HEADER    LIPOCALIN                               10-AUG-01   1GKA              
TITLE     THE MOLECULAR BASIS OF THE COLORATION MECHANISM IN LOBSTER SHELL.     
TITLE    2 BETA-CRUSTACYANIN AT 3.2 A RESOLUTION                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CRUSTACYANIN A1 SUBUNIT;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: BETA CRUSTACYANIN SUBUNIT;                                  
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: CRUSTACYANIN A2 SUBUNIT;                                   
COMPND   7 CHAIN: B                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMARUS GAMMARUS;                               
SOURCE   3 ORGANISM_COMMON: EUROPEAN LOBSTER;                                   
SOURCE   4 ORGANISM_TAXID: 6707;                                                
SOURCE   5 TISSUE: CARAPACE;                                                    
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMARUS GAMMARUS;                               
SOURCE   8 ORGANISM_COMMON: EUROPEAN LOBSTER;                                   
SOURCE   9 ORGANISM_TAXID: 6707;                                                
SOURCE  10 TISSUE: CARAPACE                                                     
KEYWDS    LIPOCALIN, CRUSTACYANIN, LOBSTER, ASTAXANTHIN, BATHOCHROMIC,          
KEYWDS   2 COLORATION                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.CIANCI,P.J.RIZKALLAH,A.OLCZAK,J.RAFTERY,N.E.CHAYEN,P.F.ZAGALSKY,    
AUTHOR   2 J.R.HELLIWELL                                                        
REVDAT   3   13-DEC-23 1GKA    1       REMARK                                   
REVDAT   2   24-FEB-09 1GKA    1       VERSN                                    
REVDAT   1   08-AUG-02 1GKA    0                                                
JRNL        AUTH   M.CIANCI,P.RIZKALLAH,A.OLCZAK,J.RAFTERY,N.CHAYEN,P.ZAGALSKY, 
JRNL        AUTH 2 J.HELLIWELL                                                  
JRNL        TITL   THE MOLECULAR BASIS OF THE COLORATION MECHANISM IN LOBSTER   
JRNL        TITL 2 SHELL: BETA -CRUSTACYANIN AT 3.2-A RESOLUTION                
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  99  9795 2002              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   12119396                                                     
JRNL        DOI    10.1073/PNAS.152088999                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.23 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.23                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 19827                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.23                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.35                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 1.00                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1845                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3085                       
REMARK   3   BIN FREE R VALUE                    : 0.3910                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2843                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 123                                     
REMARK   3   SOLVENT ATOMS            : 30                                      
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) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.39                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.42                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.50                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.031                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.777                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.55                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.525                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GKA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-AUG-01.                  
REMARK 100 THE DEPOSITION ID IS D_1290008425.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.70                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
