HEADER    ELECTRON TRANSPORT                      19-MAR-90   2TRX              
TITLE     CRYSTAL STRUCTURE OF THIOREDOXIN FROM ESCHERICHIA COLI AT 1.68        
TITLE    2 ANGSTROMS RESOLUTION                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THIOREDOXIN;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562                                                  
KEYWDS    ELECTRON TRANSPORT                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.K.KATTI,D.M.LEMASTER,H.EKLUND                                       
REVDAT   6   29-NOV-17 2TRX    1       HELIX                                    
REVDAT   5   13-JUL-11 2TRX    1       VERSN                                    
REVDAT   4   24-FEB-09 2TRX    1       VERSN                                    
REVDAT   3   01-APR-03 2TRX    1       JRNL                                     
REVDAT   2   15-JAN-93 2TRX    1       HEADER COMPND                            
REVDAT   1   15-OCT-91 2TRX    0                                                
JRNL        AUTH   S.K.KATTI,D.M.LEMASTER,H.EKLUND                              
JRNL        TITL   CRYSTAL STRUCTURE OF THIOREDOXIN FROM ESCHERICHIA COLI AT    
JRNL        TITL 2 1.68 A RESOLUTION.                                           
JRNL        REF    J.MOL.BIOL.                   V. 212   167 1990              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   2181145                                                      
JRNL        DOI    10.1016/0022-2836(90)90313-B                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.HOLMGREN,B.-O.SODERBERG,H.EKLUND,C.-I.BRANDEN              
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI              
REMARK   1  TITL 2 THIOREDOXIN-S2 TO 2.8 ANGSTROMS RESOLUTION                   
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  72  2305 1975              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   B.-O.SODERBERG,A.HOLMGREN,C.-I.BRANDEN                       
REMARK   1  TITL   STRUCTURE OF OXIDIZED THIOREDOXIN TO 4.5 ANGSTROMS           
REMARK   1  TITL 2 RESOLUTION                                                   
REMARK   1  REF    J.MOL.BIOL.                   V.  90   143 1974              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   A.HOLMGREN,B.-O.SODERBERG                                    
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC DATA FOR    
REMARK   1  TITL 2 THIOREDOXIN FROM ESCHERICHIA COLI B                          
REMARK   1  REF    J.MOL.BIOL.                   V.  54   387 1970              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.68 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROFFT                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON,FINZEL                           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.68                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 25969                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1644                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 140                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.015 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.035 ; 0.030               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.055 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.021 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.131 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.165 ; 0.500               
REMARK   3    MULTIPLE TORSION                (A) : 0.174 ; 0.500               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.180 ; 0.500               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 4.000 ; 3.000               
REMARK   3    STAGGERED                 (DEGREES) : 16.300; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 1.380 ; 1.000               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 2.280 ; 1.000               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 1.970 ; 1.000               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 3.270 ; 1.500               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2TRX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000178704.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
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       44.75000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.53000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       44.75000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       25.53000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 3680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       89.50000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       65.39562            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       55.43628            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  13   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A  47   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    TYR A  70   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG A  73   NE  -  CZ  -  NH1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ARG A  73   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    GLU A  85   OE1 -  CD  -  OE2 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    GLU A 101   OE1 -  CD  -  OE2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    PHE B  12   CB  -  CA  -  C   ANGL. DEV. =  15.5 DEGREES          
REMARK 500    ASP B  20   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    GLU B  85   CA  -  CB  -  CG  ANGL. DEV. =  13.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP B  13       20.75    144.15                                   
REMARK 500    THR B  14      -88.88   -162.21                                   
REMARK 500    VAL B  16      -40.16   -132.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              CU A 109  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A   1   N                                                      
REMARK 620 2 ASP A   2   N    86.5                                              
REMARK 620 3 ASP A   2   OD1 172.6  86.0                                        
REMARK 620 4 HOH A 405   O    89.2  92.0  91.5                                  
REMARK 620 5 ASP A  10   OD1  96.3 174.7  91.1  92.5                            
REMARK 620 6 ASP A  10   OD2  98.6 120.4  84.8 146.9  54.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 109  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B   2   N                                                      
REMARK 620 2 HOH B 478   O    88.9                                              
REMARK 620 3 ASP B   2   OD1  89.5  87.8                                        
REMARK 620 4 SER B   1   N    86.9  87.8 174.4                                  
REMARK 620 5 ASP B  10   OD1 172.0  97.4  85.7  98.3                            
REMARK 620 6 ASP B  10   OD2 117.6 151.2  81.6 103.9  55.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 109                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 109                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 607                 
DBREF  2TRX A    1   108  UNP    P0AA25   THIO_ECOLI       1    108             
DBREF  2TRX B    1   108  UNP    P0AA25   THIO_ECOLI       1    108             
SEQRES   1 A  108  SER ASP LYS ILE ILE HIS LEU THR ASP ASP SER PHE ASP          
SEQRES   2 A  108  THR ASP VAL LEU LYS ALA ASP GLY ALA ILE LEU VAL ASP          
SEQRES   3 A  108  PHE TRP ALA GLU TRP CYS GLY PRO CYS LYS MET ILE ALA          
SEQRES   4 A  108  PRO ILE LEU ASP GLU ILE ALA ASP GLU TYR GLN GLY LYS          
SEQRES   5 A  108  LEU THR VAL ALA LYS LEU ASN ILE ASP GLN ASN PRO GLY          
SEQRES   6 A  108  THR ALA PRO LYS TYR GLY ILE ARG GLY ILE PRO THR LEU          
SEQRES   7 A  108  LEU LEU PHE LYS ASN GLY GLU VAL ALA ALA THR LYS VAL          
SEQRES   8 A  108  GLY ALA LEU SER LYS GLY GLN LEU LYS GLU PHE LEU ASP          
SEQRES   9 A  108  ALA ASN LEU ALA                                              
SEQRES   1 B  108  SER ASP LYS ILE ILE HIS LEU THR ASP ASP SER PHE ASP          
SEQRES   2 B  108  THR ASP VAL LEU LYS ALA ASP GLY ALA ILE LEU VAL ASP          
SEQRES   3 B  108  PHE TRP ALA GLU TRP CYS GLY PRO CYS LYS MET ILE ALA          
SEQRES   4 B  108  PRO ILE LEU ASP GLU ILE ALA ASP GLU TYR GLN GLY LYS          
SEQRES   5 B  108  LEU THR VAL ALA LYS LEU ASN ILE ASP GLN ASN PRO GLY          
SEQRES   6 B  108  THR ALA PRO LYS TYR GLY ILE ARG GLY ILE PRO THR LEU          
SEQRES   7 B  108  LEU LEU PHE LYS ASN GLY GLU VAL ALA ALA THR LYS VAL          
SEQRES   8 B  108  GLY ALA LEU SER LYS GLY GLN LEU LYS GLU PHE LEU ASP          
SEQRES   9 B  108  ALA ASN LEU ALA                                              
HET     CU  A 109       1                                                       
HET    MPD  A 601       8                                                       
HET    MPD  A 605       8                                                       
HET    MPD  A 606       8                                                       
HET    MPD  A 607       8                                                       
HET     CU  B 109       1                                                       
HET    MPD  B 602       8                                                       
HET    MPD  B 603       8                                                       
HET    MPD  B 604       8                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
FORMUL   3   CU    2(CU 2+)                                                     
FORMUL   4  MPD    7(C6 H14 O2)                                                 
FORMUL  12  HOH   *140(H2 O)                                                    
HELIX    1 A1A SER A   11  LEU A   17  1DISORDERED IN MOLECULE B           7    
HELIX    2 A2A CYS A   32  TYR A   49  1BENT BY 30 DEGREES AT RES 39      18    
HELIX    3 A3A ASN A   59  ASN A   63  1                                   5    
HELIX    4 31A THR A   66  TYR A   70  5DISTORTED H-BONDING C-TERMINS      5    
HELIX    5 A4A SER A   95  LEU A  107  1                                  13    
HELIX    6 A1B SER B   11  LEU B   17  1DISORDERED IN MOLECULE B           7    
HELIX    7 A2B CYS B   32  TYR B   49  1BENT BY 30 DEGREES AT RES 39      18    
HELIX    8 A3B ASN B   59  ASN B   63  1                                   5    
HELIX    9 31B THR B   66  TYR B   70  5DISTORTED H-BONDING C-TERMINS      5    
HELIX   10 A4B SER B   95  LEU B  107  1                                  13    
SHEET    1 B1A 5 LYS A   3  THR A   8  0                                        
SHEET    2 B1A 5 LEU A  53  ASN A  59  1  O  VAL A  55   N  ILE A   5           
SHEET    3 B1A 5 GLY A  21  TRP A  28  1  N  TRP A  28   O  LEU A  58           
SHEET    4 B1A 5 PRO A  76  LYS A  82 -1  O  THR A  77   N  PHE A  27           
SHEET    5 B1A 5 VAL A  86  GLY A  92 -1  O  ALA A  87   N  LEU A  80           
SHEET    1 B1B 5 LYS B   3  THR B   8  0                                        
SHEET    2 B1B 5 LEU B  53  ASN B  59  1  O  VAL B  55   N  ILE B   5           
SHEET    3 B1B 5 GLY B  21  TRP B  28  1  N  TRP B  28   O  LEU B  58           
SHEET    4 B1B 5 PRO B  76  LYS B  82 -1  O  THR B  77   N  PHE B  27           
SHEET    5 B1B 5 VAL B  86  GLY B  92 -1  O  ALA B  87   N  LEU B  80           
SSBOND   1 CYS A   32    CYS A   35                          1555   1555  2.09  
SSBOND   2 CYS B   32    CYS B   35                          1555   1555  2.05  
LINK        CU    CU A 109                 N   SER A   1     1555   1555  2.05  
LINK        CU    CU A 109                 N   ASP A   2     1555   1555  2.06  
LINK        CU    CU A 109                 OD1 ASP A   2     1555   1555  2.00  
LINK        CU    CU A 109                 O   HOH A 405     1555   1555  2.65  
LINK        CU    CU B 109                 N   ASP B   2     1555   1555  2.05  
LINK        CU    CU B 109                 O   HOH B 478     1555   1555  2.63  
LINK        CU    CU B 109                 OD1 ASP B   2     1555   1555  2.06  
LINK        CU    CU B 109                 N   SER B   1     1555   1555  2.09  
LINK        CU    CU A 109                 OD1 ASP A  10     1555   4545  1.97  
LINK        CU    CU A 109                 OD2 ASP A  10     1555   4545  2.62  
LINK        CU    CU B 109                 OD1 ASP B  10     1555   4546  2.08  
LINK        CU    CU B 109                 OD2 ASP B  10     1555   4546  2.54  
CISPEP   1 ILE A   75    PRO A   76          0         0.60                     
CISPEP   2 ILE B   75    PRO B   76          0        -2.42                     
SITE     1 AC1  5 SER A   1  ASP A   2  LYS A   3  ASP A  10                    
SITE     2 AC1  5 HOH A 405                                                     
SITE     1 AC2  5 SER B   1  ASP B   2  LYS B   3  ASP B  10                    
SITE     2 AC2  5 HOH B 478                                                     
SITE     1 AC3  4 ASP A  10  ASP A  43  GLU A  44  HOH A 442                    
SITE     1 AC4  6 GLU A  44  HOH A 524  GLU B  30  TRP B  31                    
SITE     2 AC4  6 GLY B  33  LYS B  36                                          
SITE     1 AC5  5 TYR B  70  ILE B  72  THR B  77  THR B  89                    
SITE     2 AC5  5 VAL B  91                                                     
SITE     1 AC6  3 ILE B  60  ALA B  67  ILE B  72                               
SITE     1 AC7  4 MET A  37  ILE A  38  ALA A  93  LEU A  94                    
SITE     1 AC8  4 TYR A  70  GLY A  71  THR A  89  VAL A  91                    
SITE     1 AC9  8 ILE A  60  ALA A  67  ILE A  72  ARG A  73                    
SITE     2 AC9  8 GLY A  74  ILE A  75  HOH A 494  HOH B 528                    
CRYST1   89.500   51.060   60.450  90.00 113.50  90.00 C 1 2 1       8          
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      0.011173  0.000000  0.004858        0.00000                         
SCALE2      0.000000  0.019585  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018039        0.00000                         
ATOM      1  N   SER A   1      21.389  25.406  -4.628  1.00 23.22           N  
ATOM      2  CA  SER A   1      21.628  26.691  -3.983  1.00 24.42           C  
ATOM      3  C   SER A   1      20.937  26.944  -2.679  1.00 24.21           C  
ATOM      4  O   SER A   1      21.072  28.079  -2.093  1.00 24.97           O  
ATOM      5  CB  SER A   1      21.117  27.770  -5.002  1.00 28.27           C  
ATOM      6  OG  SER A   1      22.276  27.925  -5.861  1.00 32.61           O  
ATOM      7  N   ASP A   2      20.173  26.028  -2.163  1.00 21.39           N  
ATOM      8  CA  ASP A   2      19.395  26.125  -0.949  1.00 21.57           C  
ATOM      9  C   ASP A   2      20.264  26.214   0.297  1.00 20.89           C  
ATOM     10  O   ASP A   2      19.760  26.575   1.371  1.00 21.49           O  
ATOM     11  CB  ASP A   2      18.439  24.914  -0.856  1.00 22.14           C  
ATOM     12  CG  ASP A   2      19.199  23.629  -0.576  1.00 23.23           C  
ATOM     13  OD1 ASP A   2      20.107  23.371  -1.387  1.00 22.71           O  
ATOM     14  OD2 ASP A   2      18.905  22.959   0.420  1.00 23.61           O  
ATOM     15  N   LYS A   3      21.530  25.857   0.207  1.00 19.20           N  
ATOM     16  CA  LYS A   3      22.310  25.875   1.488  1.00 18.91           C  
ATOM     17  C   LYS A   3      23.353  26.982   1.459  1.00 18.43           C  
ATOM     18  O   LYS A   3      24.203  26.950   2.370  1.00 20.34           O  
ATOM     19  CB  LYS A   3      23.006  24.540   1.741  1.00 20.31           C  
ATOM     20  CG  LYS A   3      21.971  23.407   1.921  1.00 22.14           C  
ATOM     21  CD  LYS A   3      22.677  22.143   2.401  1.00 24.45           C  
ATOM     22  CE  LYS A   3      21.620  21.104   2.844  1.00 25.84           C  
ATOM     23  NZ  LYS A   3      20.830  20.757   1.615  1.00 25.55           N  
ATOM     24  N   ILE A   4      23.299  27.821   0.461  1.00 17.03           N  
ATOM     25  CA  ILE A   4      24.287  28.908   0.332  1.00 17.28           C  
ATOM     26  C   ILE A   4      23.779  30.213   0.927  1.00 17.70           C  
ATOM     27  O   ILE A   4      22.691  30.658   0.487  1.00 19.79           O  
ATOM     28  CB  ILE A   4      24.592  29.122  -1.211  1.00 19.04           C  
ATOM     29  CG1 ILE A   4      24.953  27.791  -1.886  1.00 19.62           C  
ATOM     30  CG2 ILE A   4      25.689  30.221  -1.338  1.00 19.70           C  
ATOM     31  CD1 ILE A   4      26.177  27.022  -1.384  1.00 21.32           C  
ATOM     32  N   ILE A   5      24.492  30.834   1.831  1.00 15.41           N  
ATOM     33  CA  ILE A   5      24.075  32.125   2.372  1.00 15.87           C  
ATOM     34  C  AILE A   5      24.236  33.234   1.335  0.50 15.03           C  
ATOM     35  C  BILE A   5      24.313  33.238   1.361  0.50 16.09           C  
ATOM     36  O  AILE A   5      25.272  33.309   0.663  0.50 13.96           O  
ATOM     37  O  BILE A   5      25.462  33.388   0.927  0.50 14.70           O  
ATOM     38  CB  ILE A   5      24.924  32.461   3.665  1.00 16.00           C  
ATOM     39  CG1 ILE A   5      24.887  31.389   4.747  1.00 18.03           C  
ATOM     40  CG2 ILE A   5      24.470  33.816   4.263  1.00 17.59           C  
ATOM     41  CD1 ILE A   5      23.522  30.765   5.027  1.00 20.49           C  
ATOM     42  N  AHIS A   6      23.224  34.086   1.266  0.50 14.20           N  
ATOM     43  N  BHIS A   6      23.274  34.014   1.074  0.50 16.67           N  
ATOM     44  CA AHIS A   6      23.209  35.260   0.397  0.50 14.45           C  
ATOM     45  CA BHIS A   6      23.503  35.160   0.168  0.50 17.84           C  
ATOM     46  C  AHIS A   6      23.812  36.444   1.141  0.50 14.31           C  
ATOM     47  C  BHIS A   6      23.912  36.330   1.048  0.50 16.77           C  
ATOM     48  O  AHIS A   6      23.166  36.915   2.118  0.50 15.33           O  
ATOM     49  O  BHIS A   6      23.254  36.640   2.072  0.50 17.88           O  
ATOM     50  CB AHIS A   6      21.751  35.617  -0.024  0.50 14.98           C  
ATOM     51  CB BHIS A   6      22.288  35.441  -0.746  0.50 21.08           C  
ATOM     52  CG AHIS A   6      21.706  36.884  -0.816  0.50 15.04           C  
ATOM     53  CG BHIS A   6      22.340  34.470  -1.906  0.50 24.32           C  
ATOM     54  ND1AHIS A   6      22.017  36.971  -2.134  0.50 16.10           N  
ATOM     55  ND1BHIS A   6      21.839  33.188  -1.917  0.50 25.17           N  
ATOM     56  CD2AHIS A   6      21.382  38.136  -0.410  0.50 16.04           C  
ATOM     57  CD2BHIS A   6      22.959  34.649  -3.112  0.50 24.89           C  
ATOM     58  CE1AHIS A   6      21.896  38.232  -2.528  0.50 15.49           C  
ATOM     59  CE1BHIS A   6      22.106  32.643  -3.097  0.50 25.92           C  
ATOM     60  NE2AHIS A   6      21.539  38.966  -1.497  0.50 15.68           N  
ATOM     61  NE2BHIS A   6      22.800  33.502  -3.827  0.50 26.06           N  
ATOM     62  N  ALEU A   7      24.994  36.916   0.777  0.50 12.47           N  
ATOM     63  N  BLEU A   7      25.049  36.926   0.732  0.50 13.88           N  
ATOM     64  CA  LEU A   7      25.574  38.061   1.494  1.00 12.40           C  
ATOM     65  C   LEU A   7      25.330  39.373   0.782  1.00 13.24           C  
ATOM     66  O   LEU A   7      25.161  39.412  -0.444  1.00 14.99           O  
ATOM     67  CB  LEU A   7      27.099  37.857   1.598  1.00 11.31           C  
ATOM     68  CG  LEU A   7      27.558  36.609   2.362  1.00 11.75           C  
ATOM     69  CD1 LEU A   7      29.082  36.516   2.268  1.00 12.20           C  
ATOM     70  CD2 LEU A   7      27.079  36.752   3.805  1.00 12.86           C  
ATOM     71  N   THR A   8      25.419  40.434   1.561  1.00 13.46           N  
ATOM     72  CA  THR A   8      25.457  41.807   1.037  1.00 14.06           C  
ATOM     73  C   THR A   8      26.594  42.530   1.702  1.00 13.52           C  
ATOM     74  O   THR A   8      27.142  42.063   2.682  1.00 12.78           O  
ATOM     75  CB  THR A   8      24.093  42.610   1.254  1.00 14.54           C  
ATOM     76  OG1 THR A   8      24.005  42.860   2.687  1.00 14.25           O  
ATOM     77  CG2 THR A   8      22.905  41.853   0.697  1.00 14.70           C  
ATOM     78  N   ASP A   9      26.892  43.714   1.150  1.00 14.17           N  
ATOM     79  CA  ASP A   9      27.926  44.559   1.745  1.00 15.20           C  
ATOM     80  C   ASP A   9      27.605  44.869   3.223  1.00 14.96           C  
ATOM     81  O   ASP A   9      28.482  44.846   4.093  1.00 14.69           O  
ATOM     82  CB  ASP A   9      28.201  45.815   0.929  1.00 17.36           C  
ATOM     83  CG  ASP A   9      29.028  45.578  -0.331  1.00 19.48           C  
ATOM     84  OD1 ASP A   9      28.836  46.359  -1.294  1.00 21.20           O  
ATOM     85  OD2 ASP A   9      29.843  44.606  -0.368  1.00 19.52           O  
ATOM     86  N   ASP A  10      26.354  45.192   3.500  1.00 14.77           N  
ATOM     87  CA  ASP A  10      25.970  45.537   4.868  1.00 15.43           C  
ATOM     88  C   ASP A  10      25.875  44.351   5.800  1.00 15.15           C  
ATOM     89  O   ASP A  10      26.087  44.573   7.016  1.00 17.24           O  
ATOM     90  CB  ASP A  10      24.603  46.236   4.902  1.00 15.60           C  
ATOM     91  CG  ASP A  10      24.631  47.626   4.316  1.00 17.69           C  
ATOM     92  OD1 ASP A  10      23.552  48.046   3.857  1.00 18.65           O  
