44.417  1.00 79.59           C  
ATOM   1030  CG1 VAL A 150      11.383  25.077  43.549  1.00 79.15           C  
ATOM   1031  CG2 VAL A 150       9.652  25.455  45.324  1.00 79.38           C  
ATOM   1032  N   ILE A 151      10.487  21.717  42.712  1.00 74.88           N  
ATOM   1033  CA  ILE A 151      11.150  20.832  41.757  1.00 74.81           C  
ATOM   1034  C   ILE A 151      10.107  20.147  40.838  1.00 77.96           C  
ATOM   1035  O   ILE A 151      10.427  19.859  39.682  1.00 78.40           O  
ATOM   1036  CB  ILE A 151      12.132  19.870  42.502  1.00 78.22           C  
ATOM   1037  CG1 ILE A 151      13.381  20.680  42.957  1.00 79.39           C  
ATOM   1038  CG2 ILE A 151      12.559  18.668  41.652  1.00 78.30           C  
ATOM   1039  CD1 ILE A 151      14.190  20.159  44.145  1.00 90.03           C  
ATOM   1040  N   THR A 152       8.854  19.968  41.314  1.00 72.51           N  
ATOM   1041  CA  THR A 152       7.775  19.390  40.506  1.00 71.29           C  
ATOM   1042  C   THR A 152       7.336  20.383  39.423  1.00 73.87           C  
ATOM   1043  O   THR A 152       7.214  19.984  38.256  1.00 74.80           O  
ATOM   1044  CB  THR A 152       6.642  18.855  41.384  1.00 76.56           C  
ATOM   1045  OG1 THR A 152       7.151  17.750  42.124  1.00 74.27           O  
ATOM   1046  CG2 THR A 152       5.448  18.382  40.582  1.00 75.17           C  
ATOM   1047  N   TRP A 153       7.151  21.675  39.795  1.00 67.35           N  
ATOM   1048  CA  TRP A 153       6.781  22.741  38.858  1.00 66.25           C  
ATOM   1049  C   TRP A 153       7.884  22.993  37.825  1.00 70.24           C  
ATOM   1050  O   TRP A 153       7.588  23.407  36.704  1.00 70.09           O  
ATOM   1051  CB  TRP A 153       6.463  24.031  39.598  1.00 64.71           C  
ATOM   1052  CG  TRP A 153       5.082  24.088  40.182  1.00 65.55           C  
ATOM   1053  CD1 TRP A 153       4.742  23.977  41.499  1.00 68.34           C  
ATOM   1054  CD2 TRP A 153       3.866  24.355  39.473  1.00 65.31           C  
ATOM   1055  NE1 TRP A 153       3.385  24.135  41.653  1.00 67.80           N  
ATOM   1056  CE2 TRP A 153       2.821  24.369  40.424  1.00 69.31           C  
ATOM   1057  CE3 TRP A 153       3.554  24.585  38.121  1.00 66.35           C  
ATOM   1058  CZ2 TRP A 153       1.485  24.591  40.066  1.00 68.48           C  
ATOM   1059  CZ3 TRP A 153       2.229  24.810  37.769  1.00 67.56           C  
ATOM   1060  CH2 TRP A 153       1.215  24.820  38.734  1.00 68.17           C  
ATOM   1061  N   VAL A 154       9.149  22.722  38.193  1.00 66.22           N  
ATOM   1062  CA  VAL A 154      10.290  22.876  37.298  1.00 65.78           C  
ATOM   1063  C   VAL A 154      10.261  21.760  36.251  1.00 70.46           C  
ATOM   1064  O   VAL A 154      10.298  22.071  35.064  1.00 70.91           O  
ATOM   1065  CB  VAL A 154      11.633  22.974  38.078  1.00 69.34           C  
ATOM   1066  CG1 VAL A 154      12.843  22.696  37.180  1.00 68.93           C  
ATOM   1067  CG2 VAL A 154      11.767  24.333  38.764  1.00 69.09           C  
ATOM   1068  N   VAL A 155      10.155  20.478  36.691  1.00 66.52           N  
ATOM   1069  CA  VAL A 155      10.106  19.276  35.840  1.00 66.01           C  
ATOM   1070  C   VAL A 155       8.953  19.389  34.827  1.00 68.59           C  
ATOM   1071  O   VAL A 155       9.151  19.097  33.640  1.00 67.99           O  
ATOM   1072  CB  VAL A 155      10.064  17.966  36.694  1.00 70.30           C  
ATOM   1073  CG1 VAL A 155       9.661  16.731  35.875  1.00 69.89           C  
ATOM   1074  CG2 VAL A 155      11.398  17.720  37.391  1.00 70.21           C  
ATOM   1075  N   ALA A 156       7.775  19.863  35.295  1.00 64.03           N  
ATOM   1076  CA  ALA A 156       6.591  20.084  34.468  1.00 63.62           C  
ATOM   1077  C   ALA A 156       6.910  21.032  33.299  1.00 67.61           C  
ATOM   1078  O   ALA A 156       6.550  20.724  32.163  1.00 68.40           O  
ATOM   1079  CB  ALA A 156       5.459  20.645  35.316  1.00 64.28           C  
ATOM   1080  N   VAL A 157       7.634  22.148  33.581  1.00 62.09           N  
ATOM   1081  CA  VAL A 157       8.072  23.157  32.618  1.00 60.95           C  
ATOM   1082  C   VAL A 157       8.990  22.545  31.552  1.00 65.50           C  
ATOM   1083  O   VAL A 157       8.756  22.767  30.361  1.00 65.92           O  
ATOM   1084  CB  VAL A 157       8.687  24.391  33.330  1.00 64.10           C  
ATOM   1085  CG1 VAL A 157       9.508  25.261  32.376  1.00 63.69           C  
ATOM   1086  CG2 VAL A 157       7.604  25.220  34.005  1.00 63.81           C  
ATOM   1087  N   PHE A 158      10.001  21.761  31.969  1.00 61.89           N  
ATOM   1088  CA  PHE A 158      10.927  21.081  31.058  1.00 62.30           C  
ATOM   1089  C   PHE A 158      10.207  20.044  30.175  1.00 65.39           C  
ATOM   1090  O   PHE A 158      10.566  19.879  29.007  1.00 65.27           O  
ATOM   1091  CB  PHE A 158      12.092  20.434  31.831  1.00 65.00           C  
ATOM   1092  CG  PHE A 158      13.230  21.366  32.199  1.00 67.43           C  
ATOM   1093  CD1 PHE A 158      14.135  21.805  31.233  1.00 71.64           C  
ATOM   1094  CD2 PHE A 158      13.432  21.760  33.518  1.00 69.58           C  
ATOM   1095  CE1 PHE A 158      15.196  22.653  31.575  1.00 72.60           C  
ATOM   1096  CE2 PHE A 158      14.496  22.604  33.860  1.00 72.62           C  
ATOM   1097  CZ  PHE A 158      15.374  23.038  32.889  1.00 71.10           C  
ATOM   1098  N   ALA A 159       9.170  19.382  30.716  1.00 61.11           N  
ATOM   1099  CA  ALA A 159       8.352  18.420  29.966  1.00 60.77           C  
ATOM   1100  C   ALA A 159       7.480  19.129  28.885  1.00 63.98           C  
ATOM   1101  O   ALA A 159       7.273  18.587  27.792  1.00 62.79           O  
ATOM   1102  CB  ALA A 159       7.472  17.632  30.925  1.00 61.29           C  
ATOM   1103  N   SER A 160       6.994  20.349  29.212  1.00 60.37           N  
ATOM   1104  CA  SER A 160       6.145  21.221  28.387  1.00 59.45           C  
ATOM   1105  C   SER A 160       6.935  21.952  27.326  1.00 62.75           C  
ATOM   1106  O   SER A 160       6.401  22.228  26.254  1.00 61.97           O  
ATOM   1107  CB  SER A 160       5.475  22.273  29.263  1.00 62.07           C  
ATOM   1108  OG  SER A 160       4.636  21.680  30.236  1.00 73.28           O  
ATOM   1109  N   LEU A 161       8.194  22.301  27.653  1.00 59.56           N  
ATOM   1110  CA  LEU A 161       9.147  23.080  26.859  1.00 59.55           C  
ATOM   1111  C   LEU A 161       9.159  22.779  25.326  1.00 62.54           C  
ATOM   1112  O   LEU A 161       9.002  23.747  24.568  1.00 60.97           O  
ATOM   1113  CB  LEU A 161      10.557  22.936  27.468  1.00 59.88           C  
ATOM   1114  CG  LEU A 161      11.599  24.022  27.183  1.00 64.72           C  
ATOM   1115  CD1 LEU A 161      11.083  25.420  27.546  1.00 65.28           C  
ATOM   1116  CD2 LEU A 161      12.880  23.740  27.946  1.00 66.40           C  
ATOM   1117  N   PRO A 162       9.301  21.511  24.827  1.00 59.17           N  
ATOM   1118  CA  PRO A 162       9.321  21.302  23.362  1.00 59.47           C  
ATOM   1119  C   PRO A 162       8.026  21.684  22.659  1.00 63.91           C  
ATOM   1120  O   PRO A 162       8.045  22.212  21.546  1.00 63.68           O  
ATOM   1121  CB  PRO A 162       9.603  19.803  23.222  1.00 61.03           C  
ATOM   1122  CG  PRO A 162      10.211  19.410  24.514  1.00 64.67           C  
ATOM   1123  CD  PRO A 162       9.510  20.231  25.531  1.00 60.11           C  
ATOM   1124  N   ASN A 163       6.906  21.427  23.332  1.00 60.60           N  
ATOM   1125  CA  ASN A 163       5.562  21.686  22.840  1.00 60.27           C  
ATOM   1126  C   ASN A 163       5.248  23.171  22.726  1.00 65.56           C  
ATOM   1127  O   ASN A 163       4.510  23.551  21.823  1.00 65.56           O  
ATOM   1128  CB  ASN A 163       4.560  20.968  23.701  1.00 58.89           C  
ATOM   1129  CG  ASN A 163       4.846  19.484  23.842  1.00 82.41           C  
ATOM   1130  OD1 ASN A 163       5.338  19.005  24.870  1.00 73.97           O  
ATOM   1131  ND2 ASN A 163       4.553  18.720  22.799  1.00 76.68           N  
ATOM   1132  N   ILE A 164       5.839  24.009  23.611  1.00 62.35           N  
ATOM   1133  CA  ILE A 164       5.697  25.477  23.615  1.00 61.89           C  
ATOM   1134  C   ILE A 164       6.489  26.049  22.443  1.00 63.62           C  
ATOM   1135  O   ILE A 164       6.014  26.960  21.767  1.00 63.43           O  
ATOM   1136  CB  ILE A 164       6.181  26.102  24.960  1.00 65.30           C  
ATOM   1137  CG1 ILE A 164       5.456  25.468  26.173  1.00 65.82           C  
ATOM   1138  CG2 ILE A 164       6.057  27.643  24.958  1.00 65.93           C  
ATOM   1139  CD1 ILE A 164       6.204  25.557  27.489  1.00 75.39           C  
ATOM   1140  N   ILE A 165       7.704  25.516  22.225  1.00 58.73           N  
ATOM   1141  CA  ILE A 165       8.644  25.919  21.179  1.00 57.66           C  
ATOM   1142  C   ILE A 165       8.042  25.754  19.783  1.00 60.52           C  
ATOM   1143  O   ILE A 165       7.946  26.743  19.064  1.00 60.72           O  
ATOM   1144  CB  ILE A 165      10.000  25.190  21.369  1.00 60.52           C  
ATOM   1145  CG1 ILE A 165      10.828  25.868  22.484  1.00 60.70           C  
ATOM   1146  CG2 ILE A 165      10.789  25.081  20.064  1.00 61.45           C  
ATOM   1147  CD1 ILE A 165      11.837  24.953  23.187  1.00 68.88           C  
ATOM   1148  N   PHE A 166       7.575  24.546  19.426  1.00 56.13           N  
ATOM   1149  CA  PHE A 166       6.991  24.279  18.107  1.00 55.13           C  
ATOM   1150  C   PHE A 166       5.559  24.824  17.938  1.00 56.71           C  
ATOM   1151  O   PHE A 166       4.902  24.515  16.950  1.00 56.39           O  
ATOM   1152  CB  PHE A 166       7.082  22.782  17.765  1.00 57.29           C  
ATOM   1153  CG  PHE A 166       8.499  22.248  17.773  1.00 59.32           C  
ATOM   1154  CD1 PHE A 166       9.469  22.785  16.929  1.00 62.64           C  
ATOM   1155  CD2 PHE A 166       8.855  21.190  18.601  1.00 61.39           C  
ATOM   1156  CE1 PHE A 166      10.775  22.293  16.936  1.00 63.51           C  
ATOM   1157  CE2 PHE A 166      10.162  20.693  18.602  1.00 64.56           C  
ATOM   1158  CZ  PHE A 166      11.115  21.256  17.778  1.00 62.91           C  
ATOM   1159  N   THR A 167       5.095  25.662  18.871  1.00 52.10           N  
ATOM   1160  CA  THR A 167       3.783  26.293  18.802  1.00 51.51           C  
ATOM   1161  C   THR A 167       4.006  27.744  18.428  1.00 55.76           C  
ATOM   1162  O   THR A 167       4.851  28.419  19.021  1.00 55.21           O  
ATOM   1163  CB  THR A 167       2.997  26.110  20.122  1.00 59.24           C  
ATOM   1164  OG1 THR A 167       2.710  24.725  20.295  1.00 61.14           O  
ATOM   1165  CG2 THR A 167       1.683  26.869  20.142  1.00 58.06           C  
ATOM   1166  N   ARG A 168       3.259  28.209  17.420  1.00 52.95           N  
ATOM   1167  CA  ARG A 168       3.299  29.577  16.923  1.00 52.44           C  
ATOM   1168  C   ARG A 168       1.941  29.993  16.410  1.00 58.30           C  
ATOM   1169  O   ARG A 168       1.128  29.142  16.045  1.00 57.65           O  
ATOM   1170  CB  ARG A 168       4.363  29.747  15.814  1.00 50.74           C  
ATOM   1171  CG  ARG A 168       4.122  28.918  14.551  1.00 50.31           C  
ATOM   1172  CD  ARG A 168       4.958  29.390  13.389  1.00 51.32           C  
ATOM   1173  NE  ARG A 168       4.504  30.698  12.933  1.00 61.38           N  
ATOM   1174  CZ  ARG A 168       4.757  31.206  11.734  1.00 71.03           C  
ATOM   1175  NH1 ARG A 168       5.461  30.512  10.849  1.00 58.98           N  
ATOM   1176  NH2 ARG A 168       4.306  32.407  11.410  1.00 52.96           N  
ATOM   1177  N   SER A 169       1.708  31.303  16.334  1.00 57.31           N  
ATOM   1178  CA  SER A 169       0.473  31.795  15.754  1.00 57.64           C  
ATOM   1179  C   SER A 169       0.782  32.306  14.347  1.00 59.91           C  
ATOM   1180  O   SER A 169       1.572  33.234  14.192  1.00 60.34           O  
ATOM   1181  CB  SER A 169      -0.190  32.850  16.638  1.00 62.57           C  
ATOM   1182  OG  SER A 169       0.376  34.138  16.479  1.00 73.05           O  
ATOM   1183  N   GLN A 170       0.235  31.636  13.321  1.00 55.20           N  
ATOM   1184  CA  GLN A 170       0.443  31.998  11.910  1.00 54.20           C  
ATOM   1185  C   GLN A 170      -0.857  32.364  11.168  1.00 58.48           C  
ATOM   1186  O   GLN A 170      -1.917  31.816  11.458  1.00 57.23           O  
ATOM   1187  CB  GLN A 170       1.221  30.894  11.156  1.00 54.75           C  
ATOM   1188  CG  GLN A 170       0.462  29.571  10.996  1.00 55.59           C  
ATOM   1189  CD  GLN A 170       1.214  28.469  10.286  1.00 64.52           C  
ATOM   1190  OE1 GLN A 170       0.634  27.669   9.539  1.00 50.34           O  
ATOM   1191  NE2 GLN A 170       2.512  28.353  10.550  1.00 67.24           N  
ATOM   1192  N   LYS A 171      -0.758  33.271  10.194  1.00 57.42           N  
ATOM   1193  CA  LYS A 171      -1.878  33.674   9.349  1.00 57.68           C  
ATOM   1194  C   LYS A 171      -1.914  32.726   8.154  1.00 63.43           C  
ATOM   1195  O   LYS A 171      -0.914  32.580   7.454  1.00 62.86           O  
ATOM   1196  CB  LYS A 171      -1.743  35.135   8.891  1.00 59.35           C  
ATOM   1197  CG  LYS A 171      -3.057  35.727   8.373  1.00 74.82           C  
ATOM   1198  CD  LYS A 171      -2.873  37.153   7.870  1.00 82.42           C  
ATOM   1199  CE  LYS A 171      -4.102  37.734   7.231  1.00 88.02           C  
ATOM   1200  NZ  LYS A 171      -3.886  39.155   6.848  1.00 96.78           N  
ATOM   1201  N   GLU A 172      -3.047  32.041   7.974  1.00 61.58           N  
ATOM   1202  CA  GLU A 172      -3.317  31.097   6.889  1.00 61.92           C  
ATOM   1203  C   GLU A 172      -4.394  31.737   6.004  1.00 65.72           C  
ATOM   1204  O   GLU A 172      -5.572  31.709   6.343  1.00 65.29           O  
ATOM   1205  CB  GLU A 172      -3.791  29.739   7.460  1.00 63.43           C  
ATOM   1206  CG  GLU A 172      -2.702  28.944   8.160  1.00 75.60           C  
ATOM   1207  CD  GLU A 172      -3.117  27.639   8.814  1.00 97.74           C  
ATOM   1208  OE1 GLU A 172      -4.055  26.983   8.306  1.00 94.95           O  
ATOM   1209  OE2 GLU A 172      -2.465  27.247   9.808  1.00 91.74           O  
ATOM   1210  N   GLY A 173      -3.969  32.354   4.914  1.00 63.20           N  
ATOM   1211  CA  GLY A 173      -4.866  33.059   4.013  1.00 63.62           C  
ATOM   1212  C   GLY A 173      -5.409  34.295   4.699  1.00 69.36           C  
ATOM   1213  O   GLY A 173      -4.667  35.263   4.908  1.00 69.65           O  
ATOM   1214  N   LEU A 174      -6.696  34.246   5.103  1.00 65.94           N  
ATOM   1215  CA  LEU A 174      -7.371  35.352   5.798  1.00 65.70           C  
ATOM   1216  C   LEU A 174      -7.652  35.077   7.285  1.00 67.83           C  
ATOM   1217  O   LEU A 174      -8.141  35.968   7.984  1.00 67.86           O  
ATOM   1218  CB  LEU A 174      -8.669  35.752   5.067  1.00 66.06           C  
ATOM   1219  CG  LEU A 174      -8.510  36.621   3.820  1.00 71.38           C  
ATOM   1220  CD1 LEU A 174      -9.768  36.582   2.971  1.00 71.86           C  
ATOM   1221  CD2 LEU A 174      -8.146  38.059   4.179  1.00 74.06           C  
ATOM   1222  N   HIS A 175      -7.319  33.865   7.768  1.00 62.41           N  
ATOM   1223  CA  HIS A 175      -7.535  33.444   9.153  1.00 61.22           C  
ATOM   1224  C   HIS A 175      -6.246  33.193   9.911  1.00 62.46           C  
ATOM   1225  O   HIS A 175      -5.331  32.578   9.377  1.00 61.86           O  
ATOM   1226  CB  HIS A 175      -8.379  32.164   9.177  1.00 62.13           C  
ATOM   1227  N   TYR A 176      -6.200  33.618  11.178  1.00 57.77           N  
ATOM   1228  CA  TYR A 176      -5.072  33.387  12.086  1.00 56.61           C  
ATOM   1229  C   TYR A 176      -5.315  32.093  12.890  1.00 58.50           C  
ATOM   1230  O   TYR A 176      -6.439  31.839  13.347  1.00 56.35           O  
ATOM   1231  CB  TYR A 176      -4.892  34.565  13.057  1.00 57.85           C  
ATOM   1232  CG  TYR A 176      -4.407  35.834  12.404  1.00 60.52           C  
ATOM   1233  CD1 TYR A 176      -5.301  36.724  11.810  1.00 62.67           C  
ATOM   1234  CD2 TYR A 176      -3.056  36.161  12.389  1.00 61.81           C  
ATOM   1235  CE1 TYR A 176      -4.857  37.887  11.185  1.00 64.24           C  
ATOM   1236  CE2 TYR A 176      -2.599  37.330  11.778  1.00 62.89           C  
ATOM   1237  CZ  TYR A 176      -3.504  38.200  11.187  1.00 71.03           C  
ATOM   1238  OH  TYR A 176      -3.056  39.353  10.579  1.00 73.85           O  
ATOM   1239  N   THR A 177      -4.246  31.288  13.061  1.00 55.30           N  
ATOM   1240  CA  THR A 177      -4.256  30.031  13.818  1.00 55.41           C  
ATOM   1241  C   THR A 177      -3.221  30.070  14.947  1.00 59.90           C  
ATOM   1242  O   THR A 177      -2.294  30.869  14.899  1.00 58.00           O  
ATOM   1243  CB  THR A 177      -4.046  28.805  12.898  1.00 60.67           C  
ATOM   1244  OG1 THR A 177      -2.785  28.900  12.246  1.00 56.14           O  
ATOM   1245  CG2 THR A 177      -5.159  28.637  11.862  1.00 59.15           C  
ATOM   1246  N   CYS A 178      -3.399  29.213  15.967  1.00 58.42           N  