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 : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24504                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.12400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.23                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1H91                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 78.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.70                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       84.25200            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       84.25200            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       84.25200            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       84.25200            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       84.25200            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       84.25200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THIS BETA CRUSTACYANIN IS RESPONSIBLE FOR BINDING THE                
REMARK 400  CAROTENOID ASTAXANTHIN THAT PROVIDES THE COLORATION OF              
REMARK 400  THE CARAPACE OF THE LOBSTER.                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  2006     O    HOH B  2013              1.54            
REMARK 500   SG   CYS B   115     OG1  THR B   147              2.06            
REMARK 500   N    ASP B   123     O    HOH B  2014              2.11            
REMARK 500   NE   ARG B    45     O    HOH B  2008              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  2011     O    HOH B  2011     2665     0.76            
REMARK 500   ND2  ASN A    75     ND2  ASN A    75    10665     2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A  63   CB    PHE A  63   CG     -0.123                       
REMARK 500    VAL A  64   CA    VAL A  64   CB     -0.141                       
REMARK 500    LYS A  66   CD    LYS A  66   CE      0.176                       
REMARK 500    GLU A  98   CB    GLU A  98   CG      0.136                       
REMARK 500    GLU A  98   CG    GLU A  98   CD      0.133                       
REMARK 500    GLU B  85   CG    GLU B  85   CD      0.106                       
REMARK 500    PHE B  99   CB    PHE B  99   CG     -0.103                       
REMARK 500    GLU B 145   CG    GLU B 145   CD      0.099                       
REMARK 500    GLU B 145   CD    GLU B 145   OE1     0.071                       
REMARK 500    VAL B 150   CB    VAL B 150   CG2    -0.127                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ILE A 122   CG1 -  CB  -  CG2 ANGL. DEV. = -14.4 DEGREES          
REMARK 500    ARG A 138   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG B  25   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASN B  70   N   -  CA  -  C   ANGL. DEV. = -17.8 DEGREES          
REMARK 500    PRO B  96   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    PRO B  96   C   -  N   -  CD  ANGL. DEV. = -12.9 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    ASN A  27       63.54   -109.63                                   
REMARK 500    SER A  30        8.79    -65.04                                   
REMARK 500    ALA A  32     -179.20    -57.34                                   
REMARK 500    ALA A  39      148.33   -171.77                                   
REMARK 500    ASN A  42      126.40    -24.42                                   
REMARK 500    PRO A  44       -9.12    -44.97                                   
REMARK 500    VAL A  52      104.52    -54.16                                   
REMARK 500    LYS A  61      -65.15   -100.70                                   
REMARK 500    ALA A  71     -173.55    -56.24                                   
REMARK 500    ASN A  99       37.01     71.90                                   
REMARK 500    GLU A 109      132.97   -174.29                                   
REMARK 500    TYR A 112      -25.14     61.05                                   
REMARK 500    ASN A 114      -48.31   -138.01                                   
REMARK 500    HIS A 129     -177.48   -173.88                                   
REMARK 500    SER A 130      133.98   -171.43                                   
REMARK 500    ALA A 140      -47.14    -18.92                                   
REMARK 500    ALA A 143      107.64    -46.11                                   
REMARK 500    ASP A 144       29.76    -58.53                                   
REMARK 500    ASP A 160       94.90    -65.90                                   