ATOM     93  OD2 ASP A  10      25.688  48.266   4.284  1.00 17.68           O  
ATOM     94  N   SER A  11      25.599  43.185   5.285  1.00 14.29           N  
ATOM     95  CA  SER A  11      25.473  42.022   6.151  1.00 14.24           C  
ATOM     96  C   SER A  11      26.792  41.291   6.383  1.00 13.53           C  
ATOM     97  O   SER A  11      26.799  40.365   7.215  1.00 13.75           O  
ATOM     98  CB  SER A  11      24.415  41.069   5.651  1.00 14.74           C  
ATOM     99  OG  SER A  11      24.842  40.228   4.595  1.00 16.10           O  
ATOM    100  N   PHE A  12      27.829  41.695   5.688  1.00 13.49           N  
ATOM    101  CA  PHE A  12      29.099  40.933   5.759  1.00 13.10           C  
ATOM    102  C   PHE A  12      29.645  40.748   7.165  1.00 12.77           C  
ATOM    103  O   PHE A  12      30.072  39.616   7.530  1.00 12.54           O  
ATOM    104  CB  PHE A  12      30.098  41.557   4.781  1.00 13.34           C  
ATOM    105  CG  PHE A  12      31.198  40.585   4.370  1.00 14.53           C  
ATOM    106  CD1 PHE A  12      31.018  39.815   3.237  1.00 14.81           C  
ATOM    107  CD2 PHE A  12      32.361  40.512   5.103  1.00 15.14           C  
ATOM    108  CE1 PHE A  12      32.027  38.934   2.830  1.00 16.88           C  
ATOM    109  CE2 PHE A  12      33.396  39.631   4.718  1.00 15.90           C  
ATOM    110  CZ  PHE A  12      33.194  38.843   3.569  1.00 15.90           C  
ATOM    111  N   ASP A  13      29.678  41.854   7.928  1.00 12.51           N  
ATOM    112  CA  ASP A  13      30.284  41.748   9.265  1.00 15.59           C  
ATOM    113  C   ASP A  13      29.469  40.770  10.123  1.00 15.56           C  
ATOM    114  O   ASP A  13      30.025  39.861  10.738  1.00 15.68           O  
ATOM    115  CB  ASP A  13      30.347  43.160   9.875  1.00 19.09           C  
ATOM    116  CG  ASP A  13      30.724  43.120  11.344  1.00 24.45           C  
ATOM    117  OD1 ASP A  13      29.952  43.444  12.268  1.00 28.65           O  
ATOM    118  OD2 ASP A  13      31.876  42.704  11.618  1.00 27.06           O  
ATOM    119  N   THR A  14      28.183  40.973  10.177  1.00 14.97           N  
ATOM    120  CA  THR A  14      27.293  40.140  10.978  1.00 15.48           C  
ATOM    121  C   THR A  14      27.334  38.666  10.591  1.00 15.63           C  
ATOM    122  O   THR A  14      27.340  37.786  11.453  1.00 15.60           O  
ATOM    123  CB  THR A  14      25.790  40.636  10.866  1.00 15.81           C  
ATOM    124  OG1 THR A  14      25.759  42.020  11.288  1.00 17.67           O  
ATOM    125  CG2 THR A  14      24.779  39.741  11.614  1.00 16.68           C  
ATOM    126  N   ASP A  15      27.296  38.408   9.265  1.00 13.34           N  
ATOM    127  CA  ASP A  15      27.199  37.020   8.811  1.00 13.51           C  
ATOM    128  C   ASP A  15      28.523  36.287   8.697  1.00 13.42           C  
ATOM    129  O   ASP A  15      28.547  35.054   8.868  1.00 15.24           O  
ATOM    130  CB  ASP A  15      26.537  36.983   7.405  1.00 14.64           C  
ATOM    131  CG  ASP A  15      25.058  37.319   7.424  1.00 18.00           C  
ATOM    132  OD1 ASP A  15      24.557  37.630   6.322  1.00 20.58           O  
ATOM    133  OD2 ASP A  15      24.429  37.363   8.483  1.00 19.92           O  
ATOM    134  N   VAL A  16      29.566  36.993   8.398  1.00 11.68           N  
ATOM    135  CA  VAL A  16      30.879  36.363   8.141  1.00 11.15           C  
ATOM    136  C   VAL A  16      31.831  36.654   9.285  1.00 11.18           C  
ATOM    137  O   VAL A  16      32.400  35.661   9.800  1.00 11.31           O  
ATOM    138  CB  VAL A  16      31.447  36.826   6.782  1.00 11.48           C  
ATOM    139  CG1 VAL A  16      32.817  36.213   6.498  1.00 11.71           C  
ATOM    140  CG2 VAL A  16      30.481  36.479   5.629  1.00 12.46           C  
ATOM    141  N   LEU A  17      32.031  37.909   9.621  1.00 10.68           N  
ATOM    142  CA  LEU A  17      33.084  38.203  10.586  1.00 12.88           C  
ATOM    143  C   LEU A  17      32.761  37.703  11.989  1.00 13.68           C  
ATOM    144  O   LEU A  17      33.688  37.310  12.719  1.00 13.80           O  
ATOM    145  CB  LEU A  17      33.486  39.659  10.464  1.00 14.73           C  
ATOM    146  CG  LEU A  17      33.956  40.160   9.085  1.00 16.37           C  
ATOM    147  CD1 LEU A  17      34.544  41.569   9.307  1.00 17.08           C  
ATOM    148  CD2 LEU A  17      35.017  39.223   8.541  1.00 17.02           C  
ATOM    149  N   LYS A  18      31.486  37.640  12.298  1.00 13.46           N  
ATOM    150  CA  LYS A  18      31.081  37.133  13.628  1.00 14.85           C  
ATOM    151  C   LYS A  18      30.549  35.736  13.530  1.00 15.99           C  
ATOM    152  O   LYS A  18      29.879  35.275  14.472  1.00 16.78           O  
ATOM    153  CB  LYS A  18      30.038  38.137  14.184  1.00 17.08           C  
ATOM    154  CG  LYS A  18      30.836  39.352  14.640  1.00 19.68           C  
ATOM    155  CD  LYS A  18      30.337  40.702  14.460  1.00 23.81           C  
ATOM    156  CE  LYS A  18      31.259  41.802  14.961  1.00 24.60           C  
ATOM    157  NZ  LYS A  18      32.517  42.012  14.212  1.00 24.76           N  
ATOM    158  N   ALA A  19      30.851  35.020  12.422  1.00 15.05           N  
ATOM    159  CA  ALA A  19      30.364  33.655  12.255  1.00 15.02           C  
ATOM    160  C   ALA A  19      30.972  32.709  13.295  1.00 14.79           C  
ATOM    161  O   ALA A  19      32.090  32.873  13.739  1.00 14.02           O  
ATOM    162  CB  ALA A  19      30.724  33.065  10.875  1.00 15.30           C  
ATOM    163  N   ASP A  20      30.145  31.684  13.574  1.00 15.36           N  
ATOM    164  CA  ASP A  20      30.660  30.591  14.430  1.00 17.32           C  
ATOM    165  C   ASP A  20      31.286  29.548  13.504  1.00 19.00           C  
ATOM    166  O   ASP A  20      30.536  29.074  12.611  1.00 23.43           O  
ATOM    167  CB  ASP A  20      29.450  30.052  15.203  1.00 18.57           C  
ATOM    168  CG  ASP A  20      29.806  29.030  16.240  1.00 20.00           C  
ATOM    169  OD1 ASP A  20      28.915  28.243  16.643  1.00 21.68           O  
ATOM    170  OD2 ASP A  20      30.949  29.001  16.711  1.00 22.14           O  
ATOM    171  N   GLY A  21      32.511  29.171  13.557  1.00 19.06           N  
ATOM    172  CA  GLY A  21      32.919  28.079  12.606  1.00 18.13           C  
ATOM    173  C   GLY A  21      33.401  28.709  11.285  1.00 17.12           C  
ATOM    174  O   GLY A  21      33.314  29.904  11.008  1.00 18.02           O  
ATOM    175  N   ALA A  22      33.904  27.787  10.464  1.00 15.23           N  
ATOM    176  CA  ALA A  22      34.544  28.218   9.195  1.00 14.16           C  
ATOM    177  C   ALA A  22      33.486  28.594   8.194  1.00 12.92           C  
ATOM    178  O   ALA A  22      32.452  27.923   8.145  1.00 13.79           O  
ATOM    179  CB  ALA A  22      35.336  26.994   8.711  1.00 14.83           C  
ATOM    180  N   ILE A  23      33.736  29.626   7.426  1.00 12.08           N  
ATOM    181  CA  ILE A  23      32.783  30.040   6.369  1.00 10.46           C  
ATOM    182  C   ILE A  23      33.583  30.266   5.094  1.00 10.02           C  
ATOM    183  O   ILE A  23      34.567  31.001   5.117  1.00 10.16           O  
ATOM    184  CB  ILE A  23      31.970  31.283   6.860  1.00 12.23           C  
ATOM    185  CG1AILE A  23      30.906  31.626   5.768  0.50 10.89           C  
ATOM    186  CG1BILE A  23      30.940  30.954   7.951  0.50 13.56           C  
ATOM    187  CG2AILE A  23      32.782  32.444   7.408  0.50 10.84           C  
ATOM    188  CG2BILE A  23      31.342  32.043   5.633  0.50 12.98           C  
ATOM    189  CD1AILE A  23      29.783  32.535   6.339  0.50  9.53           C  
ATOM    190  CD1BILE A  23      29.669  31.852   7.991  0.50 15.60           C  
ATOM    191  N   LEU A  24      33.114  29.721   3.978  1.00  8.44           N  
ATOM    192  CA  LEU A  24      33.785  29.852   2.683  1.00  7.85           C  
ATOM    193  C   LEU A  24      32.958  30.889   1.883  1.00  9.05           C  
ATOM    194  O   LEU A  24      31.755  30.609   1.708  1.00 11.52           O  
ATOM    195  CB  LEU A  24      33.818  28.464   2.034  1.00  9.81           C  
ATOM    196  CG  LEU A  24      34.477  28.439   0.625  1.00 10.54           C  
ATOM    197  CD1 LEU A  24      35.962  28.722   0.715  1.00 11.74           C  
ATOM    198  CD2 LEU A  24      34.190  27.053   0.016  1.00 11.91           C  
ATOM    199  N   VAL A  25      33.599  31.917   1.389  1.00  7.73           N  
ATOM    200  CA  VAL A  25      32.859  32.997   0.714  1.00  7.72           C  
ATOM    201  C   VAL A  25      33.271  32.975  -0.769  1.00  9.49           C  
ATOM    202  O   VAL A  25      34.480  33.087  -1.047  1.00 10.05           O  
ATOM    203  CB  VAL A  25      33.089  34.369   1.368  1.00  8.36           C  
ATOM    204  CG1 VAL A  25      32.361  35.403   0.557  1.00  8.76           C  
ATOM    205  CG2 VAL A  25      32.644  34.345   2.821  1.00  8.36           C  
ATOM    206  N   ASP A  26      32.297  32.856  -1.644  1.00  8.75           N  
ATOM    207  CA  ASP A  26      32.520  32.871  -3.108  1.00  9.06           C  
ATOM    208  C   ASP A  26      32.197  34.250  -3.668  1.00 10.31           C  
ATOM    209  O   ASP A  26      31.007  34.641  -3.565  1.00 11.97           O  
ATOM    210  CB  ASP A  26      31.619  31.811  -3.710  1.00  9.90           C  
ATOM    211  CG  ASP A  26      31.571  31.778  -5.235  1.00 13.37           C  
ATOM    212  OD1 ASP A  26      30.538  31.381  -5.797  1.00 14.34           O  
ATOM    213  OD2 ASP A  26      32.575  32.139  -5.860  1.00 15.28           O  
ATOM    214  N   PHE A  27      33.138  34.929  -4.262  1.00  9.89           N  
ATOM    215  CA  PHE A  27      32.981  36.242  -4.921  1.00 11.01           C  
ATOM    216  C   PHE A  27      32.738  35.935  -6.408  1.00 12.27           C  
ATOM    217  O   PHE A  27      33.564  35.282  -7.054  1.00 12.96           O  
ATOM    218  CB  PHE A  27      34.230  37.080  -4.680  1.00 11.31           C  
ATOM    219  CG  PHE A  27      34.327  37.604  -3.278  1.00 13.55           C  
ATOM    220  CD1 PHE A  27      33.871  38.881  -2.952  1.00 14.15           C  
ATOM    221  CD2 PHE A  27      34.865  36.779  -2.287  1.00 14.05           C  
ATOM    222  CE1 PHE A  27      34.000  39.377  -1.651  1.00 15.13           C  
ATOM    223  CE2 PHE A  27      34.963  37.240  -0.976  1.00 15.37           C  
ATOM    224  CZ  PHE A  27      34.500  38.530  -0.650  1.00 14.70           C  
ATOM    225  N   TRP A  28      31.585  36.341  -6.910  1.00 12.01           N  
ATOM    226  CA  TRP A  28      31.164  35.958  -8.285  1.00 14.29           C  
ATOM    227  C   TRP A  28      30.376  37.102  -8.923  1.00 14.75           C  
ATOM    228  O   TRP A  28      30.045  38.100  -8.308  1.00 14.36           O  
ATOM    229  CB  TRP A  28      30.355  34.649  -8.238  1.00 15.01           C  
ATOM    230  CG  TRP A  28      28.981  34.857  -7.680  1.00 16.81           C  
ATOM    231  CD1 TRP A  28      28.653  35.218  -6.401  1.00 16.45           C  
ATOM    232  CD2 TRP A  28      27.746  34.811  -8.398  1.00 18.37           C  
ATOM    233  NE1 TRP A  28      27.295  35.358  -6.253  1.00 18.08           N  
ATOM    234  CE2 TRP A  28      26.724  35.127  -7.496  1.00 19.33           C  
ATOM    235  CE3 TRP A  28      27.430  34.524  -9.725  1.00 20.65           C  
ATOM    236  CZ2 TRP A  28      25.384  35.178  -7.858  1.00 20.07           C  
ATOM    237  CZ3 TRP A  28      26.095  34.583 -10.085  1.00 20.67           C  
ATOM    238  CH2 TRP A  28      25.077  34.876  -9.187  1.00 21.38           C  
ATOM    239  N   ALA A  29      30.038  36.848 -10.185  1.00 16.64           N  
ATOM    240  CA  ALA A  29      29.211  37.767 -11.005  1.00 18.79           C  
ATOM    241  C   ALA A  29      28.628  36.901 -12.122  1.00 20.47           C  
ATOM    242  O   ALA A  29      29.160  35.860 -12.517  1.00 19.75           O  
ATOM    243  CB  ALA A  29      29.995  38.903 -11.591  1.00 17.90           C  
ATOM    244  N   GLU A  30      27.476  37.381 -12.590  1.00 23.83           N  
ATOM    245  CA  GLU A  30      26.743  36.601 -13.583  1.00 27.43           C  
ATOM    246  C   GLU A  30      27.450  36.460 -14.930  1.00 25.88           C  
ATOM    247  O   GLU A  30      27.282  35.429 -15.592  1.00 26.00           O  
ATOM    248  CB  GLU A  30      25.320  37.161 -13.789  1.00 32.09           C  
ATOM    249  CG  GLU A  30      24.288  36.065 -13.452  1.00 37.84           C  
ATOM    250  CD  GLU A  30      23.051  36.496 -12.731  1.00 42.35           C  
ATOM    251  OE1 GLU A  30      22.192  37.253 -13.233  1.00 45.04           O  
ATOM    252  OE2 GLU A  30      22.954  35.959 -11.597  1.00 44.11           O  
ATOM    253  N   TRP A  31      28.229  37.428 -15.272  1.00 25.14           N  
ATOM    254  CA  TRP A  31      28.977  37.467 -16.522  1.00 24.91           C  
ATOM    255  C   TRP A  31      30.202  36.571 -16.434  1.00 25.00           C  
ATOM    256  O   TRP A  31      30.873  36.415 -17.457  1.00 25.76           O  
ATOM    257  CB  TRP A  31      29.458  38.875 -16.817  1.00 26.12           C  
ATOM    258  CG  TRP A  31      29.976  39.705 -15.701  1.00 27.47           C  
ATOM    259  CD1 TRP A  31      29.258  40.617 -14.957  1.00 27.56           C  
ATOM    260  CD2 TRP A  31      31.312  39.768 -15.179  1.00 27.86           C  
ATOM    261  NE1 TRP A  31      30.055  41.230 -14.014  1.00 27.19           N  
ATOM    262  CE2 TRP A  31      31.313  40.737 -14.130  1.00 28.18           C  
ATOM    263  CE3 TRP A  31      32.488  39.082 -15.497  1.00 28.42           C  
ATOM    264  CZ2 TRP A  31      32.456  41.032 -13.393  1.00 27.99           C  
ATOM    265  CZ3 TRP A  31      33.623  39.373 -14.764  1.00 28.14           C  
ATOM    266  CH2 TRP A  31      33.601  40.333 -13.748  1.00 28.64           C  
ATOM    267  N   CYS A  32      30.492  36.041 -15.250  1.00 22.22           N  
ATOM    268  CA  CYS A  32      31.749  35.264 -15.067  1.00 20.24           C  
ATOM    269  C   CYS A  32      31.532  33.814 -15.354  1.00 19.15           C  
ATOM    270  O   CYS A  32      30.902  33.016 -14.643  1.00 18.30           O  
ATOM    271  CB  CYS A  32      32.291  35.603 -13.649  1.00 18.86           C  
ATOM    272  SG  CYS A  32      33.555  34.457 -13.062  1.00 17.52           S  
ATOM    273  N   GLY A  33      32.097  33.354 -16.498  1.00 18.02           N  
ATOM    274  CA  GLY A  33      31.923  31.972 -16.915  1.00 19.03           C  
ATOM    275  C   GLY A  33      32.459  30.955 -15.935  1.00 18.76           C  
ATOM    276  O   GLY A  33      31.737  30.037 -15.501  1.00 20.52           O  
ATOM    277  N   PRO A  34      33.727  31.073 -15.538  1.00 18.13           N  
ATOM    278  CA  PRO A  34      34.309  30.133 -14.577  1.00 17.65           C  
ATOM    279  C   PRO A  34      33.551  30.135 -13.246  1.00 17.40           C  
ATOM    280  O   PRO A  34      33.583  29.113 -12.542  1.00 16.57           O  
ATOM    281  CB  PRO A  34      35.769  30.547 -14.439  1.00 17.81           C  
ATOM    282  CG  PRO A  34      36.037  31.217 -15.761  1.00 19.11           C  
ATOM    283  CD  PRO A  34      34.728  32.036 -16.012  1.00 18.53           C  
ATOM    284  N   CYS A  35      32.981  31.281 -12.915  1.00 17.05           N  
ATOM    285  CA  CYS A  35      32.187  31.344 -11.645  1.00 16.98           C  
ATOM    286  C   CYS A  35      30.993  30.419 -11.728  1.00 18.73           C  
ATOM    287  O   CYS A  35      30.668  29.740 -10.780  1.00 17.87           O  
ATOM    288  CB  CYS A  35      31.674  32.747 -11.366  1.00 16.47           C  
ATOM    289  SG  CYS A  35      32.923  33.992 -11.125  1.00 17.50           S  
ATOM    290  N   LYS A  36      30.305  30.469 -12.886  1.00 20.01           N  
ATOM    291  CA  LYS A  36      29.144  29.598 -13.084  1.00 22.48           C  
ATOM    292  C   LYS A  36      29.594  28.167 -13.165  1.00 22.05           C  
ATOM    293  O   LYS A  36      28.882  27.273 -12.653  1.00 21.89           O  
ATOM    294  CB  LYS A  36      28.263  30.084 -14.256  1.00 25.07           C  
ATOM    295  CG  LYS A  36      27.682  31.463 -13.811  1.00 29.51           C  
ATOM    296  CD  LYS A  36      26.744  32.109 -14.816  1.00 33.00           C  
ATOM    297  CE  LYS A  36      27.465  32.446 -16.116  1.00 35.46           C  
ATOM    298  NZ  LYS A  36      26.497  32.984 -17.135  1.00 37.89           N  
ATOM    299  N   MET A  37      30.763  27.876 -13.678  1.00 22.43           N  
ATOM    300  CA  MET A  37      31.237  26.464 -13.698  1.00 23.47           C  
ATOM    301  C   MET A  37      31.420  25.847 -12.336  1.00 21.76           C  
ATOM    302  O   MET A  37      31.286  24.633 -12.113  1.00 21.64           O  
ATOM    303  CB  MET A  37      32.546  26.467 -14.523  1.00 27.28           C  
ATOM    304  CG  MET A  37      32.706  25.229 -15.353  1.00 32.69           C  
ATOM    305  SD  MET A  37      33.860  25.627 -16.719  1.00 37.76           S  
ATOM    306  CE  MET A  37      35.422  25.696 -15.895  1.00 35.87           C  
ATOM    307  N   ILE A  38      31.814  26.635 -11.313  1.00 19.09           N  
ATOM    308  CA  ILE A  38      32.052  26.055  -9.983  1.00 17.03           C  
ATOM    309  C   ILE A  38      30.802  26.102  -9.113  1.00 15.22           C  
ATOM    310  O   ILE A  38      30.824  25.543  -8.005  1.00 14.78           O  
ATOM    311  CB  ILE A  38      33.274  26.678  -9.220  1.00 17.68           C  
ATOM    312  CG1 ILE A  38      32.962  28.149  -8.873  1.00 17.93           C  
ATOM    313  CG2 ILE A  38      34.586  26.463 -10.041  1.00 18.86           C  
ATOM    314  CD1 ILE A  38      34.024  28.763  -7.912  1.00 20.51           C  
ATOM    315  N   ALA A  39      29.755  26.788  -9.558  1.00 15.45           N  
ATOM    316  CA  ALA A  39      28.531  26.837  -8.702  1.00 15.05           C  
ATOM    317  C   ALA A  39      28.045  25.493  -8.258  1.00 16.18           C  
ATOM    318  O   ALA A  39      27.771  25.243  -7.052  1.00 14.78           O  
ATOM    319  CB  ALA A  39      27.453  27.672  -9.399  1.00 16.65           C  
ATOM    320  N   PRO A  40      27.905  24.467  -9.129  1.00 15.41           N  
ATOM    321  CA  PRO A  40      27.440  23.173  -8.654  1.00 15.14           C  
ATOM    322  C   PRO A  40      28.355  22.518  -7.664  1.00 14.74           C  
ATOM    323  O   PRO A  40      27.918  21.732  -6.807  1.00 15.66           O  
ATOM    324  CB  PRO A  40      27.374  22.260  -9.914  1.00 16.37           C  
ATOM    325  CG  PRO A  40      27.364  23.253 -11.016  1.00 17.16           C  
ATOM    326  CD  PRO A  40      28.136  24.515 -10.576  1.00 16.10           C  
ATOM    327  N   ILE A  41      29.667  22.780  -7.864  1.00 13.63           N  
ATOM    328  CA  ILE A  41      30.634  22.130  -6.925  1.00 14.40           C  
ATOM    329  C   ILE A  41      30.441  22.746  -5.538  1.00 12.89           C  
ATOM    330  O   ILE A  41      30.553  21.978  -4.583  1.00 14.10           O  
ATOM    331  CB  ILE A  41      32.094  22.367  -7.392  1.00 15.66           C  
ATOM    332  CG1 ILE A  41      32.272  21.737  -8.808  1.00 16.98           C  
ATOM    333  CG2 ILE A  41      33.141  21.918  -6.344  1.00 17.36           C  
ATOM    334  CD1 ILE A  41      33.639  22.193  -9.428  1.00 17.51           C  
ATOM    335  N   LEU A  42      30.140  24.023  -5.469  1.00 12.45           N  
ATOM    336  CA  LEU A  42      29.875  24.631  -4.150  1.00 13.12           C  
ATOM    337  C   LEU A  42      28.632  24.012  -3.501  1.00 14.26           C  
ATOM    338  O   LEU A  42      28.556  23.833  -2.277  1.00 13.56           O  
ATOM    339  CB  LEU A  42      29.777  26.151  -4.301  1.00 14.88           C  
ATOM    340  CG  LEU A  42      31.108  26.853  -4.547  1.00 17.19           C  
ATOM    341  CD1 LEU A  42      30.847  28.363  -4.712  1.00 19.17           C  
ATOM    342  CD2 LEU A  42      32.043  26.610  -3.384  1.00 17.60           C  
ATOM    343  N   ASP A  43      27.614  23.697  -4.291  1.00 13.25           N  
ATOM    344  CA  ASP A  43      26.436  23.023  -3.719  1.00 14.20           C  
ATOM    345  C   ASP A  43      26.773  21.658  -3.164  1.00 14.45           C  
ATOM    346  O   ASP A  43      26.298  21.269  -2.111  1.00 14.66           O  
ATOM    347  CB  ASP A  43      25.347  22.853  -4.793  1.00 15.32           C  
ATOM    348  CG  ASP A  43      24.669  24.136  -5.146  1.00 17.51           C  
ATOM    349  OD1 ASP A  43      24.202  24.189  -6.311  1.00 19.16           O  
ATOM    350  OD2 ASP A  43      24.534  25.032  -4.296  1.00 16.41           O  
ATOM    351  N   GLU A  44      27.602  20.898  -3.914  1.00 14.18           N  
ATOM    352  CA  GLU A  44      28.024  19.586  -3.382  1.00 15.12           C  
ATOM    353  C   GLU A  44      28.805  19.702  -2.086  1.00 15.75           C  
ATOM    354  O   GLU A  44      28.620  18.913  -1.158  1.00 16.09           O  
ATOM    355  CB  GLU A  44      28.955  18.888  -4.383  1.00 17.56           C  
ATOM    356  CG  GLU A  44      28.326  18.714  -5.779  1.00 19.86           C  
ATOM    357  CD  GLU A  44      29.239  17.976  -6.722  1.00 23.23           C  
ATOM    358  OE1 GLU A  44      29.292  16.752  -6.688  1.00 25.21           O  