ATOM   1247  CA  CYS A 178      -2.507  29.069  17.119  1.00 58.86           C  
ATOM   1248  C   CYS A 178      -2.400  27.579  17.381  1.00 62.62           C  
ATOM   1249  O   CYS A 178      -3.113  27.032  18.219  1.00 64.16           O  
ATOM   1250  CB  CYS A 178      -3.027  29.839  18.332  1.00 59.81           C  
ATOM   1251  SG  CYS A 178      -2.078  29.582  19.865  1.00 64.33           S  
ATOM   1252  N   SER A 179      -1.530  26.916  16.617  1.00 58.19           N  
ATOM   1253  CA  SER A 179      -1.325  25.473  16.666  1.00 57.96           C  
ATOM   1254  C   SER A 179       0.158  25.061  16.723  1.00 62.66           C  
ATOM   1255  O   SER A 179       1.043  25.910  16.618  1.00 61.00           O  
ATOM   1256  CB  SER A 179      -2.024  24.814  15.478  1.00 60.98           C  
ATOM   1257  OG  SER A 179      -1.679  25.424  14.244  1.00 70.77           O  
ATOM   1258  N   SER A 180       0.421  23.758  16.928  1.00 61.59           N  
ATOM   1259  CA  SER A 180       1.787  23.253  16.946  1.00 62.84           C  
ATOM   1260  C   SER A 180       2.183  22.760  15.552  1.00 69.24           C  
ATOM   1261  O   SER A 180       1.409  22.067  14.889  1.00 69.87           O  
ATOM   1262  CB  SER A 180       1.980  22.172  18.010  1.00 65.45           C  
ATOM   1263  OG  SER A 180       1.811  20.865  17.492  1.00 74.52           O  
ATOM   1264  N   HIS A 181       3.374  23.147  15.105  1.00 66.10           N  
ATOM   1265  CA  HIS A 181       3.898  22.753  13.811  1.00 66.70           C  
ATOM   1266  C   HIS A 181       5.310  22.205  14.027  1.00 72.52           C  
ATOM   1267  O   HIS A 181       6.249  22.977  14.246  1.00 71.41           O  
ATOM   1268  CB  HIS A 181       3.906  23.948  12.829  1.00 67.62           C  
ATOM   1269  CG  HIS A 181       2.689  24.830  12.861  1.00 71.03           C  
ATOM   1270  ND1 HIS A 181       1.632  24.627  11.999  1.00 73.02           N  
ATOM   1271  CD2 HIS A 181       2.439  25.934  13.604  1.00 72.75           C  
ATOM   1272  CE1 HIS A 181       0.766  25.598  12.254  1.00 72.45           C  
ATOM   1273  NE2 HIS A 181       1.206  26.406  13.216  1.00 72.66           N  
ATOM   1274  N   PHE A 182       5.448  20.869  14.014  1.00 72.17           N  
ATOM   1275  CA  PHE A 182       6.732  20.194  14.216  1.00 74.11           C  
ATOM   1276  C   PHE A 182       7.629  20.312  12.972  1.00 82.91           C  
ATOM   1277  O   PHE A 182       7.101  20.548  11.873  1.00 82.46           O  
ATOM   1278  CB  PHE A 182       6.533  18.721  14.630  1.00 76.32           C  
ATOM   1279  CG  PHE A 182       5.813  18.519  15.949  1.00 78.54           C  
ATOM   1280  CD1 PHE A 182       6.356  18.991  17.138  1.00 81.80           C  
ATOM   1281  CD2 PHE A 182       4.598  17.842  16.000  1.00 81.31           C  
ATOM   1282  CE1 PHE A 182       5.678  18.822  18.346  1.00 83.13           C  
ATOM   1283  CE2 PHE A 182       3.926  17.665  17.213  1.00 84.09           C  
ATOM   1284  CZ  PHE A 182       4.469  18.155  18.376  1.00 82.35           C  
ATOM   1285  N   PRO A 183       8.984  20.174  13.105  1.00 82.39           N  
ATOM   1286  CA  PRO A 183       9.852  20.313  11.916  1.00 82.93           C  
ATOM   1287  C   PRO A 183       9.626  19.241  10.850  1.00 89.22           C  
ATOM   1288  O   PRO A 183       9.675  18.051  11.165  1.00 88.77           O  
ATOM   1289  CB  PRO A 183      11.272  20.280  12.495  1.00 84.35           C  
ATOM   1290  CG  PRO A 183      11.144  19.630  13.805  1.00 88.27           C  
ATOM   1291  CD  PRO A 183       9.781  19.930  14.328  1.00 83.57           C  
ATOM   1292  N   TYR A 184       9.357  19.680   9.597  1.00 87.42           N  
ATOM   1293  CA  TYR A 184       9.075  18.856   8.413  1.00 88.25           C  
ATOM   1294  C   TYR A 184       9.974  17.625   8.248  1.00 91.62           C  
ATOM   1295  O   TYR A 184       9.456  16.529   8.010  1.00 91.04           O  
ATOM   1296  CB  TYR A 184       9.117  19.718   7.136  1.00 90.82           C  
ATOM   1297  CG  TYR A 184       8.793  18.955   5.864  1.00 94.88           C  
ATOM   1298  CD1 TYR A 184       7.472  18.725   5.481  1.00 97.56           C  
ATOM   1299  CD2 TYR A 184       9.807  18.480   5.033  1.00 96.04           C  
ATOM   1300  CE1 TYR A 184       7.168  18.020   4.316  1.00 99.27           C  
ATOM   1301  CE2 TYR A 184       9.515  17.773   3.866  1.00 97.35           C  
ATOM   1302  CZ  TYR A 184       8.193  17.549   3.509  1.00107.10           C  
ATOM   1303  OH  TYR A 184       7.902  16.858   2.357  1.00110.10           O  
ATOM   1304  N   SER A 185      11.312  17.823   8.332  1.00 87.97           N  
ATOM   1305  CA  SER A 185      12.326  16.777   8.178  1.00 87.76           C  
ATOM   1306  C   SER A 185      12.173  15.623   9.174  1.00 92.33           C  
ATOM   1307  O   SER A 185      12.386  14.471   8.799  1.00 92.21           O  
ATOM   1308  CB  SER A 185      13.727  17.370   8.267  1.00 90.94           C  
ATOM   1309  OG  SER A 185      13.920  18.088   9.475  1.00 99.35           O  
ATOM   1310  N   GLN A 186      11.788  15.937  10.430  1.00 88.67           N  
ATOM   1311  CA  GLN A 186      11.592  14.982  11.528  1.00 87.95           C  
ATOM   1312  C   GLN A 186      10.136  15.037  12.015  1.00 90.14           C  
ATOM   1313  O   GLN A 186       9.883  14.941  13.217  1.00 89.08           O  
ATOM   1314  CB  GLN A 186      12.550  15.318  12.692  1.00 89.45           C  
ATOM   1315  CG  GLN A 186      14.037  15.250  12.359  1.00108.94           C  
ATOM   1316  CD  GLN A 186      14.870  15.729  13.520  1.00129.38           C  
ATOM   1317  OE1 GLN A 186      15.079  16.937  13.704  1.00120.87           O  
ATOM   1318  NE2 GLN A 186      15.343  14.790  14.338  1.00125.23           N  
ATOM   1319  N   TYR A 187       9.178  15.203  11.088  1.00 86.82           N  
ATOM   1320  CA  TYR A 187       7.772  15.330  11.457  1.00 87.16           C  
ATOM   1321  C   TYR A 187       7.203  14.091  12.141  1.00 90.02           C  
ATOM   1322  O   TYR A 187       6.490  14.234  13.137  1.00 89.35           O  
ATOM   1323  CB  TYR A 187       6.899  15.758  10.269  1.00 89.26           C  
ATOM   1324  CG  TYR A 187       5.590  16.383  10.710  1.00 93.07           C  
ATOM   1325  CD1 TYR A 187       5.500  17.748  10.978  1.00 95.68           C  
ATOM   1326  CD2 TYR A 187       4.448  15.607  10.895  1.00 94.17           C  
ATOM   1327  CE1 TYR A 187       4.304  18.324  11.413  1.00 97.02           C  
ATOM   1328  CE2 TYR A 187       3.250  16.172  11.332  1.00 95.12           C  
ATOM   1329  CZ  TYR A 187       3.181  17.531  11.588  1.00102.93           C  
ATOM   1330  OH  TYR A 187       2.003  18.088  12.020  1.00104.88           O  
ATOM   1331  N   GLN A 188       7.521  12.889  11.624  1.00 85.92           N  
ATOM   1332  CA  GLN A 188       7.033  11.626  12.179  1.00 85.17           C  
ATOM   1333  C   GLN A 188       7.638  11.303  13.564  1.00 87.54           C  
ATOM   1334  O   GLN A 188       6.928  10.783  14.422  1.00 86.38           O  
ATOM   1335  CB  GLN A 188       7.223  10.476  11.175  1.00 86.58           C  
ATOM   1336  CG  GLN A 188       6.356   9.238  11.459  1.00107.77           C  
ATOM   1337  CD  GLN A 188       4.868   9.521  11.515  1.00127.88           C  
ATOM   1338  OE1 GLN A 188       4.261   9.575  12.594  1.00123.23           O  
ATOM   1339  NE2 GLN A 188       4.247   9.705  10.355  1.00118.74           N  
ATOM   1340  N   PHE A 189       8.926  11.644  13.784  1.00 84.08           N  
ATOM   1341  CA  PHE A 189       9.617  11.433  15.056  1.00 83.74           C  
ATOM   1342  C   PHE A 189       8.999  12.263  16.180  1.00 87.39           C  
ATOM   1343  O   PHE A 189       8.708  11.695  17.223  1.00 86.94           O  
ATOM   1344  CB  PHE A 189      11.134  11.681  14.941  1.00 85.64           C  
ATOM   1345  CG  PHE A 189      11.888  11.542  16.248  1.00 87.53           C  
ATOM   1346  CD1 PHE A 189      12.168  10.290  16.779  1.00 91.18           C  
ATOM   1347  CD2 PHE A 189      12.302  12.666  16.952  1.00 90.01           C  
ATOM   1348  CE1 PHE A 189      12.841  10.165  17.999  1.00 92.45           C  
ATOM   1349  CE2 PHE A 189      12.981  12.541  18.166  1.00 93.05           C  
ATOM   1350  CZ  PHE A 189      13.247  11.292  18.681  1.00 91.40           C  
ATOM   1351  N   TRP A 190       8.805  13.586  15.975  1.00 84.05           N  
ATOM   1352  CA  TRP A 190       8.208  14.483  16.973  1.00 83.80           C  
ATOM   1353  C   TRP A 190       6.759  14.118  17.270  1.00 85.83           C  
ATOM   1354  O   TRP A 190       6.325  14.248  18.415  1.00 85.15           O  
ATOM   1355  CB  TRP A 190       8.333  15.954  16.558  1.00 83.08           C  
ATOM   1356  CG  TRP A 190       9.732  16.474  16.648  1.00 84.67           C  
ATOM   1357  CD1 TRP A 190      10.620  16.603  15.624  1.00 87.64           C  
ATOM   1358  CD2 TRP A 190      10.424  16.873  17.834  1.00 85.00           C  
ATOM   1359  NE1 TRP A 190      11.821  17.072  16.098  1.00 87.43           N  
ATOM   1360  CE2 TRP A 190      11.735  17.237  17.454  1.00 89.06           C  
ATOM   1361  CE3 TRP A 190      10.079  16.924  19.197  1.00 86.87           C  
ATOM   1362  CZ2 TRP A 190      12.692  17.676  18.378  1.00 88.57           C  
ATOM   1363  CZ3 TRP A 190      11.033  17.348  20.114  1.00 88.54           C  
ATOM   1364  CH2 TRP A 190      12.317  17.730  19.700  1.00 89.15           C  
ATOM   1365  N   LYS A 191       6.021  13.636  16.247  1.00 81.02           N  
ATOM   1366  CA  LYS A 191       4.632  13.189  16.370  1.00 79.94           C  
ATOM   1367  C   LYS A 191       4.603  11.972  17.311  1.00 83.44           C  
ATOM   1368  O   LYS A 191       3.813  11.954  18.252  1.00 84.14           O  
ATOM   1369  CB  LYS A 191       4.052  12.826  14.991  1.00 81.70           C  
ATOM   1370  CG  LYS A 191       2.657  13.371  14.740  1.00 90.56           C  
ATOM   1371  N   ASN A 192       5.518  11.000  17.099  1.00 78.09           N  
ATOM   1372  CA  ASN A 192       5.638   9.793  17.913  1.00 77.03           C  
ATOM   1373  C   ASN A 192       6.196  10.081  19.318  1.00 79.39           C  
ATOM   1374  O   ASN A 192       5.672   9.545  20.299  1.00 79.58           O  
ATOM   1375  CB  ASN A 192       6.497   8.739  17.192  1.00 78.08           C  
ATOM   1376  CG  ASN A 192       5.915   8.173  15.910  1.00101.32           C  
ATOM   1377  OD1 ASN A 192       4.895   8.640  15.380  1.00 98.15           O  
ATOM   1378  ND2 ASN A 192       6.583   7.171  15.351  1.00 90.54           N  
ATOM   1379  N   PHE A 193       7.253  10.916  19.413  1.00 73.70           N  
ATOM   1380  CA  PHE A 193       7.911  11.280  20.670  1.00 72.54           C  
ATOM   1381  C   PHE A 193       6.992  12.034  21.622  1.00 74.12           C  
ATOM   1382  O   PHE A 193       7.009  11.739  22.814  1.00 73.84           O  
ATOM   1383  CB  PHE A 193       9.222  12.050  20.424  1.00 74.47           C  
ATOM   1384  CG  PHE A 193      10.031  12.347  21.665  1.00 76.42           C  
ATOM   1385  CD1 PHE A 193      10.820  11.364  22.253  1.00 79.28           C  
ATOM   1386  CD2 PHE A 193      10.021  13.614  22.235  1.00 79.16           C  
ATOM   1387  CE1 PHE A 193      11.567  11.639  23.402  1.00 79.99           C  
ATOM   1388  CE2 PHE A 193      10.761  13.884  23.391  1.00 81.87           C  
ATOM   1389  CZ  PHE A 193      11.537  12.897  23.961  1.00 79.38           C  
ATOM   1390  N   GLN A 194       6.195  12.993  21.114  1.00 69.09           N  
ATOM   1391  CA  GLN A 194       5.265  13.751  21.952  1.00 68.31           C  
ATOM   1392  C   GLN A 194       4.065  12.907  22.387  1.00 72.04           C  
ATOM   1393  O   GLN A 194       3.540  13.123  23.481  1.00 70.87           O  
ATOM   1394  CB  GLN A 194       4.832  15.077  21.301  1.00 69.43           C  
ATOM   1395  CG  GLN A 194       5.945  16.116  21.117  1.00 77.06           C  
ATOM   1396  CD  GLN A 194       6.884  16.287  22.287  1.00 91.06           C  
ATOM   1397  OE1 GLN A 194       6.456  16.557  23.411  1.00 86.13           O  
ATOM   1398  NE2 GLN A 194       8.172  16.118  22.060  1.00 82.73           N  
ATOM   1399  N   THR A 195       3.657  11.925  21.548  1.00 69.37           N  
ATOM   1400  CA  THR A 195       2.562  10.985  21.839  1.00 69.33           C  
ATOM   1401  C   THR A 195       2.924  10.132  23.045  1.00 73.61           C  
ATOM   1402  O   THR A 195       2.145  10.067  23.987  1.00 73.43           O  
ATOM   1403  CB  THR A 195       2.219  10.151  20.596  1.00 75.16           C  
ATOM   1404  OG1 THR A 195       1.673  11.038  19.619  1.00 76.83           O  
ATOM   1405  CG2 THR A 195       1.225   9.017  20.888  1.00 69.76           C  
ATOM   1406  N   LEU A 196       4.117   9.514  23.025  1.00 70.75           N  
ATOM   1407  CA  LEU A 196       4.620   8.671  24.108  1.00 71.10           C  
ATOM   1408  C   LEU A 196       4.918   9.465  25.393  1.00 74.38           C  
ATOM   1409  O   LEU A 196       4.695   8.938  26.481  1.00 73.86           O  
ATOM   1410  CB  LEU A 196       5.837   7.849  23.646  1.00 71.57           C  
ATOM   1411  CG  LEU A 196       5.571   6.867  22.492  1.00 76.83           C  
ATOM   1412  CD1 LEU A 196       6.805   6.682  21.632  1.00 77.14           C  
ATOM   1413  CD2 LEU A 196       5.064   5.527  23.005  1.00 79.20           C  
ATOM   1414  N   LYS A 197       5.364  10.740  25.269  1.00 70.01           N  
ATOM   1415  CA  LYS A 197       5.633  11.623  26.414  1.00 69.17           C  
ATOM   1416  C   LYS A 197       4.333  11.987  27.189  1.00 72.57           C  
ATOM   1417  O   LYS A 197       4.344  12.019  28.420  1.00 72.34           O  
ATOM   1418  CB  LYS A 197       6.363  12.885  25.956  1.00 71.07           C  
ATOM   1419  CG  LYS A 197       7.041  13.640  27.090  1.00 86.21           C  
ATOM   1420  CD  LYS A 197       7.170  15.133  26.791  1.00 96.09           C  
ATOM   1421  CE  LYS A 197       8.461  15.486  26.108  1.00106.13           C  
ATOM   1422  NZ  LYS A 197       8.584  16.945  25.935  1.00117.12           N  
ATOM   1423  N   ILE A 198       3.229  12.255  26.467  1.00 67.70           N  
ATOM   1424  CA  ILE A 198       1.934  12.578  27.070  1.00 66.78           C  
ATOM   1425  C   ILE A 198       1.273  11.295  27.626  1.00 69.29           C  
ATOM   1426  O   ILE A 198       0.806  11.293  28.770  1.00 68.32           O  
ATOM   1427  CB  ILE A 198       1.024  13.390  26.091  1.00 69.49           C  
ATOM   1428  CG1 ILE A 198       1.609  14.807  25.854  1.00 70.26           C  
ATOM   1429  CG2 ILE A 198      -0.431  13.475  26.593  1.00 69.24           C  
ATOM   1430  CD1 ILE A 198       1.243  15.500  24.491  1.00 79.41           C  
ATOM   1431  N   VAL A 199       1.240  10.216  26.812  1.00 64.52           N  
ATOM   1432  CA  VAL A 199       0.646   8.928  27.185  1.00 63.64           C  
ATOM   1433  C   VAL A 199       1.376   8.319  28.407  1.00 66.17           C  
ATOM   1434  O   VAL A 199       0.707   8.006  29.388  1.00 64.83           O  
ATOM   1435  CB  VAL A 199       0.528   7.954  25.974  1.00 67.01           C  
ATOM   1436  CG1 VAL A 199       0.256   6.519  26.418  1.00 67.33           C  
ATOM   1437  CG2 VAL A 199      -0.537   8.418  24.990  1.00 66.06           C  
ATOM   1438  N   ILE A 200       2.731   8.218  28.376  1.00 63.23           N  
ATOM   1439  CA  ILE A 200       3.512   7.661  29.490  1.00 63.48           C  
ATOM   1440  C   ILE A 200       3.366   8.521  30.761  1.00 69.33           C  
ATOM   1441  O   ILE A 200       2.931   7.981  31.761  1.00 69.97           O  
ATOM   1442  CB  ILE A 200       4.987   7.339  29.115  1.00 66.17           C  
ATOM   1443  CG1 ILE A 200       5.040   6.071  28.231  1.00 66.70           C  
ATOM   1444  CG2 ILE A 200       5.889   7.178  30.350  1.00 65.58           C  
ATOM   1445  CD1 ILE A 200       6.204   6.013  27.230  1.00 75.19           C  
ATOM   1446  N   LEU A 201       3.659   9.826  30.718  1.00 66.77           N  
ATOM   1447  CA  LEU A 201       3.534  10.701  31.893  1.00 67.04           C  
ATOM   1448  C   LEU A 201       2.087  10.957  32.382  1.00 71.82           C  
ATOM   1449  O   LEU A 201       1.900  11.404  33.517  1.00 71.47           O  
ATOM   1450  CB  LEU A 201       4.243  12.055  31.658  1.00 67.15           C  
ATOM   1451  CG  LEU A 201       5.765  12.057  31.590  1.00 71.46           C  
ATOM   1452  CD1 LEU A 201       6.264  13.332  30.968  1.00 70.88           C  
ATOM   1453  CD2 LEU A 201       6.380  11.884  32.969  1.00 74.87           C  
ATOM   1454  N   GLY A 202       1.093  10.696  31.540  1.00 69.55           N  
ATOM   1455  CA  GLY A 202      -0.299  10.972  31.887  1.00 70.32           C  
ATOM   1456  C   GLY A 202      -1.208   9.789  32.147  1.00 74.79           C  
ATOM   1457  O   GLY A 202      -2.240   9.952  32.799  1.00 74.20           O  
ATOM   1458  N   LEU A 203      -0.850   8.603  31.632  1.00 71.53           N  
ATOM   1459  CA  LEU A 203      -1.653   7.395  31.780  1.00 71.53           C  
ATOM   1460  C   LEU A 203      -0.819   6.248  32.333  1.00 76.37           C  
ATOM   1461  O   LEU A 203      -1.057   5.847  33.463  1.00 76.53           O  
ATOM   1462  CB  LEU A 203      -2.357   7.030  30.444  1.00 71.51           C  
ATOM   1463  CG  LEU A 203      -3.067   5.657  30.343  1.00 75.76           C  