REMARK 500    CYS A 173      128.37    -39.48                                   
REMARK 500    PRO A 174       37.29    -80.47                                   
REMARK 500    LYS A 179       -5.27    -50.97                                   
REMARK 500    PRO B   4      158.23    -45.10                                   
REMARK 500    ASP B  94       69.87   -108.20                                   
REMARK 500    PRO B  96      -72.79    -34.52                                   
REMARK 500    TYR B 110      -41.84     65.39                                   
REMARK 500    THR B 112      -55.39   -124.57                                   
REMARK 500    THR B 122      -69.88   -108.48                                   
REMARK 500    ASP B 123      -69.69   -126.09                                   
REMARK 500    PRO B 137       44.98    -90.33                                   
REMARK 500    THR B 167     -151.85   -127.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B  26         0.07    SIDE CHAIN                              
REMARK 500    TYR B  53         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  9-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL. REMARK 900                                            
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AXT A1182                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D12 A1183                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AXT B1175                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B1176                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B1177                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1H91   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF LOBSTER APOCRUSTACYANIN A1 USING SOFTER X-  
REMARK 900 RAYS.                                                                
DBREF  1GKA A    2   181  PDB    1GKA     1GKA             2    181             
DBREF  1GKA B    1   174  UNP    P80007   CRA2_HOMGA       1    174             
SEQRES   1 A  180  LYS ILE PRO ASN PHE VAL VAL PRO GLY LYS CYS ALA SER          
SEQRES   2 A  180  VAL ASP ARG ASN LYS LEU TRP ALA GLU GLN THR PRO ASN          
SEQRES   3 A  180  ARG ASN SER TYR ALA GLY VAL TRP TYR GLN PHE ALA LEU          
SEQRES   4 A  180  THR ASN ASN PRO TYR GLN LEU ILE GLU LYS CYS VAL ARG          
SEQRES   5 A  180  ASN GLU TYR SER PHE ASP GLY LYS GLN PHE VAL ILE LYS          
SEQRES   6 A  180  SER THR GLY ILE ALA TYR ASP GLY ASN LEU LEU LYS ARG          
SEQRES   7 A  180  ASN GLY LYS LEU TYR PRO ASN PRO PHE GLY GLU PRO HIS          
SEQRES   8 A  180  LEU SER ILE ASP TYR GLU ASN SER PHE ALA ALA PRO LEU          
SEQRES   9 A  180  VAL ILE LEU GLU THR ASP TYR SER ASN TYR ALA CYS LEU          
SEQRES  10 A  180  TYR SER CYS ILE ASP TYR ASN PHE GLY TYR HIS SER ASP          
SEQRES  11 A  180  PHE SER PHE ILE PHE SER ARG SER ALA ASN LEU ALA ASP          
SEQRES  12 A  180  GLN TYR VAL LYS LYS CYS GLU ALA ALA PHE LYS ASN ILE          
SEQRES  13 A  180  ASN VAL ASP THR THR ARG PHE VAL LYS THR VAL GLN GLY          
SEQRES  14 A  180  SER SER CYS PRO TYR ASP THR GLN LYS THR VAL                  
SEQRES   1 B  174  ASP GLY ILE PRO SER PHE VAL THR ALA GLY LYS CYS ALA          
SEQRES   2 B  174  SER VAL ALA ASN GLN ASP ASN PHE ASP LEU ARG ARG TYR          
SEQRES   3 B  174  ALA GLY ARG TRP TYR GLN THR HIS ILE ILE GLU ASN ALA          
SEQRES   4 B  174  TYR GLN PRO VAL THR ARG CYS ILE HIS SER ASN TYR GLU          
SEQRES   5 B  174  TYR SER THR ASN ASP TYR GLY PHE LYS VAL THR THR ALA          
SEQRES   6 B  174  GLY PHE ASN PRO ASN ASP GLU TYR LEU LYS ILE ASP PHE          
SEQRES   7 B  174  LYS VAL TYR PRO THR LYS GLU PHE PRO ALA ALA HIS MET          
SEQRES   8 B  174  LEU ILE ASP ALA PRO SER VAL PHE ALA ALA PRO TYR GLU          
SEQRES   9 B  174  VAL ILE GLU THR ASP TYR GLU THR TYR SER CYS VAL TYR          
SEQRES  10 B  174  SER CYS ILE THR THR ASP ASN TYR LYS SER GLU PHE ALA          
SEQRES  11 B  174  PHE VAL PHE SER ARG THR PRO GLN THR SER GLY PRO ALA          
SEQRES  12 B  174  VAL GLU LYS THR ALA ALA VAL PHE ASN LYS ASN GLY VAL          
SEQRES  13 B  174  GLU PHE SER LYS PHE VAL PRO VAL SER HIS THR ALA GLU          
SEQRES  14 B  174  CYS VAL TYR ARG ALA                                          