ATOM    359  OE2 GLU A  44      29.904  18.712  -7.486  1.00 24.23           O  
ATOM    360  N   ILE A  45      29.699  20.697  -2.061  1.00 14.65           N  
ATOM    361  CA  ILE A  45      30.540  20.890  -0.844  1.00 15.35           C  
ATOM    362  C   ILE A  45      29.646  21.324   0.307  1.00 14.09           C  
ATOM    363  O   ILE A  45      29.876  20.931   1.457  1.00 14.26           O  
ATOM    364  CB  ILE A  45      31.663  21.938  -1.165  1.00 17.37           C  
ATOM    365  CG1 ILE A  45      32.836  21.317  -1.947  1.00 18.51           C  
ATOM    366  CG2 ILE A  45      32.184  22.704   0.090  1.00 18.76           C  
ATOM    367  CD1 ILE A  45      33.458  20.023  -1.445  1.00 19.79           C  
ATOM    368  N   ALA A  46      28.680  22.180   0.041  1.00 13.61           N  
ATOM    369  CA  ALA A  46      27.741  22.632   1.117  1.00 14.18           C  
ATOM    370  C   ALA A  46      27.034  21.437   1.762  1.00 16.26           C  
ATOM    371  O   ALA A  46      26.827  21.425   3.005  1.00 16.75           O  
ATOM    372  CB  ALA A  46      26.770  23.670   0.573  1.00 13.19           C  
ATOM    373  N   ASP A  47      26.633  20.487   0.934  1.00 16.20           N  
ATOM    374  CA  ASP A  47      25.998  19.256   1.488  1.00 18.29           C  
ATOM    375  C   ASP A  47      27.007  18.387   2.223  1.00 18.48           C  
ATOM    376  O   ASP A  47      26.779  17.932   3.366  1.00 20.01           O  
ATOM    377  CB  ASP A  47      25.239  18.534   0.367  1.00 20.25           C  
ATOM    378  CG AASP A  47      23.877  19.132   0.076  0.50 19.52           C  
ATOM    379  CG BASP A  47      24.860  17.102   0.699  0.50 22.33           C  
ATOM    380  OD1AASP A  47      23.048  19.368   0.965  0.50 19.93           O  
ATOM    381  OD1BASP A  47      25.027  16.146  -0.078  0.50 24.28           O  
ATOM    382  OD2AASP A  47      23.521  19.424  -1.092  0.50 20.78           O  
ATOM    383  OD2BASP A  47      24.356  16.903   1.815  0.50 24.21           O  
ATOM    384  N   GLU A  48      28.133  18.128   1.612  1.00 18.19           N  
ATOM    385  CA  GLU A  48      29.133  17.236   2.160  1.00 20.03           C  
ATOM    386  C   GLU A  48      29.727  17.767   3.452  1.00 20.36           C  
ATOM    387  O   GLU A  48      30.065  16.922   4.320  1.00 19.98           O  
ATOM    388  CB  GLU A  48      30.288  16.881   1.222  1.00 22.08           C  
ATOM    389  CG AGLU A  48      29.878  16.097   0.001  0.50 23.22           C  
ATOM    390  CG BGLU A  48      31.372  15.982   1.785  0.50 24.50           C  
ATOM    391  CD AGLU A  48      30.874  15.856  -1.084  0.50 24.57           C  
ATOM    392  CD BGLU A  48      32.387  15.377   0.888  0.50 25.93           C  
ATOM    393  OE1AGLU A  48      30.500  15.474  -2.178  0.50 25.49           O  
ATOM    394  OE1BGLU A  48      33.384  14.801   1.307  0.50 26.62           O  
ATOM    395  OE2AGLU A  48      32.049  16.115  -0.781  0.50 25.61           O  
ATOM    396  OE2BGLU A  48      32.104  15.515  -0.318  0.50 27.54           O  
ATOM    397  N   TYR A  49      29.815  19.077   3.589  1.00 18.36           N  
ATOM    398  CA  TYR A  49      30.521  19.621   4.781  1.00 19.05           C  
ATOM    399  C   TYR A  49      29.521  20.270   5.720  1.00 19.83           C  
ATOM    400  O   TYR A  49      29.927  21.012   6.600  1.00 20.19           O  
ATOM    401  CB  TYR A  49      31.633  20.574   4.366  1.00 18.28           C  
ATOM    402  CG  TYR A  49      32.898  19.961   3.818  1.00 19.11           C  
ATOM    403  CD1 TYR A  49      32.952  19.443   2.543  1.00 20.12           C  
ATOM    404  CD2 TYR A  49      34.093  19.919   4.573  1.00 20.77           C  
ATOM    405  CE1 TYR A  49      34.097  18.868   2.024  1.00 21.72           C  
ATOM    406  CE2 TYR A  49      35.275  19.347   4.060  1.00 20.41           C  
ATOM    407  CZ  TYR A  49      35.274  18.844   2.787  1.00 22.29           C  
ATOM    408  OH  TYR A  49      36.397  18.294   2.200  1.00 23.76           O  
ATOM    409  N   GLN A  50      28.257  19.959   5.495  1.00 21.00           N  
ATOM    410  CA  GLN A  50      27.179  20.532   6.346  1.00 23.89           C  
ATOM    411  C   GLN A  50      27.481  20.263   7.806  1.00 24.87           C  
ATOM    412  O   GLN A  50      27.843  19.159   8.243  1.00 25.36           O  
ATOM    413  CB  GLN A  50      25.855  19.960   5.899  1.00 26.01           C  
ATOM    414  CG  GLN A  50      24.635  20.600   6.512  1.00 29.12           C  
ATOM    415  CD  GLN A  50      23.410  19.936   5.876  1.00 31.71           C  
ATOM    416  OE1 GLN A  50      23.517  18.792   5.390  1.00 34.06           O  
ATOM    417  NE2 GLN A  50      22.329  20.705   5.892  1.00 31.60           N  
ATOM    418  N   GLY A  51      27.342  21.298   8.614  1.00 25.01           N  
ATOM    419  CA  GLY A  51      27.738  21.106  10.023  1.00 26.18           C  
ATOM    420  C   GLY A  51      29.189  21.425  10.288  1.00 27.45           C  
ATOM    421  O   GLY A  51      29.497  21.693  11.469  1.00 29.49           O  
ATOM    422  N   LYS A  52      30.113  21.446   9.355  1.00 26.17           N  
ATOM    423  CA  LYS A  52      31.510  21.764   9.590  1.00 25.10           C  
ATOM    424  C   LYS A  52      31.934  23.047   8.862  1.00 22.67           C  
ATOM    425  O   LYS A  52      33.017  23.598   9.177  1.00 23.03           O  
ATOM    426  CB  LYS A  52      32.459  20.704   8.966  1.00 29.07           C  
ATOM    427  CG  LYS A  52      31.968  19.269   9.129  1.00 33.45           C  
ATOM    428  CD  LYS A  52      32.647  18.337   8.103  1.00 35.54           C  
ATOM    429  CE  LYS A  52      31.932  16.979   8.126  1.00 37.91           C  
ATOM    430  NZ  LYS A  52      31.800  16.419   6.753  1.00 38.70           N  
ATOM    431  N   LEU A  53      31.106  23.442   7.898  1.00 18.68           N  
ATOM    432  CA  LEU A  53      31.450  24.605   7.068  1.00 16.96           C  
ATOM    433  C   LEU A  53      30.151  25.264   6.592  1.00 15.56           C  
ATOM    434  O   LEU A  53      29.272  24.454   6.279  1.00 16.53           O  
ATOM    435  CB  LEU A  53      32.228  24.022   5.866  1.00 17.08           C  
ATOM    436  CG  LEU A  53      32.651  25.042   4.832  1.00 18.17           C  
ATOM    437  CD1 LEU A  53      33.842  25.892   5.310  1.00 18.51           C  
ATOM    438  CD2 LEU A  53      33.022  24.328   3.525  1.00 19.30           C  
ATOM    439  N   THR A  54      30.109  26.568   6.584  1.00 13.07           N  
ATOM    440  CA  THR A  54      29.052  27.341   5.928  1.00 12.96           C  
ATOM    441  C   THR A  54      29.579  27.892   4.598  1.00 13.26           C  
ATOM    442  O   THR A  54      30.717  28.358   4.553  1.00 13.02           O  
ATOM    443  CB  THR A  54      28.557  28.544   6.830  1.00 16.39           C  
ATOM    444  OG1 THR A  54      28.055  27.907   8.061  1.00 18.27           O  
ATOM    445  CG2 THR A  54      27.431  29.360   6.198  1.00 18.67           C  
ATOM    446  N   VAL A  55      28.769  27.770   3.550  1.00 11.70           N  
ATOM    447  CA  VAL A  55      29.222  28.360   2.267  1.00 11.55           C  
ATOM    448  C   VAL A  55      28.350  29.584   1.997  1.00 11.22           C  
ATOM    449  O   VAL A  55      27.137  29.566   2.233  1.00 12.29           O  
ATOM    450  CB  VAL A  55      29.093  27.286   1.166  1.00 12.00           C  
ATOM    451  CG1 VAL A  55      29.543  27.820  -0.190  1.00 13.57           C  
ATOM    452  CG2 VAL A  55      29.809  25.980   1.537  1.00 12.95           C  
ATOM    453  N   ALA A  56      28.967  30.634   1.486  1.00  8.60           N  
ATOM    454  CA  ALA A  56      28.230  31.880   1.209  1.00  8.68           C  
ATOM    455  C   ALA A  56      28.670  32.478  -0.123  1.00 10.46           C  
ATOM    456  O   ALA A  56      29.781  32.160  -0.565  1.00 10.51           O  
ATOM    457  CB  ALA A  56      28.512  32.816   2.410  1.00 10.56           C  
ATOM    458  N   LYS A  57      27.846  33.338  -0.695  1.00 11.12           N  
ATOM    459  CA  LYS A  57      28.140  34.021  -1.952  1.00 12.26           C  
ATOM    460  C   LYS A  57      27.946  35.530  -1.868  1.00 12.22           C  
ATOM    461  O   LYS A  57      26.974  35.978  -1.228  1.00 13.38           O  
ATOM    462  CB  LYS A  57      27.194  33.542  -3.092  1.00 14.21           C  
ATOM    463  CG  LYS A  57      27.596  32.160  -3.606  1.00 17.04           C  
ATOM    464  CD  LYS A  57      26.558  31.676  -4.639  1.00 18.97           C  
ATOM    465  CE  LYS A  57      27.070  30.401  -5.313  1.00 21.48           C  
ATOM    466  NZ  LYS A  57      26.036  29.830  -6.273  1.00 23.94           N  
ATOM    467  N   LEU A  58      28.826  36.221  -2.583  1.00  9.80           N  
ATOM    468  CA  LEU A  58      28.691  37.690  -2.664  1.00 10.88           C  
ATOM    469  C   LEU A  58      28.857  38.050  -4.145  1.00 13.04           C  
ATOM    470  O   LEU A  58      29.933  37.847  -4.690  1.00 11.67           O  
ATOM    471  CB  LEU A  58      29.665  38.408  -1.747  1.00 11.30           C  
ATOM    472  CG  LEU A  58      29.460  39.945  -1.761  1.00 12.68           C  
ATOM    473  CD1ALEU A  58      29.506  40.469  -0.336  0.50 11.88           C  
ATOM    474  CD1BLEU A  58      28.350  40.432  -0.847  0.50 11.43           C  
ATOM    475  CD2ALEU A  58      30.461  40.624  -2.663  0.50 11.17           C  
ATOM    476  CD2BLEU A  58      30.779  40.575  -1.341  0.50 13.77           C  
ATOM    477  N   ASN A  59      27.733  38.539  -4.680  1.00 12.95           N  
ATOM    478  CA  ASN A  59      27.741  38.998  -6.102  1.00 14.64           C  
ATOM    479  C   ASN A  59      28.373  40.374  -6.128  1.00 15.71           C  
ATOM    480  O   ASN A  59      27.835  41.349  -5.540  1.00 16.49           O  
ATOM    481  CB  ASN A  59      26.271  38.978  -6.564  1.00 15.92           C  
ATOM    482  CG  ASN A  59      26.208  39.429  -8.032  1.00 17.45           C  
ATOM    483  OD1 ASN A  59      26.661  40.532  -8.311  1.00 18.79           O  
ATOM    484  ND2 ASN A  59      25.700  38.534  -8.850  1.00 21.56           N  
ATOM    485  N   ILE A  60      29.501  40.517  -6.826  1.00 15.51           N  
ATOM    486  CA  ILE A  60      30.230  41.784  -6.828  1.00 17.36           C  
ATOM    487  C   ILE A  60      29.594  42.892  -7.703  1.00 16.71           C  
ATOM    488  O   ILE A  60      30.062  44.009  -7.506  1.00 18.88           O  
ATOM    489  CB  ILE A  60      31.732  41.539  -7.247  1.00 16.96           C  
ATOM    490  CG1 ILE A  60      31.791  40.998  -8.707  1.00 18.62           C  
ATOM    491  CG2 ILE A  60      32.426  40.634  -6.195  1.00 17.73           C  
ATOM    492  CD1 ILE A  60      33.206  41.362  -9.299  1.00 21.03           C  
ATOM    493  N   ASP A  61      28.660  42.559  -8.533  1.00 17.84           N  
ATOM    494  CA  ASP A  61      27.982  43.600  -9.348  1.00 19.93           C  
ATOM    495  C   ASP A  61      26.996  44.318  -8.413  1.00 20.41           C  
ATOM    496  O   ASP A  61      26.880  45.548  -8.474  1.00 21.40           O  
ATOM    497  CB  ASP A  61      27.224  43.002 -10.515  1.00 20.73           C  
ATOM    498  CG  ASP A  61      28.155  42.578 -11.643  1.00 22.29           C  
ATOM    499  OD1 ASP A  61      29.275  43.023 -11.776  1.00 24.32           O  
ATOM    500  OD2 ASP A  61      27.652  41.731 -12.396  1.00 25.39           O  
ATOM    501  N   GLN A  62      26.348  43.477  -7.609  1.00 20.64           N  
ATOM    502  CA  GLN A  62      25.316  44.023  -6.688  1.00 20.92           C  
ATOM    503  C   GLN A  62      25.887  44.593  -5.422  1.00 20.79           C  
ATOM    504  O   GLN A  62      25.228  45.439  -4.768  1.00 21.69           O  
ATOM    505  CB  GLN A  62      24.305  42.932  -6.357  1.00 23.27           C  
ATOM    506  CG  GLN A  62      23.513  42.535  -7.599  1.00 26.91           C  
ATOM    507  CD  GLN A  62      22.927  41.163  -7.442  1.00 29.51           C  
ATOM    508  OE1 GLN A  62      22.889  40.574  -6.367  1.00 30.66           O  
ATOM    509  NE2 GLN A  62      22.437  40.593  -8.558  1.00 32.21           N  
ATOM    510  N   ASN A  63      27.059  44.181  -4.989  1.00 18.99           N  
ATOM    511  CA  ASN A  63      27.725  44.603  -3.750  1.00 17.84           C  
ATOM    512  C   ASN A  63      29.180  44.894  -4.070  1.00 19.71           C  
ATOM    513  O   ASN A  63      30.044  44.018  -3.875  1.00 19.31           O  
ATOM    514  CB  ASN A  63      27.592  43.470  -2.724  1.00 16.90           C  
ATOM    515  CG  ASN A  63      26.143  43.165  -2.397  1.00 16.09           C  
ATOM    516  OD1 ASN A  63      25.615  43.912  -1.540  1.00 16.23           O  
ATOM    517  ND2 ASN A  63      25.548  42.140  -2.957  1.00 15.51           N  
ATOM    518  N   PRO A  64      29.452  46.060  -4.566  1.00 21.61           N  
ATOM    519  CA  PRO A  64      30.824  46.384  -4.999  1.00 23.16           C  
ATOM    520  C   PRO A  64      31.760  46.805  -3.907  1.00 23.19           C  
ATOM    521  O   PRO A  64      32.952  47.008  -4.208  1.00 25.21           O  
ATOM    522  CB  PRO A  64      30.589  47.552  -5.961  1.00 23.16           C  
ATOM    523  CG  PRO A  64      29.371  48.241  -5.391  1.00 23.54           C  
ATOM    524  CD  PRO A  64      28.450  47.059  -5.018  1.00 22.42           C  
ATOM    525  N   GLY A  65      31.322  46.971  -2.677  1.00 22.26           N  
ATOM    526  CA  GLY A  65      32.139  47.479  -1.593  1.00 21.33           C  
ATOM    527  C   GLY A  65      33.026  46.472  -0.910  1.00 21.65           C  
ATOM    528  O   GLY A  65      34.080  46.911  -0.398  1.00 23.20           O  
ATOM    529  N   THR A  66      32.689  45.181  -0.915  1.00 18.95           N  
ATOM    530  CA  THR A  66      33.471  44.241  -0.136  1.00 19.29           C  
ATOM    531  C   THR A  66      34.785  43.766  -0.811  1.00 18.41           C  
ATOM    532  O   THR A  66      35.771  43.733  -0.049  1.00 17.22           O  
ATOM    533  CB  THR A  66      32.665  42.975   0.357  1.00 19.44           C  
ATOM    534  OG1 THR A  66      31.598  43.518   1.177  1.00 19.00           O  
ATOM    535  CG2 THR A  66      33.500  41.987   1.203  1.00 19.24           C  
ATOM    536  N   ALA A  67      34.711  43.426  -2.064  1.00 18.41           N  
ATOM    537  CA  ALA A  67      35.904  42.817  -2.726  1.00 20.02           C  
ATOM    538  C   ALA A  67      37.179  43.665  -2.537  1.00 21.19           C  
ATOM    539  O   ALA A  67      38.247  43.146  -2.213  1.00 19.61           O  
ATOM    540  CB  ALA A  67      35.583  42.592  -4.193  1.00 19.09           C  
ATOM    541  N   PRO A  68      37.050  44.959  -2.751  1.00 23.12           N  
ATOM    542  CA  PRO A  68      38.199  45.868  -2.643  1.00 24.69           C  
ATOM    543  C   PRO A  68      38.812  45.855  -1.267  1.00 25.21           C  
ATOM    544  O   PRO A  68      40.047  46.056  -1.176  1.00 25.99           O  
ATOM    545  CB  PRO A  68      37.691  47.243  -3.032  1.00 25.48           C  
ATOM    546  CG  PRO A  68      36.385  47.009  -3.737  1.00 25.53           C  
ATOM    547  CD  PRO A  68      35.891  45.627  -3.363  1.00 24.38           C  
ATOM    548  N   LYS A  69      38.025  45.610  -0.227  1.00 25.30           N  
ATOM    549  CA  LYS A  69      38.624  45.544   1.106  1.00 26.12           C  
ATOM    550  C   LYS A  69      39.521  44.351   1.320  1.00 25.65           C  
ATOM    551  O   LYS A  69      40.323  44.428   2.261  1.00 26.00           O  
ATOM    552  CB  LYS A  69      37.573  45.467   2.226  1.00 28.52           C  
ATOM    553  CG  LYS A  69      36.479  46.535   2.056  1.00 31.48           C  
ATOM    554  CD  LYS A  69      35.465  46.325   3.192  1.00 33.78           C  
ATOM    555  CE  LYS A  69      34.137  46.964   2.896  1.00 35.78           C  
ATOM    556  NZ  LYS A  69      33.166  46.536   3.962  1.00 38.12           N  
ATOM    557  N   TYR A  70      39.368  43.314   0.509  1.00 23.09           N  
ATOM    558  CA  TYR A  70      40.164  42.083   0.661  1.00 23.75           C  
ATOM    559  C   TYR A  70      41.205  41.961  -0.442  1.00 23.36           C  
ATOM    560  O   TYR A  70      41.861  40.924  -0.606  1.00 25.05           O  
ATOM    561  CB  TYR A  70      39.155  40.893   0.729  1.00 23.13           C  
ATOM    562  CG  TYR A  70      38.431  40.964   2.096  1.00 21.93           C  
ATOM    563  CD1 TYR A  70      37.192  41.519   2.274  1.00 21.08           C  
ATOM    564  CD2 TYR A  70      39.125  40.485   3.205  1.00 21.65           C  
ATOM    565  CE1 TYR A  70      36.601  41.591   3.530  1.00 21.72           C  
ATOM    566  CE2 TYR A  70      38.563  40.542   4.483  1.00 22.51           C  
ATOM    567  CZ  TYR A  70      37.319  41.120   4.626  1.00 21.52           C  
ATOM    568  OH  TYR A  70      36.832  41.147   5.891  1.00 24.23           O  
ATOM    569  N   GLY A  71      41.293  43.022  -1.238  1.00 23.22           N  
ATOM    570  CA  GLY A  71      42.279  43.098  -2.325  1.00 24.01           C  
ATOM    571  C   GLY A  71      41.971  42.096  -3.428  1.00 23.93           C  
ATOM    572  O   GLY A  71      42.913  41.672  -4.147  1.00 25.05           O  
ATOM    573  N   ILE A  72      40.706  41.776  -3.625  1.00 22.22           N  
ATOM    574  CA  ILE A  72      40.344  40.806  -4.673  1.00 23.02           C  
ATOM    575  C   ILE A  72      40.559  41.485  -6.012  1.00 24.82           C  
ATOM    576  O   ILE A  72      40.107  42.616  -6.136  1.00 25.78           O  
ATOM    577  CB  ILE A  72      38.859  40.339  -4.474  1.00 22.80           C  
ATOM    578  CG1 ILE A  72      38.868  39.478  -3.147  1.00 23.61           C  
ATOM    579  CG2 ILE A  72      38.275  39.580  -5.684  1.00 22.39           C  
ATOM    580  CD1 ILE A  72      37.457  39.211  -2.618  1.00 23.95           C  
ATOM    581  N   ARG A  73      41.138  40.764  -6.940  1.00 25.70           N  
ATOM    582  CA  ARG A  73      41.505  41.354  -8.233  1.00 28.72           C  
ATOM    583  C   ARG A  73      40.815  40.627  -9.364  1.00 26.64           C  
ATOM    584  O   ARG A  73      40.729  41.187 -10.480  1.00 28.31           O  
ATOM    585  CB  ARG A  73      43.057  41.284  -8.392  1.00 33.96           C  
ATOM    586  CG  ARG A  73      43.712  42.658  -8.585  1.00 39.79           C  
ATOM    587  CD  ARG A  73      44.921  42.718  -9.463  1.00 42.75           C  
ATOM    588  NE  ARG A  73      44.607  43.038 -10.873  1.00 46.10           N  
ATOM    589  CZ  ARG A  73      45.527  43.222 -11.821  1.00 47.31           C  
ATOM    590  NH1 ARG A  73      45.307  43.365 -13.138  1.00 47.57           N  
ATOM    591  NH2 ARG A  73      46.814  43.298 -11.412  1.00 48.24           N  
ATOM    592  N   GLY A  74      40.347  39.410  -9.153  1.00 22.67           N  
ATOM    593  CA  GLY A  74      39.693  38.627 -10.211  1.00 20.30           C  
ATOM    594  C   GLY A  74      38.665  37.693  -9.552  1.00 19.13           C  
ATOM    595  O   GLY A  74      38.682  37.542  -8.309  1.00 20.32           O  
ATOM    596  N   ILE A  75      37.797  37.119 -10.360  1.00 17.88           N  
ATOM    597  CA  ILE A  75      36.772  36.178  -9.880  1.00 15.70           C  
ATOM    598  C   ILE A  75      36.777  34.937 -10.769  1.00 16.22           C  
ATOM    599  O   ILE A  75      37.087  35.045 -11.993  1.00 16.90           O  
ATOM    600  CB  ILE A  75      35.389  36.898  -9.741  1.00 15.91           C  
ATOM    601  CG1 ILE A  75      34.935  37.634 -11.013  1.00 16.44           C  
ATOM    602  CG2 ILE A  75      35.415  37.871  -8.520  1.00 15.23           C  
ATOM    603  CD1 ILE A  75      33.394  37.923 -11.020  1.00 17.79           C  
ATOM    604  N   PRO A  76      36.424  33.786 -10.258  1.00 14.73           N  
ATOM    605  CA  PRO A  76      36.002  33.584  -8.873  1.00 14.69           C  
ATOM    606  C   PRO A  76      37.212  33.655  -7.942  1.00 12.99           C  
ATOM    607  O   PRO A  76      38.316  33.247  -8.305  1.00 13.87           O  
ATOM    608  CB  PRO A  76      35.410  32.162  -8.835  1.00 15.07           C  
ATOM    609  CG  PRO A  76      36.121  31.464  -9.950  1.00 15.09           C  
ATOM    610  CD  PRO A  76      36.447  32.515 -10.980  1.00 16.18           C  
ATOM    611  N   THR A  77      36.905  34.167  -6.757  1.00 10.97           N  
ATOM    612  CA  THR A  77      37.919  34.083  -5.649  1.00 10.60           C  
ATOM    613  C   THR A  77      37.182  33.451  -4.461  1.00 10.97           C  
ATOM    614  O   THR A  77      36.013  33.905  -4.258  1.00  9.68           O  
ATOM    615  CB  THR A  77      38.591  35.429  -5.274  1.00 11.88           C  
ATOM    616  OG1 THR A  77      39.464  35.757  -6.397  1.00 12.88           O  
ATOM    617  CG2 THR A  77      39.486  35.277  -4.019  1.00 12.63           C  
ATOM    618  N   LEU A  78      37.807  32.521  -3.793  1.00  8.99           N  
ATOM    619  CA  LEU A  78      37.209  31.885  -2.606  1.00  8.94           C  
ATOM    620  C   LEU A  78      38.006  32.393  -1.399  1.00  9.92           C  
ATOM    621  O   LEU A  78      39.246  32.269  -1.360  1.00 10.31           O  
ATOM    622  CB  LEU A  78      37.189  30.360  -2.681  1.00 11.07           C  
ATOM    623  CG  LEU A  78      36.389  29.720  -3.835  1.00 13.40           C  
ATOM    624  CD1 LEU A  78      36.714  28.233  -3.912  1.00 15.30           C  
ATOM    625  CD2 LEU A  78      34.922  29.990  -3.582  1.00 14.61           C  