ATOM   1464  CD1 LEU A 203      -4.457   5.695  30.961  1.00 75.75           C  
ATOM   1465  CD2 LEU A 203      -3.154   5.199  28.903  1.00 77.29           C  
ATOM   1466  N   VAL A 204       0.171   5.753  31.561  1.00 73.31           N  
ATOM   1467  CA  VAL A 204       1.053   4.632  31.915  1.00 73.55           C  
ATOM   1468  C   VAL A 204       1.726   4.824  33.302  1.00 78.79           C  
ATOM   1469  O   VAL A 204       1.468   4.019  34.196  1.00 77.97           O  
ATOM   1470  CB  VAL A 204       2.075   4.309  30.786  1.00 77.00           C  
ATOM   1471  CG1 VAL A 204       2.917   3.088  31.134  1.00 76.73           C  
ATOM   1472  CG2 VAL A 204       1.368   4.090  29.453  1.00 76.66           C  
ATOM   1473  N   LEU A 205       2.544   5.884  33.474  1.00 76.99           N  
ATOM   1474  CA  LEU A 205       3.253   6.206  34.716  1.00 77.85           C  
ATOM   1475  C   LEU A 205       2.335   6.363  35.929  1.00 83.40           C  
ATOM   1476  O   LEU A 205       2.566   5.634  36.893  1.00 83.36           O  
ATOM   1477  CB  LEU A 205       4.162   7.429  34.565  1.00 78.14           C  
ATOM   1478  CG  LEU A 205       5.261   7.564  35.605  1.00 83.64           C  
ATOM   1479  CD1 LEU A 205       6.536   6.814  35.157  1.00 84.42           C  
ATOM   1480  CD2 LEU A 205       5.545   9.032  35.901  1.00 85.14           C  
ATOM   1481  N   PRO A 206       1.291   7.238  35.936  1.00 80.62           N  
ATOM   1482  CA  PRO A 206       0.426   7.315  37.124  1.00 80.86           C  
ATOM   1483  C   PRO A 206      -0.373   6.032  37.387  1.00 86.42           C  
ATOM   1484  O   PRO A 206      -0.687   5.744  38.545  1.00 85.56           O  
ATOM   1485  CB  PRO A 206      -0.487   8.501  36.821  1.00 82.36           C  
ATOM   1486  CG  PRO A 206      -0.516   8.598  35.361  1.00 86.39           C  
ATOM   1487  CD  PRO A 206       0.844   8.195  34.899  1.00 82.01           C  
ATOM   1488  N   LEU A 207      -0.689   5.259  36.321  1.00 84.62           N  
ATOM   1489  CA  LEU A 207      -1.427   4.002  36.453  1.00 85.42           C  
ATOM   1490  C   LEU A 207      -0.603   2.968  37.211  1.00 90.27           C  
ATOM   1491  O   LEU A 207      -1.175   2.231  38.011  1.00 90.52           O  
ATOM   1492  CB  LEU A 207      -1.846   3.454  35.092  1.00 85.92           C  
ATOM   1493  CG  LEU A 207      -3.116   2.617  35.069  1.00 91.60           C  
ATOM   1494  CD1 LEU A 207      -4.353   3.495  35.002  1.00 91.93           C  
ATOM   1495  CD2 LEU A 207      -3.106   1.662  33.879  1.00 94.99           C  
ATOM   1496  N   LEU A 208       0.736   2.943  36.992  1.00 86.43           N  
ATOM   1497  CA  LEU A 208       1.660   2.048  37.698  1.00 86.15           C  
ATOM   1498  C   LEU A 208       1.689   2.426  39.184  1.00 90.44           C  
ATOM   1499  O   LEU A 208       1.571   1.546  40.037  1.00 89.61           O  
ATOM   1500  CB  LEU A 208       3.085   2.098  37.100  1.00 86.07           C  
ATOM   1501  CG  LEU A 208       3.256   1.617  35.651  1.00 90.66           C  
ATOM   1502  CD1 LEU A 208       4.549   2.125  35.064  1.00 90.75           C  
ATOM   1503  CD2 LEU A 208       3.177   0.095  35.537  1.00 93.11           C  
ATOM   1504  N   VAL A 209       1.777   3.751  39.474  1.00 87.89           N  
ATOM   1505  CA  VAL A 209       1.787   4.363  40.814  1.00 88.11           C  
ATOM   1506  C   VAL A 209       0.474   4.034  41.553  1.00 92.92           C  
ATOM   1507  O   VAL A 209       0.510   3.693  42.734  1.00 92.10           O  
ATOM   1508  CB  VAL A 209       2.076   5.896  40.739  1.00 92.09           C  
ATOM   1509  CG1 VAL A 209       1.958   6.568  42.107  1.00 91.89           C  
ATOM   1510  CG2 VAL A 209       3.454   6.169  40.136  1.00 91.95           C  
ATOM   1511  N   MET A 210      -0.668   4.090  40.841  1.00 90.63           N  
ATOM   1512  CA  MET A 210      -1.981   3.758  41.390  1.00 91.04           C  
ATOM   1513  C   MET A 210      -2.058   2.268  41.753  1.00 95.15           C  
ATOM   1514  O   MET A 210      -2.690   1.921  42.745  1.00 94.60           O  
ATOM   1515  CB  MET A 210      -3.086   4.114  40.392  1.00 93.85           C  
ATOM   1516  CG  MET A 210      -4.437   4.268  41.046  1.00 98.40           C  
ATOM   1517  SD  MET A 210      -5.832   4.100  39.920  1.00103.67           S  
ATOM   1518  CE  MET A 210      -5.874   2.291  39.702  1.00100.49           C  
ATOM   1519  N   VAL A 211      -1.410   1.395  40.954  1.00 92.14           N  
ATOM   1520  CA  VAL A 211      -1.386  -0.049  41.193  1.00 92.06           C  
ATOM   1521  C   VAL A 211      -0.453  -0.387  42.360  1.00 95.62           C  
ATOM   1522  O   VAL A 211      -0.911  -0.994  43.325  1.00 95.00           O  
ATOM   1523  CB  VAL A 211      -1.090  -0.867  39.903  1.00 96.36           C  
ATOM   1524  CG1 VAL A 211      -0.749  -2.325  40.217  1.00 96.27           C  
ATOM   1525  CG2 VAL A 211      -2.267  -0.799  38.929  1.00 96.24           C  
ATOM   1526  N   ILE A 212       0.831   0.021  42.280  1.00 92.54           N  
ATOM   1527  CA  ILE A 212       1.862  -0.212  43.305  1.00 92.80           C  
ATOM   1528  C   ILE A 212       1.419   0.260  44.702  1.00 98.17           C  
ATOM   1529  O   ILE A 212       1.393  -0.547  45.636  1.00 97.51           O  
ATOM   1530  CB  ILE A 212       3.241   0.409  42.883  1.00 95.92           C  
ATOM   1531  CG1 ILE A 212       3.823  -0.294  41.638  1.00 96.52           C  
ATOM   1532  CG2 ILE A 212       4.263   0.407  44.042  1.00 96.31           C  
ATOM   1533  CD1 ILE A 212       4.750   0.591  40.770  1.00104.32           C  
ATOM   1534  N   CYS A 213       1.068   1.559  44.826  1.00 95.90           N  
ATOM   1535  CA  CYS A 213       0.705   2.203  46.082  1.00 96.06           C  
ATOM   1536  C   CYS A 213      -0.601   1.701  46.696  1.00100.08           C  
ATOM   1537  O   CYS A 213      -0.565   1.238  47.831  1.00 99.84           O  
ATOM   1538  CB  CYS A 213       0.708   3.723  45.948  1.00 96.52           C  
ATOM   1539  SG  CYS A 213       2.309   4.425  45.464  1.00100.45           S  
ATOM   1540  N   TYR A 214      -1.735   1.779  45.973  1.00 96.59           N  
ATOM   1541  CA  TYR A 214      -3.038   1.394  46.518  1.00 96.54           C  
ATOM   1542  C   TYR A 214      -3.181  -0.085  46.861  1.00100.61           C  
ATOM   1543  O   TYR A 214      -3.968  -0.403  47.749  1.00 99.84           O  
ATOM   1544  CB  TYR A 214      -4.193   1.866  45.633  1.00 98.01           C  
ATOM   1545  CG  TYR A 214      -4.399   3.364  45.707  1.00100.17           C  
ATOM   1546  CD1 TYR A 214      -4.844   3.972  46.880  1.00102.22           C  
ATOM   1547  CD2 TYR A 214      -4.130   4.178  44.612  1.00100.91           C  
ATOM   1548  CE1 TYR A 214      -5.013   5.353  46.961  1.00102.72           C  
ATOM   1549  CE2 TYR A 214      -4.312   5.558  44.675  1.00101.76           C  
ATOM   1550  CZ  TYR A 214      -4.750   6.142  45.852  1.00108.60           C  
ATOM   1551  OH  TYR A 214      -4.911   7.504  45.914  1.00108.93           O  
ATOM   1552  N   SER A 215      -2.417  -0.978  46.217  1.00 98.12           N  
ATOM   1553  CA  SER A 215      -2.460  -2.396  46.581  1.00 98.24           C  
ATOM   1554  C   SER A 215      -1.590  -2.606  47.824  1.00101.62           C  
ATOM   1555  O   SER A 215      -1.853  -3.516  48.610  1.00101.21           O  
ATOM   1556  CB  SER A 215      -2.017  -3.295  45.427  1.00102.49           C  
ATOM   1557  OG  SER A 215      -0.662  -3.085  45.069  1.00113.78           O  
ATOM   1558  N   GLY A 216      -0.589  -1.738  47.993  1.00 97.78           N  
ATOM   1559  CA  GLY A 216       0.313  -1.740  49.138  1.00 97.70           C  
ATOM   1560  C   GLY A 216      -0.336  -1.146  50.373  1.00101.54           C  
ATOM   1561  O   GLY A 216      -0.067  -1.590  51.493  1.00100.68           O  
ATOM   1562  N   ILE A 217      -1.201  -0.133  50.173  1.00 98.62           N  
ATOM   1563  CA  ILE A 217      -1.949   0.540  51.236  1.00 98.78           C  
ATOM   1564  C   ILE A 217      -3.031  -0.420  51.741  1.00102.29           C  
ATOM   1565  O   ILE A 217      -3.113  -0.656  52.947  1.00101.80           O  
ATOM   1566  CB  ILE A 217      -2.519   1.922  50.770  1.00102.18           C  
ATOM   1567  CG1 ILE A 217      -1.398   2.959  50.545  1.00102.73           C  
ATOM   1568  CG2 ILE A 217      -3.563   2.476  51.754  1.00103.45           C  
ATOM   1569  CD1 ILE A 217      -1.706   4.021  49.449  1.00110.17           C  
ATOM   1570  N   LEU A 218      -3.828  -0.989  50.810  1.00 99.01           N  
ATOM   1571  CA  LEU A 218      -4.923  -1.928  51.083  1.00 99.25           C  
ATOM   1572  C   LEU A 218      -4.470  -3.146  51.896  1.00104.07           C  
ATOM   1573  O   LEU A 218      -5.187  -3.563  52.806  1.00103.63           O  
ATOM   1574  CB  LEU A 218      -5.600  -2.362  49.770  1.00 99.37           C  
ATOM   1575  CG  LEU A 218      -6.958  -3.053  49.876  1.00104.22           C  
ATOM   1576  CD1 LEU A 218      -8.064  -2.058  50.185  1.00104.34           C  
ATOM   1577  CD2 LEU A 218      -7.281  -3.790  48.597  1.00106.94           C  
ATOM   1578  N   LYS A 219      -3.274  -3.688  51.592  1.00101.43           N  
ATOM   1579  CA  LYS A 219      -2.704  -4.828  52.312  1.00101.59           C  
ATOM   1580  C   LYS A 219      -2.219  -4.438  53.717  1.00105.16           C  
ATOM   1581  O   LYS A 219      -2.178  -5.297  54.594  1.00104.63           O  
ATOM   1582  CB  LYS A 219      -1.601  -5.516  51.493  1.00104.67           C  
ATOM   1583  CG  LYS A 219      -2.142  -6.424  50.385  1.00121.28           C  
ATOM   1584  CD  LYS A 219      -1.027  -7.049  49.558  1.00133.07           C  
ATOM   1585  CE  LYS A 219      -1.559  -8.045  48.555  1.00147.83           C  
ATOM   1586  NZ  LYS A 219      -0.468  -8.804  47.885  1.00157.72           N  
ATOM   1587  N   THR A 220      -1.876  -3.148  53.936  1.00101.85           N  
ATOM   1588  CA  THR A 220      -1.456  -2.619  55.244  1.00101.81           C  
ATOM   1589  C   THR A 220      -2.703  -2.306  56.094  1.00106.07           C  
ATOM   1590  O   THR A 220      -2.641  -2.397  57.321  1.00106.14           O  
ATOM   1591  CB  THR A 220      -0.494  -1.424  55.078  1.00109.64           C  
ATOM   1592  OG1 THR A 220       0.539  -1.784  54.161  1.00112.03           O  
ATOM   1593  CG2 THR A 220       0.151  -0.988  56.388  1.00106.69           C  
ATOM   1594  N   LEU A 221      -3.742  -1.825  55.429  1.00102.22           N  
ATOM   1595  CA  LEU A 221      -5.042  -1.564  56.017  1.00101.72           C  
ATOM   1596  C   LEU A 221      -5.740  -2.814  56.448  1.00105.49           C  
ATOM   1597  O   LEU A 221      -6.368  -2.849  57.476  1.00105.16           O  
ATOM   1598  CB  LEU A 221      -5.935  -0.885  54.995  1.00101.64           C  
ATOM   1599  CG  LEU A 221      -5.852   0.616  54.775  1.00106.22           C  
ATOM   1600  CD1 LEU A 221      -6.769   0.972  53.632  1.00106.32           C  
ATOM   1601  CD2 LEU A 221      -6.270   1.373  56.013  1.00108.51           C  
ATOM   1602  N   LEU A 222      -5.658  -3.832  55.614  1.00101.71           N  
ATOM   1603  CA  LEU A 222      -6.319  -5.092  55.863  1.00101.20           C  
ATOM   1604  C   LEU A 222      -5.783  -5.758  57.085  1.00105.15           C  
ATOM   1605  O   LEU A 222      -6.520  -6.369  57.825  1.00104.40           O  
ATOM   1606  CB  LEU A 222      -6.160  -6.011  54.681  1.00101.21           C  
ATOM   1607  CG  LEU A 222      -6.786  -5.434  53.433  1.00106.22           C  
ATOM   1608  CD1 LEU A 222      -6.730  -6.442  52.308  1.00106.15           C  
ATOM   1609  CD2 LEU A 222      -8.219  -5.062  53.734  1.00110.07           C  
ATOM   1610  N   ARG A 223      -4.487  -5.655  57.295  1.00102.38           N  
ATOM   1611  CA  ARG A 223      -3.898  -6.265  58.455  1.00140.51           C  
ATOM   1612  C   ARG A 223      -4.558  -5.626  59.661  1.00173.41           C  
ATOM   1613  O   ARG A 223      -4.861  -6.297  60.620  1.00135.88           O  
ATOM   1614  CB  ARG A 223      -2.388  -6.054  58.482  1.00140.91           C  
ATOM   1615  N   MET A1001      -4.818  -4.335  59.597  1.00 95.19           N  
ATOM   1616  CA  MET A1001      -5.292  -3.577  60.743  1.00 95.24           C  
ATOM   1617  C   MET A1001      -6.709  -3.861  61.202  1.00 96.65           C  
ATOM   1618  O   MET A1001      -7.122  -3.376  62.241  1.00 96.21           O  
ATOM   1619  CB  MET A1001      -5.152  -2.092  60.485  1.00 98.06           C  
ATOM   1620  CG  MET A1001      -3.742  -1.655  60.155  1.00102.38           C  
ATOM   1621  SD  MET A1001      -3.445   0.071  60.543  1.00107.28           S  
ATOM   1622  CE  MET A1001      -5.089   0.760  60.493  1.00104.02           C  
ATOM   1623  N   LYS A1002      -7.480  -4.570  60.396  1.00 91.05           N  
ATOM   1624  CA  LYS A1002      -8.868  -4.843  60.728  1.00 89.66           C  
ATOM   1625  C   LYS A1002      -9.034  -5.760  61.943  1.00 91.63           C  
ATOM   1626  O   LYS A1002      -8.256  -6.675  62.159  1.00 91.16           O  
ATOM   1627  CB  LYS A1002      -9.614  -5.384  59.508  1.00 91.50           C  
ATOM   1628  N   LYS A1003     -10.073  -5.507  62.727  1.00 86.65           N  
ATOM   1629  CA  LYS A1003     -10.333  -6.244  63.950  1.00 85.89           C  
ATOM   1630  C   LYS A1003     -11.514  -7.159  63.773  1.00 88.52           C  
ATOM   1631  O   LYS A1003     -12.504  -6.791  63.170  1.00 88.28           O  
ATOM   1632  CB  LYS A1003     -10.620  -5.288  65.092  1.00 88.46           C  
ATOM   1633  CG  LYS A1003      -9.380  -4.726  65.747  1.00104.66           C  
ATOM   1634  CD  LYS A1003      -9.729  -3.659  66.762  1.00117.31           C  
ATOM   1635  CE  LYS A1003      -8.776  -2.483  66.693  1.00130.80           C  
ATOM   1636  NZ  LYS A1003      -8.104  -2.345  65.371  1.00140.99           N  
ATOM   1637  N   TYR A1004     -11.397  -8.365  64.296  1.00 83.92           N  
ATOM   1638  CA  TYR A1004     -12.407  -9.393  64.077  1.00 83.25           C  
ATOM   1639  C   TYR A1004     -13.026  -9.854  65.390  1.00 87.40           C  
ATOM   1640  O   TYR A1004     -12.297 -10.163  66.332  1.00 86.35           O  
ATOM   1641  CB  TYR A1004     -11.831 -10.560  63.261  1.00 83.66           C  
ATOM   1642  CG  TYR A1004     -11.644 -10.234  61.794  1.00 84.46           C  
ATOM   1643  CD1 TYR A1004     -10.477  -9.630  61.338  1.00 85.77           C  
ATOM   1644  CD2 TYR A1004     -12.616 -10.564  60.855  1.00 85.33           C  
ATOM   1645  CE1 TYR A1004     -10.286  -9.350  59.986  1.00 85.23           C  
ATOM   1646  CE2 TYR A1004     -12.439 -10.283  59.498  1.00 86.00           C  
ATOM   1647  CZ  TYR A1004     -11.272  -9.670  59.070  1.00 90.50           C  
ATOM   1648  OH  TYR A1004     -11.084  -9.375  57.741  1.00 87.62           O  
ATOM   1649  N   THR A1005     -14.376  -9.878  65.447  1.00 84.76           N  
ATOM   1650  CA  THR A1005     -15.168 -10.252  66.625  1.00 85.11           C  
ATOM   1651  C   THR A1005     -15.734 -11.670  66.515  1.00 90.36           C  
ATOM   1652  O   THR A1005     -16.210 -12.060  65.449  1.00 90.53           O  
ATOM   1653  CB  THR A1005     -16.314  -9.229  66.832  1.00 93.63           C  
ATOM   1654  OG1 THR A1005     -15.784  -7.907  66.789  1.00 92.33           O  
ATOM   1655  CG2 THR A1005     -17.066  -9.423  68.152  1.00 93.18           C  
ATOM   1656  N   CYS A1006     -15.726 -12.416  67.633  1.00 87.40           N  
ATOM   1657  CA  CYS A1006     -16.326 -13.744  67.714  1.00 87.36           C  
ATOM   1658  C   CYS A1006     -17.845 -13.551  67.833  1.00 91.83           C  
ATOM   1659  O   CYS A1006     -18.322 -12.873  68.743  1.00 91.13           O  
ATOM   1660  CB  CYS A1006     -15.762 -14.533  68.895  1.00 87.54           C  
ATOM   1661  SG  CYS A1006     -16.615 -16.105  69.220  1.00 91.31           S  
ATOM   1662  N   THR A1007     -18.595 -14.129  66.903  1.00 89.29           N  
ATOM   1663  CA  THR A1007     -20.057 -14.025  66.883  1.00 89.51           C  
ATOM   1664  C   THR A1007     -20.735 -14.862  67.997  1.00 94.56           C  
ATOM   1665  O   THR A1007     -21.901 -14.602  68.326  1.00 94.34           O  
ATOM   1666  CB  THR A1007     -20.588 -14.348  65.480  1.00 95.27           C  
ATOM   1667  OG1 THR A1007     -19.993 -15.564  64.998  1.00 90.44           O  
ATOM   1668  CG2 THR A1007     -20.362 -13.194  64.497  1.00 92.78           C  
ATOM   1669  N   VAL A1008     -19.994 -15.839  68.586  1.00 91.24           N  
ATOM   1670  CA  VAL A1008     -20.455 -16.725  69.666  1.00 90.84           C  
ATOM   1671  C   VAL A1008     -20.432 -16.002  71.034  1.00 95.29           C  
ATOM   1672  O   VAL A1008     -21.499 -15.814  71.634  1.00 95.53           O  
ATOM   1673  CB  VAL A1008     -19.682 -18.078  69.687  1.00 94.26           C  
ATOM   1674  CG1 VAL A1008     -20.119 -18.964  70.855  1.00 93.91           C  
ATOM   1675  CG2 VAL A1008     -19.822 -18.823  68.359  1.00 93.87           C  
ATOM   1676  N   CYS A1009     -19.229 -15.595  71.512  1.00 90.73           N  
ATOM   1677  CA  CYS A1009     -19.055 -14.933  72.807  1.00 90.14           C  
ATOM   1678  C   CYS A1009     -18.907 -13.410  72.707  1.00 93.13           C  
ATOM   1679  O   CYS A1009     -19.493 -12.687  73.522  1.00 94.03           O  
ATOM   1680  CB  CYS A1009     -17.908 -15.559  73.600  1.00 90.70           C  