HET    AXT  A1182      44                                                       
HET    D12  A1183      12                                                       
HET    AXT  B1175      44                                                       
HET    TRS  B1176       8                                                       
HET    EPE  B1177      15                                                       
HETNAM     AXT ASTAXANTHIN                                                      
HETNAM     D12 DODECANE                                                         
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETSYN     AXT 3,3'-DIHYDROXY-BETA,BETA-CAROTENE-4,4'-DIONE                     
HETSYN     TRS TRIS BUFFER                                                      
HETSYN     EPE HEPES                                                            
FORMUL   3  AXT    2(C40 H52 O4)                                                
FORMUL   4  D12    C12 H26                                                      
FORMUL   6  TRS    C4 H12 N O3 1+                                               
FORMUL   7  EPE    C8 H18 N2 O4 S                                               
FORMUL   8  HOH   *30(H2 O)                                                     
HELIX    1   1 ASP A   16  THR A   25  1                                  10    
HELIX    2   2 ARG A   28  ALA A   32  5                                   5    
HELIX    3   3 TYR A  146  LYS A  155  1                                  10    
HELIX    4   4 ASP A  160  PHE A  164  5                                   5    
HELIX    5   5 PRO A  174  LYS A  179  1                                   6    
HELIX    6   6 GLY B  141  GLY B  155  1                                  15    
HELIX    7   7 GLU B  157  PHE B  161  5                                   5    
SHEET    1  AA10 VAL A   8  PRO A   9  0                                        
SHEET    2  AA10 TYR A 128  SER A 137 -1  O  HIS A 129   N  VAL A   8           
SHEET    3  AA10 TYR A 115  ASP A 123 -1  O  ALA A 116   N  PHE A 136           
SHEET    4  AA10 ALA A 103  THR A 110 -1  O  VAL A 106   N  TYR A 119           
SHEET    5  AA10 LEU A  93  ILE A  95 -1  O  LEU A  93   N  LEU A 105           
SHEET    6  AA10 LEU A  76  PRO A  85 -1  O  TYR A  84   N  SER A  94           
SHEET    7  AA10 PHE A  63  ALA A  71 -1  O  PHE A  63   N  LEU A  83           
SHEET    8  AA10 ILE A  48  PHE A  58 -1  N  GLU A  49   O  ILE A  70           
SHEET    9  AA10 GLY A  33  LEU A  40 -1  O  GLY A  33   N  TYR A  56           
SHEET   10  AA10 VAL A   8  PRO A   9  0                                        
SHEET    1  BA 3 VAL B   7  ALA B   9  0                                        
SHEET    2  BA 3 TYR B 125  SER B 134 -1  O  LYS B 126   N  THR B   8           
SHEET    3  BA 3 GLY B  28  ILE B  35 -1  O  TYR B  31   N  SER B 134           
SHEET    1  BB 7 VAL B   7  ALA B   9  0                                        
SHEET    2  BB 7 TYR B 125  SER B 134 -1  O  LYS B 126   N  THR B   8           
SHEET    3  BB 7 TYR B 113  THR B 121 -1  O  SER B 114   N  PHE B 133           
SHEET    4  BB 7 ALA B 101  THR B 108 -1  O  GLU B 104   N  TYR B 117           
SHEET    5  BB 7 HIS B  90  ASP B  94 -1  O  MET B  91   N  TYR B 103           
SHEET    6  BB 7 LYS B  79  TYR B  81 -1  O  LYS B  79   N  ASP B  94           
SHEET    7  BB 7 GLY B  59  PHE B  67 -1  O  PHE B  60   N  VAL B  80           
SSBOND   1 CYS A   12    CYS A  121                          1555   1555  2.04  
SSBOND   2 CYS A   51    CYS A  173                          1555   1555  2.05  
SSBOND   3 CYS A  117    CYS A  150                          1555   1555  2.08  
SSBOND   4 CYS B   12    CYS B  119                          1555   1555  2.03  
SSBOND   5 CYS B   46    CYS B  170                          1555   1555  2.07  
SITE     1 AC1 24 PHE A   6  VAL A   7  TYR A  45  GLN A  46                    
SITE     2 AC1 24 ASN A  54  SER A  67  ILE A  95  TYR A  97                    
SITE     3 AC1 24 ALA A 103  SER A 120  TYR A 124  PHE A 126                    
SITE     4 AC1 24 TYR A 128  PHE A 132  PHE A 134  PHE A 136                    
SITE     5 AC1 24 D12 A1183  HOH A2007  PHE B  86  HIS B  90                    
SITE     6 AC1 24 PHE B  99  ALA B 100  ALA B 101  PRO B 102                    