ATOM    626  N   LEU A  79      37.313  32.936  -0.398  1.00 10.15           N  
ATOM    627  CA  LEU A  79      37.980  33.300   0.873  1.00  9.35           C  
ATOM    628  C   LEU A  79      37.477  32.361   1.950  1.00  9.49           C  
ATOM    629  O   LEU A  79      36.248  32.217   2.097  1.00 10.84           O  
ATOM    630  CB  LEU A  79      37.648  34.766   1.234  1.00 11.68           C  
ATOM    631  CG  LEU A  79      38.653  35.845   0.863  1.00 14.83           C  
ATOM    632  CD1 LEU A  79      39.135  35.800  -0.526  1.00 16.15           C  
ATOM    633  CD2 LEU A  79      38.069  37.222   1.183  1.00 15.30           C  
ATOM    634  N   LEU A  80      38.371  31.774   2.732  1.00  9.17           N  
ATOM    635  CA  LEU A  80      37.997  30.904   3.860  1.00  9.93           C  
ATOM    636  C   LEU A  80      38.238  31.724   5.150  1.00 10.65           C  
ATOM    637  O   LEU A  80      39.398  32.062   5.413  1.00 11.34           O  
ATOM    638  CB  LEU A  80      38.784  29.574   3.858  1.00 10.60           C  
ATOM    639  CG  LEU A  80      38.448  28.615   4.995  1.00 11.90           C  
ATOM    640  CD1ALEU A  80      36.958  28.211   4.920  0.50  9.78           C  
ATOM    641  CD1BLEU A  80      38.001  27.284   4.372  0.50 15.59           C  
ATOM    642  CD2ALEU A  80      39.362  27.404   4.944  0.50  9.34           C  
ATOM    643  CD2BLEU A  80      39.706  28.263   5.756  0.50 14.05           C  
ATOM    644  N   PHE A  81      37.170  32.068   5.844  1.00 10.35           N  
ATOM    645  CA  PHE A  81      37.268  32.831   7.107  1.00 11.21           C  
ATOM    646  C   PHE A  81      37.107  31.869   8.286  1.00 12.37           C  
ATOM    647  O   PHE A  81      36.328  30.907   8.298  1.00 12.89           O  
ATOM    648  CB  PHE A  81      36.150  33.876   7.203  1.00 12.17           C  
ATOM    649  CG  PHE A  81      36.301  35.089   6.339  1.00 12.31           C  
ATOM    650  CD1 PHE A  81      36.835  36.291   6.815  1.00 12.86           C  
ATOM    651  CD2 PHE A  81      35.865  35.026   5.007  1.00 11.60           C  
ATOM    652  CE1 PHE A  81      36.983  37.397   5.987  1.00 12.87           C  
ATOM    653  CE2 PHE A  81      36.037  36.114   4.190  1.00 13.00           C  
ATOM    654  CZ  PHE A  81      36.555  37.335   4.645  1.00 13.70           C  
ATOM    655  N   LYS A  82      37.910  32.197   9.316  1.00 14.04           N  
ATOM    656  CA  LYS A  82      37.779  31.529  10.629  1.00 17.14           C  
ATOM    657  C   LYS A  82      38.029  32.608  11.697  1.00 16.20           C  
ATOM    658  O   LYS A  82      38.972  33.361  11.520  1.00 14.23           O  
ATOM    659  CB  LYS A  82      38.751  30.427  10.930  1.00 19.17           C  
ATOM    660  CG  LYS A  82      38.532  29.183  10.117  1.00 23.77           C  
ATOM    661  CD  LYS A  82      39.760  28.268  10.306  1.00 27.67           C  
ATOM    662  CE  LYS A  82      39.342  27.001  11.031  1.00 30.63           C  
ATOM    663  NZ  LYS A  82      40.531  26.057  10.908  1.00 32.49           N  
ATOM    664  N   ASN A  83      37.147  32.680  12.690  1.00 16.95           N  
ATOM    665  CA  ASN A  83      37.409  33.656  13.781  1.00 16.48           C  
ATOM    666  C   ASN A  83      37.595  35.057  13.331  1.00 15.43           C  
ATOM    667  O   ASN A  83      38.470  35.755  13.902  1.00 15.74           O  
ATOM    668  CB  ASN A  83      38.619  33.151  14.611  1.00 18.87           C  
ATOM    669  CG  ASN A  83      38.424  31.748  15.095  1.00 20.65           C  
ATOM    670  OD1 ASN A  83      37.302  31.326  15.456  1.00 23.64           O  
ATOM    671  ND2 ASN A  83      39.470  30.925  15.052  1.00 21.65           N  
ATOM    672  N   GLY A  84      36.886  35.550  12.318  1.00 13.73           N  
ATOM    673  CA  GLY A  84      36.897  36.914  11.872  1.00 14.74           C  
ATOM    674  C   GLY A  84      38.041  37.329  10.970  1.00 16.70           C  
ATOM    675  O   GLY A  84      38.177  38.548  10.670  1.00 19.22           O  
ATOM    676  N   GLU A  85      38.785  36.333  10.523  1.00 16.70           N  
ATOM    677  CA  GLU A  85      39.942  36.663   9.678  1.00 19.63           C  
ATOM    678  C   GLU A  85      40.069  35.681   8.524  1.00 16.02           C  
ATOM    679  O   GLU A  85      39.611  34.561   8.671  1.00 15.75           O  
ATOM    680  CB  GLU A  85      41.201  36.499  10.560  1.00 24.65           C  
ATOM    681  CG  GLU A  85      42.142  37.572  10.330  1.00 30.62           C  
ATOM    682  CD  GLU A  85      43.338  37.479  11.268  1.00 33.38           C  
ATOM    683  OE1 GLU A  85      43.191  37.262  12.461  1.00 34.87           O  
ATOM    684  OE2 GLU A  85      44.369  37.655  10.564  1.00 35.34           O  
ATOM    685  N   VAL A  86      40.707  36.171   7.457  1.00 14.67           N  
ATOM    686  CA  VAL A  86      40.964  35.221   6.333  1.00 13.47           C  
ATOM    687  C   VAL A  86      41.995  34.197   6.738  1.00 13.45           C  
ATOM    688  O   VAL A  86      43.132  34.561   7.146  1.00 15.92           O  
ATOM    689  CB  VAL A  86      41.359  36.050   5.094  1.00 14.39           C  
ATOM    690  CG1 VAL A  86      41.802  35.113   3.961  1.00 16.21           C  
ATOM    691  CG2 VAL A  86      40.248  36.963   4.594  1.00 15.87           C  
ATOM    692  N   ALA A  87      41.715  32.919   6.611  1.00 11.40           N  
ATOM    693  CA  ALA A  87      42.602  31.835   6.921  1.00 11.11           C  
ATOM    694  C   ALA A  87      43.286  31.334   5.632  1.00 10.68           C  
ATOM    695  O   ALA A  87      44.438  30.854   5.697  1.00 10.35           O  
ATOM    696  CB  ALA A  87      41.818  30.688   7.546  1.00 12.23           C  
ATOM    697  N   ALA A  88      42.610  31.459   4.502  1.00 10.16           N  
ATOM    698  CA  ALA A  88      43.226  30.914   3.248  1.00 10.02           C  
ATOM    699  C   ALA A  88      42.413  31.468   2.098  1.00 10.01           C  
ATOM    700  O   ALA A  88      41.243  31.795   2.307  1.00  9.15           O  
ATOM    701  CB  ALA A  88      43.265  29.405   3.240  1.00 10.15           C  
ATOM    702  N   THR A  89      43.029  31.514   0.922  1.00  9.31           N  
ATOM    703  CA  THR A  89      42.279  31.994  -0.245  1.00  9.33           C  
ATOM    704  C   THR A  89      42.665  31.122  -1.457  1.00 10.66           C  
ATOM    705  O   THR A  89      43.752  30.540  -1.444  1.00  8.29           O  
ATOM    706  CB  THR A  89      42.486  33.488  -0.557  1.00 11.86           C  
ATOM    707  OG1 THR A  89      43.850  33.625  -1.060  1.00 14.41           O  
ATOM    708  CG2 THR A  89      42.319  34.444   0.612  1.00 10.53           C  
ATOM    709  N   LYS A  90      41.766  31.139  -2.414  1.00  9.83           N  
ATOM    710  CA  LYS A  90      42.043  30.413  -3.677  1.00 12.40           C  
ATOM    711  C   LYS A  90      41.429  31.219  -4.803  1.00 12.13           C  
ATOM    712  O   LYS A  90      40.231  31.565  -4.772  1.00 12.88           O  
ATOM    713  CB  LYS A  90      41.542  28.998  -3.639  1.00 13.92           C  
ATOM    714  CG  LYS A  90      42.280  28.042  -4.648  1.00 18.71           C  
ATOM    715  CD  LYS A  90      41.774  28.232  -6.032  1.00 20.82           C  
ATOM    716  CE  LYS A  90      42.572  27.446  -7.107  1.00 21.79           C  
ATOM    717  NZ  LYS A  90      43.823  28.243  -7.408  1.00 21.88           N  
ATOM    718  N   VAL A  91      42.254  31.573  -5.775  1.00 11.97           N  
ATOM    719  CA  VAL A  91      41.773  32.339  -6.936  1.00 13.03           C  
ATOM    720  C   VAL A  91      41.590  31.432  -8.159  1.00 14.74           C  
ATOM    721  O   VAL A  91      42.479  30.601  -8.447  1.00 15.31           O  
ATOM    722  CB  VAL A  91      42.808  33.448  -7.245  1.00 12.85           C  
ATOM    723  CG1 VAL A  91      42.346  34.297  -8.423  1.00 14.18           C  
ATOM    724  CG2 VAL A  91      43.129  34.344  -6.073  1.00 14.09           C  
ATOM    725  N   GLY A  92      40.469  31.564  -8.838  1.00 15.11           N  
ATOM    726  CA  GLY A  92      40.292  30.805 -10.092  1.00 14.98           C  
ATOM    727  C   GLY A  92      39.498  29.557  -9.912  1.00 16.83           C  
ATOM    728  O   GLY A  92      39.301  29.052  -8.774  1.00 18.24           O  
ATOM    729  N   ALA A  93      38.954  29.048 -11.025  1.00 16.71           N  
ATOM    730  CA  ALA A  93      38.185  27.789 -10.910  1.00 17.49           C  
ATOM    731  C   ALA A  93      39.076  26.617 -10.531  1.00 17.11           C  
ATOM    732  O   ALA A  93      40.320  26.619 -10.672  1.00 16.52           O  
ATOM    733  CB  ALA A  93      37.507  27.529 -12.243  1.00 19.35           C  
ATOM    734  N   LEU A  94      38.448  25.591 -10.015  1.00 17.22           N  
ATOM    735  CA  LEU A  94      39.082  24.368  -9.525  1.00 18.27           C  
ATOM    736  C   LEU A  94      38.034  23.257  -9.531  1.00 18.29           C  
ATOM    737  O   LEU A  94      36.834  23.558  -9.610  1.00 20.10           O  
ATOM    738  CB  LEU A  94      39.698  24.549  -8.135  1.00 18.90           C  
ATOM    739  CG  LEU A  94      38.835  24.570  -6.899  1.00 20.71           C  
ATOM    740  CD1 LEU A  94      39.671  24.836  -5.646  1.00 21.10           C  
ATOM    741  CD2 LEU A  94      37.739  25.625  -7.024  1.00 21.42           C  
ATOM    742  N   SER A  95      38.509  22.049  -9.458  1.00 17.77           N  
ATOM    743  CA  SER A  95      37.643  20.852  -9.439  1.00 19.03           C  
ATOM    744  C   SER A  95      37.182  20.559  -8.028  1.00 19.50           C  
ATOM    745  O   SER A  95      37.769  21.083  -7.044  1.00 17.85           O  
ATOM    746  CB  SER A  95      38.459  19.679 -10.001  1.00 19.60           C  
ATOM    747  OG  SER A  95      39.380  19.220  -9.029  1.00 20.61           O  
ATOM    748  N   LYS A  96      36.127  19.737  -7.927  1.00 18.38           N  
ATOM    749  CA  LYS A  96      35.701  19.325  -6.580  1.00 18.50           C  
ATOM    750  C   LYS A  96      36.822  18.695  -5.757  1.00 18.03           C  
ATOM    751  O   LYS A  96      36.933  18.969  -4.545  1.00 16.89           O  
ATOM    752  CB  LYS A  96      34.541  18.331  -6.661  1.00 20.54           C  
ATOM    753  CG  LYS A  96      33.998  17.930  -5.266  1.00 23.16           C  
ATOM    754  CD  LYS A  96      32.933  16.840  -5.525  1.00 26.86           C  
ATOM    755  CE  LYS A  96      32.488  16.116  -4.292  1.00 29.09           C  
ATOM    756  NZ  LYS A  96      31.232  15.343  -4.606  1.00 32.67           N  
ATOM    757  N   GLY A  97      37.644  17.832  -6.375  1.00 17.44           N  
ATOM    758  CA  GLY A  97      38.720  17.180  -5.608  1.00 17.45           C  
ATOM    759  C   GLY A  97      39.731  18.213  -5.104  1.00 17.05           C  
ATOM    760  O   GLY A  97      40.186  18.049  -3.967  1.00 19.29           O  
ATOM    761  N   GLN A  98      40.049  19.185  -5.879  1.00 15.92           N  
ATOM    762  CA  GLN A  98      41.003  20.249  -5.490  1.00 16.85           C  
ATOM    763  C   GLN A  98      40.380  21.063  -4.375  1.00 15.24           C  
ATOM    764  O   GLN A  98      41.075  21.406  -3.413  1.00 14.70           O  
ATOM    765  CB  GLN A  98      41.349  21.149  -6.665  1.00 18.99           C  
ATOM    766  CG  GLN A  98      42.139  20.418  -7.756  1.00 21.85           C  
ATOM    767  CD  GLN A  98      42.299  21.343  -8.946  1.00 24.29           C  
ATOM    768  OE1 GLN A  98      41.395  21.919  -9.505  1.00 25.13           O  
ATOM    769  NE2 GLN A  98      43.592  21.527  -9.277  1.00 27.89           N  
ATOM    770  N   LEU A  99      39.074  21.339  -4.498  1.00 14.52           N  
ATOM    771  CA  LEU A  99      38.435  22.146  -3.424  1.00 13.74           C  
ATOM    772  C   LEU A  99      38.480  21.419  -2.087  1.00 14.21           C  
ATOM    773  O   LEU A  99      38.739  21.957  -0.980  1.00 14.39           O  
ATOM    774  CB  LEU A  99      37.028  22.567  -3.879  1.00 14.07           C  
ATOM    775  CG  LEU A  99      36.233  23.382  -2.826  1.00 15.28           C  
ATOM    776  CD1 LEU A  99      37.011  24.596  -2.327  1.00 15.20           C  
ATOM    777  CD2 LEU A  99      34.920  23.852  -3.468  1.00 16.76           C  
ATOM    778  N   LYS A 100      38.178  20.117  -2.134  1.00 14.83           N  
ATOM    779  CA  LYS A 100      38.195  19.291  -0.926  1.00 17.25           C  
ATOM    780  C   LYS A 100      39.570  19.305  -0.292  1.00 16.19           C  
ATOM    781  O   LYS A 100      39.711  19.449   0.926  1.00 15.40           O  
ATOM    782  CB  LYS A 100      37.752  17.840  -1.139  1.00 19.67           C  
ATOM    783  CG  LYS A 100      36.229  17.877  -1.349  1.00 24.84           C  
ATOM    784  CD  LYS A 100      35.667  16.524  -1.723  1.00 28.62           C  
ATOM    785  CE  LYS A 100      35.866  15.550  -0.542  1.00 31.48           C  
ATOM    786  NZ  LYS A 100      34.870  14.428  -0.766  1.00 34.70           N  
ATOM    787  N   GLU A 101      40.601  19.184  -1.129  1.00 17.16           N  
ATOM    788  CA  GLU A 101      41.969  19.195  -0.546  1.00 18.15           C  
ATOM    789  C   GLU A 101      42.315  20.538   0.086  1.00 16.50           C  
ATOM    790  O   GLU A 101      42.960  20.633   1.143  1.00 16.77           O  
ATOM    791  CB  GLU A 101      42.979  18.945  -1.641  1.00 22.32           C  
ATOM    792  CG  GLU A 101      43.199  17.512  -2.062  1.00 27.45           C  
ATOM    793  CD  GLU A 101      44.530  17.385  -2.812  1.00 30.43           C  
ATOM    794  OE1 GLU A 101      45.505  16.966  -2.193  1.00 32.98           O  
ATOM    795  OE2 GLU A 101      44.405  17.834  -3.964  1.00 31.71           O  
ATOM    796  N   PHE A 102      41.901  21.595  -0.587  1.00 14.76           N  
ATOM    797  CA  PHE A 102      42.101  22.950  -0.063  1.00 13.09           C  
ATOM    798  C   PHE A 102      41.367  23.076   1.276  1.00 13.38           C  
ATOM    799  O   PHE A 102      41.949  23.650   2.209  1.00 14.41           O  
ATOM    800  CB  PHE A 102      41.643  23.981  -1.084  1.00 13.54           C  
ATOM    801  CG  PHE A 102      41.539  25.386  -0.613  1.00 13.43           C  
ATOM    802  CD1 PHE A 102      40.329  25.914  -0.147  1.00 14.79           C  
ATOM    803  CD2 PHE A 102      42.676  26.182  -0.631  1.00 14.85           C  
ATOM    804  CE1 PHE A 102      40.247  27.240   0.266  1.00 15.75           C  
ATOM    805  CE2 PHE A 102      42.606  27.522  -0.215  1.00 14.75           C  
ATOM    806  CZ  PHE A 102      41.415  28.037   0.263  1.00 15.61           C  
ATOM    807  N   LEU A 103      40.120  22.586   1.350  1.00 13.41           N  
ATOM    808  CA  LEU A 103      39.410  22.700   2.656  1.00 14.15           C  
ATOM    809  C   LEU A 103      40.055  21.873   3.740  1.00 15.45           C  
ATOM    810  O   LEU A 103      40.251  22.311   4.896  1.00 16.18           O  
ATOM    811  CB  LEU A 103      37.932  22.366   2.474  1.00 13.82           C  
ATOM    812  CG  LEU A 103      37.181  23.342   1.578  1.00 15.30           C  
ATOM    813  CD1 LEU A 103      35.830  22.720   1.212  1.00 14.22           C  
ATOM    814  CD2 LEU A 103      37.030  24.669   2.306  1.00 15.21           C  
ATOM    815  N   ASP A 104      40.362  20.632   3.377  1.00 17.99           N  
ATOM    816  CA  ASP A 104      40.924  19.710   4.407  1.00 19.48           C  
ATOM    817  C   ASP A 104      42.228  20.243   4.975  1.00 20.07           C  
ATOM    818  O   ASP A 104      42.499  20.025   6.159  1.00 20.72           O  
ATOM    819  CB  ASP A 104      41.059  18.289   3.858  1.00 21.94           C  
ATOM    820  CG  ASP A 104      39.666  17.719   3.612  1.00 24.56           C  
ATOM    821  OD1 ASP A 104      38.631  18.256   4.015  1.00 25.10           O  
ATOM    822  OD2 ASP A 104      39.677  16.690   2.876  1.00 27.45           O  
ATOM    823  N   ALA A 105      43.038  20.916   4.183  1.00 19.24           N  
ATOM    824  CA  ALA A 105      44.278  21.547   4.617  1.00 19.04           C  
ATOM    825  C   ALA A 105      44.054  22.641   5.643  1.00 21.27           C  
ATOM    826  O   ALA A 105      45.012  22.973   6.371  1.00 20.85           O  
ATOM    827  CB  ALA A 105      45.048  22.144   3.421  1.00 18.17           C  
ATOM    828  N   ASN A 106      42.843  23.210   5.657  1.00 20.25           N  
ATOM    829  CA  ASN A 106      42.587  24.329   6.538  1.00 22.59           C  
ATOM    830  C   ASN A 106      41.570  24.027   7.617  1.00 25.74           C  
ATOM    831  O   ASN A 106      41.434  24.979   8.427  1.00 27.14           O  
ATOM    832  CB  ASN A 106      42.041  25.562   5.767  1.00 21.45           C  
ATOM    833  CG  ASN A 106      43.074  26.085   4.824  1.00 21.12           C  
ATOM    834  OD1 ASN A 106      43.982  26.759   5.351  1.00 22.28           O  
ATOM    835  ND2 ASN A 106      43.055  25.826   3.528  1.00 21.39           N  
ATOM    836  N   LEU A 107      40.919  22.900   7.599  1.00 29.33           N  
ATOM    837  CA  LEU A 107      39.812  22.787   8.605  1.00 34.50           C  
ATOM    838  C   LEU A 107      40.275  22.037   9.847  1.00 39.17           C  
ATOM    839  O   LEU A 107      39.571  22.111  10.885  1.00 41.13           O  
ATOM    840  CB  LEU A 107      38.573  22.199   7.965  1.00 33.33           C  
ATOM    841  CG  LEU A 107      37.838  23.048   6.951  1.00 33.80           C  
ATOM    842  CD1 LEU A 107      36.655  22.236   6.405  1.00 33.67           C  
ATOM    843  CD2 LEU A 107      37.366  24.327   7.605  1.00 33.80           C  
ATOM    844  N   ALA A 108      41.357  21.341   9.676  1.00 42.93           N  
ATOM    845  CA  ALA A 108      42.151  20.619  10.674  1.00 46.31           C  
ATOM    846  C   ALA A 108      42.632  19.312  10.013  1.00 48.21           C  
ATOM    847  O   ALA A 108      41.703  18.483   9.767  1.00 49.54           O  
ATOM    848  CB  ALA A 108      41.441  20.369  11.988  1.00 46.65           C  
ATOM    849  OXT ALA A 108      43.857  19.249   9.766  1.00 49.19           O  
TER     850      ALA A 108                                                      
ATOM    851  N   SER B   1       9.147  31.220  23.823  1.00 28.73           N  
ATOM    852  CA  SER B   1       9.382  32.527  24.427  1.00 30.33           C  
ATOM    853  C   SER B   1       8.629  32.863  25.689  1.00 29.90           C  
ATOM    854  O   SER B   1       8.743  34.011  26.208  1.00 30.15           O  
ATOM    855  CB  SER B   1       9.073  33.599  23.355  1.00 32.50           C  
ATOM    856  OG  SER B   1       9.769  33.144  22.172  1.00 36.47           O  
ATOM    857  N   ASP B   2       7.883  31.951  26.267  1.00 28.77           N  
ATOM    858  CA  ASP B   2       7.110  32.139  27.471  1.00 27.48           C  
ATOM    859  C   ASP B   2       8.046  32.352  28.660  1.00 25.85           C  
ATOM    860  O   ASP B   2       7.596  32.992  29.606  1.00 26.04           O  
ATOM    861  CB  ASP B   2       6.172  30.931  27.676  1.00 29.16           C  
ATOM    862  CG  ASP B   2       6.940  29.664  27.972  1.00 29.86           C  
ATOM    863  OD1 ASP B   2       7.791  29.210  27.188  1.00 30.68           O  
ATOM    864  OD2 ASP B   2       6.754  29.090  29.071  1.00 30.62           O  
ATOM    865  N   LYS B   3       9.274  31.864  28.610  1.00 24.79           N  
ATOM    866  CA  LYS B   3      10.143  32.018  29.811  1.00 25.00           C  
ATOM    867  C   LYS B   3      11.253  33.059  29.615  1.00 24.31           C  
ATOM    868  O   LYS B   3      12.170  33.065  30.435  1.00 24.69           O  
ATOM    869  CB  LYS B   3      10.778  30.698  30.247  1.00 26.05           C  
ATOM    870  CG  LYS B   3       9.738  29.706  30.773  1.00 28.33           C  
ATOM    871  CD  LYS B   3      10.289  28.323  31.108  1.00 30.13           C  
ATOM    872  CE  LYS B   3       9.118  27.342  31.326  1.00 31.62           C  
ATOM    873  NZ  LYS B   3       8.753  26.735  30.022  1.00 32.41           N  
ATOM    874  N   ILE B   4      11.123  33.874  28.621  1.00 23.10           N  
ATOM    875  CA  ILE B   4      12.111  34.962  28.375  1.00 22.91           C  
ATOM    876  C   ILE B   4      11.612  36.321  28.792  1.00 22.37           C  
ATOM    877  O   ILE B   4      10.453  36.664  28.426  1.00 23.92           O  
ATOM    878  CB  ILE B   4      12.557  34.804  26.875  1.00 23.31           C  
ATOM    879  CG1 ILE B   4      13.229  33.424  26.789  1.00 24.24           C  
ATOM    880  CG2 ILE B   4      13.480  35.995  26.497  1.00 22.00           C  
ATOM    881  CD1 ILE B   4      13.937  32.992  25.520  1.00 26.30           C  
ATOM    882  N   ILE B   5      12.367  37.081  29.554  1.00 21.10           N  
ATOM    883  CA  ILE B   5      12.027  38.440  29.972  1.00 23.29           C  
ATOM    884  C   ILE B   5      12.372  39.429  28.838  1.00 23.28           C  
ATOM    885  O   ILE B   5      13.474  39.356  28.267  1.00 21.93           O  
ATOM    886  CB  ILE B   5      12.795  38.902  31.264  1.00 24.85           C  
ATOM    887  CG1 ILE B   5      12.724  37.963  32.455  1.00 27.62           C  
ATOM    888  CG2 ILE B   5      12.349  40.346  31.673  1.00 27.13           C  
ATOM    889  CD1 ILE B   5      11.346  37.388  32.799  1.00 28.69           C  
ATOM    890  N  AHIS B   6      11.446  40.298  28.479  0.50 23.56           N  
ATOM    891  N  BHIS B   6      11.456  40.335  28.600  0.50 23.88           N  
ATOM    892  CA AHIS B   6      11.783  41.302  27.424  0.50 23.82           C  