ATOM   1681  SG  CYS A1009     -16.244 -15.061  73.062  1.00 94.73           S  
ATOM   1682  N   GLY A1010     -18.119 -12.943  71.739  1.00 87.21           N  
ATOM   1683  CA  GLY A1010     -17.855 -11.522  71.541  1.00 85.86           C  
ATOM   1684  C   GLY A1010     -16.390 -11.141  71.618  1.00 87.20           C  
ATOM   1685  O   GLY A1010     -16.072  -9.949  71.682  1.00 86.98           O  
ATOM   1686  N   TYR A1011     -15.481 -12.144  71.615  1.00 81.54           N  
ATOM   1687  CA  TYR A1011     -14.028 -11.926  71.678  1.00 80.34           C  
ATOM   1688  C   TYR A1011     -13.541 -11.105  70.474  1.00 80.99           C  
ATOM   1689  O   TYR A1011     -13.732 -11.535  69.331  1.00 81.10           O  
ATOM   1690  CB  TYR A1011     -13.267 -13.271  71.767  1.00 81.55           C  
ATOM   1691  CG  TYR A1011     -11.766 -13.144  71.610  1.00 83.04           C  
ATOM   1692  CD1 TYR A1011     -10.956 -12.816  72.694  1.00 84.89           C  
ATOM   1693  CD2 TYR A1011     -11.153 -13.350  70.379  1.00 83.66           C  
ATOM   1694  CE1 TYR A1011      -9.575 -12.675  72.550  1.00 85.03           C  
ATOM   1695  CE2 TYR A1011      -9.778 -13.185  70.218  1.00 84.29           C  
ATOM   1696  CZ  TYR A1011      -8.991 -12.855  71.306  1.00 88.54           C  
ATOM   1697  OH  TYR A1011      -7.634 -12.704  71.150  1.00 86.89           O  
ATOM   1698  N   ILE A1012     -12.908  -9.943  70.738  1.00 73.69           N  
ATOM   1699  CA  ILE A1012     -12.376  -9.078  69.692  1.00 72.19           C  
ATOM   1700  C   ILE A1012     -10.882  -9.325  69.545  1.00 74.87           C  
ATOM   1701  O   ILE A1012     -10.116  -9.015  70.459  1.00 73.90           O  
ATOM   1702  CB  ILE A1012     -12.752  -7.571  69.864  1.00 75.10           C  
ATOM   1703  CG1 ILE A1012     -14.292  -7.373  69.792  1.00 75.78           C  
ATOM   1704  CG2 ILE A1012     -12.016  -6.685  68.834  1.00 74.93           C  
ATOM   1705  CD1 ILE A1012     -14.839  -5.934  69.988  1.00 81.85           C  
ATOM   1706  N   TYR A1013     -10.481  -9.923  68.389  1.00 70.96           N  
ATOM   1707  CA  TYR A1013      -9.093 -10.208  68.030  1.00 69.32           C  
ATOM   1708  C   TYR A1013      -8.436  -8.902  67.570  1.00 73.05           C  
ATOM   1709  O   TYR A1013      -8.880  -8.312  66.582  1.00 72.28           O  
ATOM   1710  CB  TYR A1013      -8.975 -11.329  66.934  1.00 68.59           C  
ATOM   1711  CG  TYR A1013      -7.569 -11.440  66.362  1.00 67.91           C  
ATOM   1712  CD1 TYR A1013      -6.555 -12.084  67.067  1.00 69.21           C  
ATOM   1713  CD2 TYR A1013      -7.223 -10.785  65.182  1.00 68.33           C  
ATOM   1714  CE1 TYR A1013      -5.234 -12.069  66.618  1.00 68.93           C  
ATOM   1715  CE2 TYR A1013      -5.908 -10.770  64.719  1.00 68.96           C  
ATOM   1716  CZ  TYR A1013      -4.915 -11.405  65.444  1.00 74.35           C  
ATOM   1717  OH  TYR A1013      -3.629 -11.423  64.968  1.00 73.51           O  
ATOM   1718  N   ASN A1014      -7.397  -8.450  68.277  1.00 69.87           N  
ATOM   1719  CA  ASN A1014      -6.698  -7.248  67.847  1.00 70.51           C  
ATOM   1720  C   ASN A1014      -5.399  -7.696  67.196  1.00 76.37           C  
ATOM   1721  O   ASN A1014      -4.653  -8.412  67.868  1.00 76.83           O  
ATOM   1722  CB  ASN A1014      -6.437  -6.297  69.021  1.00 71.92           C  
ATOM   1723  CG  ASN A1014      -5.773  -4.992  68.631  1.00102.50           C  
ATOM   1724  OD1 ASN A1014      -5.914  -4.490  67.511  1.00 97.89           O  
ATOM   1725  ND2 ASN A1014      -5.062  -4.379  69.562  1.00 97.00           N  
ATOM   1726  N   PRO A1015      -5.121  -7.350  65.900  1.00 73.75           N  
ATOM   1727  CA  PRO A1015      -3.860  -7.802  65.255  1.00 73.91           C  
ATOM   1728  C   PRO A1015      -2.589  -7.351  65.977  1.00 78.66           C  
ATOM   1729  O   PRO A1015      -1.655  -8.142  66.114  1.00 76.44           O  
ATOM   1730  CB  PRO A1015      -3.943  -7.214  63.838  1.00 75.42           C  
ATOM   1731  CG  PRO A1015      -5.372  -6.903  63.625  1.00 79.67           C  
ATOM   1732  CD  PRO A1015      -5.926  -6.536  64.966  1.00 75.21           C  
ATOM   1733  N   GLU A1016      -2.600  -6.090  66.480  1.00 78.30           N  
ATOM   1734  CA  GLU A1016      -1.546  -5.409  67.246  1.00 79.54           C  
ATOM   1735  C   GLU A1016      -1.154  -6.174  68.528  1.00 84.69           C  
ATOM   1736  O   GLU A1016      -0.010  -6.048  68.979  1.00 84.88           O  
ATOM   1737  CB  GLU A1016      -1.983  -3.977  67.613  1.00 81.22           C  
ATOM   1738  CG  GLU A1016      -2.114  -3.034  66.425  1.00 95.38           C  
ATOM   1739  CD  GLU A1016      -2.328  -1.576  66.790  1.00126.49           C  
ATOM   1740  OE1 GLU A1016      -1.514  -0.729  66.352  1.00125.79           O  
ATOM   1741  OE2 GLU A1016      -3.306  -1.277  67.514  1.00124.11           O  
ATOM   1742  N   ASP A1017      -2.112  -6.948  69.114  1.00 80.52           N  
ATOM   1743  CA  ASP A1017      -1.906  -7.778  70.309  1.00 79.74           C  
ATOM   1744  C   ASP A1017      -1.634  -9.241  69.937  1.00 82.87           C  
ATOM   1745  O   ASP A1017      -0.878  -9.923  70.631  1.00 82.59           O  
ATOM   1746  CB  ASP A1017      -3.126  -7.715  71.249  1.00 81.18           C  
ATOM   1747  CG  ASP A1017      -3.577  -6.332  71.684  1.00 88.02           C  
ATOM   1748  OD1 ASP A1017      -2.726  -5.414  71.747  1.00 88.28           O  
ATOM   1749  OD2 ASP A1017      -4.779  -6.169  71.980  1.00 91.24           O  
ATOM   1750  N   GLY A1018      -2.258  -9.706  68.858  1.00 78.81           N  
ATOM   1751  CA  GLY A1018      -2.147 -11.082  68.403  1.00 78.41           C  
ATOM   1752  C   GLY A1018      -2.753 -12.029  69.419  1.00 82.12           C  
ATOM   1753  O   GLY A1018      -3.772 -11.704  70.035  1.00 82.70           O  
ATOM   1754  N   ASP A1019      -2.113 -13.196  69.611  1.00 77.27           N  
ATOM   1755  CA  ASP A1019      -2.495 -14.232  70.577  1.00 76.35           C  
ATOM   1756  C   ASP A1019      -1.234 -15.055  70.921  1.00 79.07           C  
ATOM   1757  O   ASP A1019      -1.070 -16.168  70.426  1.00 77.55           O  
ATOM   1758  CB  ASP A1019      -3.649 -15.102  70.045  1.00 78.06           C  
ATOM   1759  CG  ASP A1019      -4.279 -16.040  71.059  1.00 89.51           C  
ATOM   1760  OD1 ASP A1019      -4.236 -15.729  72.270  1.00 89.21           O  
ATOM   1761  OD2 ASP A1019      -4.889 -17.036  70.638  1.00 98.91           O  
ATOM   1762  N   PRO A1020      -0.309 -14.497  71.744  1.00 76.11           N  
ATOM   1763  CA  PRO A1020       0.960 -15.197  72.027  1.00 75.92           C  
ATOM   1764  C   PRO A1020       0.858 -16.585  72.667  1.00 79.53           C  
ATOM   1765  O   PRO A1020       1.689 -17.443  72.360  1.00 78.49           O  
ATOM   1766  CB  PRO A1020       1.701 -14.216  72.930  1.00 77.76           C  
ATOM   1767  CG  PRO A1020       1.105 -12.878  72.602  1.00 81.95           C  
ATOM   1768  CD  PRO A1020      -0.332 -13.164  72.386  1.00 77.36           C  
ATOM   1769  N   ASP A1021      -0.152 -16.807  73.535  1.00 76.69           N  
ATOM   1770  CA  ASP A1021      -0.389 -18.083  74.223  1.00 76.68           C  
ATOM   1771  C   ASP A1021      -0.526 -19.261  73.245  1.00 80.19           C  
ATOM   1772  O   ASP A1021       0.058 -20.326  73.468  1.00 78.94           O  
ATOM   1773  CB  ASP A1021      -1.630 -17.986  75.139  1.00 78.77           C  
ATOM   1774  CG  ASP A1021      -1.493 -17.075  76.354  1.00 90.80           C  
ATOM   1775  OD1 ASP A1021      -0.347 -16.885  76.840  1.00 92.18           O  
ATOM   1776  OD2 ASP A1021      -2.537 -16.596  76.856  1.00 94.23           O  
ATOM   1777  N   ASN A1022      -1.286 -19.048  72.157  1.00 77.16           N  
ATOM   1778  CA  ASN A1022      -1.538 -20.041  71.112  1.00 76.71           C  
ATOM   1779  C   ASN A1022      -0.453 -20.018  70.023  1.00 79.64           C  
ATOM   1780  O   ASN A1022      -0.422 -20.918  69.180  1.00 80.01           O  
ATOM   1781  CB  ASN A1022      -2.937 -19.838  70.507  1.00 78.99           C  
ATOM   1782  CG  ASN A1022      -4.089 -19.906  71.491  1.00110.63           C  
ATOM   1783  OD1 ASN A1022      -4.083 -19.285  72.563  1.00107.79           O  
ATOM   1784  ND2 ASN A1022      -5.158 -20.575  71.091  1.00105.54           N  
ATOM   1785  N   GLY A1023       0.416 -19.002  70.058  1.00 74.74           N  
ATOM   1786  CA  GLY A1023       1.526 -18.839  69.123  1.00 74.01           C  
ATOM   1787  C   GLY A1023       1.304 -17.882  67.967  1.00 76.67           C  
ATOM   1788  O   GLY A1023       1.928 -18.028  66.911  1.00 77.79           O  
ATOM   1789  N   VAL A1024       0.425 -16.899  68.150  1.00 70.81           N  
ATOM   1790  CA  VAL A1024       0.118 -15.871  67.152  1.00 69.81           C  
ATOM   1791  C   VAL A1024       0.845 -14.557  67.579  1.00 73.89           C  
ATOM   1792  O   VAL A1024       0.399 -13.864  68.504  1.00 73.33           O  
ATOM   1793  CB  VAL A1024      -1.418 -15.686  66.972  1.00 72.84           C  
ATOM   1794  CG1 VAL A1024      -1.741 -14.592  65.960  1.00 72.44           C  
ATOM   1795  CG2 VAL A1024      -2.100 -16.998  66.595  1.00 72.46           C  
ATOM   1796  N   ASN A1025       1.974 -14.244  66.902  1.00 70.17           N  
ATOM   1797  CA  ASN A1025       2.813 -13.054  67.128  1.00 69.65           C  
ATOM   1798  C   ASN A1025       2.056 -11.715  66.918  1.00 73.01           C  
ATOM   1799  O   ASN A1025       1.183 -11.655  66.051  1.00 72.17           O  
ATOM   1800  CB  ASN A1025       4.044 -13.098  66.213  1.00 68.94           C  
ATOM   1801  CG  ASN A1025       5.198 -13.910  66.749  1.00 88.99           C  
ATOM   1802  OD1 ASN A1025       5.309 -15.116  66.512  1.00 71.13           O  
ATOM   1803  ND2 ASN A1025       6.113 -13.248  67.449  1.00 87.60           N  
ATOM   1804  N   PRO A1026       2.381 -10.627  67.666  1.00 69.41           N  
ATOM   1805  CA  PRO A1026       1.695  -9.343  67.427  1.00 69.09           C  
ATOM   1806  C   PRO A1026       2.020  -8.731  66.053  1.00 72.98           C  
ATOM   1807  O   PRO A1026       3.156  -8.823  65.569  1.00 72.00           O  
ATOM   1808  CB  PRO A1026       2.188  -8.452  68.576  1.00 70.41           C  
ATOM   1809  CG  PRO A1026       2.816  -9.379  69.555  1.00 74.74           C  
ATOM   1810  CD  PRO A1026       3.369 -10.496  68.752  1.00 70.54           C  
ATOM   1811  N   GLY A1027       1.004  -8.119  65.445  1.00 69.64           N  
ATOM   1812  CA  GLY A1027       1.082  -7.473  64.138  1.00 69.69           C  
ATOM   1813  C   GLY A1027       0.396  -8.268  63.047  1.00 74.44           C  
ATOM   1814  O   GLY A1027      -0.107  -7.696  62.074  1.00 74.14           O  
ATOM   1815  N   THR A1028       0.380  -9.606  63.223  1.00 70.97           N  
ATOM   1816  CA  THR A1028      -0.184 -10.620  62.337  1.00 70.18           C  
ATOM   1817  C   THR A1028      -1.654 -10.370  62.004  1.00 72.89           C  
ATOM   1818  O   THR A1028      -2.469 -10.117  62.893  1.00 72.16           O  
ATOM   1819  CB  THR A1028       0.062 -12.014  62.940  1.00 79.28           C  
ATOM   1820  OG1 THR A1028       1.460 -12.163  63.182  1.00 80.11           O  
ATOM   1821  CG2 THR A1028      -0.428 -13.157  62.048  1.00 79.32           C  
ATOM   1822  N   ASP A1029      -1.968 -10.444  60.701  1.00 68.79           N  
ATOM   1823  CA  ASP A1029      -3.306 -10.306  60.142  1.00 68.24           C  
ATOM   1824  C   ASP A1029      -4.122 -11.506  60.606  1.00 72.15           C  
ATOM   1825  O   ASP A1029      -3.585 -12.617  60.719  1.00 71.16           O  
ATOM   1826  CB  ASP A1029      -3.217 -10.328  58.600  1.00 69.57           C  
ATOM   1827  CG  ASP A1029      -4.451  -9.925  57.800  1.00 75.85           C  
ATOM   1828  OD1 ASP A1029      -5.584 -10.104  58.304  1.00 75.80           O  
ATOM   1829  OD2 ASP A1029      -4.290  -9.496  56.644  1.00 82.16           O  
ATOM   1830  N   PHE A1030      -5.423 -11.285  60.858  1.00 68.55           N  
ATOM   1831  CA  PHE A1030      -6.332 -12.360  61.235  1.00 67.51           C  
ATOM   1832  C   PHE A1030      -6.421 -13.397  60.087  1.00 69.05           C  
ATOM   1833  O   PHE A1030      -6.338 -14.597  60.345  1.00 68.06           O  
ATOM   1834  CB  PHE A1030      -7.714 -11.799  61.630  1.00 69.22           C  
ATOM   1835  CG  PHE A1030      -8.728 -12.850  62.027  1.00 70.79           C  
ATOM   1836  CD1 PHE A1030      -8.664 -13.468  63.273  1.00 73.79           C  
ATOM   1837  CD2 PHE A1030      -9.733 -13.239  61.146  1.00 73.12           C  
ATOM   1838  CE1 PHE A1030      -9.582 -14.464  63.626  1.00 74.91           C  
ATOM   1839  CE2 PHE A1030     -10.644 -14.244  61.495  1.00 76.14           C  
ATOM   1840  CZ  PHE A1030     -10.564 -14.848  62.731  1.00 74.34           C  
ATOM   1841  N   LYS A1031      -6.531 -12.922  58.827  1.00 64.04           N  
ATOM   1842  CA  LYS A1031      -6.606 -13.766  57.639  1.00 63.20           C  
ATOM   1843  C   LYS A1031      -5.359 -14.636  57.527  1.00 66.21           C  
ATOM   1844  O   LYS A1031      -5.489 -15.822  57.228  1.00 65.55           O  
ATOM   1845  CB  LYS A1031      -6.800 -12.918  56.374  1.00 65.41           C  
ATOM   1846  N   ASP A1032      -4.165 -14.068  57.847  1.00 62.36           N  
ATOM   1847  CA  ASP A1032      -2.858 -14.749  57.815  1.00 62.03           C  
ATOM   1848  C   ASP A1032      -2.697 -15.874  58.851  1.00 65.52           C  
ATOM   1849  O   ASP A1032      -1.774 -16.672  58.733  1.00 65.09           O  
ATOM   1850  CB  ASP A1032      -1.697 -13.734  57.941  1.00 64.06           C  
ATOM   1851  CG  ASP A1032      -1.362 -12.948  56.682  1.00 74.50           C  
ATOM   1852  OD1 ASP A1032      -1.565 -13.490  55.573  1.00 77.85           O  
ATOM   1853  OD2 ASP A1032      -0.816 -11.819  56.809  1.00 74.64           O  
ATOM   1854  N   ILE A1033      -3.576 -15.936  59.857  1.00 62.47           N  
ATOM   1855  CA  ILE A1033      -3.550 -16.947  60.921  1.00 62.41           C  
ATOM   1856  C   ILE A1033      -4.014 -18.327  60.387  1.00 66.55           C  
ATOM   1857  O   ILE A1033      -5.009 -18.378  59.662  1.00 65.79           O  
ATOM   1858  CB  ILE A1033      -4.410 -16.445  62.141  1.00 65.37           C  
ATOM   1859  CG1 ILE A1033      -3.742 -15.252  62.850  1.00 65.25           C  
ATOM   1860  CG2 ILE A1033      -4.784 -17.555  63.141  1.00 66.09           C  
ATOM   1861  CD1 ILE A1033      -4.667 -14.434  63.653  1.00 66.31           C  
ATOM   1862  N   PRO A1034      -3.337 -19.450  60.767  1.00 63.35           N  
ATOM   1863  CA  PRO A1034      -3.824 -20.785  60.357  1.00 63.31           C  
ATOM   1864  C   PRO A1034      -5.265 -21.068  60.809  1.00 69.36           C  
ATOM   1865  O   PRO A1034      -5.705 -20.580  61.854  1.00 68.80           O  
ATOM   1866  CB  PRO A1034      -2.842 -21.745  61.044  1.00 64.62           C  
ATOM   1867  CG  PRO A1034      -1.623 -20.935  61.301  1.00 68.72           C  
ATOM   1868  CD  PRO A1034      -2.137 -19.564  61.620  1.00 64.42           C  
ATOM   1869  N   ASP A1035      -5.993 -21.867  60.024  1.00 68.27           N  
ATOM   1870  CA  ASP A1035      -7.384 -22.216  60.302  1.00 69.20           C  
ATOM   1871  C   ASP A1035      -7.590 -23.023  61.598  1.00 77.00           C  
ATOM   1872  O   ASP A1035      -8.628 -22.851  62.243  1.00 77.79           O  
ATOM   1873  CB  ASP A1035      -8.013 -22.924  59.098  1.00 70.81           C  
ATOM   1874  CG  ASP A1035      -8.268 -21.988  57.932  1.00 78.48           C  
ATOM   1875  OD1 ASP A1035      -8.994 -20.981  58.125  1.00 79.72           O  
ATOM   1876  OD2 ASP A1035      -7.773 -22.279  56.816  1.00 79.09           O  
ATOM   1877  N   ASP A1036      -6.593 -23.845  62.009  1.00 74.89           N  
ATOM   1878  CA  ASP A1036      -6.629 -24.661  63.236  1.00 75.22           C  
ATOM   1879  C   ASP A1036      -6.729 -23.834  64.549  1.00 79.94           C  
ATOM   1880  O   ASP A1036      -7.064 -24.387  65.602  1.00 79.23           O  
ATOM   1881  CB  ASP A1036      -5.435 -25.633  63.286  1.00 77.17           C  
ATOM   1882  CG  ASP A1036      -4.087 -24.960  63.431  1.00 86.18           C  
ATOM   1883  OD1 ASP A1036      -3.646 -24.761  64.577  1.00 86.50           O  
ATOM   1884  OD2 ASP A1036      -3.460 -24.662  62.394  1.00 93.13           O  
ATOM   1885  N   TRP A1037      -6.449 -22.521  64.479  1.00 77.28           N  
ATOM   1886  CA  TRP A1037      -6.528 -21.620  65.621  1.00 77.71           C  
ATOM   1887  C   TRP A1037      -7.980 -21.483  66.071  1.00 81.09           C  
ATOM   1888  O   TRP A1037      -8.889 -21.452  65.233  1.00 80.28           O  
ATOM   1889  CB  TRP A1037      -5.930 -20.262  65.242  1.00 77.14           C  
ATOM   1890  CG  TRP A1037      -5.986 -19.210  66.314  1.00 78.67           C  
ATOM   1891  CD1 TRP A1037      -5.033 -18.945  67.251  1.00 81.67           C  
ATOM   1892  CD2 TRP A1037      -7.023 -18.233  66.505  1.00 78.77           C  
ATOM   1893  NE1 TRP A1037      -5.414 -17.871  68.025  1.00 81.13           N  
ATOM   1894  CE2 TRP A1037      -6.635 -17.420  67.595  1.00 82.76           C  
ATOM   1895  CE3 TRP A1037      -8.260 -17.987  65.878  1.00 80.28           C  
ATOM   1896  CZ2 TRP A1037      -7.433 -16.365  68.066  1.00 82.40           C  
ATOM   1897  CZ3 TRP A1037      -9.051 -16.948  66.350  1.00 82.08           C  