ATOM    893  CA BHIS B   6      11.499  41.454  27.655  0.50 24.43           C  
ATOM    894  C  AHIS B   6      12.112  42.569  28.198  0.50 23.83           C  
ATOM    895  C  BHIS B   6      12.099  42.667  28.345  0.50 24.22           C  
ATOM    896  O  AHIS B   6      11.293  43.004  29.019  0.50 24.90           O  
ATOM    897  O  BHIS B   6      11.409  43.240  29.220  0.50 25.13           O  
ATOM    898  CB AHIS B   6      10.723  41.492  26.337  0.50 25.05           C  
ATOM    899  CB BHIS B   6      10.083  41.863  27.152  0.50 26.02           C  
ATOM    900  CG AHIS B   6      10.753  40.389  25.310  0.50 25.47           C  
ATOM    901  CG BHIS B   6      10.031  43.189  26.458  0.50 27.28           C  
ATOM    902  ND1AHIS B   6      10.205  39.140  25.505  0.50 25.64           N  
ATOM    903  ND1BHIS B   6      10.441  43.381  25.160  0.50 28.24           N  
ATOM    904  CD2AHIS B   6      11.291  40.384  24.070  0.50 25.75           C  
ATOM    905  CD2BHIS B   6       9.615  44.403  26.911  0.50 27.64           C  
ATOM    906  CE1AHIS B   6      10.408  38.411  24.421  0.50 25.78           C  
ATOM    907  CE1BHIS B   6      10.271  44.649  24.848  0.50 27.81           C  
ATOM    908  NE2AHIS B   6      11.070  39.138  23.542  0.50 26.15           N  
ATOM    909  NE2BHIS B   6       9.778  45.294  25.877  0.50 27.98           N  
ATOM    910  N   LEU B   7      13.299  43.080  27.978  1.00 22.96           N  
ATOM    911  CA  LEU B   7      13.863  44.251  28.660  1.00 21.75           C  
ATOM    912  C   LEU B   7      13.666  45.510  27.788  1.00 22.36           C  
ATOM    913  O   LEU B   7      13.390  45.374  26.588  1.00 21.99           O  
ATOM    914  CB  LEU B   7      15.336  44.010  28.935  1.00 21.16           C  
ATOM    915  CG  LEU B   7      15.746  42.851  29.806  1.00 21.24           C  
ATOM    916  CD1 LEU B   7      17.266  42.779  29.919  1.00 20.64           C  
ATOM    917  CD2 LEU B   7      15.148  43.035  31.208  1.00 22.44           C  
ATOM    918  N   THR B   8      13.846  46.641  28.484  1.00 23.64           N  
ATOM    919  CA  THR B   8      13.814  47.943  27.774  1.00 23.56           C  
ATOM    920  C   THR B   8      14.959  48.762  28.296  1.00 23.75           C  
ATOM    921  O   THR B   8      15.655  48.358  29.271  1.00 23.54           O  
ATOM    922  CB  THR B   8      12.425  48.698  27.922  1.00 23.99           C  
ATOM    923  OG1 THR B   8      12.325  49.049  29.323  1.00 25.13           O  
ATOM    924  CG2 THR B   8      11.212  47.933  27.427  1.00 24.53           C  
ATOM    925  N   ASP B   9      15.161  49.941  27.696  1.00 23.67           N  
ATOM    926  CA  ASP B   9      16.280  50.793  28.171  1.00 24.42           C  
ATOM    927  C   ASP B   9      16.145  51.125  29.656  1.00 25.42           C  
ATOM    928  O   ASP B   9      17.187  51.347  30.308  1.00 25.84           O  
ATOM    929  CB  ASP B   9      16.421  52.028  27.283  1.00 25.00           C  
ATOM    930  CG  ASP B   9      17.108  51.709  25.964  1.00 26.51           C  
ATOM    931  OD1 ASP B   9      16.781  52.371  24.953  1.00 25.75           O  
ATOM    932  OD2 ASP B   9      17.970  50.789  25.891  1.00 25.82           O  
ATOM    933  N   ASP B  10      14.961  51.165  30.191  1.00 27.35           N  
ATOM    934  CA  ASP B  10      14.725  51.490  31.621  1.00 29.00           C  
ATOM    935  C   ASP B  10      15.036  50.362  32.601  1.00 30.33           C  
ATOM    936  O   ASP B  10      14.916  50.561  33.840  1.00 29.31           O  
ATOM    937  CB  ASP B  10      13.297  52.052  31.738  1.00 28.66           C  
ATOM    938  CG  ASP B  10      13.137  53.452  31.119  1.00 29.28           C  
ATOM    939  OD1 ASP B  10      11.971  53.755  30.734  1.00 28.41           O  
ATOM    940  OD2 ASP B  10      14.085  54.248  30.968  1.00 28.39           O  
ATOM    941  N   SER B  11      15.528  49.207  32.157  1.00 31.34           N  
ATOM    942  CA  SER B  11      15.883  48.030  32.953  1.00 32.46           C  
ATOM    943  C   SER B  11      17.272  48.047  33.588  1.00 33.52           C  
ATOM    944  O   SER B  11      17.735  47.184  34.340  1.00 32.70           O  
ATOM    945  CB  SER B  11      15.916  46.836  31.976  1.00 31.90           C  
ATOM    946  OG  SER B  11      14.538  46.575  31.754  1.00 32.01           O  
ATOM    947  N   PHE B  12      17.955  49.052  33.132  1.00 35.22           N  
ATOM    948  CA  PHE B  12      19.393  49.232  33.506  1.00 39.37           C  
ATOM    949  C   PHE B  12      19.233  50.378  34.510  1.00 44.08           C  
ATOM    950  O   PHE B  12      19.282  51.562  34.205  1.00 44.75           O  
ATOM    951  CB  PHE B  12      20.244  49.258  32.262  1.00 35.57           C  
ATOM    952  CG  PHE B  12      20.263  47.918  31.537  1.00 32.41           C  
ATOM    953  CD1 PHE B  12      19.211  47.535  30.713  1.00 30.40           C  
ATOM    954  CD2 PHE B  12      21.338  47.046  31.715  1.00 31.15           C  
ATOM    955  CE1 PHE B  12      19.223  46.311  30.069  1.00 29.36           C  
ATOM    956  CE2 PHE B  12      21.381  45.823  31.060  1.00 29.58           C  
ATOM    957  CZ  PHE B  12      20.312  45.448  30.230  1.00 29.00           C  
ATOM    958  N   ASP B  13      18.857  49.806  35.646  1.00 49.90           N  
ATOM    959  CA  ASP B  13      18.489  50.349  36.947  1.00 54.42           C  
ATOM    960  C   ASP B  13      17.366  49.469  37.532  1.00 55.98           C  
ATOM    961  O   ASP B  13      16.664  50.017  38.431  1.00 56.85           O  
ATOM    962  CB  ASP B  13      18.081  51.821  36.843  1.00 56.28           C  
ATOM    963  CG  ASP B  13      18.222  52.724  38.044  1.00 57.90           C  
ATOM    964  OD1 ASP B  13      17.254  52.984  38.798  1.00 58.64           O  
ATOM    965  OD2 ASP B  13      19.358  53.249  38.229  1.00 58.64           O  
ATOM    966  N   THR B  14      17.171  48.215  37.096  1.00 56.82           N  
ATOM    967  CA  THR B  14      15.955  47.514  37.600  1.00 57.90           C  
ATOM    968  C   THR B  14      15.967  45.998  37.448  1.00 58.03           C  
ATOM    969  O   THR B  14      16.352  45.228  38.352  1.00 57.15           O  
ATOM    970  CB  THR B  14      14.629  48.105  36.945  1.00 58.39           C  
ATOM    971  OG1 THR B  14      14.517  49.533  37.254  1.00 59.28           O  
ATOM    972  CG2 THR B  14      13.324  47.405  37.368  1.00 58.42           C  
ATOM    973  N   ASP B  15      15.478  45.565  36.289  1.00 57.93           N  
ATOM    974  CA  ASP B  15      15.365  44.178  35.865  1.00 58.36           C  
ATOM    975  C   ASP B  15      16.733  43.509  35.667  1.00 57.97           C  
ATOM    976  O   ASP B  15      16.749  42.261  35.470  1.00 58.43           O  
ATOM    977  CB  ASP B  15      14.532  44.014  34.586  1.00 58.90           C  
ATOM    978  CG  ASP B  15      13.040  44.088  34.751  1.00 59.73           C  
ATOM    979  OD1 ASP B  15      12.476  43.913  35.835  1.00 59.94           O  
ATOM    980  OD2 ASP B  15      12.411  44.356  33.694  1.00 60.52           O  
ATOM    981  N   VAL B  16      17.837  44.240  35.646  1.00 57.05           N  
ATOM    982  CA  VAL B  16      19.140  43.552  35.516  1.00 55.61           C  
ATOM    983  C   VAL B  16      20.120  44.096  36.551  1.00 55.40           C  
ATOM    984  O   VAL B  16      20.825  43.252  37.151  1.00 55.79           O  
ATOM    985  CB  VAL B  16      19.717  43.502  34.107  1.00 55.03           C  
ATOM    986  CG1 VAL B  16      20.631  42.275  33.964  1.00 54.62           C  
ATOM    987  CG2 VAL B  16      18.673  43.496  33.012  1.00 54.86           C  
ATOM    988  N   LEU B  17      20.130  45.390  36.794  1.00 54.05           N  
ATOM    989  CA  LEU B  17      21.151  45.828  37.785  1.00 53.84           C  
ATOM    990  C   LEU B  17      20.629  45.718  39.200  1.00 54.29           C  
ATOM    991  O   LEU B  17      21.348  45.449  40.202  1.00 53.78           O  
ATOM    992  CB  LEU B  17      21.601  47.195  37.284  1.00 54.03           C  
ATOM    993  CG  LEU B  17      21.728  47.374  35.777  1.00 53.38           C  
ATOM    994  CD1 LEU B  17      22.276  48.763  35.507  1.00 53.41           C  
ATOM    995  CD2 LEU B  17      22.647  46.303  35.213  1.00 52.70           C  
ATOM    996  N   LYS B  18      19.303  45.975  39.283  1.00 54.33           N  
ATOM    997  CA  LYS B  18      18.682  45.827  40.644  1.00 53.18           C  
ATOM    998  C   LYS B  18      18.474  44.310  40.791  1.00 50.91           C  
ATOM    999  O   LYS B  18      18.732  43.733  41.855  1.00 51.64           O  
ATOM   1000  CB  LYS B  18      17.408  46.587  40.850  1.00 54.78           C  
ATOM   1001  CG  LYS B  18      17.340  48.081  41.049  1.00 56.27           C  
ATOM   1002  CD  LYS B  18      18.523  48.890  40.582  1.00 57.49           C  
ATOM   1003  CE  LYS B  18      19.562  49.192  41.628  1.00 58.73           C  
ATOM   1004  NZ  LYS B  18      19.988  48.032  42.458  1.00 59.16           N  
ATOM   1005  N   ALA B  19      18.042  43.764  39.644  1.00 47.12           N  
ATOM   1006  CA  ALA B  19      17.785  42.334  39.562  1.00 43.51           C  
ATOM   1007  C   ALA B  19      19.040  41.584  40.037  1.00 41.07           C  
ATOM   1008  O   ALA B  19      20.108  41.836  39.456  1.00 40.82           O  
ATOM   1009  CB  ALA B  19      17.516  41.850  38.179  1.00 43.27           C  
ATOM   1010  N   ASP B  20      18.787  40.740  41.008  1.00 36.80           N  
ATOM   1011  CA  ASP B  20      19.888  39.898  41.514  1.00 33.96           C  
ATOM   1012  C   ASP B  20      19.881  38.628  40.646  1.00 29.83           C  
ATOM   1013  O   ASP B  20      19.143  38.530  39.626  1.00 31.26           O  
ATOM   1014  CB  ASP B  20      19.734  39.659  43.003  1.00 34.57           C  
ATOM   1015  CG  ASP B  20      18.705  38.592  43.318  1.00 36.60           C  
ATOM   1016  OD1 ASP B  20      18.831  37.718  44.181  1.00 37.32           O  
ATOM   1017  OD2 ASP B  20      17.681  38.610  42.576  1.00 38.18           O  
ATOM   1018  N   GLY B  21      20.675  37.664  41.060  1.00 25.13           N  
ATOM   1019  CA  GLY B  21      20.759  36.386  40.383  1.00 20.45           C  
ATOM   1020  C   GLY B  21      21.557  36.567  39.065  1.00 17.60           C  
ATOM   1021  O   GLY B  21      22.094  37.635  38.764  1.00 16.99           O  
ATOM   1022  N   ALA B  22      21.617  35.450  38.397  1.00 15.06           N  
ATOM   1023  CA  ALA B  22      22.410  35.350  37.142  1.00 13.28           C  
ATOM   1024  C   ALA B  22      21.386  35.532  36.005  1.00 13.13           C  
ATOM   1025  O   ALA B  22      20.373  34.831  35.948  1.00 13.37           O  
ATOM   1026  CB  ALA B  22      23.102  34.015  37.078  1.00 13.83           C  
ATOM   1027  N   ILE B  23      21.692  36.457  35.117  1.00 11.03           N  
ATOM   1028  CA  ILE B  23      20.818  36.806  34.011  1.00 12.13           C  
ATOM   1029  C   ILE B  23      21.646  36.846  32.701  1.00 10.35           C  
ATOM   1030  O   ILE B  23      22.654  37.554  32.713  1.00 10.59           O  
ATOM   1031  CB  ILE B  23      20.152  38.192  34.228  1.00 14.81           C  
ATOM   1032  CG1 ILE B  23      19.431  38.167  35.616  1.00 18.20           C  
ATOM   1033  CG2 ILE B  23      19.145  38.512  33.081  1.00 15.27           C  
ATOM   1034  CD1 ILE B  23      19.138  39.649  36.001  1.00 20.91           C  
ATOM   1035  N   LEU B  24      21.115  36.179  31.717  1.00  9.11           N  
ATOM   1036  CA  LEU B  24      21.806  36.146  30.397  1.00  8.10           C  
ATOM   1037  C   LEU B  24      20.983  37.061  29.486  1.00 10.08           C  
ATOM   1038  O   LEU B  24      19.775  36.732  29.370  1.00 10.45           O  
ATOM   1039  CB  LEU B  24      21.868  34.701  29.931  1.00 10.04           C  
ATOM   1040  CG  LEU B  24      22.474  34.535  28.520  1.00 11.55           C  
ATOM   1041  CD1 LEU B  24      23.986  34.780  28.622  1.00 13.90           C  
ATOM   1042  CD2 LEU B  24      22.140  33.094  28.102  1.00 12.35           C  
ATOM   1043  N   VAL B  25      21.557  38.100  28.931  1.00  8.99           N  
ATOM   1044  CA  VAL B  25      20.807  39.066  28.102  1.00  8.92           C  
ATOM   1045  C   VAL B  25      21.278  38.951  26.652  1.00 10.20           C  
ATOM   1046  O   VAL B  25      22.478  39.078  26.394  1.00 11.05           O  
ATOM   1047  CB  VAL B  25      21.018  40.509  28.593  1.00  9.27           C  
ATOM   1048  CG1 VAL B  25      20.251  41.526  27.736  1.00 10.50           C  
ATOM   1049  CG2 VAL B  25      20.639  40.664  30.076  1.00 10.68           C  
ATOM   1050  N   ASP B  26      20.299  38.712  25.786  1.00  9.98           N  
ATOM   1051  CA  ASP B  26      20.583  38.656  24.317  1.00  9.27           C  
ATOM   1052  C   ASP B  26      20.221  40.029  23.687  1.00 10.64           C  
ATOM   1053  O   ASP B  26      19.047  40.444  23.769  1.00 11.97           O  
ATOM   1054  CB  ASP B  26      19.760  37.509  23.763  1.00 10.63           C  
ATOM   1055  CG  ASP B  26      19.680  37.399  22.260  1.00 12.39           C  
ATOM   1056  OD1 ASP B  26      18.629  36.880  21.781  1.00 14.48           O  
ATOM   1057  OD2 ASP B  26      20.626  37.761  21.537  1.00 15.07           O  
ATOM   1058  N   PHE B  27      21.251  40.662  23.125  1.00  9.89           N  
ATOM   1059  CA  PHE B  27      21.005  41.909  22.319  1.00 10.90           C  
ATOM   1060  C   PHE B  27      20.802  41.462  20.873  1.00 11.23           C  
ATOM   1061  O   PHE B  27      21.679  40.772  20.329  1.00 12.58           O  
ATOM   1062  CB  PHE B  27      22.216  42.822  22.470  1.00 11.18           C  
ATOM   1063  CG  PHE B  27      22.334  43.456  23.808  1.00 12.81           C  
ATOM   1064  CD1 PHE B  27      21.958  44.799  23.997  1.00 14.43           C  
ATOM   1065  CD2 PHE B  27      22.773  42.734  24.913  1.00 14.10           C  
ATOM   1066  CE1 PHE B  27      22.069  45.416  25.234  1.00 14.57           C  
ATOM   1067  CE2 PHE B  27      22.870  43.322  26.185  1.00 14.69           C  
ATOM   1068  CZ  PHE B  27      22.522  44.672  26.334  1.00 14.42           C  
ATOM   1069  N   TRP B  28      19.649  41.814  20.280  1.00 12.40           N  
ATOM   1070  CA  TRP B  28      19.285  41.313  18.950  1.00 12.31           C  
ATOM   1071  C   TRP B  28      18.428  42.368  18.215  1.00 12.07           C  
ATOM   1072  O   TRP B  28      18.046  43.385  18.783  1.00 13.39           O  
ATOM   1073  CB  TRP B  28      18.488  39.995  19.101  1.00 13.10           C  
ATOM   1074  CG  TRP B  28      17.112  40.231  19.662  1.00 13.68           C  
ATOM   1075  CD1 TRP B  28      16.719  40.658  20.888  1.00 14.49           C  
ATOM   1076  CD2 TRP B  28      15.872  40.156  18.909  1.00 15.17           C  
ATOM   1077  NE1 TRP B  28      15.353  40.817  20.984  1.00 15.26           N  
ATOM   1078  CE2 TRP B  28      14.841  40.523  19.752  1.00 14.78           C  
ATOM   1079  CE3 TRP B  28      15.616  39.827  17.569  1.00 16.80           C  
ATOM   1080  CZ2 TRP B  28      13.501  40.577  19.351  1.00 16.41           C  
ATOM   1081  CZ3 TRP B  28      14.295  39.862  17.157  1.00 18.01           C  
ATOM   1082  CH2 TRP B  28      13.245  40.219  18.025  1.00 17.26           C  
ATOM   1083  N   ALA B  29      18.226  41.996  16.970  1.00 13.18           N  
ATOM   1084  CA  ALA B  29      17.313  42.786  16.087  1.00 15.93           C  
ATOM   1085  C   ALA B  29      16.715  41.819  15.067  1.00 16.58           C  
ATOM   1086  O   ALA B  29      17.303  40.764  14.786  1.00 16.49           O  
ATOM   1087  CB  ALA B  29      18.070  43.924  15.428  1.00 14.90           C  
ATOM   1088  N   GLU B  30      15.576  42.223  14.494  1.00 20.22           N  
ATOM   1089  CA  GLU B  30      14.864  41.297  13.586  1.00 22.57           C  
ATOM   1090  C   GLU B  30      15.566  41.105  12.270  1.00 21.64           C  
ATOM   1091  O   GLU B  30      15.416  40.047  11.616  1.00 21.37           O  
ATOM   1092  CB  GLU B  30      13.388  41.731  13.413  1.00 27.83           C  
ATOM   1093  CG  GLU B  30      12.475  41.166  14.499  1.00 34.91           C  
ATOM   1094  CD  GLU B  30      11.126  41.683  14.846  1.00 39.12           C  
ATOM   1095  OE1 GLU B  30      10.663  42.791  14.528  1.00 41.76           O  
ATOM   1096  OE2 GLU B  30      10.448  40.860  15.556  1.00 40.13           O  
ATOM   1097  N   TRP B  31      16.390  42.081  11.922  1.00 20.25           N  
ATOM   1098  CA  TRP B  31      17.109  41.963  10.629  1.00 21.17           C  
ATOM   1099  C   TRP B  31      18.357  41.097  10.711  1.00 20.43           C  
ATOM   1100  O   TRP B  31      19.042  40.835   9.720  1.00 21.85           O  
ATOM   1101  CB  TRP B  31      17.446  43.396  10.222  1.00 20.96           C  
ATOM   1102  CG  TRP B  31      18.060  44.280  11.245  1.00 20.73           C  
ATOM   1103  CD1 TRP B  31      17.421  45.185  12.044  1.00 20.45           C  
ATOM   1104  CD2 TRP B  31      19.443  44.374  11.587  1.00 21.47           C  
ATOM   1105  NE1 TRP B  31      18.335  45.849  12.841  1.00 21.22           N  
ATOM   1106  CE2 TRP B  31      19.577  45.366  12.575  1.00 21.55           C  
ATOM   1107  CE3 TRP B  31      20.586  43.701  11.140  1.00 22.15           C  
ATOM   1108  CZ2 TRP B  31      20.792  45.717  13.164  1.00 21.26           C  
ATOM   1109  CZ3 TRP B  31      21.800  44.070  11.727  1.00 21.99           C  
ATOM   1110  CH2 TRP B  31      21.904  45.064  12.690  1.00 21.21           C  
ATOM   1111  N   CYS B  32      18.705  40.603  11.897  1.00 18.22           N  
ATOM   1112  CA  CYS B  32      19.956  39.881  12.161  1.00 16.70           C  
ATOM   1113  C   CYS B  32      19.742  38.381  12.015  1.00 16.37           C  
ATOM   1114  O   CYS B  32      19.042  37.756  12.830  1.00 16.23           O  
ATOM   1115  CB  CYS B  32      20.376  40.283  13.580  1.00 16.47           C  
ATOM   1116  SG  CYS B  32      21.690  39.258  14.277  1.00 15.96           S  
ATOM   1117  N   GLY B  33      20.316  37.821  10.952  1.00 16.20           N  
ATOM   1118  CA  GLY B  33      20.168  36.408  10.671  1.00 15.83           C  
ATOM   1119  C   GLY B  33      20.612  35.502  11.813  1.00 16.74           C  
ATOM   1120  O   GLY B  33      19.833  34.648  12.289  1.00 17.19           O  
ATOM   1121  N   PRO B  34      21.854  35.630  12.213  1.00 15.83           N  
ATOM   1122  CA  PRO B  34      22.392  34.814  13.325  1.00 16.19           C  
ATOM   1123  C   PRO B  34      21.573  35.014  14.601  1.00 15.21           C  
ATOM   1124  O   PRO B  34      21.503  34.056  15.406  1.00 15.72           O  
ATOM   1125  CB  PRO B  34      23.848  35.237  13.440  1.00 16.11           C  
ATOM   1126  CG  PRO B  34      24.173  35.857  12.095  1.00 16.18           C  
ATOM   1127  CD  PRO B  34      22.894  36.540  11.665  1.00 16.46           C  
ATOM   1128  N   CYS B  35      20.961  36.179  14.773  1.00 14.11           N  
ATOM   1129  CA  CYS B  35      20.119  36.409  15.973  1.00 15.07           C  
ATOM   1130  C   CYS B  35      18.921  35.468  15.978  1.00 17.96           C  
ATOM   1131  O   CYS B  35      18.576  34.877  17.011  1.00 17.56           O  
ATOM   1132  CB  CYS B  35      19.606  37.839  16.048  1.00 15.47           C  
ATOM   1133  SG  CYS B  35      20.968  38.954  16.173  1.00 15.77           S  
ATOM   1134  N   LYS B  36      18.302  35.338  14.804  1.00 17.56           N  
ATOM   1135  CA  LYS B  36      17.182  34.396  14.660  1.00 20.79           C  
ATOM   1136  C   LYS B  36      17.572  32.963  14.866  1.00 20.42           C  
ATOM   1137  O   LYS B  36      16.756  32.179  15.418  1.00 20.93           O  
ATOM   1138  CB  LYS B  36      16.546  34.577  13.246  1.00 23.86           C  
ATOM   1139  CG  LYS B  36      15.959  36.005  13.224  1.00 28.07           C  
ATOM   1140  CD  LYS B  36      14.806  36.135  12.223  1.00 32.27           C  
ATOM   1141  CE  LYS B  36      15.197  37.006  11.055  1.00 35.17           C  
ATOM   1142  NZ  LYS B  36      14.011  37.678  10.441  1.00 37.64           N  
ATOM   1143  N   MET B  37      18.742  32.551  14.449  1.00 21.73           N  
ATOM   1144  CA  MET B  37      19.253  31.197  14.593  1.00 24.57           C  
ATOM   1145  C   MET B  37      19.372  30.822  16.066  1.00 22.92           C  
ATOM   1146  O   MET B  37      19.152  29.643  16.410  1.00 23.67           O  
ATOM   1147  CB  MET B  37      20.601  31.008  13.880  1.00 28.25           C  
ATOM   1148  CG  MET B  37      20.421  31.168  12.383  1.00 34.60           C  
ATOM   1149  SD  MET B  37      22.066  30.951  11.561  1.00 41.63           S  
ATOM   1150  CE  MET B  37      21.967  32.278  10.324  1.00 40.29           C  
ATOM   1151  N   ILE B  38      19.742  31.786  16.922  1.00 19.90           N  
ATOM   1152  CA  ILE B  38      19.897  31.406  18.329  1.00 18.94           C  
ATOM   1153  C   ILE B  38      18.627  31.492  19.144  1.00 17.92           C  
ATOM   1154  O   ILE B  38      18.627  30.947  20.276  1.00 16.77           O  
ATOM   1155  CB  ILE B  38      21.108  32.140  19.030  1.00 18.68           C  
ATOM   1156  CG1 ILE B  38      20.827  33.631  19.187  1.00 18.42           C  
ATOM   1157  CG2 ILE B  38      22.439  31.835  18.290  1.00 19.54           C  
ATOM   1158  CD1 ILE B  38      21.845  34.380  20.109  1.00 20.27           C  
ATOM   1159  N   ALA B  39      17.564  32.065  18.639  1.00 17.67           N  