ATOM   1898  CH2 TRP A1037      -8.633 -16.141  67.424  1.00 82.77           C  
ATOM   1899  N   VAL A1038      -8.190 -21.429  67.400  1.00 77.95           N  
ATOM   1900  CA  VAL A1038      -9.514 -21.300  68.034  1.00 77.83           C  
ATOM   1901  C   VAL A1038      -9.640 -20.029  68.891  1.00 82.69           C  
ATOM   1902  O   VAL A1038      -8.630 -19.383  69.190  1.00 81.48           O  
ATOM   1903  CB  VAL A1038      -9.939 -22.565  68.835  1.00 81.36           C  
ATOM   1904  CG1 VAL A1038     -10.269 -23.729  67.908  1.00 81.12           C  
ATOM   1905  CG2 VAL A1038      -8.894 -22.953  69.889  1.00 81.12           C  
ATOM   1906  N   CYS A1039     -10.888 -19.688  69.302  1.00 80.76           N  
ATOM   1907  CA  CYS A1039     -11.175 -18.539  70.166  1.00 80.91           C  
ATOM   1908  C   CYS A1039     -10.555 -18.782  71.549  1.00 85.68           C  
ATOM   1909  O   CYS A1039     -10.823 -19.820  72.160  1.00 84.64           O  
ATOM   1910  CB  CYS A1039     -12.678 -18.272  70.261  1.00 81.04           C  
ATOM   1911  SG  CYS A1039     -13.127 -16.849  71.297  1.00 84.81           S  
ATOM   1912  N   PRO A1040      -9.708 -17.857  72.054  1.00 84.30           N  
ATOM   1913  CA  PRO A1040      -9.089 -18.075  73.373  1.00 85.10           C  
ATOM   1914  C   PRO A1040     -10.065 -17.999  74.564  1.00 93.04           C  
ATOM   1915  O   PRO A1040      -9.629 -18.158  75.709  1.00 93.94           O  
ATOM   1916  CB  PRO A1040      -7.983 -17.008  73.430  1.00 86.36           C  
ATOM   1917  CG  PRO A1040      -7.895 -16.426  72.044  1.00 90.31           C  
ATOM   1918  CD  PRO A1040      -9.253 -16.586  71.461  1.00 85.78           C  
ATOM   1919  N   LEU A1041     -11.380 -17.784  74.306  1.00 90.69           N  
ATOM   1920  CA  LEU A1041     -12.406 -17.722  75.350  1.00 91.00           C  
ATOM   1921  C   LEU A1041     -13.330 -18.941  75.329  1.00 96.36           C  
ATOM   1922  O   LEU A1041     -13.437 -19.622  76.351  1.00 96.44           O  
ATOM   1923  CB  LEU A1041     -13.215 -16.407  75.306  1.00 91.01           C  
ATOM   1924  CG  LEU A1041     -12.468 -15.096  75.644  1.00 95.43           C  
ATOM   1925  CD1 LEU A1041     -13.329 -13.900  75.353  1.00 95.41           C  
ATOM   1926  CD2 LEU A1041     -12.052 -15.037  77.104  1.00 97.26           C  
ATOM   1927  N   CYS A1042     -13.967 -19.237  74.171  1.00 93.31           N  
ATOM   1928  CA  CYS A1042     -14.887 -20.373  74.036  1.00 93.44           C  
ATOM   1929  C   CYS A1042     -14.274 -21.579  73.315  1.00 98.18           C  
ATOM   1930  O   CYS A1042     -14.501 -22.714  73.743  1.00 98.10           O  
ATOM   1931  CB  CYS A1042     -16.214 -19.953  73.404  1.00 93.69           C  
ATOM   1932  SG  CYS A1042     -16.096 -19.412  71.678  1.00 97.40           S  
ATOM   1933  N   GLY A1043     -13.538 -21.326  72.228  1.00 94.76           N  
ATOM   1934  CA  GLY A1043     -12.874 -22.359  71.435  1.00 93.91           C  
ATOM   1935  C   GLY A1043     -13.501 -22.667  70.089  1.00 95.77           C  
ATOM   1936  O   GLY A1043     -13.529 -23.833  69.680  1.00 94.70           O  
ATOM   1937  N   VAL A1044     -13.997 -21.626  69.383  1.00 91.64           N  
ATOM   1938  CA  VAL A1044     -14.605 -21.757  68.049  1.00 91.18           C  
ATOM   1939  C   VAL A1044     -13.618 -21.333  66.950  1.00 95.32           C  
ATOM   1940  O   VAL A1044     -12.747 -20.491  67.195  1.00 95.21           O  
ATOM   1941  CB  VAL A1044     -15.997 -21.074  67.882  1.00 94.73           C  
ATOM   1942  CG1 VAL A1044     -17.030 -21.653  68.841  1.00 94.57           C  
ATOM   1943  CG2 VAL A1044     -15.916 -19.553  67.998  1.00 94.45           C  
ATOM   1944  N   GLY A1045     -13.781 -21.908  65.759  1.00 91.46           N  
ATOM   1945  CA  GLY A1045     -12.947 -21.618  64.597  1.00 91.06           C  
ATOM   1946  C   GLY A1045     -13.129 -20.226  64.021  1.00 93.70           C  
ATOM   1947  O   GLY A1045     -14.117 -19.542  64.316  1.00 93.63           O  
ATOM   1948  N   LYS A1046     -12.169 -19.808  63.167  1.00 88.50           N  
ATOM   1949  CA  LYS A1046     -12.114 -18.512  62.472  1.00 87.52           C  
ATOM   1950  C   LYS A1046     -13.358 -18.193  61.609  1.00 91.58           C  
ATOM   1951  O   LYS A1046     -13.572 -17.035  61.250  1.00 90.67           O  
ATOM   1952  CB  LYS A1046     -10.858 -18.454  61.591  1.00 89.07           C  
ATOM   1953  CG  LYS A1046      -9.523 -18.409  62.336  1.00 87.71           C  
ATOM   1954  CD  LYS A1046      -8.338 -18.368  61.373  1.00 84.79           C  
ATOM   1955  CE  LYS A1046      -8.257 -17.063  60.623  1.00 87.50           C  
ATOM   1956  NZ  LYS A1046      -7.513 -17.191  59.349  1.00 95.62           N  
ATOM   1957  N   ASP A1047     -14.140 -19.225  61.239  1.00 89.12           N  
ATOM   1958  CA  ASP A1047     -15.360 -19.103  60.429  1.00 89.03           C  
ATOM   1959  C   ASP A1047     -16.463 -18.341  61.177  1.00 93.38           C  
ATOM   1960  O   ASP A1047     -17.157 -17.516  60.576  1.00 93.17           O  
ATOM   1961  CB  ASP A1047     -15.855 -20.486  59.959  1.00 90.50           C  
ATOM   1962  CG  ASP A1047     -15.781 -21.567  61.018  1.00 97.34           C  
ATOM   1963  OD1 ASP A1047     -14.678 -22.132  61.221  1.00 97.69           O  
ATOM   1964  OD2 ASP A1047     -16.826 -21.850  61.647  1.00101.22           O  
ATOM   1965  N   GLN A1048     -16.584 -18.584  62.498  1.00 89.48           N  
ATOM   1966  CA  GLN A1048     -17.568 -17.937  63.363  1.00 88.69           C  
ATOM   1967  C   GLN A1048     -17.038 -16.608  63.908  1.00 90.70           C  
ATOM   1968  O   GLN A1048     -17.347 -16.234  65.038  1.00 90.33           O  
ATOM   1969  CB  GLN A1048     -18.018 -18.890  64.486  1.00 90.14           C  
ATOM   1970  N   PHE A1049     -16.255 -15.895  63.080  1.00 86.06           N  
ATOM   1971  CA  PHE A1049     -15.670 -14.582  63.345  1.00 85.49           C  
ATOM   1972  C   PHE A1049     -16.090 -13.606  62.241  1.00 90.86           C  
ATOM   1973  O   PHE A1049     -16.063 -13.973  61.062  1.00 90.74           O  
ATOM   1974  CB  PHE A1049     -14.133 -14.671  63.415  1.00 86.69           C  
ATOM   1975  CG  PHE A1049     -13.550 -14.918  64.785  1.00 87.34           C  
ATOM   1976  CD1 PHE A1049     -13.538 -16.195  65.335  1.00 89.55           C  
ATOM   1977  CD2 PHE A1049     -12.981 -13.880  65.512  1.00 88.61           C  
ATOM   1978  CE1 PHE A1049     -12.991 -16.422  66.601  1.00 90.08           C  
ATOM   1979  CE2 PHE A1049     -12.430 -14.108  66.774  1.00 91.16           C  
ATOM   1980  CZ  PHE A1049     -12.439 -15.376  67.310  1.00 89.16           C  
ATOM   1981  N   GLU A1050     -16.473 -12.370  62.616  1.00 88.23           N  
ATOM   1982  CA  GLU A1050     -16.897 -11.349  61.652  1.00 88.81           C  
ATOM   1983  C   GLU A1050     -16.065 -10.068  61.715  1.00 93.69           C  
ATOM   1984  O   GLU A1050     -15.454  -9.784  62.745  1.00 92.59           O  
ATOM   1985  CB  GLU A1050     -18.399 -11.047  61.782  1.00 90.33           C  
ATOM   1986  CG  GLU A1050     -19.258 -12.066  61.052  1.00102.34           C  
ATOM   1987  CD  GLU A1050     -20.678 -11.637  60.735  1.00129.43           C  
ATOM   1988  OE1 GLU A1050     -21.088 -11.795  59.562  1.00115.95           O  
ATOM   1989  OE2 GLU A1050     -21.386 -11.163  61.655  1.00130.83           O  
ATOM   1990  N   GLU A1051     -16.038  -9.304  60.603  1.00 91.80           N  
ATOM   1991  CA  GLU A1051     -15.281  -8.056  60.483  1.00 92.36           C  
ATOM   1992  C   GLU A1051     -15.879  -6.914  61.317  1.00 98.34           C  
ATOM   1993  O   GLU A1051     -17.095  -6.706  61.300  1.00 98.47           O  
ATOM   1994  CB  GLU A1051     -15.143  -7.642  59.003  1.00 93.65           C  
ATOM   1995  CG  GLU A1051     -14.065  -6.595  58.750  1.00104.61           C  
ATOM   1996  CD  GLU A1051     -13.911  -6.087  57.327  1.00125.97           C  
ATOM   1997  OE1 GLU A1051     -14.933  -5.982  56.611  1.00127.32           O  
ATOM   1998  OE2 GLU A1051     -12.767  -5.745  56.944  1.00113.61           O  
ATOM   1999  N   VAL A1052     -15.048  -6.235  62.077  1.00 95.61           N  
ATOM   2000  CA  VAL A1052     -15.547  -5.149  62.864  1.00 96.05           C  
ATOM   2001  C   VAL A1052     -15.682  -3.979  61.918  1.00101.07           C  
ATOM   2002  O   VAL A1052     -14.741  -3.634  61.230  1.00100.74           O  
ATOM   2003  CB  VAL A1052     -14.591  -4.856  64.025  1.00100.03           C  
ATOM   2004  CG1 VAL A1052     -14.768  -3.448  64.566  1.00 99.75           C  
ATOM   2005  CG2 VAL A1052     -14.820  -5.870  65.122  1.00 99.79           C  
ATOM   2006  N   GLU A1053     -16.850  -3.354  61.903  1.00 98.25           N  
ATOM   2007  CA  GLU A1053     -17.058  -2.222  61.033  1.00 98.32           C  
ATOM   2008  C   GLU A1053     -16.079  -1.185  61.491  1.00102.65           C  
ATOM   2009  O   GLU A1053     -15.864  -1.014  62.675  1.00102.64           O  
ATOM   2010  CB  GLU A1053     -18.477  -1.686  61.167  1.00 99.76           C  
ATOM   2011  N   GLU A1054     -15.470  -0.489  60.552  1.00 98.95           N  
ATOM   2012  CA  GLU A1054     -14.462   0.480  60.905  1.00123.20           C  
ATOM   2013  C   GLU A1054     -14.964   1.870  60.667  1.00159.22           C  
ATOM   2014  O   GLU A1054     -15.678   2.127  59.707  1.00124.96           O  
ATOM   2015  CB  GLU A1054     -13.206   0.278  60.075  1.00124.37           C  
ATOM   2016  CG  GLU A1054     -12.168   1.364  60.292  1.00131.06           C  
ATOM   2017  CD  GLU A1054     -11.664   1.380  61.710  1.00141.94           C  
ATOM   2018  OE1 GLU A1054     -10.470   1.639  61.915  1.00132.45           O  
ATOM   2019  OE2 GLU A1054     -12.469   1.119  62.618  1.00131.02           O  
ATOM   2020  N   GLU A 227     -14.583   2.772  61.558  1.00122.91           N  
ATOM   2021  CA  GLU A 227     -14.767   4.185  61.310  1.00122.54           C  
ATOM   2022  C   GLU A 227     -13.544   4.571  60.504  1.00125.91           C  
ATOM   2023  O   GLU A 227     -12.506   4.953  61.046  1.00125.72           O  
ATOM   2024  CB  GLU A 227     -14.819   4.980  62.613  1.00123.86           C  
ATOM   2025  N   LYS A 228     -13.684   4.449  59.193  1.00121.28           N  
ATOM   2026  CA  LYS A 228     -12.615   4.774  58.297  1.00120.36           C  
ATOM   2027  C   LYS A 228     -12.757   6.257  58.155  1.00123.53           C  
ATOM   2028  O   LYS A 228     -13.296   6.749  57.178  1.00123.22           O  
ATOM   2029  CB  LYS A 228     -12.824   4.096  56.947  1.00122.33           C  
ATOM   2030  CG  LYS A 228     -11.843   2.974  56.632  1.00132.96           C  
ATOM   2031  CD  LYS A 228     -12.502   1.602  56.717  1.00141.15           C  
ATOM   2032  CE  LYS A 228     -13.080   1.146  55.382  1.00148.00           C  
ATOM   2033  NZ  LYS A 228     -14.212   0.190  55.532  1.00151.99           N  
ATOM   2034  N   LYS A 229     -12.331   6.968  59.186  1.00119.16           N  
ATOM   2035  CA  LYS A 229     -12.179   8.397  59.096  1.00118.43           C  
ATOM   2036  C   LYS A 229     -10.720   8.794  59.144  1.00120.36           C  
ATOM   2037  O   LYS A 229     -10.397   9.922  58.826  1.00120.04           O  
ATOM   2038  CB  LYS A 229     -12.955   9.096  60.189  1.00121.27           C  
ATOM   2039  CG  LYS A 229     -14.355   9.486  59.772  1.00137.70           C  
ATOM   2040  CD  LYS A 229     -15.120  10.084  60.938  1.00146.88           C  
ATOM   2041  CE  LYS A 229     -15.815  11.379  60.552  1.00157.87           C  
ATOM   2042  NZ  LYS A 229     -17.122  11.159  59.868  1.00167.17           N  
ATOM   2043  N   ARG A 230      -9.853   7.889  59.595  1.00114.96           N  
ATOM   2044  CA  ARG A 230      -8.402   8.013  59.437  1.00113.79           C  
ATOM   2045  C   ARG A 230      -7.989   7.863  57.981  1.00116.19           C  
ATOM   2046  O   ARG A 230      -7.110   8.544  57.458  1.00115.18           O  
ATOM   2047  CB  ARG A 230      -7.697   6.952  60.267  1.00113.20           C  
ATOM   2048  CG  ARG A 230      -8.404   6.606  61.560  1.00123.68           C  
ATOM   2049  CD  ARG A 230      -8.478   5.113  61.781  1.00130.70           C  
ATOM   2050  NE  ARG A 230      -7.231   4.560  62.284  1.00137.94           N  
ATOM   2051  CZ  ARG A 230      -7.161   3.638  63.235  1.00152.89           C  
ATOM   2052  NH1 ARG A 230      -8.262   3.175  63.794  1.00141.00           N  
ATOM   2053  NH2 ARG A 230      -5.991   3.181  63.635  1.00140.21           N  
ATOM   2054  N   HIS A 231      -8.664   6.908  57.373  1.00112.46           N  
ATOM   2055  CA  HIS A 231      -8.505   6.418  56.007  1.00112.12           C  
ATOM   2056  C   HIS A 231      -9.375   7.242  55.045  1.00113.93           C  
ATOM   2057  O   HIS A 231      -9.524   6.886  53.872  1.00113.95           O  
ATOM   2058  CB  HIS A 231      -8.812   4.899  55.924  1.00113.19           C  
ATOM   2059  CG  HIS A 231      -8.304   4.095  57.090  1.00116.80           C  
ATOM   2060  ND1 HIS A 231      -7.074   4.366  57.684  1.00118.61           N  
ATOM   2061  CD2 HIS A 231      -8.875   3.048  57.730  1.00118.70           C  
ATOM   2062  CE1 HIS A 231      -6.952   3.494  58.671  1.00118.10           C  
ATOM   2063  NE2 HIS A 231      -8.005   2.675  58.734  1.00118.49           N  
ATOM   2064  N   ARG A 232      -9.923   8.368  55.552  1.00108.45           N  
ATOM   2065  CA  ARG A 232     -10.722   9.330  54.793  1.00107.25           C  
ATOM   2066  C   ARG A 232      -9.779  10.127  53.893  1.00107.76           C  
ATOM   2067  O   ARG A 232     -10.188  10.576  52.822  1.00107.63           O  
ATOM   2068  CB  ARG A 232     -11.486  10.269  55.740  1.00107.40           C  
ATOM   2069  N   ASP A 233      -8.510  10.288  54.338  1.00101.03           N  
ATOM   2070  CA  ASP A 233      -7.440  10.961  53.606  1.00 99.22           C  
ATOM   2071  C   ASP A 233      -7.083  10.123  52.374  1.00 99.94           C  
ATOM   2072  O   ASP A 233      -6.894  10.673  51.291  1.00 99.04           O  
ATOM   2073  CB  ASP A 233      -6.218  11.136  54.515  1.00100.75           C  
ATOM   2074  N   VAL A 234      -7.044   8.783  52.553  1.00 94.48           N  
ATOM   2075  CA  VAL A 234      -6.753   7.748  51.552  1.00 93.00           C  
ATOM   2076  C   VAL A 234      -7.929   7.621  50.571  1.00 93.89           C  
ATOM   2077  O   VAL A 234      -7.703   7.470  49.369  1.00 94.07           O  
ATOM   2078  CB  VAL A 234      -6.430   6.384  52.237  1.00 96.81           C  
ATOM   2079  CG1 VAL A 234      -6.103   5.298  51.213  1.00 96.52           C  
ATOM   2080  CG2 VAL A 234      -5.295   6.524  53.244  1.00 96.63           C  
ATOM   2081  N   ARG A 235      -9.171   7.662  51.087  1.00 86.97           N  
ATOM   2082  CA  ARG A 235     -10.400   7.561  50.301  1.00 85.14           C  
ATOM   2083  C   ARG A 235     -10.597   8.746  49.355  1.00 85.42           C  
ATOM   2084  O   ARG A 235     -11.127   8.552  48.266  1.00 84.30           O  
ATOM   2085  CB  ARG A 235     -11.620   7.384  51.216  1.00 85.47           C  
ATOM   2086  N   LEU A 236     -10.163   9.962  49.755  1.00 80.22           N  
ATOM   2087  CA  LEU A 236     -10.305  11.163  48.923  1.00 79.20           C  
ATOM   2088  C   LEU A 236      -9.301  11.188  47.773  1.00 82.27           C  
ATOM   2089  O   LEU A 236      -9.697  11.364  46.620  1.00 81.45           O  
ATOM   2090  CB  LEU A 236     -10.219  12.452  49.763  1.00 78.91           C  
ATOM   2091  CG  LEU A 236     -10.179  13.769  48.972  1.00 83.31           C  
ATOM   2092  CD1 LEU A 236     -11.537  14.424  48.912  1.00 83.59           C  
ATOM   2093  CD2 LEU A 236      -9.141  14.713  49.536  1.00 85.48           C  
ATOM   2094  N   ILE A 237      -8.008  11.018  48.095  1.00 78.69           N  
ATOM   2095  CA  ILE A 237      -6.910  11.040  47.131  1.00 78.60           C  
ATOM   2096  C   ILE A 237      -7.090   9.917  46.096  1.00 82.65           C  
ATOM   2097  O   ILE A 237      -6.721  10.108  44.936  1.00 82.91           O  
ATOM   2098  CB  ILE A 237      -5.535  11.066  47.865  1.00 81.81           C  
ATOM   2099  CG1 ILE A 237      -5.322  12.470  48.495  1.00 82.36           C  
ATOM   2100  CG2 ILE A 237      -4.352  10.705  46.941  1.00 82.43           C  
ATOM   2101  CD1 ILE A 237      -4.488  12.530  49.762  1.00 91.04           C  
ATOM   2102  N   PHE A 238      -7.747   8.799  46.493  1.00 78.50           N  
ATOM   2103  CA  PHE A 238      -8.073   7.678  45.608  1.00 77.76           C  
ATOM   2104  C   PHE A 238      -9.132   8.102  44.596  1.00 79.89           C  
ATOM   2105  O   PHE A 238      -9.074   7.665  43.445  1.00 79.26           O  
ATOM   2106  CB  PHE A 238      -8.531   6.450  46.413  1.00 79.62           C  
ATOM   2107  CG  PHE A 238      -8.870   5.229  45.589  1.00 81.27           C  
ATOM   2108  CD1 PHE A 238      -7.866   4.425  45.062  1.00 84.72           C  
ATOM   2109  CD2 PHE A 238     -10.194   4.867  45.366  1.00 83.40           C  
ATOM   2110  CE1 PHE A 238      -8.180   3.293  44.305  1.00 85.96           C  
ATOM   2111  CE2 PHE A 238     -10.509   3.736  44.608  1.00 86.50           C  
ATOM   2112  CZ  PHE A 238      -9.501   2.957  44.080  1.00 84.98           C  
ATOM   2113  N   THR A 239     -10.087   8.966  45.026  1.00 75.01           N  
ATOM   2114  CA  THR A 239     -11.154   9.488  44.170  1.00 73.92           C  