ATOM   1160  CA  ALA B  39      16.349  32.190  19.469  1.00 18.49           C  
ATOM   1161  C   ALA B  39      15.820  30.885  20.016  1.00 19.29           C  
ATOM   1162  O   ALA B  39      15.485  30.849  21.235  1.00 18.27           O  
ATOM   1163  CB  ALA B  39      15.295  32.990  18.699  1.00 19.13           C  
ATOM   1164  N   PRO B  40      15.733  29.814  19.263  1.00 19.99           N  
ATOM   1165  CA  PRO B  40      15.234  28.546  19.797  1.00 20.07           C  
ATOM   1166  C   PRO B  40      16.176  27.976  20.847  1.00 20.07           C  
ATOM   1167  O   PRO B  40      15.706  27.252  21.762  1.00 20.18           O  
ATOM   1168  CB  PRO B  40      15.125  27.613  18.604  1.00 20.85           C  
ATOM   1169  CG  PRO B  40      15.981  28.255  17.538  1.00 22.17           C  
ATOM   1170  CD  PRO B  40      15.909  29.760  17.793  1.00 21.60           C  
ATOM   1171  N   ILE B  41      17.472  28.227  20.671  1.00 18.08           N  
ATOM   1172  CA  ILE B  41      18.433  27.721  21.655  1.00 18.06           C  
ATOM   1173  C   ILE B  41      18.186  28.388  22.995  1.00 16.79           C  
ATOM   1174  O   ILE B  41      18.305  27.707  24.041  1.00 16.37           O  
ATOM   1175  CB  ILE B  41      19.906  27.980  21.198  1.00 19.20           C  
ATOM   1176  CG1 ILE B  41      20.221  27.177  19.916  1.00 20.84           C  
ATOM   1177  CG2 ILE B  41      20.915  27.657  22.321  1.00 20.66           C  
ATOM   1178  CD1 ILE B  41      21.525  27.765  19.256  1.00 21.79           C  
ATOM   1179  N   LEU B  42      17.888  29.691  22.964  1.00 15.57           N  
ATOM   1180  CA  LEU B  42      17.653  30.390  24.240  1.00 15.77           C  
ATOM   1181  C   LEU B  42      16.382  29.891  24.923  1.00 16.18           C  
ATOM   1182  O   LEU B  42      16.348  29.869  26.160  1.00 16.61           O  
ATOM   1183  CB  LEU B  42      17.635  31.915  24.099  1.00 15.24           C  
ATOM   1184  CG  LEU B  42      18.897  32.537  23.525  1.00 16.99           C  
ATOM   1185  CD1 LEU B  42      18.634  33.997  23.186  1.00 18.42           C  
ATOM   1186  CD2 LEU B  42      20.007  32.350  24.543  1.00 16.52           C  
ATOM   1187  N   ASP B  43      15.392  29.531  24.132  1.00 17.23           N  
ATOM   1188  CA  ASP B  43      14.167  28.938  24.734  1.00 19.07           C  
ATOM   1189  C   ASP B  43      14.521  27.647  25.477  1.00 18.97           C  
ATOM   1190  O   ASP B  43      13.999  27.430  26.584  1.00 19.36           O  
ATOM   1191  CB  ASP B  43      13.106  28.656  23.657  1.00 20.14           C  
ATOM   1192  CG  ASP B  43      12.366  29.919  23.272  1.00 22.35           C  
ATOM   1193  OD1 ASP B  43      11.882  29.893  22.123  1.00 24.80           O  
ATOM   1194  OD2 ASP B  43      12.229  30.858  24.031  1.00 22.30           O  
ATOM   1195  N   GLU B  44      15.328  26.825  24.873  1.00 18.64           N  
ATOM   1196  CA  GLU B  44      15.720  25.557  25.504  1.00 20.55           C  
ATOM   1197  C   GLU B  44      16.495  25.763  26.788  1.00 19.21           C  
ATOM   1198  O   GLU B  44      16.251  25.056  27.779  1.00 20.02           O  
ATOM   1199  CB  GLU B  44      16.552  24.687  24.574  1.00 23.07           C  
ATOM   1200  CG  GLU B  44      15.741  24.259  23.331  1.00 28.27           C  
ATOM   1201  CD  GLU B  44      16.497  23.306  22.435  1.00 32.79           C  
ATOM   1202  OE1 GLU B  44      17.329  22.501  22.847  1.00 35.03           O  
ATOM   1203  OE2 GLU B  44      16.186  23.463  21.212  1.00 36.03           O  
ATOM   1204  N   ILE B  45      17.430  26.703  26.766  1.00 17.29           N  
ATOM   1205  CA  ILE B  45      18.270  27.035  27.945  1.00 16.65           C  
ATOM   1206  C   ILE B  45      17.354  27.584  29.027  1.00 15.29           C  
ATOM   1207  O   ILE B  45      17.510  27.274  30.227  1.00 15.61           O  
ATOM   1208  CB  ILE B  45      19.395  28.059  27.535  1.00 17.35           C  
ATOM   1209  CG1 ILE B  45      20.451  27.406  26.632  1.00 18.50           C  
ATOM   1210  CG2 ILE B  45      20.045  28.814  28.730  1.00 18.81           C  
ATOM   1211  CD1 ILE B  45      21.308  26.278  27.182  1.00 20.61           C  
ATOM   1212  N   ALA B  46      16.381  28.396  28.656  1.00 15.53           N  
ATOM   1213  CA  ALA B  46      15.480  28.973  29.661  1.00 16.69           C  
ATOM   1214  C   ALA B  46      14.737  27.829  30.379  1.00 19.41           C  
ATOM   1215  O   ALA B  46      14.480  27.949  31.603  1.00 19.23           O  
ATOM   1216  CB  ALA B  46      14.522  29.968  29.066  1.00 17.45           C  
ATOM   1217  N   ASP B  47      14.381  26.799  29.617  1.00 19.93           N  
ATOM   1218  CA  ASP B  47      13.686  25.633  30.209  1.00 21.67           C  
ATOM   1219  C   ASP B  47      14.609  24.801  31.106  1.00 21.58           C  
ATOM   1220  O   ASP B  47      14.256  24.509  32.282  1.00 21.63           O  
ATOM   1221  CB  ASP B  47      13.031  24.777  29.105  1.00 23.89           C  
ATOM   1222  CG AASP B  47      11.569  25.189  28.956  0.50 24.82           C  
ATOM   1223  CG BASP B  47      12.373  23.524  29.694  0.50 25.47           C  
ATOM   1224  OD1AASP B  47      10.823  25.162  29.957  0.50 26.02           O  
ATOM   1225  OD1BASP B  47      12.726  22.388  29.322  0.50 26.53           O  
ATOM   1226  OD2AASP B  47      11.208  25.524  27.809  0.50 25.41           O  
ATOM   1227  OD2BASP B  47      11.504  23.680  30.585  0.50 25.78           O  
ATOM   1228  N   GLU B  48      15.746  24.471  30.570  1.00 20.93           N  
ATOM   1229  CA  GLU B  48      16.705  23.622  31.263  1.00 23.42           C  
ATOM   1230  C   GLU B  48      17.230  24.270  32.546  1.00 24.12           C  
ATOM   1231  O   GLU B  48      17.552  23.504  33.491  1.00 24.75           O  
ATOM   1232  CB  GLU B  48      17.915  23.254  30.425  1.00 26.09           C  
ATOM   1233  CG  GLU B  48      17.608  22.304  29.271  1.00 30.21           C  
ATOM   1234  CD  GLU B  48      18.812  22.000  28.409  1.00 33.03           C  
ATOM   1235  OE1 GLU B  48      18.403  21.660  27.283  1.00 34.87           O  
ATOM   1236  OE2 GLU B  48      19.966  22.067  28.804  1.00 34.27           O  
ATOM   1237  N   TYR B  49      17.302  25.583  32.592  1.00 22.79           N  
ATOM   1238  CA  TYR B  49      17.894  26.268  33.751  1.00 23.14           C  
ATOM   1239  C   TYR B  49      16.856  27.021  34.573  1.00 22.40           C  
ATOM   1240  O   TYR B  49      17.292  27.856  35.376  1.00 20.45           O  
ATOM   1241  CB  TYR B  49      19.031  27.179  33.295  1.00 25.21           C  
ATOM   1242  CG  TYR B  49      20.250  26.506  32.747  1.00 28.44           C  
ATOM   1243  CD1 TYR B  49      20.300  25.901  31.500  1.00 30.16           C  
ATOM   1244  CD2 TYR B  49      21.446  26.532  33.487  1.00 30.77           C  
ATOM   1245  CE1 TYR B  49      21.448  25.298  30.980  1.00 32.02           C  
ATOM   1246  CE2 TYR B  49      22.628  25.950  33.007  1.00 31.75           C  
ATOM   1247  CZ  TYR B  49      22.604  25.338  31.763  1.00 32.53           C  
ATOM   1248  OH  TYR B  49      23.770  24.782  31.313  1.00 35.26           O  
ATOM   1249  N   GLN B  50      15.557  26.686  34.466  1.00 21.77           N  
ATOM   1250  CA  GLN B  50      14.598  27.537  35.223  1.00 22.91           C  
ATOM   1251  C   GLN B  50      14.913  27.410  36.725  1.00 21.71           C  
ATOM   1252  O   GLN B  50      15.208  26.293  37.146  1.00 22.27           O  
ATOM   1253  CB  GLN B  50      13.119  27.320  35.004  1.00 26.17           C  
ATOM   1254  CG  GLN B  50      12.596  25.937  35.202  1.00 30.19           C  
ATOM   1255  CD  GLN B  50      11.203  25.825  34.552  1.00 32.23           C  
ATOM   1256  OE1 GLN B  50      11.055  24.902  33.726  1.00 35.16           O  
ATOM   1257  NE2 GLN B  50      10.319  26.761  34.872  1.00 31.55           N  
ATOM   1258  N   GLY B  51      14.851  28.557  37.344  1.00 20.23           N  
ATOM   1259  CA  GLY B  51      15.125  28.629  38.785  1.00 20.71           C  
ATOM   1260  C   GLY B  51      16.595  28.890  39.044  1.00 20.66           C  
ATOM   1261  O   GLY B  51      16.956  29.298  40.182  1.00 21.19           O  
ATOM   1262  N   LYS B  52      17.463  28.717  38.043  1.00 19.51           N  
ATOM   1263  CA  LYS B  52      18.881  28.971  38.273  1.00 19.82           C  
ATOM   1264  C   LYS B  52      19.412  30.131  37.444  1.00 18.48           C  
ATOM   1265  O   LYS B  52      20.369  30.817  37.835  1.00 19.41           O  
ATOM   1266  CB  LYS B  52      19.681  27.724  37.881  1.00 23.85           C  
ATOM   1267  CG  LYS B  52      19.390  26.588  38.890  1.00 29.59           C  
ATOM   1268  CD  LYS B  52      20.017  25.292  38.366  1.00 34.52           C  
ATOM   1269  CE  LYS B  52      19.719  24.137  39.345  1.00 37.67           C  
ATOM   1270  NZ  LYS B  52      20.065  24.608  40.748  1.00 40.15           N  
ATOM   1271  N   LEU B  53      18.824  30.278  36.258  1.00 16.06           N  
ATOM   1272  CA  LEU B  53      19.320  31.343  35.326  1.00 15.75           C  
ATOM   1273  C   LEU B  53      18.089  32.036  34.690  1.00 14.98           C  
ATOM   1274  O   LEU B  53      17.158  31.242  34.404  1.00 16.71           O  
ATOM   1275  CB  LEU B  53      20.170  30.647  34.244  1.00 15.01           C  
ATOM   1276  CG  LEU B  53      20.581  31.605  33.101  1.00 16.11           C  
ATOM   1277  CD1 LEU B  53      21.618  32.571  33.570  1.00 16.37           C  
ATOM   1278  CD2 LEU B  53      21.070  30.737  31.952  1.00 17.00           C  
ATOM   1279  N   THR B  54      18.119  33.343  34.531  1.00 13.61           N  
ATOM   1280  CA  THR B  54      16.990  34.018  33.821  1.00 14.29           C  
ATOM   1281  C   THR B  54      17.535  34.418  32.438  1.00 13.12           C  
ATOM   1282  O   THR B  54      18.692  34.883  32.462  1.00 12.69           O  
ATOM   1283  CB  THR B  54      16.510  35.280  34.632  1.00 17.07           C  
ATOM   1284  OG1 THR B  54      16.045  34.771  35.916  1.00 19.08           O  
ATOM   1285  CG2 THR B  54      15.495  36.163  33.899  1.00 18.26           C  
ATOM   1286  N   VAL B  55      16.746  34.215  31.414  1.00 12.19           N  
ATOM   1287  CA  VAL B  55      17.144  34.606  30.037  1.00 11.91           C  
ATOM   1288  C   VAL B  55      16.289  35.822  29.669  1.00 13.88           C  
ATOM   1289  O   VAL B  55      15.069  35.841  29.943  1.00 12.80           O  
ATOM   1290  CB  VAL B  55      16.989  33.432  29.059  1.00 13.65           C  
ATOM   1291  CG1 VAL B  55      17.405  33.811  27.643  1.00 13.58           C  
ATOM   1292  CG2 VAL B  55      17.740  32.179  29.494  1.00 14.22           C  
ATOM   1293  N   ALA B  56      16.956  36.839  29.121  1.00 11.50           N  
ATOM   1294  CA  ALA B  56      16.245  38.106  28.783  1.00 10.67           C  
ATOM   1295  C   ALA B  56      16.736  38.546  27.389  1.00 12.04           C  
ATOM   1296  O   ALA B  56      17.818  38.144  26.920  1.00 12.38           O  
ATOM   1297  CB  ALA B  56      16.565  39.097  29.853  1.00 10.32           C  
ATOM   1298  N   LYS B  57      15.872  39.367  26.794  1.00 11.76           N  
ATOM   1299  CA  LYS B  57      16.210  39.853  25.430  1.00 12.90           C  
ATOM   1300  C   LYS B  57      16.015  41.366  25.387  1.00 13.02           C  
ATOM   1301  O   LYS B  57      15.099  41.898  26.040  1.00 13.80           O  
ATOM   1302  CB  LYS B  57      15.305  39.260  24.350  1.00 14.00           C  
ATOM   1303  CG  LYS B  57      15.596  37.827  23.988  1.00 15.59           C  
ATOM   1304  CD  LYS B  57      14.511  37.291  23.028  1.00 18.08           C  
ATOM   1305  CE  LYS B  57      14.922  35.943  22.532  1.00 20.33           C  
ATOM   1306  NZ  LYS B  57      13.968  35.436  21.511  1.00 22.73           N  
ATOM   1307  N   LEU B  58      16.854  41.999  24.623  1.00 12.44           N  
ATOM   1308  CA  LEU B  58      16.703  43.450  24.404  1.00 13.94           C  
ATOM   1309  C   LEU B  58      16.832  43.673  22.881  1.00 13.70           C  
ATOM   1310  O   LEU B  58      17.874  43.365  22.309  1.00 13.20           O  
ATOM   1311  CB  LEU B  58      17.728  44.225  25.230  1.00 13.87           C  
ATOM   1312  CG  LEU B  58      17.526  45.760  25.021  1.00 15.37           C  
ATOM   1313  CD1ALEU B  58      17.747  46.481  26.338  0.50 14.85           C  
ATOM   1314  CD1BLEU B  58      16.520  46.283  26.036  0.50 14.94           C  
ATOM   1315  CD2ALEU B  58      18.459  46.254  23.932  0.50 13.51           C  
ATOM   1316  CD2BLEU B  58      18.834  46.488  25.178  0.50 16.87           C  
ATOM   1317  N   ASN B  59      15.779  44.258  22.319  1.00 13.80           N  
ATOM   1318  CA  ASN B  59      15.766  44.545  20.861  1.00 14.82           C  
ATOM   1319  C   ASN B  59      16.443  45.904  20.669  1.00 15.62           C  
ATOM   1320  O   ASN B  59      15.895  46.903  21.212  1.00 16.34           O  
ATOM   1321  CB  ASN B  59      14.310  44.523  20.370  1.00 16.20           C  
ATOM   1322  CG  ASN B  59      14.298  44.775  18.858  1.00 18.25           C  
ATOM   1323  OD1 ASN B  59      14.590  45.915  18.479  1.00 18.69           O  
ATOM   1324  ND2 ASN B  59      14.017  43.813  18.007  1.00 20.32           N  
ATOM   1325  N   ILE B  60      17.540  45.988  19.953  1.00 14.17           N  
ATOM   1326  CA  ILE B  60      18.265  47.255  19.874  1.00 15.15           C  
ATOM   1327  C   ILE B  60      17.610  48.280  18.929  1.00 16.65           C  
ATOM   1328  O   ILE B  60      17.991  49.472  19.037  1.00 17.67           O  
ATOM   1329  CB  ILE B  60      19.758  47.021  19.467  1.00 16.15           C  
ATOM   1330  CG1 ILE B  60      19.816  46.458  18.031  1.00 16.72           C  
ATOM   1331  CG2 ILE B  60      20.500  46.118  20.506  1.00 16.29           C  
ATOM   1332  CD1 ILE B  60      21.254  46.555  17.440  1.00 19.88           C  
ATOM   1333  N   ASP B  61      16.697  47.856  18.107  1.00 16.36           N  
ATOM   1334  CA  ASP B  61      15.943  48.797  17.216  1.00 18.57           C  
ATOM   1335  C   ASP B  61      14.943  49.565  18.078  1.00 20.69           C  
ATOM   1336  O   ASP B  61      14.752  50.778  17.900  1.00 21.65           O  
ATOM   1337  CB  ASP B  61      15.265  48.088  16.067  1.00 18.05           C  
ATOM   1338  CG  ASP B  61      16.175  47.577  14.986  1.00 18.43           C  
ATOM   1339  OD1 ASP B  61      17.308  48.028  14.800  1.00 21.15           O  
ATOM   1340  OD2 ASP B  61      15.795  46.651  14.252  1.00 20.69           O  
ATOM   1341  N   GLN B  62      14.358  48.859  19.051  1.00 21.42           N  
ATOM   1342  CA  GLN B  62      13.357  49.535  19.911  1.00 22.86           C  
ATOM   1343  C   GLN B  62      13.989  50.196  21.108  1.00 22.24           C  
ATOM   1344  O   GLN B  62      13.355  51.102  21.681  1.00 23.04           O  
ATOM   1345  CB  GLN B  62      12.257  48.585  20.400  1.00 24.85           C  
ATOM   1346  CG  GLN B  62      11.551  47.891  19.276  1.00 28.65           C  
ATOM   1347  CD  GLN B  62      10.820  46.643  19.680  1.00 31.25           C  
ATOM   1348  OE1 GLN B  62       9.877  46.244  18.980  1.00 35.25           O  
ATOM   1349  NE2 GLN B  62      11.191  45.954  20.742  1.00 32.04           N  
ATOM   1350  N   ASN B  63      15.148  49.769  21.530  1.00 20.39           N  
ATOM   1351  CA  ASN B  63      15.789  50.308  22.737  1.00 20.82           C  
ATOM   1352  C   ASN B  63      17.260  50.577  22.410  1.00 21.69           C  
ATOM   1353  O   ASN B  63      18.148  49.757  22.707  1.00 21.02           O  
ATOM   1354  CB  ASN B  63      15.688  49.275  23.874  1.00 20.83           C  
ATOM   1355  CG  ASN B  63      14.258  49.112  24.353  1.00 21.45           C  
ATOM   1356  OD1 ASN B  63      13.837  49.993  25.108  1.00 23.24           O  
ATOM   1357  ND2 ASN B  63      13.603  48.080  23.903  1.00 21.70           N  
ATOM   1358  N   PRO B  64      17.523  51.710  21.792  1.00 21.69           N  
ATOM   1359  CA  PRO B  64      18.848  51.958  21.263  1.00 21.80           C  
ATOM   1360  C   PRO B  64      19.811  52.558  22.248  1.00 21.91           C  
ATOM   1361  O   PRO B  64      20.971  52.755  21.857  1.00 22.11           O  
ATOM   1362  CB  PRO B  64      18.608  52.888  20.064  1.00 23.39           C  
ATOM   1363  CG  PRO B  64      17.363  53.658  20.457  1.00 23.46           C  
ATOM   1364  CD  PRO B  64      16.492  52.655  21.244  1.00 23.53           C  
ATOM   1365  N   GLY B  65      19.399  52.854  23.451  1.00 20.70           N  
ATOM   1366  CA  GLY B  65      20.245  53.466  24.453  1.00 21.53           C  
ATOM   1367  C   GLY B  65      21.135  52.499  25.222  1.00 21.90           C  
ATOM   1368  O   GLY B  65      22.194  52.933  25.709  1.00 22.36           O  
ATOM   1369  N   THR B  66      20.778  51.229  25.289  1.00 19.09           N  
ATOM   1370  CA  THR B  66      21.577  50.369  26.177  1.00 20.24           C  
ATOM   1371  C   THR B  66      22.855  49.825  25.564  1.00 20.25           C  
ATOM   1372  O   THR B  66      23.874  49.811  26.305  1.00 20.76           O  
ATOM   1373  CB  THR B  66      20.701  49.201  26.785  1.00 21.21           C  
ATOM   1374  OG1 THR B  66      19.678  49.835  27.606  1.00 21.42           O  
ATOM   1375  CG2 THR B  66      21.508  48.208  27.640  1.00 20.04           C  
ATOM   1376  N   ALA B  67      22.860  49.384  24.330  1.00 20.21           N  
ATOM   1377  CA  ALA B  67      24.038  48.749  23.711  1.00 21.46           C  
ATOM   1378  C   ALA B  67      25.299  49.604  23.797  1.00 23.27           C  
ATOM   1379  O   ALA B  67      26.355  49.090  24.177  1.00 22.52           O  
ATOM   1380  CB  ALA B  67      23.785  48.321  22.270  1.00 21.41           C  
ATOM   1381  N   PRO B  68      25.213  50.891  23.474  1.00 25.12           N  
ATOM   1382  CA  PRO B  68      26.337  51.820  23.564  1.00 25.49           C  
ATOM   1383  C   PRO B  68      26.955  51.914  24.946  1.00 26.04           C  
ATOM   1384  O   PRO B  68      28.160  52.172  25.026  1.00 26.54           O  
ATOM   1385  CB  PRO B  68      25.750  53.170  23.127  1.00 26.21           C  
ATOM   1386  CG  PRO B  68      24.608  52.755  22.216  1.00 26.47           C  
ATOM   1387  CD  PRO B  68      24.011  51.529  22.875  1.00 25.82           C  
ATOM   1388  N   LYS B  69      26.218  51.715  26.021  1.00 26.02           N  
ATOM   1389  CA  LYS B  69      26.712  51.750  27.394  1.00 26.82           C  
ATOM   1390  C   LYS B  69      27.669  50.588  27.648  1.00 26.08           C  
ATOM   1391  O   LYS B  69      28.502  50.721  28.567  1.00 26.20           O  
ATOM   1392  CB  LYS B  69      25.649  51.606  28.489  1.00 28.84           C  
ATOM   1393  CG  LYS B  69      24.537  52.658  28.462  1.00 31.25           C  
ATOM   1394  CD  LYS B  69      23.538  52.275  29.547  1.00 33.59           C  
ATOM   1395  CE  LYS B  69      22.433  53.290  29.787  1.00 35.57           C  
ATOM   1396  NZ  LYS B  69      21.598  52.744  30.917  1.00 36.47           N  
ATOM   1397  N   TYR B  70      27.511  49.525  26.855  1.00 23.96           N  
ATOM   1398  CA  TYR B  70      28.385  48.369  27.068  1.00 23.98           C  
ATOM   1399  C   TYR B  70      29.428  48.191  25.992  1.00 23.64           C  
ATOM   1400  O   TYR B  70      30.138  47.172  25.984  1.00 24.27           O  
ATOM   1401  CB  TYR B  70      27.545  47.058  27.206  1.00 23.71           C  
ATOM   1402  CG  TYR B  70      26.713  47.109  28.457  1.00 24.15           C  
ATOM   1403  CD1 TYR B  70      25.358  47.437  28.480  1.00 24.56           C  
ATOM   1404  CD2 TYR B  70      27.342  46.900  29.702  1.00 24.08           C  
ATOM   1405  CE1 TYR B  70      24.644  47.501  29.656  1.00 24.92           C  
ATOM   1406  CE2 TYR B  70      26.642  46.964  30.878  1.00 23.93           C  
ATOM   1407  CZ  TYR B  70      25.298  47.270  30.866  1.00 24.58           C  
ATOM   1408  OH  TYR B  70      24.670  47.342  32.084  1.00 25.82           O  
ATOM   1409  N   GLY B  71      29.487  49.138  25.081  1.00 23.85           N  
ATOM   1410  CA  GLY B  71      30.431  49.161  23.958  1.00 23.44           C  
ATOM   1411  C   GLY B  71      30.087  48.035  22.991  1.00 23.26           C  
ATOM   1412  O   GLY B  71      30.984  47.478  22.340  1.00 23.76           O  
ATOM   1413  N   ILE B  72      28.801  47.703  22.873  1.00 22.39           N  
ATOM   1414  CA  ILE B  72      28.414  46.621  21.949  1.00 22.89           C  
ATOM   1415  C   ILE B  72      28.516  47.115  20.513  1.00 24.20           C  
ATOM   1416  O   ILE B  72      27.920  48.157  20.275  1.00 25.56           O  
ATOM   1417  CB  ILE B  72      26.968  46.109  22.315  1.00 21.72           C  
ATOM   1418  CG1 ILE B  72      27.085  45.388  23.696  1.00 22.28           C  
ATOM   1419  CG2 ILE B  72      26.377  45.187  21.228  1.00 21.27           C  
ATOM   1420  CD1 ILE B  72      25.777  45.214  24.505  1.00 23.02           C  
ATOM   1421  N   ARG B  73      29.146  46.379  19.651  1.00 25.76           N  
ATOM   1422  CA  ARG B  73      29.320  46.807  18.251  1.00 29.99           C  
ATOM   1423  C   ARG B  73      28.785  45.814  17.244  1.00 29.33           C  
ATOM   1424  O   ARG B  73      28.894  46.095  16.018  1.00 31.04           O  
ATOM   1425  CB  ARG B  73      30.828  46.997  17.957  1.00 34.68           C  
ATOM   1426  CG  ARG B  73      31.614  47.800  18.988  1.00 39.54           C  
ATOM   1427  CD  ARG B  73      33.094  47.738  18.683  1.00 44.37           C  
ATOM   1428  NE  ARG B  73      33.343  48.509  17.438  1.00 48.48           N  
ATOM   1429  CZ  ARG B  73      33.810  49.775  17.464  1.00 50.61           C  
ATOM   1430  NH1 ARG B  73      33.968  50.484  16.337  1.00 51.21           N  
ATOM   1431  NH2 ARG B  73      34.163  50.319  18.652  1.00 51.80           N  
ATOM   1432  N   GLY B  74      28.288  44.666  17.678  1.00 26.09           N  
ATOM   1433  CA  GLY B  74      27.794  43.618  16.740  1.00 22.47           C  
ATOM   1434  C   GLY B  74      26.712  42.803  17.478  1.00 19.46           C  
ATOM   1435  O   GLY B  74      26.707  42.863  18.715  1.00 18.11           O  
ATOM   1436  N   ILE B  75      25.898  42.125  16.703  1.00 16.80           N  
ATOM   1437  CA  ILE B  75      24.819  41.312  17.307  1.00 14.22           C  
ATOM   1438  C   ILE B  75      24.791  39.976  16.572  1.00 14.02           C  
ATOM   1439  O   ILE B  75      25.331  39.894  15.439  1.00 16.05           O  
ATOM   1440  CB  ILE B  75      23.451  42.032  17.349  1.00 13.41           C  
ATOM   1441  CG1 ILE B  75      23.137  42.566  15.915  1.00 15.89           C  
ATOM   1442  CG2 ILE B  75      23.393  43.189  18.375  1.00 13.98           C  
ATOM   1443  CD1 ILE B  75      21.640  43.053  15.804  1.00 15.40           C  
ATOM   1444  N   PRO B  76      24.341  38.934  17.240  1.00 12.72           N  
ATOM   1445  CA  PRO B  76      23.922  38.971  18.636  1.00 11.90           C  
ATOM   1446  C   PRO B  76      25.113  39.144  19.588  1.00 12.27           C  
ATOM   1447  O   PRO B  76      26.186  38.661  19.233  1.00 12.68           O  
ATOM   1448  CB  PRO B  76      23.279  37.607  18.864  1.00 12.30           C  
ATOM   1449  CG  PRO B  76      23.927  36.700  17.843  1.00 12.49           C  
ATOM   1450  CD  PRO B  76      24.355  37.582  16.675  1.00 12.67           C  
ATOM   1451  N   THR B  77      24.855  39.779  20.743  1.00 10.83           N  
ATOM   1452  CA  THR B  77      25.873  39.843  21.811  1.00 10.50           C  
ATOM   1453  C   THR B  77      25.120  39.326  23.062  1.00  9.29           C  
ATOM   1454  O   THR B  77      23.992  39.764  23.272  1.00 10.15           O  
ATOM   1455  CB  THR B  77      26.510  41.232  22.106  1.00 11.68           C  
ATOM   1456  OG1 THR B  77      27.352  41.530  20.937  1.00 11.99           O  
ATOM   1457  CG2 THR B  77      27.418  41.216  23.373  1.00 10.95           C  
ATOM   1458  N   LEU B  78      25.747  38.418  23.780  1.00  8.55           N  
ATOM   1459  CA  LEU B  78      25.169  37.909  25.021  1.00  9.35           C  
ATOM   1460  C   LEU B  78      25.971  38.495  26.177  1.00  8.97           C  
ATOM   1461  O   LEU B  78      27.220  38.403  26.099  1.00 10.50           O  
ATOM   1462  CB  LEU B  78      25.267  36.370  25.072  1.00 11.37           C  
ATOM   1463  CG  LEU B  78      24.619  35.596  23.931  1.00 14.20           C  
ATOM   1464  CD1 LEU B  78      24.887  34.101  24.073  1.00 16.65           C  
ATOM   1465  CD2 LEU B  78      23.119  35.912  24.049  1.00 15.60           C  
ATOM   1466  N   LEU B  79      25.269  39.087  27.141  1.00  9.04           N  
ATOM   1467  CA  LEU B  79      25.964  39.551  28.383  1.00  9.53           C  
ATOM   1468  C   LEU B  79      25.498  38.653  29.508  1.00  9.88           C  
ATOM   1469  O   LEU B  79      24.252  38.402  29.605  1.00 10.71           O  
ATOM   1470  CB  LEU B  79      25.540  41.018  28.614  1.00 12.97           C  
ATOM   1471  CG  LEU B  79      26.494  42.124  28.228  1.00 16.03           C  
ATOM   1472  CD1 LEU B  79      27.022  42.043  26.820  1.00 16.16           C  
ATOM   1473  CD2 LEU B  79      25.805  43.466  28.517  1.00 16.93           C  
ATOM   1474  N   LEU B  80      26.390  38.189  30.361  1.00  8.93           N  
ATOM   1475  CA  LEU B  80      25.972  37.400  31.531  1.00  8.63           C  
ATOM   1476  C   LEU B  80      26.189  38.325  32.761  1.00 10.03           C  
ATOM   1477  O   LEU B  80      27.332  38.797  32.954  1.00 10.25           O  
ATOM   1478  CB  LEU B  80      26.770  36.101  31.610  1.00 10.35           C  
ATOM   1479  CG  LEU B  80      26.490  35.262  32.878  1.00 11.50           C  
ATOM   1480  CD1ALEU B  80      25.109  34.654  32.771  0.50  7.99           C  
ATOM   1481  CD1BLEU B  80      26.653  33.781  32.574  0.50 13.64           C  
ATOM   1482  CD2ALEU B  80      27.624  34.249  33.054  0.50  6.57           C  
ATOM   1483  CD2BLEU B  80      27.529  35.632  33.926  0.50 14.72           C  
ATOM   1484  N   PHE B  81      25.110  38.605  33.443  1.00  9.86           N  
ATOM   1485  CA  PHE B  81      25.184  39.436  34.676  1.00 10.36           C  
ATOM   1486  C   PHE B  81      25.136  38.514  35.912  1.00 11.21           C  
ATOM   1487  O   PHE B  81      24.440  37.501  35.875  1.00 12.08           O  
ATOM   1488  CB  PHE B  81      24.008  40.420  34.788  1.00 11.09           C  
ATOM   1489  CG  PHE B  81      24.055  41.528  33.766  1.00 11.92           C  
ATOM   1490  CD1 PHE B  81      24.576  42.761  34.132  1.00 12.24           C  
ATOM   1491  CD2 PHE B  81      23.578  41.273  32.463  1.00 12.14           C  
ATOM   1492  CE1 PHE B  81      24.678  43.806  33.224  1.00 12.34           C  
ATOM   1493  CE2 PHE B  81      23.652  42.342  31.539  1.00 13.01           C  
ATOM   1494  CZ  PHE B  81      24.173  43.581  31.944  1.00 12.98           C  
ATOM   1495  N   LYS B  82      25.909  38.911  36.910  1.00 11.58           N  
ATOM   1496  CA  LYS B  82      25.906  38.257  38.218  1.00 12.81           C  
ATOM   1497  C   LYS B  82      25.556  39.369  39.223  1.00 14.63           C  
ATOM   1498  O   LYS B  82      26.373  40.257  39.369  1.00 14.99           O  
ATOM   1499  CB  LYS B  82      27.222  37.641  38.610  1.00 12.86           C  
ATOM   1500  CG  LYS B  82      27.574  36.336  37.908  1.00 12.89           C  
ATOM   1501  CD  LYS B  82      28.979  35.887  38.390  1.00 14.24           C  
ATOM   1502  CE  LYS B  82      29.375  34.606  37.686  1.00 14.65           C  
ATOM   1503  NZ  LYS B  82      30.793  34.270  38.033  1.00 15.30           N  
ATOM   1504  N   ASN B  83      24.370  39.237  39.797  1.00 16.60           N  
ATOM   1505  CA  ASN B  83      23.922  40.224  40.794  1.00 20.93           C  
ATOM   1506  C   ASN B  83      24.118  41.637  40.289  1.00 21.83           C  
ATOM   1507  O   ASN B  83      24.732  42.494  40.944  1.00 24.20           O  
ATOM   1508  CB  ASN B  83      24.654  39.892  42.109  1.00 23.72           C  
ATOM   1509  CG  ASN B  83      24.073  40.646  43.311  1.00 27.18           C  
ATOM   1510  OD1 ASN B  83      24.817  41.276  44.090  1.00 29.89           O  
ATOM   1511  ND2 ASN B  83      22.761  40.570  43.394  1.00 27.36           N  
ATOM   1512  N   GLY B  84      23.708  41.929  39.073  1.00 21.06           N  
ATOM   1513  CA  GLY B  84      23.739  43.277  38.526  1.00 21.11           C  
ATOM   1514  C   GLY B  84      25.003  43.715  37.810  1.00 21.67           C  
ATOM   1515  O   GLY B  84      24.898  44.756  37.094  1.00 23.56           O  
ATOM   1516  N   GLU B  85      26.104  42.998  37.902  1.00 19.40           N  
ATOM   1517  CA  GLU B  85      27.345  43.444  37.204  1.00 19.73           C  
ATOM   1518  C   GLU B  85      27.679  42.453  36.070  1.00 16.01           C  
ATOM   1519  O   GLU B  85      27.400  41.280  36.221  1.00 12.58           O  
ATOM   1520  CB  GLU B  85      28.548  43.378  38.080  1.00 24.68           C  
ATOM   1521  CG  GLU B  85      28.766  44.119  39.409  1.00 32.09           C  
ATOM   1522  CD  GLU B  85      30.026  43.557  40.059  1.00 35.14           C  
ATOM   1523  OE1 GLU B  85      30.002  42.779  41.004  1.00 38.21           O  
ATOM   1524  OE2 GLU B  85      31.067  43.898  39.428  1.00 37.66           O  
ATOM   1525  N   VAL B  86      28.263  42.965  34.994  1.00 14.94           N  
ATOM   1526  CA  VAL B  86      28.629  42.050  33.888  1.00 13.61           C  
ATOM   1527  C   VAL B  86      29.709  41.115  34.343  1.00 14.16           C  
ATOM   1528  O   VAL B  86      30.739  41.613  34.881  1.00 16.56           O  
ATOM   1529  CB  VAL B  86      29.097  42.895  32.670  1.00 15.45           C  
ATOM   1530  CG1 VAL B  86      29.706  42.002  31.553  1.00 16.93           C  
ATOM   1531  CG2 VAL B  86      28.000  43.769  32.098  1.00 16.80           C  
ATOM   1532  N   ALA B  87      29.572  39.823  34.121  1.00 11.00           N  
ATOM   1533  CA  ALA B  87      30.558  38.837  34.470  1.00 11.55           C  
ATOM   1534  C   ALA B  87      31.177  38.159  33.253  1.00 11.03           C  
ATOM   1535  O   ALA B  87      32.253  37.574  33.394  1.00 11.03           O  
ATOM   1536  CB  ALA B  87      29.952  37.768  35.390  1.00 13.50           C  
ATOM   1537  N   ALA B  88      30.527  38.205  32.092  1.00  8.45           N  
ATOM   1538  CA  ALA B  88      31.086  37.546  30.915  1.00  7.80           C  
ATOM   1539  C   ALA B  88      30.307  38.051  29.696  1.00  7.67           C  
ATOM   1540  O   ALA B  88      29.161  38.499  29.857  1.00  8.89           O  
ATOM   1541  CB  ALA B  88      30.984  36.013  30.990  1.00  7.59           C  
ATOM   1542  N   THR B  89      30.966  38.030  28.574  1.00  8.49           N  
ATOM   1543  CA  THR B  89      30.248  38.414  27.319  1.00  9.41           C  
ATOM   1544  C   THR B  89      30.682  37.453  26.221  1.00  9.32           C  
ATOM   1545  O   THR B  89      31.742  36.835  26.251  1.00  7.78           O  
ATOM   1546  CB  THR B  89      30.542  39.923  26.951  1.00 10.89           C  
ATOM   1547  OG1 THR B  89      31.901  39.966  26.488  1.00 12.88           O  
ATOM   1548  CG2 THR B  89      30.350  40.913  28.094  1.00 11.67           C  
ATOM   1549  N   LYS B  90      29.830  37.433  25.177  1.00  9.37           N  
ATOM   1550  CA  LYS B  90      30.131  36.589  23.992  1.00  9.46           C  
ATOM   1551  C   LYS B  90      29.539  37.273  22.785  1.00 10.76           C  
ATOM   1552  O   LYS B  90      28.310  37.532  22.788  1.00 11.02           O  
ATOM   1553  CB  LYS B  90      29.501  35.236  24.218  1.00 10.64           C  
ATOM   1554  CG  LYS B  90      30.140  34.129  23.353  1.00 14.15           C  
ATOM   1555  CD  LYS B  90      29.596  34.159  21.929  1.00 14.89           C  
ATOM   1556  CE  LYS B  90      30.285  33.040  21.113  1.00 15.37           C  
ATOM   1557  NZ  LYS B  90      30.344  33.375  19.683  1.00 15.66           N  
ATOM   1558  N   VAL B  91      30.354  37.590  21.807  1.00  9.94           N  
ATOM   1559  CA  VAL B  91      29.803  38.241  20.602  1.00 11.17           C  
ATOM   1560  C   VAL B  91      29.618  37.153  19.529  1.00 10.07           C  
ATOM   1561  O   VAL B  91      30.585  36.382  19.295  1.00 11.22           O  
ATOM   1562  CB  VAL B  91      30.775  39.346  20.143  1.00 13.03           C  
ATOM   1563  CG1 VAL B  91      30.264  39.991  18.825  1.00 14.29           C  
ATOM   1564  CG2 VAL B  91      31.023  40.371  21.236  1.00 13.64           C  
ATOM   1565  N   GLY B  92      28.466  37.160  18.900  1.00 10.29           N  
ATOM   1566  CA  GLY B  92      28.231  36.229  17.756  1.00 10.33           C  
ATOM   1567  C   GLY B  92      27.432  34.997  18.153  1.00 12.66           C  
ATOM   1568  O   GLY B  92      27.400  34.646  19.327  1.00 12.97           O  
ATOM   1569  N   ALA B  93      26.816  34.382  17.139  1.00 12.35           N  
ATOM   1570  CA  ALA B  93      26.036  33.144  17.367  1.00 13.48           C  
ATOM   1571  C   ALA B  93      26.908  32.002  17.851  1.00 13.53           C  
ATOM   1572  O   ALA B  93      28.142  31.991  17.696  1.00 13.54           O  
ATOM   1573  CB  ALA B  93      25.385  32.764  16.019  1.00 15.85           C  
ATOM   1574  N   LEU B  94      26.241  31.040  18.510  1.00 12.81           N  
ATOM   1575  CA  LEU B  94      26.925  29.808  18.959  1.00 13.21           C  
ATOM   1576  C   LEU B  94      25.906  28.666  19.005  1.00 14.26           C  
ATOM   1577  O   LEU B  94      24.696  28.980  18.984  1.00 14.33           O  
ATOM   1578  CB  LEU B  94      27.620  30.066  20.315  1.00 13.94           C  
ATOM   1579  CG  LEU B  94      26.812  30.118  21.594  1.00 14.70           C  
ATOM   1580  CD1 LEU B  94      27.752  30.475  22.763  1.00 14.91           C  
ATOM   1581  CD2 LEU B  94      25.657  31.110  21.543  1.00 16.62           C  
ATOM   1582  N   SER B  95      26.384  27.443  19.082  1.00 14.18           N  
ATOM   1583  CA  SER B  95      25.514  26.270  19.189  1.00 14.94           C  
ATOM   1584  C   SER B  95      25.000  26.080  20.623  1.00 15.79           C  
ATOM   1585  O   SER B  95      25.474  26.667  21.587  1.00 14.43           O  
ATOM   1586  CB  SER B  95      26.323  25.049  18.728  1.00 15.23           C  
ATOM   1587  OG  SER B  95      27.252  24.722  19.755  1.00 16.34           O  
ATOM   1588  N   LYS B  96      24.033  25.188  20.794  1.00 15.59           N  
ATOM   1589  CA  LYS B  96      23.563  24.888  22.146  1.00 17.02           C  
ATOM   1590  C   LYS B  96      24.700  24.351  23.010  1.00 15.21           C  
ATOM   1591  O   LYS B  96      24.765  24.803  24.175  1.00 15.62           O  
ATOM   1592  CB  LYS B  96      22.407  23.903  22.175  1.00 19.22           C  
ATOM   1593  CG  LYS B  96      21.882  23.690  23.619  1.00 21.86           C  
ATOM   1594  CD  LYS B  96      20.651  22.779  23.436  1.00 25.50           C  
ATOM   1595  CE  LYS B  96      19.944  22.577  24.765  1.00 27.81           C  
ATOM   1596  NZ  LYS B  96      19.453  21.155  24.737  1.00 30.75           N  
ATOM   1597  N   GLY B  97      25.524  23.483  22.461  1.00 13.92           N  
ATOM   1598  CA  GLY B  97      26.675  22.881  23.181  1.00 13.11           C  
ATOM   1599  C   GLY B  97      27.662  23.957  23.593  1.00 13.07           C  
ATOM   1600  O   GLY B  97      28.144  23.965  24.729  1.00 13.86           O  
ATOM   1601  N   GLN B  98      27.942  24.883  22.715  1.00 12.47           N  
ATOM   1602  CA  GLN B  98      28.858  25.982  23.051  1.00 11.96           C  
ATOM   1603  C   GLN B  98      28.212  26.869  24.116  1.00 11.98           C  
ATOM   1604  O   GLN B  98      28.979  27.376  24.955  1.00 11.85           O  
ATOM   1605  CB  GLN B  98      29.234  26.812  21.830  1.00 13.22           C  
ATOM   1606  CG  GLN B  98      30.195  26.049  20.905  1.00 14.42           C  
ATOM   1607  CD  GLN B  98      30.405  26.800  19.599  1.00 15.12           C  
ATOM   1608  OE1 GLN B  98      29.337  27.170  18.934  1.00 14.08           O  
ATOM   1609  NE2 GLN B  98      31.567  27.092  19.206  1.00 17.95           N  
ATOM   1610  N   LEU B  99      26.907  27.122  24.054  1.00 10.46           N  
ATOM   1611  CA  LEU B  99      26.333  27.993  25.113  1.00 11.68           C  
ATOM   1612  C   LEU B  99      26.411  27.284  26.458  1.00 11.81           C  
ATOM   1613  O   LEU B  99      26.700  27.989  27.454  1.00 11.26           O  
ATOM   1614  CB  LEU B  99      24.885  28.368  24.703  1.00 13.04           C  
ATOM   1615  CG  LEU B  99      24.170  29.302  25.679  1.00 14.62           C  
ATOM   1616  CD1 LEU B  99      24.980  30.554  25.960  1.00 15.08           C  
ATOM   1617  CD2 LEU B  99      22.787  29.662  25.121  1.00 16.28           C  
ATOM   1618  N   LYS B 100      26.116  25.986  26.486  1.00 12.46           N  
ATOM   1619  CA  LYS B 100      26.312  25.258  27.775  1.00 14.80           C  
ATOM   1620  C   LYS B 100      27.752  25.354  28.262  1.00 13.88           C  
ATOM   1621  O   LYS B 100      27.936  25.522  29.498  1.00 14.98           O  
ATOM   1622  CB  LYS B 100      25.807  23.805  27.740  1.00 17.98           C  
ATOM   1623  CG  LYS B 100      24.328  23.876  27.331  1.00 22.43           C  
ATOM   1624  CD  LYS B 100      23.309  22.952  27.854  1.00 26.13           C  
ATOM   1625  CE  LYS B 100      23.701  21.502  27.950  1.00 29.23           C  
ATOM   1626  NZ  LYS B 100      22.415  20.707  28.089  1.00 31.04           N  
ATOM   1627  N   GLU B 101      28.762  25.253  27.396  1.00 13.77           N  
ATOM   1628  CA  GLU B 101      30.169  25.408  27.800  1.00 14.07           C  
ATOM   1629  C   GLU B 101      30.445  26.804  28.335  1.00 13.17           C  
ATOM   1630  O   GLU B 101      31.132  26.937  29.363  1.00 13.40           O  
ATOM   1631  CB  GLU B 101      31.110  25.227  26.594  1.00 16.68           C  
ATOM   1632  CG  GLU B 101      31.233  23.743  26.168  1.00 19.04           C  
ATOM   1633  CD  GLU B 101      32.163  23.666  24.968  1.00 20.67           C  
ATOM   1634  OE1 GLU B 101      32.049  24.300  23.940  1.00 21.77           O  
ATOM   1635  OE2 GLU B 101      33.159  22.998  25.258  1.00 23.29           O  
ATOM   1636  N   PHE B 102      29.892  27.797  27.679  1.00 12.08           N  
ATOM   1637  CA  PHE B 102      30.034  29.208  28.114  1.00 11.43           C  
ATOM   1638  C   PHE B 102      29.443  29.351  29.521  1.00 12.01           C  
ATOM   1639  O   PHE B 102      30.074  29.975  30.394  1.00 11.82           O  
ATOM   1640  CB  PHE B 102      29.374  30.146  27.099  1.00 12.52           C  
ATOM   1641  CG  PHE B 102      29.437  31.611  27.444  1.00 13.39           C  
ATOM   1642  CD1 PHE B 102      28.314  32.227  28.006  1.00 14.60           C  
ATOM   1643  CD2 PHE B 102      30.616  32.326  27.240  1.00 13.17           C  
ATOM   1644  CE1 PHE B 102      28.335  33.601  28.318  1.00 15.32           C  
ATOM   1645  CE2 PHE B 102      30.616  33.692  27.562  1.00 12.39           C  
ATOM   1646  CZ  PHE B 102      29.492  34.312  28.079  1.00 12.95           C  
ATOM   1647  N   LEU B 103      28.274  28.749  29.746  1.00 11.99           N  
ATOM   1648  CA  LEU B 103      27.686  28.882  31.111  1.00 11.95           C  
ATOM   1649  C   LEU B 103      28.495  28.116  32.145  1.00 11.33           C  
ATOM   1650  O   LEU B 103      28.672  28.671  33.226  1.00 13.13           O  
ATOM   1651  CB  LEU B 103      26.208  28.428  31.066  1.00 11.91           C  
ATOM   1652  CG  LEU B 103      25.333  29.287  30.193  1.00 12.27           C  
ATOM   1653  CD1 LEU B 103      23.929  28.699  30.009  1.00 15.35           C  
ATOM   1654  CD2 LEU B 103      25.252  30.682  30.806  1.00 13.53           C  
ATOM   1655  N   ASP B 104      28.936  26.927  31.836  1.00 12.67           N  
ATOM   1656  CA  ASP B 104      29.717  26.116  32.783  1.00 15.82           C  
ATOM   1657  C   ASP B 104      30.981  26.853  33.173  1.00 15.39           C  
ATOM   1658  O   ASP B 104      31.459  26.778  34.346  1.00 15.00           O  
ATOM   1659  CB  ASP B 104      30.007  24.727  32.178  1.00 19.47           C  
ATOM   1660  CG  ASP B 104      30.581  23.875  33.307  1.00 23.99           C  
ATOM   1661  OD1 ASP B 104      29.830  23.513  34.245  1.00 26.85           O  
ATOM   1662  OD2 ASP B 104      31.819  23.635  33.336  1.00 25.69           O  
ATOM   1663  N   ALA B 105      31.492  27.627  32.203  1.00 12.02           N  
ATOM   1664  CA  ALA B 105      32.746  28.350  32.557  1.00 12.49           C  
ATOM   1665  C   ALA B 105      32.553  29.477  33.558  1.00 12.99           C  
ATOM   1666  O   ALA B 105      33.510  29.980  34.151  1.00 14.77           O  
ATOM   1667  CB  ALA B 105      33.374  28.898  31.259  1.00 12.58           C  
ATOM   1668  N   ASN B 106      31.313  29.927  33.725  1.00 10.58           N  
ATOM   1669  CA  ASN B 106      31.005  31.138  34.466  1.00 11.76           C  
ATOM   1670  C   ASN B 106      30.131  30.879  35.696  1.00 13.46           C  
ATOM   1671  O   ASN B 106      30.153  31.789  36.523  1.00 14.23           O  
ATOM   1672  CB  ASN B 106      30.268  32.099  33.510  1.00 11.88           C  
ATOM   1673  CG  ASN B 106      31.226  32.806  32.564  1.00 12.35           C  
ATOM   1674  OD1 ASN B 106      32.002  33.657  32.973  1.00 13.38           O  
ATOM   1675  ND2 ASN B 106      31.216  32.466  31.270  1.00 12.95           N  
ATOM   1676  N   LEU B 107      29.443  29.770  35.796  1.00 15.28           N  
ATOM   1677  CA  LEU B 107      28.450  29.682  36.903  1.00 18.38           C  
ATOM   1678  C   LEU B 107      28.687  28.441  37.757  1.00 21.98           C  
ATOM   1679  O   LEU B 107      29.074  27.448  37.159  1.00 23.49           O  
ATOM   1680  CB  LEU B 107      27.026  29.618  36.332  1.00 18.70           C  
ATOM   1681  CG  LEU B 107      26.609  30.873  35.569  1.00 19.61           C  
ATOM   1682  CD1 LEU B 107      25.303  30.582  34.863  1.00 20.52           C  
ATOM   1683  CD2 LEU B 107      26.492  32.044  36.530  1.00 20.72           C  
ATOM   1684  N   ALA B 108      28.470  28.652  39.045  1.00 25.81           N  
ATOM   1685  CA  ALA B 108      28.548  27.541  40.012  1.00 29.38           C  
ATOM   1686  C   ALA B 108      27.113  27.194  40.424  1.00 31.86           C  
ATOM   1687  O   ALA B 108      26.183  27.969  40.106  1.00 32.16           O  
ATOM   1688  CB  ALA B 108      29.368  27.921  41.227  1.00 30.02           C  
ATOM   1689  OXT ALA B 108      26.995  26.160  41.099  1.00 35.42           O  
TER    1690      ALA B 108                                                      
HETATM 1691 CU    CU A 109      20.784  24.263  -3.038  1.00 19.01          CU  
HETATM 1692  C1  MPD A 601      22.066  43.909   7.477  0.75 29.38           C  
HETATM 1693  C2  MPD A 601      21.051  44.948   7.040  0.75 30.39           C  