ATOM   2115  C   THR A 239     -10.589  10.511  43.191  1.00 76.31           C  
ATOM   2116  O   THR A 239     -11.012  10.524  42.041  1.00 76.63           O  
ATOM   2117  CB  THR A 239     -12.335  10.033  44.979  1.00 79.16           C  
ATOM   2118  OG1 THR A 239     -12.555   9.218  46.126  1.00 79.14           O  
ATOM   2119  CG2 THR A 239     -13.614  10.088  44.165  1.00 76.63           C  
ATOM   2120  N   ILE A 240      -9.618  11.337  43.624  1.00 71.31           N  
ATOM   2121  CA  ILE A 240      -8.982  12.319  42.744  1.00 70.98           C  
ATOM   2122  C   ILE A 240      -8.328  11.562  41.586  1.00 75.13           C  
ATOM   2123  O   ILE A 240      -8.595  11.895  40.431  1.00 74.73           O  
ATOM   2124  CB  ILE A 240      -7.970  13.259  43.486  1.00 74.05           C  
ATOM   2125  CG1 ILE A 240      -8.612  13.963  44.707  1.00 74.33           C  
ATOM   2126  CG2 ILE A 240      -7.342  14.288  42.521  1.00 74.25           C  
ATOM   2127  CD1 ILE A 240      -7.593  14.582  45.751  1.00 79.14           C  
ATOM   2128  N   MET A 241      -7.527  10.508  41.899  1.00 72.33           N  
ATOM   2129  CA  MET A 241      -6.832   9.683  40.906  1.00 72.59           C  
ATOM   2130  C   MET A 241      -7.771   8.883  40.025  1.00 75.02           C  
ATOM   2131  O   MET A 241      -7.525   8.841  38.824  1.00 75.00           O  
ATOM   2132  CB  MET A 241      -5.767   8.771  41.540  1.00 75.48           C  
ATOM   2133  CG  MET A 241      -4.652   8.378  40.564  1.00 79.71           C  
ATOM   2134  SD  MET A 241      -3.163   7.715  41.372  1.00 84.55           S  
ATOM   2135  CE  MET A 241      -1.862   8.455  40.375  1.00 81.21           C  
ATOM   2136  N   ILE A 242      -8.834   8.257  40.598  1.00 70.47           N  
ATOM   2137  CA  ILE A 242      -9.809   7.462  39.829  1.00 70.20           C  
ATOM   2138  C   ILE A 242     -10.592   8.353  38.843  1.00 72.39           C  
ATOM   2139  O   ILE A 242     -10.714   7.992  37.663  1.00 71.31           O  
ATOM   2140  CB  ILE A 242     -10.735   6.574  40.739  1.00 73.54           C  
ATOM   2141  CG1 ILE A 242     -10.007   5.301  41.257  1.00 73.84           C  
ATOM   2142  CG2 ILE A 242     -12.093   6.216  40.086  1.00 74.33           C  
ATOM   2143  CD1 ILE A 242      -9.647   4.174  40.210  1.00 78.61           C  
ATOM   2144  N   VAL A 243     -11.085   9.522  39.321  1.00 68.02           N  
ATOM   2145  CA  VAL A 243     -11.856  10.466  38.497  1.00 67.57           C  
ATOM   2146  C   VAL A 243     -10.946  11.120  37.411  1.00 71.24           C  
ATOM   2147  O   VAL A 243     -11.437  11.376  36.310  1.00 70.78           O  
ATOM   2148  CB  VAL A 243     -12.687  11.480  39.343  1.00 70.78           C  
ATOM   2149  CG1 VAL A 243     -13.409  12.496  38.467  1.00 70.50           C  
ATOM   2150  CG2 VAL A 243     -13.710  10.743  40.208  1.00 70.34           C  
ATOM   2151  N   TYR A 244      -9.623  11.288  37.682  1.00 67.84           N  
ATOM   2152  CA  TYR A 244      -8.652  11.799  36.695  1.00 67.72           C  
ATOM   2153  C   TYR A 244      -8.628  10.878  35.460  1.00 72.73           C  
ATOM   2154  O   TYR A 244      -8.570  11.363  34.326  1.00 72.11           O  
ATOM   2155  CB  TYR A 244      -7.238  11.892  37.294  1.00 68.67           C  
ATOM   2156  CG  TYR A 244      -6.190  12.346  36.301  1.00 70.52           C  
ATOM   2157  CD1 TYR A 244      -5.473  11.425  35.543  1.00 72.42           C  
ATOM   2158  CD2 TYR A 244      -5.894  13.694  36.138  1.00 71.55           C  
ATOM   2159  CE1 TYR A 244      -4.520  11.837  34.614  1.00 73.44           C  
ATOM   2160  CE2 TYR A 244      -4.920  14.117  35.236  1.00 72.55           C  
ATOM   2161  CZ  TYR A 244      -4.244  13.186  34.466  1.00 79.61           C  
ATOM   2162  OH  TYR A 244      -3.278  13.591  33.577  1.00 81.40           O  
ATOM   2163  N   PHE A 245      -8.673   9.553  35.699  1.00 69.80           N  
ATOM   2164  CA  PHE A 245      -8.694   8.536  34.665  1.00 69.56           C  
ATOM   2165  C   PHE A 245     -10.027   8.484  33.886  1.00 71.13           C  
ATOM   2166  O   PHE A 245     -10.024   8.011  32.758  1.00 71.56           O  
ATOM   2167  CB  PHE A 245      -8.303   7.169  35.243  1.00 72.01           C  
ATOM   2168  CG  PHE A 245      -6.861   7.062  35.697  1.00 74.31           C  
ATOM   2169  CD1 PHE A 245      -5.813   7.343  34.823  1.00 78.21           C  
ATOM   2170  CD2 PHE A 245      -6.548   6.600  36.967  1.00 76.68           C  
ATOM   2171  CE1 PHE A 245      -4.480   7.219  35.235  1.00 79.07           C  
ATOM   2172  CE2 PHE A 245      -5.215   6.479  37.377  1.00 79.71           C  
ATOM   2173  CZ  PHE A 245      -4.192   6.785  36.508  1.00 77.78           C  
ATOM   2174  N   LEU A 246     -11.143   8.998  34.435  1.00 65.00           N  
ATOM   2175  CA  LEU A 246     -12.412   9.001  33.681  1.00 63.94           C  
ATOM   2176  C   LEU A 246     -12.447  10.121  32.635  1.00 66.81           C  
ATOM   2177  O   LEU A 246     -13.146  10.010  31.621  1.00 66.25           O  
ATOM   2178  CB  LEU A 246     -13.650   9.104  34.599  1.00 63.80           C  
ATOM   2179  CG  LEU A 246     -13.936   7.931  35.528  1.00 68.37           C  
ATOM   2180  CD1 LEU A 246     -14.945   8.308  36.576  1.00 68.50           C  
ATOM   2181  CD2 LEU A 246     -14.423   6.731  34.762  1.00 71.29           C  
ATOM   2182  N   PHE A 247     -11.703  11.204  32.893  1.00 62.68           N  
ATOM   2183  CA  PHE A 247     -11.644  12.367  32.019  1.00 62.18           C  
ATOM   2184  C   PHE A 247     -10.416  12.393  31.107  1.00 64.27           C  
ATOM   2185  O   PHE A 247     -10.538  12.804  29.948  1.00 64.61           O  
ATOM   2186  CB  PHE A 247     -11.725  13.656  32.847  1.00 64.36           C  
ATOM   2187  CG  PHE A 247     -13.088  13.920  33.439  1.00 66.79           C  
ATOM   2188  CD1 PHE A 247     -13.468  13.338  34.645  1.00 70.10           C  
ATOM   2189  CD2 PHE A 247     -13.994  14.752  32.795  1.00 69.54           C  
ATOM   2190  CE1 PHE A 247     -14.738  13.571  35.184  1.00 70.85           C  
ATOM   2191  CE2 PHE A 247     -15.261  14.986  33.338  1.00 71.99           C  
ATOM   2192  CZ  PHE A 247     -15.623  14.391  34.527  1.00 69.79           C  
ATOM   2193  N   TRP A 248      -9.244  11.958  31.618  1.00 58.49           N  
ATOM   2194  CA  TRP A 248      -8.012  12.013  30.844  1.00 57.27           C  
ATOM   2195  C   TRP A 248      -7.617  10.697  30.162  1.00 63.06           C  
ATOM   2196  O   TRP A 248      -7.030  10.778  29.079  1.00 63.81           O  
ATOM   2197  CB  TRP A 248      -6.848  12.593  31.661  1.00 54.87           C  
ATOM   2198  CG  TRP A 248      -6.833  14.099  31.665  1.00 55.06           C  
ATOM   2199  CD1 TRP A 248      -7.032  14.917  32.739  1.00 57.76           C  
ATOM   2200  CD2 TRP A 248      -6.673  14.971  30.526  1.00 54.58           C  
ATOM   2201  NE1 TRP A 248      -6.934  16.238  32.358  1.00 56.86           N  
ATOM   2202  CE2 TRP A 248      -6.727  16.300  31.002  1.00 58.33           C  
ATOM   2203  CE3 TRP A 248      -6.486  14.754  29.146  1.00 55.29           C  
ATOM   2204  CZ2 TRP A 248      -6.620  17.407  30.150  1.00 57.50           C  
ATOM   2205  CZ3 TRP A 248      -6.372  15.851  28.310  1.00 56.64           C  
ATOM   2206  CH2 TRP A 248      -6.452  17.158  28.809  1.00 57.27           C  
ATOM   2207  N   ALA A 249      -7.953   9.511  30.728  1.00 59.15           N  
ATOM   2208  CA  ALA A 249      -7.627   8.251  30.052  1.00 58.76           C  
ATOM   2209  C   ALA A 249      -8.277   8.107  28.652  1.00 63.15           C  
ATOM   2210  O   ALA A 249      -7.525   7.735  27.754  1.00 62.32           O  
ATOM   2211  CB  ALA A 249      -7.931   7.051  30.925  1.00 59.35           C  
ATOM   2212  N   PRO A 250      -9.580   8.477  28.388  1.00 60.99           N  
ATOM   2213  CA  PRO A 250     -10.112   8.367  27.002  1.00 61.33           C  
ATOM   2214  C   PRO A 250      -9.302   9.123  25.945  1.00 68.02           C  
ATOM   2215  O   PRO A 250      -9.108   8.605  24.847  1.00 67.74           O  
ATOM   2216  CB  PRO A 250     -11.546   8.908  27.108  1.00 62.58           C  
ATOM   2217  CG  PRO A 250     -11.908   8.767  28.537  1.00 66.82           C  
ATOM   2218  CD  PRO A 250     -10.633   8.953  29.315  1.00 62.34           C  
ATOM   2219  N   TYR A 251      -8.795  10.322  26.286  1.00 66.65           N  
ATOM   2220  CA  TYR A 251      -7.963  11.108  25.380  1.00 67.62           C  
ATOM   2221  C   TYR A 251      -6.619  10.434  25.121  1.00 73.58           C  
ATOM   2222  O   TYR A 251      -6.169  10.411  23.977  1.00 73.32           O  
ATOM   2223  CB  TYR A 251      -7.771  12.548  25.892  1.00 69.23           C  
ATOM   2224  CG  TYR A 251      -6.690  13.323  25.162  1.00 70.82           C  
ATOM   2225  CD1 TYR A 251      -6.901  13.812  23.873  1.00 72.52           C  
ATOM   2226  CD2 TYR A 251      -5.445  13.536  25.743  1.00 71.75           C  
ATOM   2227  CE1 TYR A 251      -5.896  14.488  23.182  1.00 72.93           C  
ATOM   2228  CE2 TYR A 251      -4.435  14.217  25.065  1.00 72.86           C  
ATOM   2229  CZ  TYR A 251      -4.668  14.702  23.789  1.00 78.21           C  
ATOM   2230  OH  TYR A 251      -3.676  15.382  23.136  1.00 76.77           O  
ATOM   2231  N   ASN A 252      -5.972   9.918  26.183  1.00 71.49           N  
ATOM   2232  CA  ASN A 252      -4.665   9.255  26.116  1.00 71.60           C  
ATOM   2233  C   ASN A 252      -4.681   8.018  25.207  1.00 75.83           C  
ATOM   2234  O   ASN A 252      -3.725   7.802  24.458  1.00 75.48           O  
ATOM   2235  CB  ASN A 252      -4.143   8.930  27.524  1.00 72.28           C  
ATOM   2236  CG  ASN A 252      -3.506  10.115  28.222  1.00 91.54           C  
ATOM   2237  OD1 ASN A 252      -2.346  10.457  27.981  1.00 88.24           O  
ATOM   2238  ND2 ASN A 252      -4.237  10.772  29.103  1.00 79.99           N  
ATOM   2239  N   ILE A 253      -5.794   7.257  25.219  1.00 72.49           N  
ATOM   2240  CA  ILE A 253      -5.956   6.056  24.394  1.00 72.43           C  
ATOM   2241  C   ILE A 253      -6.093   6.435  22.923  1.00 76.73           C  
ATOM   2242  O   ILE A 253      -5.327   5.926  22.102  1.00 76.39           O  
ATOM   2243  CB  ILE A 253      -7.094   5.121  24.908  1.00 75.46           C  
ATOM   2244  CG1 ILE A 253      -6.852   4.713  26.390  1.00 75.72           C  
ATOM   2245  CG2 ILE A 253      -7.248   3.876  24.016  1.00 75.99           C  
ATOM   2246  CD1 ILE A 253      -8.125   4.479  27.211  1.00 84.31           C  
ATOM   2247  N   VAL A 254      -7.022   7.361  22.607  1.00 73.53           N  
ATOM   2248  CA  VAL A 254      -7.266   7.871  21.251  1.00 73.78           C  
ATOM   2249  C   VAL A 254      -5.981   8.501  20.654  1.00 79.26           C  
ATOM   2250  O   VAL A 254      -5.698   8.269  19.482  1.00 79.47           O  
ATOM   2251  CB  VAL A 254      -8.493   8.827  21.199  1.00 77.72           C  
ATOM   2252  CG1 VAL A 254      -8.737   9.373  19.789  1.00 77.41           C  
ATOM   2253  CG2 VAL A 254      -9.750   8.142  21.728  1.00 77.40           C  
ATOM   2254  N   LEU A 255      -5.189   9.241  21.472  1.00 76.62           N  
ATOM   2255  CA  LEU A 255      -3.905   9.859  21.088  1.00 76.95           C  
ATOM   2256  C   LEU A 255      -2.913   8.812  20.555  1.00 81.76           C  
ATOM   2257  O   LEU A 255      -2.223   9.061  19.572  1.00 81.01           O  
ATOM   2258  CB  LEU A 255      -3.285  10.612  22.291  1.00 76.95           C  
ATOM   2259  CG  LEU A 255      -2.049  11.498  22.025  1.00 81.13           C  
ATOM   2260  CD1 LEU A 255      -2.436  12.814  21.401  1.00 81.13           C  
ATOM   2261  CD2 LEU A 255      -1.313  11.790  23.303  1.00 82.87           C  
ATOM   2262  N   LEU A 256      -2.860   7.648  21.200  1.00 79.88           N  
ATOM   2263  CA  LEU A 256      -2.002   6.537  20.801  1.00 80.50           C  
ATOM   2264  C   LEU A 256      -2.542   5.862  19.535  1.00 85.74           C  
ATOM   2265  O   LEU A 256      -1.758   5.383  18.720  1.00 85.37           O  
ATOM   2266  CB  LEU A 256      -1.916   5.517  21.943  1.00 80.54           C  
ATOM   2267  CG  LEU A 256      -0.668   4.661  21.970  1.00 85.32           C  
ATOM   2268  CD1 LEU A 256       0.494   5.426  22.574  1.00 85.42           C  
ATOM   2269  CD2 LEU A 256      -0.909   3.399  22.758  1.00 88.80           C  
ATOM   2270  N   LEU A 257      -3.877   5.833  19.382  1.00 83.28           N  
ATOM   2271  CA  LEU A 257      -4.571   5.228  18.244  1.00 83.65           C  
ATOM   2272  C   LEU A 257      -4.466   6.062  16.969  1.00 87.92           C  
ATOM   2273  O   LEU A 257      -4.330   5.492  15.889  1.00 87.48           O  
ATOM   2274  CB  LEU A 257      -6.053   4.976  18.578  1.00 83.98           C  
ATOM   2275  CG  LEU A 257      -6.362   3.928  19.661  1.00 89.08           C  
ATOM   2276  CD1 LEU A 257      -7.755   4.132  20.211  1.00 89.62           C  
ATOM   2277  CD2 LEU A 257      -6.184   2.490  19.147  1.00 90.70           C  
ATOM   2278  N   ASN A 258      -4.550   7.405  17.093  1.00 84.86           N  
ATOM   2279  CA  ASN A 258      -4.485   8.356  15.984  1.00 85.10           C  
ATOM   2280  C   ASN A 258      -3.063   8.503  15.433  1.00 90.36           C  
ATOM   2281  O   ASN A 258      -2.893   8.560  14.214  1.00 90.38           O  
ATOM   2282  CB  ASN A 258      -5.066   9.705  16.400  1.00 87.26           C  
ATOM   2283  CG  ASN A 258      -5.105  10.747  15.298  1.00123.19           C  
ATOM   2284  OD1 ASN A 258      -6.126  10.954  14.623  1.00122.51           O  
ATOM   2285  ND2 ASN A 258      -3.987  11.412  15.065  1.00115.69           N  
ATOM   2286  N   THR A 259      -2.053   8.604  16.327  1.00 87.55           N  
ATOM   2287  CA  THR A 259      -0.632   8.730  15.967  1.00 87.43           C  
ATOM   2288  C   THR A 259      -0.130   7.415  15.363  1.00 91.98           C  
ATOM   2289  O   THR A 259       0.598   7.430  14.365  1.00 91.48           O  
ATOM   2290  CB  THR A 259       0.199   9.170  17.186  1.00 93.65           C  
ATOM   2291  OG1 THR A 259      -0.299  10.423  17.662  1.00 93.55           O  
ATOM   2292  CG2 THR A 259       1.693   9.281  16.881  1.00 90.84           C  
ATOM   2293  N   PHE A 260      -0.524   6.289  15.968  1.00 89.28           N  
ATOM   2294  CA  PHE A 260      -0.129   4.977  15.485  1.00 89.44           C  
ATOM   2295  C   PHE A 260      -1.290   4.290  14.752  1.00 96.41           C  
ATOM   2296  O   PHE A 260      -1.633   3.150  15.061  1.00 96.39           O  
ATOM   2297  CB  PHE A 260       0.486   4.128  16.621  1.00 90.58           C  
ATOM   2298  CG  PHE A 260       1.648   4.782  17.338  1.00 91.56           C  
ATOM   2299  CD1 PHE A 260       2.915   4.807  16.765  1.00 94.34           C  
ATOM   2300  CD2 PHE A 260       1.479   5.359  18.589  1.00 93.31           C  
ATOM   2301  CE1 PHE A 260       3.992   5.409  17.428  1.00 95.08           C  
ATOM   2302  CE2 PHE A 260       2.559   5.951  19.258  1.00 96.07           C  
ATOM   2303  CZ  PHE A 260       3.809   5.973  18.671  1.00 94.15           C  
ATOM   2304  N   GLN A 261      -1.900   4.993  13.774  1.00 95.26           N  
ATOM   2305  CA  GLN A 261      -2.999   4.421  12.990  1.00 96.32           C  
ATOM   2306  C   GLN A 261      -2.477   3.454  11.928  1.00103.10           C  
ATOM   2307  O   GLN A 261      -3.094   2.413  11.704  1.00103.44           O  
ATOM   2308  CB  GLN A 261      -3.959   5.480  12.415  1.00 97.66           C  
ATOM   2309  CG  GLN A 261      -3.332   6.530  11.509  1.00113.65           C  
ATOM   2310  CD  GLN A 261      -4.361   7.501  10.992  1.00129.86           C  
ATOM   2311  OE1 GLN A 261      -4.722   7.500   9.809  1.00123.27           O  
ATOM   2312  NE2 GLN A 261      -4.871   8.340  11.875  1.00123.74           N  
ATOM   2313  N   GLU A 262      -1.322   3.766  11.315  1.00100.90           N  
ATOM   2314  CA  GLU A 262      -0.686   2.886  10.335  1.00101.62           C  
ATOM   2315  C   GLU A 262       0.020   1.742  11.075  1.00108.17           C  
ATOM   2316  O   GLU A 262       0.600   1.969  12.144  1.00108.28           O  
ATOM   2317  CB  GLU A 262       0.314   3.667   9.469  1.00102.91           C  
ATOM   2318  N   PHE A 263      -0.064   0.506  10.527  1.00105.78           N  
ATOM   2319  CA  PHE A 263       0.553  -0.731  11.049  1.00105.92           C  
ATOM   2320  C   PHE A 263       0.074  -1.162  12.458  1.00109.84           C  
ATOM   2321  O   PHE A 263       0.375  -2.285  12.873  1.00108.73           O  
ATOM   2322  CB  PHE A 263       2.095  -0.657  11.002  1.00107.70           C  
ATOM   2323  N   PHE A 264      -0.686  -0.300  13.166  1.00107.46           N  
ATOM   2324  CA  PHE A 264      -1.212  -0.585  14.506  1.00108.00           C  
ATOM   2325  C   PHE A 264      -2.729  -0.336  14.647  1.00113.08           C  
ATOM   2326  O   PHE A 264      -3.249  -0.318  15.768  1.00112.60           O  
ATOM   2327  CB  PHE A 264      -0.416   0.181  15.579  1.00109.93           C  
ATOM   2328  CG  PHE A 264       0.926  -0.420  15.920  1.00111.69           C  
ATOM   2329  CD1 PHE A 264       2.066  -0.061  15.210  1.00115.23           C  
ATOM   2330  CD2 PHE A 264       1.053  -1.331  16.963  1.00113.73           C  
ATOM   2331  CE1 PHE A 264       3.310  -0.615  15.530  1.00116.31           C  
ATOM   2332  CE2 PHE A 264       2.296  -1.885  17.279  1.00116.71           C  
ATOM   2333  CZ  PHE A 264       3.415  -1.523  16.562  1.00115.11           C  
ATOM   2334  N   GLY A 265      -3.418  -0.178  13.515  1.00110.69           N  
ATOM   2335  CA  GLY A 265      -4.859   0.050  13.464  1.00111.04           C  
ATOM   2336  C   GLY A 265      -5.395   0.273  12.063  1.00116.18           C  
ATOM   2337  O   GLY A 265      -4.890  -0.320  11.103  1.00115.73           O  
ATOM   2338  N   LEU A 266      -6.420   1.146  11.939  1.00113.62           N  
ATOM   2339  CA  LEU A 266      -7.067   1.486  10.667  1.00113.63           C  
ATOM   2340  C   LEU A 266      -6.562   2.822  10.097  1.00117.89           C  
ATOM   2341  O   LEU A 266      -6.797   3.886  10.676  1.00117.51           O  
ATOM   2342  CB  LEU A 266      -8.594   1.476  10.813  1.00113.66           C  
ATOM   2343  N   ASN A 267      -5.852   2.747   8.963  1.00114.64           N  
ATOM   2344  CA  ASN A 267      -5.255   3.892   8.278  1.00114.58           C  
ATOM   2345  C   ASN A 267      -6.152   4.500   7.180  1.00118.50           C  
ATOM   2346  O   ASN A 267      -5.837   5.586   6.678  1.00117.88           O  
ATOM   2347  CB  ASN A 267      -3.874   3.499   7.725  1.00115.53           C  
ATOM   2348  CG  ASN A 267      -3.036   4.661   7.246  1.00143.56           C  
ATOM   2349  OD1 ASN A 267      -2.412   5.379   8.038  1.00140.11           O  
ATOM   2350  ND2 ASN A 267      -2.983   4.859   5.939  1.00136.00           N  
ATOM   2351  N   ASN A 268      -7.281   3.824   6.832  1.00115.19           N  
ATOM   2352  CA  ASN A 268      -8.222   4.258   5.782  1.00115.15           C  
ATOM   2353  C   ASN A 268      -8.802   5.683   5.999  1.00119.12           C  
ATOM   2354  O   ASN A 268      -8.752   6.214   7.114  1.00118.98           O  
ATOM   2355  CB  ASN A 268      -9.338   3.224   5.562  1.00115.77           C  
ATOM   2356  CG  ASN A 268     -10.244   3.015   6.743  1.00137.31           C  
ATOM   2357  OD1 ASN A 268     -11.305   3.640   6.858  1.00129.96           O  
ATOM   2358  ND2 ASN A 268      -9.862   2.109   7.633  1.00129.02           N  
ATOM   2359  N   CYS A 269      -9.318   6.297   4.912  1.00115.27           N  
ATOM   2360  CA  CYS A 269      -9.853   7.659   4.884  1.00115.05           C  
ATOM   2361  C   CYS A 269     -10.945   7.927   5.916  1.00117.34           C  
ATOM   2362  O   CYS A 269     -10.853   8.926   6.627  1.00116.98           O  
ATOM   2363  CB  CYS A 269     -10.313   8.038   3.481  1.00115.75           C  
ATOM   2364  SG  CYS A 269     -10.900   9.748   3.332  1.00120.09           S  
ATOM   2365  N   SER A 270     -11.972   7.066   5.990  1.00112.83           N  
ATOM   2366  CA  SER A 270     -13.081   7.242   6.933  1.00112.31           C  
ATOM   2367  C   SER A 270     -12.637   7.133   8.399  1.00114.66           C  
ATOM   2368  O   SER A 270     -12.965   8.011   9.199  1.00113.95           O  
ATOM   2369  CB  SER A 270     -14.215   6.263   6.635  1.00116.21           C  
ATOM   2370  OG  SER A 270     -15.352   6.516   7.447  1.00124.81           O  
ATOM   2371  N   SER A 271     -11.876   6.074   8.731  1.00110.22           N  
ATOM   2372  CA  SER A 271     -11.372   5.785  10.075  1.00109.51           C  
ATOM   2373  C   SER A 271     -10.440   6.866  10.638  1.00112.40           C  
ATOM   2374  O   SER A 271     -10.441   7.091  11.849  1.00112.17           O  
ATOM   2375  CB  SER A 271     -10.672   4.433  10.100  1.00112.78           C  
ATOM   2376  OG  SER A 271     -11.537   3.399   9.662  1.00121.40           O  
ATOM   2377  N   SER A 272      -9.648   7.523   9.770  1.00107.77           N  
ATOM   2378  CA  SER A 272      -8.715   8.581  10.167  1.00106.91           C  
ATOM   2379  C   SER A 272      -9.455   9.844  10.599  1.00108.61           C  
ATOM   2380  O   SER A 272      -9.061  10.473  11.583  1.00107.84           O  
ATOM   2381  CB  SER A 272      -7.737   8.887   9.038  1.00110.53           C  
ATOM   2382  OG  SER A 272      -8.428   9.202   7.841  1.00119.41           O  
ATOM   2383  N   ASN A 273     -10.534  10.201   9.871  1.00103.73           N  
ATOM   2384  CA  ASN A 273     -11.372  11.363  10.172  1.00102.99           C  
ATOM   2385  C   ASN A 273     -12.154  11.131  11.460  1.00105.44           C  
ATOM   2386  O   ASN A 273     -12.396  12.089  12.194  1.00105.72           O  
ATOM   2387  CB  ASN A 273     -12.318  11.684   9.011  1.00104.83           C  
ATOM   2388  CG  ASN A 273     -11.879  12.844   8.145  1.00126.29           C  
ATOM   2389  OD1 ASN A 273     -11.738  13.980   8.607  1.00120.62           O  
ATOM   2390  ND2 ASN A 273     -11.694  12.590   6.859  1.00116.46           N  
ATOM   2391  N   ARG A 274     -12.530   9.860  11.737  1.00 99.89           N  
ATOM   2392  CA  ARG A 274     -13.244   9.437  12.949  1.00 98.78           C  
ATOM   2393  C   ARG A 274     -12.331   9.544  14.168  1.00 99.10           C  
ATOM   2394  O   ARG A 274     -12.798   9.925  15.243  1.00 98.15           O  
ATOM   2395  CB  ARG A 274     -13.757   7.991  12.819  1.00100.63           C  
ATOM   2396  CG  ARG A 274     -14.960   7.829  11.899  1.00116.26           C  
ATOM   2397  CD  ARG A 274     -15.255   6.366  11.641  1.00133.17           C  
ATOM   2398  NE  ARG A 274     -16.309   5.853  12.520  1.00149.02           N  
ATOM   2399  CZ  ARG A 274     -17.600   5.822  12.198  1.00167.89           C  
ATOM   2400  NH1 ARG A 274     -18.013   6.280  11.022  1.00156.80           N  
ATOM   2401  NH2 ARG A 274     -18.489   5.336  13.057  1.00155.81           N  
ATOM   2402  N   LEU A 275     -11.032   9.198  13.995  1.00 93.45           N  
ATOM   2403  CA  LEU A 275     -10.009   9.246  15.044  1.00 91.94           C  
ATOM   2404  C   LEU A 275      -9.662  10.682  15.433  1.00 92.79           C  
ATOM   2405  O   LEU A 275      -9.485  10.954  16.623  1.00 92.30           O  
ATOM   2406  CB  LEU A 275      -8.738   8.480  14.626  1.00 91.82           C  
ATOM   2407  CG  LEU A 275      -8.736   6.964  14.831  1.00 96.42           C  
ATOM   2408  CD1 LEU A 275      -7.743   6.296  13.906  1.00 96.61           C  
ATOM   2409  CD2 LEU A 275      -8.438   6.589  16.281  1.00 98.41           C  
ATOM   2410  N   ASP A 276      -9.565  11.593  14.433  1.00 87.11           N  
ATOM   2411  CA  ASP A 276      -9.258  13.008  14.640  1.00 85.99           C  
ATOM   2412  C   ASP A 276     -10.399  13.692  15.386  1.00 86.63           C  
ATOM   2413  O   ASP A 276     -10.139  14.471  16.303  1.00 85.41           O  
ATOM   2414  CB  ASP A 276      -8.969  13.706  13.302  1.00 88.42           C  
ATOM   2415  CG  ASP A 276      -8.344  15.090  13.426  1.00101.38           C  
ATOM   2416  OD1 ASP A 276      -7.218  15.189  13.980  1.00101.36           O  
ATOM   2417  OD2 ASP A 276      -8.954  16.070  12.923  1.00107.41           O  
ATOM   2418  N   GLN A 277     -11.659  13.369  15.010  1.00 82.05           N  
ATOM   2419  CA  GLN A 277     -12.887  13.869  15.640  1.00 81.10           C  
ATOM   2420  C   GLN A 277     -12.961  13.406  17.099  1.00 81.75           C  
ATOM   2421  O   GLN A 277     -13.239  14.228  17.971  1.00 80.84           O  
ATOM   2422  CB  GLN A 277     -14.134  13.393  14.876  1.00 82.77           C  
ATOM   2423  CG  GLN A 277     -14.763  14.453  13.979  1.00107.55           C  
ATOM   2424  CD  GLN A 277     -16.247  14.213  13.776  1.00133.12           C  
ATOM   2425  OE1 GLN A 277     -16.676  13.199  13.209  1.00129.44           O  
ATOM   2426  NE2 GLN A 277     -17.065  15.150  14.235  1.00126.30           N  
ATOM   2427  N   ALA A 278     -12.677  12.098  17.358  1.00 76.46           N  
ATOM   2428  CA  ALA A 278     -12.668  11.474  18.692  1.00 75.23           C  
ATOM   2429  C   ALA A 278     -11.610  12.098  19.596  1.00 77.00           C  
ATOM   2430  O   ALA A 278     -11.826  12.165  20.802  1.00 75.24           O  
ATOM   2431  CB  ALA A 278     -12.439   9.975  18.580  1.00 75.78           C  
ATOM   2432  N   MET A 279     -10.485  12.584  19.003  1.00 73.28           N  
ATOM   2433  CA  MET A 279      -9.382  13.237  19.711  1.00 72.65           C  
ATOM   2434  C   MET A 279      -9.793  14.606  20.241  1.00 73.93           C  
ATOM   2435  O   MET A 279      -9.426  14.940  21.365  1.00 74.17           O  
ATOM   2436  CB  MET A 279      -8.122  13.340  18.838  1.00 75.33           C  
ATOM   2437  CG  MET A 279      -6.872  13.724  19.623  1.00 79.38           C  
ATOM   2438  SD  MET A 279      -5.463  14.188  18.587  1.00 83.77           S  
ATOM   2439  CE  MET A 279      -4.656  12.625  18.467  1.00 80.49           C  
ATOM   2440  N   GLN A 280     -10.545  15.387  19.454  1.00 68.41           N  
ATOM   2441  CA  GLN A 280     -11.012  16.714  19.864  1.00 67.74           C  
ATOM   2442  C   GLN A 280     -12.028  16.604  21.010  1.00 70.02           C  
ATOM   2443  O   GLN A 280     -11.939  17.347  21.987  1.00 68.30           O  
ATOM   2444  CB  GLN A 280     -11.624  17.467  18.672  1.00 69.28           C  
ATOM   2445  CG  GLN A 280     -10.605  17.983  17.652  1.00 86.89           C  
ATOM   2446  CD  GLN A 280     -11.282  18.430  16.374  1.00108.04           C  
ATOM   2447  OE1 GLN A 280     -11.919  19.489  16.308  1.00101.82           O  
ATOM   2448  NE2 GLN A 280     -11.167  17.627  15.328  1.00101.15           N  
ATOM   2449  N   VAL A 281     -12.963  15.641  20.889  1.00 67.24           N  
ATOM   2450  CA  VAL A 281     -14.049  15.328  21.827  1.00 66.99           C  
ATOM   2451  C   VAL A 281     -13.505  14.889  23.181  1.00 70.56           C  
ATOM   2452  O   VAL A 281     -13.968  15.393  24.201  1.00 69.88           O  
ATOM   2453  CB  VAL A 281     -15.039  14.301  21.202  1.00 71.03           C  
ATOM   2454  CG1 VAL A 281     -15.993  13.725  22.241  1.00 71.08           C  
ATOM   2455  CG2 VAL A 281     -15.826  14.932  20.053  1.00 70.84           C  
ATOM   2456  N   THR A 282     -12.503  13.987  23.181  1.00 67.28           N  
ATOM   2457  CA  THR A 282     -11.873  13.452  24.388  1.00 67.25           C  
ATOM   2458  C   THR A 282     -10.877  14.444  25.053  1.00 71.66           C  
ATOM   2459  O   THR A 282     -10.577  14.298  26.245  1.00 72.73           O  
ATOM   2460  CB  THR A 282     -11.248  12.076  24.121  1.00 75.73           C  
ATOM   2461  OG1 THR A 282     -10.293  12.171  23.067  1.00 76.49           O  
ATOM   2462  CG2 THR A 282     -12.285  11.007  23.803  1.00 72.71           C  
ATOM   2463  N   GLU A 283     -10.383  15.441  24.307  1.00 67.25           N  
ATOM   2464  CA  GLU A 283      -9.507  16.482  24.865  1.00 66.82           C  
ATOM   2465  C   GLU A 283     -10.394  17.575  25.496  1.00 70.34           C  
ATOM   2466  O   GLU A 283      -9.937  18.316  26.371  1.00 69.14           O  
ATOM   2467  CB  GLU A 283      -8.579  17.081  23.789  1.00 67.83           C  
ATOM   2468  CG  GLU A 283      -7.294  17.666  24.354  1.00 73.01           C  
ATOM   2469  CD  GLU A 283      -6.508  18.564  23.416  1.00 85.76           C  
ATOM   2470  OE1 GLU A 283      -6.137  19.678  23.849  1.00 68.82           O  
ATOM   2471  OE2 GLU A 283      -6.237  18.148  22.264  1.00 75.76           O  
ATOM   2472  N   THR A 284     -11.663  17.668  25.032  1.00 67.58           N  
ATOM   2473  CA  THR A 284     -12.692  18.581  25.541  1.00 67.66           C  
ATOM   2474  C   THR A 284     -13.172  18.063  26.913  1.00 72.14           C  
ATOM   2475  O   THR A 284     -13.394  18.865  27.823  1.00 71.53           O  
ATOM   2476  CB  THR A 284     -13.818  18.751  24.507  1.00 73.58           C  
ATOM   2477  OG1 THR A 284     -13.260  19.326  23.323  1.00 75.02           O  
ATOM   2478  CG2 THR A 284     -14.945  19.637  25.004  1.00 71.12           C  
ATOM   2479  N   LEU A 285     -13.290  16.722  27.058  1.00 69.03           N  
ATOM   2480  CA  LEU A 285     -13.681  16.041  28.297  1.00 69.04           C  
ATOM   2481  C   LEU A 285     -12.565  16.187  29.340  1.00 73.89           C  
ATOM   2482  O   LEU A 285     -12.857  16.559  30.476  1.00 74.26           O  
ATOM   2483  CB  LEU A 285     -14.016  14.551  28.032  1.00 68.88           C  
ATOM   2484  CG  LEU A 285     -14.395  13.654  29.233  1.00 72.87           C  
ATOM   2485  CD1 LEU A 285     -15.811  13.909  29.691  1.00 72.46           C  
ATOM   2486  CD2 LEU A 285     -14.268  12.190  28.872  1.00 75.38           C  
ATOM   2487  N   GLY A 286     -11.316  15.924  28.934  1.00 69.85           N  
ATOM   2488  CA  GLY A 286     -10.132  16.054  29.775  1.00 69.55           C  
ATOM   2489  C   GLY A 286      -9.961  17.451  30.334  1.00 74.31           C  
ATOM   2490  O   GLY A 286      -9.588  17.617  31.494  1.00 73.69           O  
ATOM   2491  N   MET A 287     -10.244  18.464  29.512  1.00 72.69           N  
ATOM   2492  CA  MET A 287     -10.177  19.873  29.893  1.00 73.22           C  
ATOM   2493  C   MET A 287     -11.197  20.190  31.005  1.00 77.41           C  
ATOM   2494  O   MET A 287     -10.863  20.917  31.938  1.00 76.93           O  
ATOM   2495  CB  MET A 287     -10.416  20.753  28.661  1.00 75.86           C  
ATOM   2496  CG  MET A 287     -10.504  22.219  28.976  1.00 80.42           C  
ATOM   2497  SD  MET A 287     -11.883  23.021  28.127  1.00 85.77           S  
ATOM   2498  CE  MET A 287     -13.290  22.365  29.023  1.00 82.25           C  
ATOM   2499  N   THR A 288     -12.423  19.611  30.910  1.00 73.79           N  
ATOM   2500  CA  THR A 288     -13.540  19.771  31.851  1.00 73.06           C  
ATOM   2501  C   THR A 288     -13.152  19.350  33.270  1.00 76.08           C  
ATOM   2502  O   THR A 288     -13.720  19.875  34.224  1.00 76.23           O  
ATOM   2503  CB  THR A 288     -14.772  18.994  31.342  1.00 83.27           C  
ATOM   2504  OG1 THR A 288     -14.994  19.315  29.974  1.00 82.30           O  
ATOM   2505  CG2 THR A 288     -16.048  19.290  32.133  1.00 85.67           C  
ATOM   2506  N   HIS A 289     -12.173  18.425  33.409  1.00 70.70           N  
ATOM   2507  CA  HIS A 289     -11.717  17.891  34.688  1.00 69.65           C  
ATOM   2508  C   HIS A 289     -11.165  18.947  35.649  1.00 74.45           C  
ATOM   2509  O   HIS A 289     -11.240  18.737  36.856  1.00 75.39           O  
ATOM   2510  CB  HIS A 289     -10.713  16.764  34.457  1.00 70.06           C  
ATOM   2511  CG  HIS A 289     -10.130  16.185  35.702  1.00 73.36           C  
ATOM   2512  ND1 HIS A 289      -8.875  16.559  36.150  1.00 75.04           N  
ATOM   2513  CD2 HIS A 289     -10.647  15.276  36.557  1.00 75.13           C  
ATOM   2514  CE1 HIS A 289      -8.666  15.862  37.253  1.00 74.54           C  
ATOM   2515  NE2 HIS A 289      -9.708  15.085  37.546  1.00 74.95           N  
ATOM   2516  N   CYS A 290     -10.660  20.086  35.143  1.00 70.98           N  
ATOM   2517  CA  CYS A 290     -10.094  21.152  35.986  1.00 71.13           C  
ATOM   2518  C   CYS A 290     -11.139  21.819  36.935  1.00 75.89           C  
ATOM   2519  O   CYS A 290     -10.751  22.432  37.929  1.00 75.80           O  
ATOM   2520  CB  CYS A 290      -9.347  22.184  35.141  1.00 71.18           C  
ATOM   2521  SG  CYS A 290     -10.400  23.087  33.978  1.00 74.78           S  
ATOM   2522  N   CYS A 291     -12.446  21.655  36.648  1.00 72.60           N  
ATOM   2523  CA  CYS A 291     -13.576  22.171  37.436  1.00 72.01           C  
ATOM   2524  C   CYS A 291     -14.236  21.075  38.313  1.00 76.52           C  
ATOM   2525  O   CYS A 291     -15.107  21.381  39.134  1.00 77.57           O  
ATOM   2526  CB  CYS A 291     -14.597  22.851  36.520  1.00 71.91           C  
ATOM   2527  SG  CYS A 291     -15.796  21.727  35.750  1.00 75.71           S  
ATOM   2528  N   ILE A 292     -13.812  19.809  38.127  1.00 71.70           N  
ATOM   2529  CA  ILE A 292     -14.339  18.613  38.795  1.00 70.89           C  
ATOM   2530  C   ILE A 292     -13.756  18.398  40.211  1.00 74.38           C  
ATOM   2531  O   ILE A 292     -14.508  17.999  41.109  1.00 73.94           O  
ATOM   2532  CB  ILE A 292     -14.165  17.366  37.861  1.00 73.38           C  
ATOM   2533  CG1 ILE A 292     -15.165  17.388  36.660  1.00 72.90           C  
ATOM   2534  CG2 ILE A 292     -14.195  16.022  38.598  1.00 74.33           C  
ATOM   2535  CD1 ILE A 292     -16.707  17.262  36.959  1.00 76.11           C  
ATOM   2536  N   ASN A 293     -12.441  18.661  40.408  1.00 70.01           N  
ATOM   2537  CA  ASN A 293     -11.739  18.469  41.685  1.00 69.29           C  
ATOM   2538  C   ASN A 293     -12.434  19.136  42.916  1.00 73.20           C  
ATOM   2539  O   ASN A 293     -12.533  18.455  43.941  1.00 72.38           O  
ATOM   2540  CB  ASN A 293     -10.271  18.867  41.580  1.00 68.32           C  
ATOM   2541  CG  ASN A 293      -9.353  17.711  41.231  1.00 90.73           C  
ATOM   2542  OD1 ASN A 293      -9.731  16.528  41.267  1.00 83.54           O  
ATOM   2543  ND2 ASN A 293      -8.104  18.027  40.924  1.00 84.18           N  
ATOM   2544  N   PRO A 294     -12.987  20.381  42.864  1.00 70.21           N  
ATOM   2545  CA  PRO A 294     -13.681  20.915  44.052  1.00 69.86           C  
ATOM   2546  C   PRO A 294     -14.914  20.097  44.452  1.00 72.65           C  
ATOM   2547  O   PRO A 294     -15.108  19.881  45.644  1.00 71.69           O  
ATOM   2548  CB  PRO A 294     -14.042  22.345  43.642  1.00 71.83           C  