HETATM 1694  O2  MPD A 601      21.454  45.555   5.787  0.75 19.79           O  
HETATM 1695  CM  MPD A 601      19.729  44.241   6.724  0.75 23.44           C  
HETATM 1696  C3  MPD A 601      20.760  45.938   8.129  0.75 24.28           C  
HETATM 1697  C4  MPD A 601      21.848  46.902   8.496  0.75 31.16           C  
HETATM 1698  O4  MPD A 601      22.241  47.681   7.324  0.75 22.95           O  
HETATM 1699  C5  MPD A 601      21.296  47.867   9.549  0.75 25.64           C  
HETATM 1700  C1  MPD A 605      38.885  22.843 -15.734  0.55 58.02           C  
HETATM 1701  C2  MPD A 605      38.357  23.149 -14.327  0.55 57.51           C  
HETATM 1702  O2  MPD A 605      38.951  22.205 -13.404  0.55 60.33           O  
HETATM 1703  CM  MPD A 605      38.841  24.546 -13.964  0.55 58.26           C  
HETATM 1704  C3  MPD A 605      36.853  23.060 -14.340  0.55 55.70           C  
HETATM 1705  C4  MPD A 605      36.188  22.809 -13.014  0.55 52.17           C  
HETATM 1706  O4  MPD A 605      36.082  24.048 -12.271  0.55 56.02           O  
HETATM 1707  C5  MPD A 605      34.765  22.285 -13.243  0.55 60.57           C  
HETATM 1708  C1  MPD A 606      46.534  38.537  -1.632  0.75 43.14           C  
HETATM 1709  C2  MPD A 606      45.507  39.104  -2.604  0.75 54.26           C  
HETATM 1710  O2  MPD A 606      44.567  39.924  -1.859  0.75 61.78           O  
HETATM 1711  CM  MPD A 606      46.248  39.979  -3.614  0.75 50.04           C  
HETATM 1712  C3  MPD A 606      44.757  38.025  -3.364  0.75 39.98           C  
HETATM 1713  C4  MPD A 606      43.803  37.284  -2.448  0.75 51.13           C  
HETATM 1714  O4  MPD A 606      42.566  38.025  -2.315  0.75 49.20           O  
HETATM 1715  C5  MPD A 606      43.526  35.900  -2.974  0.75 38.60           C  
HETATM 1716  C1  MPD A 607      36.391  40.671 -10.529  0.55 59.17           C  
HETATM 1717  C2  MPD A 607      36.963  42.083 -10.334  0.55 52.06           C  
HETATM 1718  O2  MPD A 607      38.332  42.019 -10.812  0.55 56.27           O  
HETATM 1719  CM  MPD A 607      36.174  43.007 -11.248  0.55 55.53           C  
HETATM 1720  C3  MPD A 607      36.878  42.435  -8.876  0.55 45.78           C  
HETATM 1721  C4  MPD A 607      37.139  43.865  -8.497  0.55 62.34           C  
HETATM 1722  O4  MPD A 607      36.527  44.172  -7.213  0.55 50.30           O  
HETATM 1723  C5  MPD A 607      38.626  44.172  -8.469  0.55 59.00           C  
HETATM 1724 CU    CU B 109       8.410  30.145  25.459  1.00 27.45          CU  
HETATM 1725  C1  MPD B 602      17.306  39.938   7.332  0.65 42.44           C  
HETATM 1726  C2  MPD B 602      16.650  38.717   7.986  0.65 50.51           C  
HETATM 1727  O2  MPD B 602      15.836  39.197   9.110  0.65 48.14           O  
HETATM 1728  CM  MPD B 602      15.659  38.121   6.995  0.65 56.00           C  
HETATM 1729  C3  MPD B 602      17.700  37.796   8.526  0.65 39.68           C  
HETATM 1730  C4  MPD B 602      18.104  36.594   7.718  0.65 45.04           C  
HETATM 1731  O4  MPD B 602      19.533  36.606   7.510  0.65 44.28           O  
HETATM 1732  C5  MPD B 602      17.679  35.298   8.388  0.65 43.42           C  
HETATM 1733  C1  MPD B 603      30.072  43.542  24.478  1.00 42.91           C  
HETATM 1734  C2  MPD B 603      31.603  43.598  24.490  1.00 51.69           C  
HETATM 1735  O2  MPD B 603      32.078  42.477  25.274  1.00 42.39           O  
HETATM 1736  CM  MPD B 603      32.022  43.392  23.036  1.00 62.02           C  
HETATM 1737  C3  MPD B 603      32.051  44.923  25.038  1.00 45.21           C  
HETATM 1738  C4  MPD B 603      33.527  45.130  25.222  1.00 50.88           C  
HETATM 1739  O4  MPD B 603      33.795  46.571  25.183  1.00 61.26           O  
HETATM 1740  C5  MPD B 603      34.023  44.686  26.593  1.00 45.03           C  
HETATM 1741  C1  MPD B 604      25.097  47.924  14.515  0.55 55.95           C  
HETATM 1742  C2  MPD B 604      24.874  48.498  15.918  0.55 49.56           C  
HETATM 1743  O2  MPD B 604      26.010  49.334  16.246  0.55 59.92           O  
HETATM 1744  CM  MPD B 604      23.617  49.354  15.870  0.55 52.36           C  
HETATM 1745  C3  MPD B 604      24.723  47.353  16.880  0.55 47.14           C  
HETATM 1746  C4  MPD B 604      25.018  47.660  18.319  0.55 50.81           C  
HETATM 1747  O4  MPD B 604      24.769  49.035  18.680  0.55 54.34           O  
HETATM 1748  C5  MPD B 604      24.176  46.744  19.200  0.55 54.26           C  
HETATM 1749  O   HOH A 402      29.396  44.583   6.834  0.95 17.71           O  
HETATM 1750  O   HOH A 403      30.033  30.918  -8.325  0.99 19.30           O  
HETATM 1751  O   HOH A 404      26.404  26.318   3.759  0.93 16.54           O  
HETATM 1752  O   HOH A 405      23.214  24.483  -2.005  0.99 19.24           O  
HETATM 1753  O   HOH A 406      34.701  18.605 -10.205  0.80 24.92           O  
HETATM 1754  O   HOH A 408      26.118  27.177  -5.744  1.00 23.72           O  
HETATM 1755  O   HOH A 410      25.391  38.875  -3.080  1.00 16.95           O  
HETATM 1756  O   HOH A 412      34.070  34.782  14.482  1.00 19.24           O  
HETATM 1757  O   HOH A 413      27.065  23.698   4.464  1.00 22.97           O  
HETATM 1758  O   HOH A 414      31.420  17.802  -9.789  1.00 35.41           O  
HETATM 1759  O   HOH A 419      20.405  20.444  -1.363  0.87 14.35           O  
HETATM 1760  O   HOH A 420      27.137  35.289  14.507  0.99 16.97           O  
HETATM 1761  O   HOH A 421      22.211  38.936   9.064  0.83 22.15           O  
HETATM 1762  O   HOH A 422      26.265  37.758  13.963  0.92 19.86           O  
HETATM 1763  O   HOH A 425      30.314  27.607   9.940  0.83 24.68           O  
HETATM 1764  O   HOH A 428      34.879  34.306  10.677  1.00 15.61           O  
HETATM 1765  O   HOH A 429      50.990  40.405  -8.192  0.87 28.10           O  
HETATM 1766  O   HOH A 431      31.217  30.708  18.815  1.00 23.99           O  
HETATM 1767  O   HOH A 435      23.417  39.866 -11.209  0.95 58.28           O  
HETATM 1768  O   HOH A 436      25.154  36.195  -4.365  0.83 16.51           O  
HETATM 1769  O   HOH A 437      27.688  45.864  11.163  0.84 39.62           O  
HETATM 1770  O   HOH A 438      41.585  37.690  -6.557  1.00 26.00           O  
HETATM 1771  O   HOH A 439      33.905  25.070  11.188  0.93 28.66           O  
HETATM 1772  O   HOH A 442      23.063  18.508  -3.461  0.99 34.96           O  
HETATM 1773  O   HOH A 443      37.320  16.226  -8.844  0.53 20.96           O  
HETATM 1774  O   HOH A 444      27.067  31.239  -8.518  1.00 30.97           O  
HETATM 1775  O   HOH A 446      27.019  31.968  12.723  1.00 39.16           O  
HETATM 1776  O   HOH A 447      34.344  32.015  12.274  1.00 20.18           O  
HETATM 1777  O   HOH A 448      26.583  42.753  13.840  0.68 20.95           O  
HETATM 1778  O   HOH A 449      23.792  21.934  -1.257  1.00 27.06           O  
HETATM 1779  O   HOH A 450      28.265  48.699   3.462  0.76 32.65           O  
HETATM 1780  O   HOH A 451      32.677  43.572  -3.878  1.00 20.44           O  
HETATM 1781  O   HOH A 452      39.242  30.479 -13.452  0.92 22.25           O  
HETATM 1782  O   HOH A 455      22.786  36.877  -6.246  0.89 49.28           O  
HETATM 1783  O   HOH A 456      44.544  37.043   7.616  0.89 21.95           O  
HETATM 1784  O   HOH A 457      23.096  40.753  -3.886  0.84 30.95           O  
HETATM 1785  O   HOH A 462      26.956  34.176  11.585  0.65 56.67           O  
HETATM 1786  O   HOH A 463      31.317  44.696 -11.258  1.00 54.48           O  
HETATM 1787  O   HOH A 468      17.282  27.973   1.776  0.48 35.87           O  
HETATM 1788  O   HOH A 470      26.774  43.547   9.407  1.00 19.87           O  
HETATM 1789  O   HOH A 471      22.692  37.720   4.567  1.00 49.53           O  
HETATM 1790  O   HOH A 472      25.997  39.690 -11.700  1.00 27.33           O  
HETATM 1791  O   HOH A 473      22.444  17.403   3.042  1.00 29.98           O  
HETATM 1792  O   HOH A 474      31.363  44.873   3.548  1.00 30.24           O  
HETATM 1793  O   HOH A 476      24.063  28.777  -8.231  0.41 19.45           O  
HETATM 1794  O   HOH A 477      33.111  15.725   4.613  0.59 55.53           O  
HETATM 1795  O   HOH A 485      40.113  15.366  -2.934  0.82 36.14           O  
HETATM 1796  O   HOH A 486      20.529  33.519   2.725  0.83 37.02           O  
HETATM 1797  O   HOH A 487      38.147  30.341  -6.631  0.45 19.23           O  
HETATM 1798  O   HOH A 489      34.219  30.778  15.387  1.00 35.60           O  
HETATM 1799  O   HOH A 490      23.311  30.350  -4.870  0.89 43.21           O  
HETATM 1800  O   HOH A 493      26.302  33.010   9.388  1.00 35.47           O  
HETATM 1801  O   HOH A 494      33.856  44.861  -6.185  0.69 28.86           O  
HETATM 1802  O   HOH A 496      26.832  23.970   7.918  0.96 33.88           O  
HETATM 1803  O   HOH A 499      32.336  45.189  -8.847  0.64 31.28           O  
HETATM 1804  O   HOH A 507      48.313  39.117  -7.404  0.91 36.09           O  
HETATM 1805  O   HOH A 508      38.027  38.230 -13.035  0.65 25.27           O  
HETATM 1806  O   HOH A 511      23.687  26.159  -7.975  0.79 43.05           O  
HETATM 1807  O   HOH A 512      36.269  14.370  -7.049  0.81 44.67           O  
HETATM 1808  O   HOH A 514      33.548  34.773 -18.224  0.89 45.79           O  
HETATM 1809  O   HOH A 515      34.629  39.412  14.209  1.00 38.90           O  
HETATM 1810  O   HOH A 516      28.235  48.776  -1.657  0.52 28.71           O  
HETATM 1811  O   HOH A 517      31.197  47.729   2.436  1.00 51.00           O  
HETATM 1812  O   HOH A 518      40.828  17.147  -9.551  1.00 46.48           O  
HETATM 1813  O   HOH A 519      24.671  48.042  -8.260  1.00 60.99           O  
HETATM 1814  O   HOH A 520      41.229  35.973  14.431  0.72 26.55           O  
HETATM 1815  O   HOH A 521      40.083  34.555 -11.154  0.79 42.63           O  
HETATM 1816  O   HOH A 524      30.993  15.284  -8.418  0.93 53.96           O  
HETATM 1817  O   HOH A 525      47.422  15.529  -1.183  1.00 57.93           O  
HETATM 1818  O   HOH A 527      31.932  19.490 -11.721  0.57 37.80           O  
HETATM 1819  O   HOH A 530      15.324  23.895  -1.238  0.93 44.28           O  
HETATM 1820  O   HOH A 534      37.079  40.916  11.859  0.53 29.08           O  
HETATM 1821  O   HOH A 536      19.795  37.957   2.660  0.47 35.80           O  
HETATM 1822  O   HOH A 539      27.226  30.760   9.922  0.85 46.28           O  
HETATM 1823  O   HOH A 540      40.612  45.488   5.505  0.59 40.36           O  
HETATM 1824  O   HOH B 401      30.339  33.478  16.727  1.00 17.61           O  
HETATM 1825  O   HOH B 407      32.247  34.886  35.483  0.93 17.79           O  
HETATM 1826  O   HOH B 409      20.165  50.675  17.627  0.67 24.40           O  
HETATM 1827  O   HOH B 411      14.090  32.923  22.264  1.00 28.71           O  
HETATM 1828  O   HOH B 415      29.670  43.595  20.432  1.00 24.28           O  
HETATM 1829  O   HOH B 416      13.385  44.732  24.036  1.00 23.38           O  
HETATM 1830  O   HOH B 417      32.639  36.673  17.385  1.00 23.61           O  
HETATM 1831  O   HOH B 418      12.458  23.913  25.361  1.00 60.26           O  
HETATM 1832  O   HOH B 423       8.144  26.529  27.446  1.00 25.34           O  
HETATM 1833  O   HOH B 424      21.941  40.212  37.784  1.00 20.01           O  
HETATM 1834  O   HOH B 426      24.147  26.938  36.069  0.89 54.36           O  
HETATM 1835  O   HOH B 427      14.336  21.913  34.304  0.52 42.12           O  
HETATM 1836  O   HOH B 430      23.698  27.164  38.624  0.60 49.93           O  
HETATM 1837  O   HOH B 432      14.897  30.303  33.070  1.00 19.07           O  
HETATM 1838  O   HOH B 433      13.251  41.824  22.915  0.91 18.74           O  
HETATM 1839  O   HOH B 434       8.009  36.229  28.935  0.84 38.88           O  
HETATM 1840  O   HOH B 440      18.122  34.742  37.746  0.73 24.99           O  
HETATM 1841  O   HOH B 441      22.732  23.891  18.590  1.00 29.20           O  
HETATM 1842  O   HOH B 445      31.725  41.195  37.394  0.45 18.55           O  
HETATM 1843  O   HOH B 453      20.666  49.174  22.459  1.00 19.46           O  
HETATM 1844  O   HOH B 454      10.761  47.139  23.353  1.00 50.09           O  
HETATM 1845  O   HOH B 458      14.163  44.503  15.165  1.00 21.91           O  
HETATM 1846  O   HOH B 459      21.688  50.552  20.015  0.91 30.60           O  
HETATM 1847  O   HOH B 460      28.779  45.769  35.273  0.81 32.95           O  
HETATM 1848  O   HOH B 461       9.933  29.502  36.191  0.78 51.80           O  
HETATM 1849  O   HOH B 464      24.011  55.568  25.064  0.98 58.43           O  
HETATM 1850  O   HOH B 465      14.563  31.294  36.210  1.00 33.02           O  
HETATM 1851  O   HOH B 466      26.157  25.462  34.268  1.00 51.84           O  
HETATM 1852  O   HOH B 467      28.464  40.269  41.187  1.00 36.34           O  
HETATM 1853  O   HOH B 469      32.362  44.336  35.588  1.00 50.52           O  
HETATM 1854  O   HOH B 475      32.777  32.205  38.249  1.00 24.27           O  
HETATM 1855  O   HOH B 478      10.784  30.401  26.569  1.00 24.41           O  
HETATM 1856  O   HOH B 479      14.240  32.771  31.963  1.00 18.27           O  
HETATM 1857  O   HOH B 480      18.077  36.413  19.223  1.00 18.28           O  
HETATM 1858  O   HOH B 481      14.999  36.724  18.976  0.93 24.75           O  
HETATM 1859  O   HOH B 482      14.125  47.487  12.124  0.83 26.19           O  
HETATM 1860  O   HOH B 483      20.384  33.084  39.541  0.83 29.84           O  
HETATM 1861  O   HOH B 484      13.515  53.986  19.363  0.87 37.68           O  
HETATM 1862  O   HOH B 488      19.681  51.587  29.578  1.00 31.84           O  
HETATM 1863  O   HOH B 491      25.435  48.145  34.353  1.00 39.53           O  
HETATM 1864  O   HOH B 492      16.293  52.706  16.743  0.96 31.60           O  
HETATM 1865  O   HOH B 495      11.517  28.234  27.761  0.91 30.96           O  
HETATM 1866  O   HOH B 497      12.213  46.373  30.839  0.49 33.68           O  
HETATM 1867  O   HOH B 498      19.234  49.659  14.769  1.00 59.59           O  
HETATM 1868  O   HOH B 500       5.160  29.087  31.065  0.76 44.39           O  
HETATM 1869  O   HOH B 501      25.404  21.709  20.090  0.61 26.77           O  
HETATM 1870  O   HOH B 502      11.137  24.946  22.821  0.81 48.72           O  
HETATM 1871  O   HOH B 503      27.680  51.069  19.720  0.67 59.82           O  
HETATM 1872  O   HOH B 504      23.342  51.470  32.735  1.00 52.80           O  
HETATM 1873  O   HOH B 505       8.659  40.224  29.995  0.95 48.02           O  
HETATM 1874  O   HOH B 506      30.411  25.431  36.620  1.00 51.19           O  
HETATM 1875  O   HOH B 509      13.538  24.890  20.764  0.90 41.62           O  
HETATM 1876  O   HOH B 510      26.264  25.199  31.597  1.00 43.81           O  
HETATM 1877  O   HOH B 513      13.709  35.631  17.058  0.86 32.66           O  
HETATM 1878  O   HOH B 522      24.194  19.021  29.933  0.60 45.73           O  
HETATM 1879  O   HOH B 523      19.945  22.792  19.860  0.91 49.51           O  
HETATM 1880  O   HOH B 526      18.801  53.874  31.989  0.60 37.91           O  
HETATM 1881  O   HOH B 528      15.771  41.061  42.160  1.00 43.05           O  
HETATM 1882  O   HOH B 529      29.038  22.833  19.098  0.58 27.76           O  
HETATM 1883  O   HOH B 531      18.858  38.057  46.752  0.71 39.43           O  
HETATM 1884  O   HOH B 532      11.134  36.262  22.719  0.67 36.86           O  
HETATM 1885  O   HOH B 533      17.378  37.038  38.611  0.82 43.41           O  
HETATM 1886  O   HOH B 535      12.748  47.737  32.940  0.85 56.90           O  
HETATM 1887  O   HOH B 537      26.985  50.290  33.430  1.00 60.67           O  
HETATM 1888  O   HOH B 538      12.233  30.720  19.502  0.42 26.30           O  
CONECT    1 1691                                                                
CONECT    7 1691                                                                
CONECT   13 1691                                                                
CONECT  272  289                                                                
CONECT  289  272                                                                
CONECT  851 1724                                                                
CONECT  857 1724                                                                
CONECT  863 1724                                                                
CONECT 1116 1133                                                                
CONECT 1133 1116                                                                
CONECT 1691    1    7   13 1752                                                 
CONECT 1692 1693                                                                
CONECT 1693 1692 1694 1695 1696                                                 
CONECT 1694 1693                                                                
CONECT 1695 1693                                                                
CONECT 1696 1693 1697                                                           
CONECT 1697 1696 1698 1699                                                      
CONECT 1698 1697                                                                
CONECT 1699 1697                                                                
CONECT 1700 1701                                                                
CONECT 1701 1700 1702 1703 1704                                                 
CONECT 1702 1701                                                                
CONECT 1703 1701                                                                
CONECT 1704 1701 1705                                                           
CONECT 1705 1704 1706 1707                                                      
CONECT 1706 1705                                                                
CONECT 1707 1705                                                                
CONECT 1708 1709                                                                
CONECT 1709 1708 1710 1711 1712                                                 
CONECT 1710 1709                                                                
CONECT 1711 1709                                                                
CONECT 1712 1709 1713                                                           
CONECT 1713 1712 1714 1715                                                      
CONECT 1714 1713                                                                
CONECT 1715 1713                                                                
CONECT 1716 1717                                                                
CONECT 1717 1716 1718 1719 1720                                                 
CONECT 1718 1717                                                                
CONECT 1719 1717                                                                
CONECT 1720 1717 1721                                                           
CONECT 1721 1720 1722 1723                                                      
CONECT 1722 1721                                                                
CONECT 1723 1721                                                                
CONECT 1724  851  857  863 1855                                                 
CONECT 1725 1726                                                                
CONECT 1726 1725 1727 1728 1729                                                 
CONECT 1727 1726                                                                
CONECT 1728 1726                                                                
CONECT 1729 1726 1730                                                           
CONECT 1730 1729 1731 1732                                                      
CONECT 1731 1730                                                                
CONECT 1732 1730                                                                
CONECT 1733 1734                                                                
CONECT 1734 1733 1735 1736 1737                                                 
CONECT 1735 1734                                                                
CONECT 1736 1734                                                                
CONECT 1737 1734 1738                                                           
CONECT 1738 1737 1739 1740                                                      
CONECT 1739 1738                                                                
CONECT 1740 1738                                                                
CONECT 1741 1742                                                                
CONECT 1742 1741 1743 1744 1745                                                 
CONECT 1743 1742                                                                
CONECT 1744 1742                                                                
CONECT 1745 1742 1746                                                           
CONECT 1746 1745 1747 1748                                                      
CONECT 1747 1746                                                                
CONECT 1748 1746                                                                
CONECT 1752 1691                                                                
CONECT 1855 1724                                                                
MASTER      355    0    9   10   10    0   14    6 1842    2   70   18          
END                                                                             