ATOM   2549  CG  PRO A 294     -13.131  22.656  42.509  1.00 76.52           C  
ATOM   2550  CD  PRO A 294     -12.993  21.380  41.776  1.00 72.05           C  
ATOM   2551  N   ILE A 295     -15.705  19.594  43.471  1.00 69.84           N  
ATOM   2552  CA  ILE A 295     -16.885  18.742  43.704  1.00 70.27           C  
ATOM   2553  C   ILE A 295     -16.529  17.484  44.528  1.00 78.22           C  
ATOM   2554  O   ILE A 295     -17.301  17.101  45.402  1.00 78.98           O  
ATOM   2555  CB  ILE A 295     -17.617  18.371  42.392  1.00 72.87           C  
ATOM   2556  CG1 ILE A 295     -17.896  19.600  41.513  1.00 73.22           C  
ATOM   2557  CG2 ILE A 295     -18.895  17.563  42.653  1.00 72.88           C  
ATOM   2558  CD1 ILE A 295     -18.054  19.226  40.030  1.00 83.70           C  
ATOM   2559  N   ILE A 296     -15.367  16.855  44.264  1.00 76.77           N  
ATOM   2560  CA  ILE A 296     -14.890  15.673  45.004  1.00 77.28           C  
ATOM   2561  C   ILE A 296     -14.641  16.054  46.486  1.00 82.80           C  
ATOM   2562  O   ILE A 296     -15.053  15.303  47.370  1.00 81.65           O  
ATOM   2563  CB  ILE A 296     -13.642  15.001  44.330  1.00 80.17           C  
ATOM   2564  CG1 ILE A 296     -13.898  14.664  42.850  1.00 80.54           C  
ATOM   2565  CG2 ILE A 296     -13.173  13.755  45.093  1.00 80.26           C  
ATOM   2566  CD1 ILE A 296     -12.631  14.635  41.975  1.00 88.59           C  
ATOM   2567  N   TYR A 297     -14.003  17.225  46.747  1.00 81.72           N  
ATOM   2568  CA  TYR A 297     -13.721  17.707  48.111  1.00 82.87           C  
ATOM   2569  C   TYR A 297     -15.016  17.978  48.872  1.00 89.40           C  
ATOM   2570  O   TYR A 297     -15.100  17.662  50.058  1.00 89.51           O  
ATOM   2571  CB  TYR A 297     -12.862  18.995  48.129  1.00 84.12           C  
ATOM   2572  CG  TYR A 297     -11.524  18.976  47.412  1.00 86.94           C  
ATOM   2573  CD1 TYR A 297     -10.796  17.798  47.271  1.00 89.79           C  
ATOM   2574  CD2 TYR A 297     -10.947  20.155  46.951  1.00 87.60           C  
ATOM   2575  CE1 TYR A 297      -9.556  17.784  46.626  1.00 91.63           C  
ATOM   2576  CE2 TYR A 297      -9.705  20.156  46.317  1.00 88.56           C  
ATOM   2577  CZ  TYR A 297      -9.009  18.973  46.162  1.00 96.92           C  
ATOM   2578  OH  TYR A 297      -7.792  18.999  45.519  1.00 96.65           O  
ATOM   2579  N   ALA A 298     -16.017  18.560  48.185  1.00 87.42           N  
ATOM   2580  CA  ALA A 298     -17.331  18.909  48.726  1.00 87.92           C  
ATOM   2581  C   ALA A 298     -18.142  17.697  49.184  1.00 94.45           C  
ATOM   2582  O   ALA A 298     -18.957  17.830  50.096  1.00 93.91           O  
ATOM   2583  CB  ALA A 298     -18.120  19.693  47.690  1.00 88.51           C  
ATOM   2584  N   PHE A 299     -17.916  16.525  48.558  1.00 93.50           N  
ATOM   2585  CA  PHE A 299     -18.645  15.280  48.826  1.00 94.40           C  
ATOM   2586  C   PHE A 299     -17.873  14.245  49.638  1.00101.10           C  
ATOM   2587  O   PHE A 299     -18.406  13.731  50.623  1.00100.53           O  
ATOM   2588  CB  PHE A 299     -19.133  14.667  47.505  1.00 96.17           C  
ATOM   2589  CG  PHE A 299     -20.357  15.332  46.930  1.00 98.05           C  
ATOM   2590  CD1 PHE A 299     -20.306  16.643  46.470  1.00101.17           C  
ATOM   2591  CD2 PHE A 299     -21.554  14.637  46.820  1.00101.16           C  
ATOM   2592  CE1 PHE A 299     -21.442  17.261  45.949  1.00102.51           C  
ATOM   2593  CE2 PHE A 299     -22.691  15.254  46.286  1.00104.33           C  
ATOM   2594  CZ  PHE A 299     -22.627  16.562  45.851  1.00102.29           C  
ATOM   2595  N   VAL A 300     -16.637  13.919  49.217  1.00100.04           N  
ATOM   2596  CA  VAL A 300     -15.800  12.915  49.879  1.00100.80           C  
ATOM   2597  C   VAL A 300     -15.243  13.464  51.199  1.00106.39           C  
ATOM   2598  O   VAL A 300     -15.460  12.861  52.251  1.00106.04           O  
ATOM   2599  CB  VAL A 300     -14.702  12.314  48.947  1.00104.86           C  
ATOM   2600  CG1 VAL A 300     -14.023  11.107  49.594  1.00104.75           C  
ATOM   2601  CG2 VAL A 300     -15.279  11.922  47.591  1.00104.70           C  
ATOM   2602  N   GLY A 301     -14.567  14.608  51.131  1.00104.46           N  
ATOM   2603  CA  GLY A 301     -13.984  15.259  52.296  1.00105.17           C  
ATOM   2604  C   GLY A 301     -15.035  15.847  53.212  1.00111.13           C  
ATOM   2605  O   GLY A 301     -15.822  16.699  52.788  1.00110.83           O  
ATOM   2606  N   GLU A 302     -15.071  15.371  54.468  1.00109.07           N  
ATOM   2607  CA  GLU A 302     -16.024  15.852  55.471  1.00109.41           C  
ATOM   2608  C   GLU A 302     -15.654  17.264  55.964  1.00113.72           C  
ATOM   2609  O   GLU A 302     -16.542  18.026  56.347  1.00113.24           O  
ATOM   2610  CB  GLU A 302     -16.110  14.866  56.649  1.00110.92           C  
ATOM   2611  CG  GLU A 302     -17.429  14.929  57.405  1.00123.10           C  
ATOM   2612  CD  GLU A 302     -17.485  14.100  58.673  1.00143.20           C  
ATOM   2613  OE1 GLU A 302     -16.921  14.541  59.701  1.00129.71           O  
ATOM   2614  OE2 GLU A 302     -18.115  13.017  58.644  1.00138.62           O  
ATOM   2615  N   GLU A 303     -14.342  17.605  55.931  1.00110.56           N  
ATOM   2616  CA  GLU A 303     -13.745  18.883  56.364  1.00110.37           C  
ATOM   2617  C   GLU A 303     -14.332  20.086  55.612  1.00114.53           C  
ATOM   2618  O   GLU A 303     -14.640  21.102  56.240  1.00114.21           O  
ATOM   2619  CB  GLU A 303     -12.203  18.876  56.220  1.00111.68           C  
ATOM   2620  CG  GLU A 303     -11.490  17.613  56.695  1.00122.18           C  
ATOM   2621  CD  GLU A 303     -11.457  16.428  55.739  1.00142.87           C  
ATOM   2622  OE1 GLU A 303     -11.650  16.633  54.517  1.00144.26           O  
ATOM   2623  OE2 GLU A 303     -11.237  15.293  56.216  1.00130.66           O  
ATOM   2624  N   PHE A 304     -14.478  19.962  54.271  1.00111.03           N  
ATOM   2625  CA  PHE A 304     -15.020  20.996  53.380  1.00110.61           C  
ATOM   2626  C   PHE A 304     -16.490  21.292  53.690  1.00113.47           C  
ATOM   2627  O   PHE A 304     -16.924  22.442  53.582  1.00112.15           O  
ATOM   2628  CB  PHE A 304     -14.843  20.591  51.906  1.00112.38           C  
ATOM   2629  N   ARG A 305     -17.242  20.246  54.094  1.00110.29           N  
ATOM   2630  CA  ARG A 305     -18.654  20.323  54.477  1.00110.16           C  
ATOM   2631  C   ARG A 305     -18.815  21.106  55.789  1.00113.48           C  
ATOM   2632  O   ARG A 305     -19.778  21.861  55.941  1.00112.56           O  
ATOM   2633  CB  ARG A 305     -19.263  18.914  54.603  1.00110.61           C  
ATOM   2634  CG  ARG A 305     -19.472  18.215  53.273  1.00121.77           C  
ATOM   2635  CD  ARG A 305     -20.389  17.016  53.395  1.00134.52           C  
ATOM   2636  NE  ARG A 305     -19.646  15.756  53.432  1.00148.88           N  
ATOM   2637  CZ  ARG A 305     -20.192  14.555  53.253  1.00167.35           C  
ATOM   2638  NH1 ARG A 305     -21.495  14.439  53.018  1.00156.36           N  
ATOM   2639  NH2 ARG A 305     -19.442  13.462  53.301  1.00155.28           N  
ATOM   2640  N   ASN A 306     -17.853  20.935  56.717  1.00110.01           N  
ATOM   2641  CA  ASN A 306     -17.821  21.588  58.026  1.00109.55           C  
ATOM   2642  C   ASN A 306     -17.649  23.106  57.922  1.00113.09           C  
ATOM   2643  O   ASN A 306     -18.132  23.824  58.798  1.00112.86           O  
ATOM   2644  CB  ASN A 306     -16.742  20.961  58.927  1.00110.14           C  
ATOM   2645  CG  ASN A 306     -16.886  19.465  59.160  1.00131.21           C  
ATOM   2646  OD1 ASN A 306     -15.909  18.715  59.122  1.00122.58           O  
ATOM   2647  ND2 ASN A 306     -18.102  18.989  59.416  1.00123.69           N  
ATOM   2648  N   TYR A 307     -16.995  23.594  56.841  1.00109.28           N  
ATOM   2649  CA  TYR A 307     -16.778  25.023  56.576  1.00108.93           C  
ATOM   2650  C   TYR A 307     -18.101  25.764  56.336  1.00113.09           C  
ATOM   2651  O   TYR A 307     -18.240  26.919  56.743  1.00112.85           O  
ATOM   2652  CB  TYR A 307     -15.823  25.218  55.387  1.00109.92           C  
ATOM   2653  N   LEU A 308     -19.074  25.087  55.697  1.00109.57           N  
ATOM   2654  CA  LEU A 308     -20.402  25.628  55.411  1.00132.00           C  
ATOM   2655  C   LEU A 308     -21.336  25.347  56.585  1.00129.93           C  
ATOM   2656  O   LEU A 308     -22.030  26.245  57.053  1.00 76.13           O  
ATOM   2657  CB  LEU A 308     -20.962  25.008  54.124  1.00132.07           C  
TER    2658      LEU A 308                                                      
HETATM 2659 ZN    ZN A2001     -15.477 -17.145  71.423  1.00 88.81          ZN2+
HETATM 2660  C24 OLC A2002     -11.595   4.250  20.191  1.00102.79           C  
HETATM 2661  C5  OLC A2002     -12.803   4.821  29.553  1.00106.24           C  
HETATM 2662  C4  OLC A2002     -11.825   4.617  28.390  1.00106.36           C  
HETATM 2663  C3  OLC A2002     -12.608   4.610  27.078  1.00106.14           C  
HETATM 2664  C2  OLC A2002     -11.822   3.841  26.013  1.00106.18           C  
HETATM 2665  C21 OLC A2002     -11.997   4.092  22.658  1.00104.38           C  
HETATM 2666  C1  OLC A2002     -11.496   4.781  24.843  1.00106.31           C  
HETATM 2667  C22 OLC A2002     -11.896   5.043  21.469  1.00103.95           C  
HETATM 2668  O19 OLC A2002     -10.483   5.478  24.871  1.00107.10           O  
HETATM 2669  O25 OLC A2002     -11.703   5.104  19.042  1.00102.02           O  
HETATM 2670  O23 OLC A2002     -13.123   5.755  21.319  1.00105.13           O  
HETATM 2671  O20 OLC A2002     -12.418   4.814  23.830  1.00105.27           O  
HETATM 2672  C4  A4X A2003      -8.778  22.804  22.891  1.00 57.74           C  
HETATM 2673  C14 A4X A2003      -7.859  24.995  20.209  1.00 58.52           C  
HETATM 2674  C5  A4X A2003      -5.722  22.043  21.310  1.00 54.90           C  
HETATM 2675  C6  A4X A2003      -5.588  23.288  23.664  1.00 58.72           C  
HETATM 2676  C11 A4X A2003      -8.683  21.824  24.067  1.00 56.27           C  
HETATM 2677  C7  A4X A2003      -8.438  24.100  21.314  1.00 58.96           C  
HETATM 2678  C8  A4X A2003      -3.310  22.918  21.404  1.00 60.51           C  
HETATM 2679  C9  A4X A2003      -3.188  23.573  22.804  1.00 60.32           C  
HETATM 2680  C10 A4X A2003      -2.872  20.582  23.399  1.00 55.73           C  
HETATM 2681  C12 A4X A2003      -2.909  19.173  22.820  1.00 54.50           C  
HETATM 2682  C13 A4X A2003      -1.768  18.399  23.462  1.00 59.99           C  
HETATM 2683  N1  A4X A2003      -7.777  23.334  22.182  1.00 58.69           N  
HETATM 2684  N2  A4X A2003      -4.072  21.382  23.045  1.00 59.26           N  
HETATM 2685  C3  A4X A2003      -4.116  22.722  23.678  1.00 59.98           C  
HETATM 2686  N3  A4X A2003      -9.931  23.275  22.425  1.00 58.78           N  
HETATM 2687  C21 A4X A2003      -1.067  16.189  19.590  1.00 67.28           C  
HETATM 2688  C23 A4X A2003      -0.941  14.948  18.687  1.00 68.09           C  
HETATM 2689  C18 A4X A2003       0.541  14.612  18.409  1.00 69.58           C  
HETATM 2690  F1  A4X A2003       1.108  15.621  17.646  1.00 72.50           F  
HETATM 2691  F2  A4X A2003       0.579  13.466  17.710  1.00 69.26           F  
HETATM 2692  C24 A4X A2003       1.327  14.409  19.733  1.00 68.20           C  
HETATM 2693  C22 A4X A2003       1.212  15.652  20.640  1.00 67.25           C  
HETATM 2694  C17 A4X A2003      -0.273  16.007  20.905  1.00 67.56           C  
HETATM 2695  C16 A4X A2003      -0.399  17.296  21.722  1.00 68.01           C  
HETATM 2696  O1  A4X A2003       0.331  18.272  21.502  1.00 71.15           O  
HETATM 2697  N5  A4X A2003      -1.404  17.263  22.615  1.00 63.76           N  
HETATM 2698  C15 A4X A2003      -2.102  17.962  24.899  1.00 61.88           C  
HETATM 2699  C25 A4X A2003      -1.151  17.933  25.847  1.00 61.15           C  
HETATM 2700  C27 A4X A2003      -1.585  17.578  27.052  1.00 63.79           C  
HETATM 2701  S1  A4X A2003      -3.222  17.297  26.874  1.00 67.37           S  
HETATM 2702  C26 A4X A2003      -3.339  17.630  25.294  1.00 64.08           C  
HETATM 2703  C2  A4X A2003      -4.242  21.706  21.609  1.00 57.59           C  
HETATM 2704  C1  A4X A2003      -6.264  23.175  22.235  1.00 57.18           C  
HETATM 2705  N4  A4X A2003      -9.740  24.002  21.547  1.00 60.26           N  
HETATM 2706  C20 A4X A2003      -8.983  22.542  25.390  1.00 55.41           C  
HETATM 2707  C19 A4X A2003      -9.643  20.654  23.852  1.00 56.98           C  
CONECT    6 2364                                                                
CONECT  648 1251                                                                
CONECT 1251  648                                                                
CONECT 1661 2659                                                                
CONECT 1681 2659                                                                
CONECT 1911 2659                                                                
CONECT 1932 2659                                                                
CONECT 2364    6                                                                
CONECT 2659 1661 1681 1911 1932                                                 
CONECT 2660 2667 2669                                                           
CONECT 2661 2662                                                                
CONECT 2662 2661 2663                                                           
CONECT 2663 2662 2664                                                           
CONECT 2664 2663 2666                                                           
CONECT 2665 2667 2671                                                           
CONECT 2666 2664 2668 2671                                                      
CONECT 2667 2660 2665 2670                                                      
CONECT 2668 2666                                                                
CONECT 2669 2660                                                                
CONECT 2670 2667                                                                
CONECT 2671 2665 2666                                                           
CONECT 2672 2676 2683 2686                                                      
CONECT 2673 2677                                                                
CONECT 2674 2703 2704                                                           
CONECT 2675 2685 2704                                                           
CONECT 2676 2672 2706 2707                                                      
CONECT 2677 2673 2683 2705                                                      
CONECT 2678 2679 2703                                                           
CONECT 2679 2678 2685                                                           
CONECT 2680 2681 2684                                                           
CONECT 2681 2680 2682                                                           
CONECT 2682 2681 2697 2698                                                      
CONECT 2683 2672 2677 2704                                                      
CONECT 2684 2680 2685 2703                                                      
CONECT 2685 2675 2679 2684                                                      
CONECT 2686 2672 2705                                                           
CONECT 2687 2688 2694                                                           
CONECT 2688 2687 2689                                                           
CONECT 2689 2688 2690 2691 2692                                                 
CONECT 2690 2689                                                                
CONECT 2691 2689                                                                
CONECT 2692 2689 2693                                                           
CONECT 2693 2692 2694                                                           
CONECT 2694 2687 2693 2695                                                      
CONECT 2695 2694 2696 2697                                                      
CONECT 2696 2695                                                                
CONECT 2697 2682 2695                                                           
CONECT 2698 2682 2699 2702                                                      
CONECT 2699 2698 2700                                                           
CONECT 2700 2699 2701                                                           
CONECT 2701 2700 2702                                                           
CONECT 2702 2698 2701                                                           
CONECT 2703 2674 2678 2684                                                      
CONECT 2704 2674 2675 2683                                                      
CONECT 2705 2677 2686                                                           
CONECT 2706 2676                                                                
CONECT 2707 2676                                                                
MASTER      348    0    3   13    5    0    5    6 2706    1   57   30          
END