SITE     1 AC2  6 TYR A  45  PHE A 101  ALA A 102  AXT A1182                    
SITE     2 AC2  6 PHE B  99  AXT B1175                                          
SITE     1 AC3 22 ASN A  86  HIS A  92  SER A  94  PRO A 104                    
SITE     2 AC3 22 D12 A1183  ILE B   3  PRO B   4  PHE B   6                    
SITE     3 AC3 22 GLN B  32  ASN B  38  TYR B  40  GLN B  41                    
SITE     4 AC3 22 THR B  64  PHE B  78  ILE B  93  ALA B 101                    
SITE     5 AC3 22 SER B 118  THR B 122  SER B 127  PHE B 129                    
SITE     6 AC3 22 PHE B 131  HOH B2019                                          
SITE     1 AC4  5 GLN B  18  ARG B  25  TYR B 110  PRO B 137                    
SITE     2 AC4  5 GLN B 138                                                     
SITE     1 AC5  5 ASN A  18  TRP A  21  PRO A  91  LYS B  11                    
SITE     2 AC5  5 CYS B  12                                                     
CRYST1  155.466  155.466  168.504  90.00  90.00 120.00 P 63 2 2     12          
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      0.006432  0.003714  0.000000        0.00000                         
SCALE2      0.000000  0.007427  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005934        0.00000                         
ATOM      1  N   LYS A   2      26.251  86.140  21.804  1.00 42.45           N  
ATOM      2  CA  LYS A   2      27.086  84.933  21.449  1.00 42.74           C  
ATOM      3  C   LYS A   2      28.499  85.085  20.710  1.00 43.49           C  
ATOM      4  O   LYS A   2      29.321  84.135  20.726  1.00 43.43           O  
ATOM      5  CB  LYS A   2      26.201  83.940  20.669  1.00 41.87           C  
ATOM      6  CG  LYS A   2      25.771  82.747  21.435  1.00 41.08           C  
ATOM      7  CD  LYS A   2      25.595  81.593  20.521  1.00 41.11           C  
ATOM      8  CE  LYS A   2      25.452  80.340  21.375  1.00 42.68           C  
ATOM      9  NZ  LYS A   2      26.687  79.477  21.370  1.00 43.05           N  
ATOM     10  N   ILE A   3      28.816  86.212  20.059  1.00 43.60           N  
ATOM     11  CA  ILE A   3      30.138  86.275  19.418  1.00 44.26           C  
ATOM     12  C   ILE A   3      31.158  86.270  20.530  1.00 45.51           C  
ATOM     13  O   ILE A   3      31.105  87.139  21.393  1.00 46.60           O  
ATOM     14  CB  ILE A   3      30.363  87.582  18.687  1.00 44.47           C  
ATOM     15  CG1 ILE A   3      29.259  87.825  17.679  1.00 44.43           C  
ATOM     16  CG2 ILE A   3      31.729  87.576  18.018  1.00 43.55           C  
ATOM     17  CD1 ILE A   3      29.759  88.560  16.473  1.00 43.51           C  
ATOM     18  N   PRO A   4      32.121  85.343  20.541  1.00 46.57           N  
ATOM     19  CA  PRO A   4      33.055  85.425  21.673  1.00 47.62           C  
ATOM     20  C   PRO A   4      33.725  86.771  21.936  1.00 48.72           C  
ATOM     21  O   PRO A   4      33.894  87.622  21.020  1.00 48.75           O  
ATOM     22  CB  PRO A   4      34.063  84.330  21.376  1.00 47.03           C  
ATOM     23  CG  PRO A   4      33.210  83.301  20.825  1.00 48.16           C  
ATOM     24  CD  PRO A   4      32.305  84.071  19.839  1.00 47.97           C  
ATOM     25  N   ASN A   5      34.088  86.958  23.210  1.00 49.50           N  
ATOM     26  CA  ASN A   5      34.760  88.178  23.635  1.00 49.96           C  
ATOM     27  C   ASN A   5      36.167  88.305  23.006  1.00 47.86           C  
ATOM     28  O   ASN A   5      36.640  89.429  22.794  1.00 47.32           O  
ATOM     29  CB  ASN A   5      34.810  88.256  25.184  1.00 54.18           C  
ATOM     30  CG  ASN A   5      33.659  89.163  25.798  1.00 58.49           C  
ATOM     31  OD1 ASN A   5      33.653  90.428  25.660  1.00 59.69           O  
ATOM     32  ND2 ASN A   5      32.690  88.505  26.480  1.00 60.81           N  
ATOM     33  N   PHE A   6      36.807  87.169  22.681  1.00 45.21           N  
ATOM     34  CA  PHE A   6      38.129  87.187  22.056  1.00 42.39           C  
ATOM     35  C   PHE A   6      38.162  87.427  20.586  1.00 42.01           C  
ATOM     36  O   PHE A   6      39.246  87.539  20.016  1.00 42.13           O  
ATOM     37  CB  PHE A   6      38.946  85.926  22.323  1.00 40.16           C  
ATOM     38  CG  PHE A   6      38.245  84.674  22.076  1.00 37.12           C  
ATOM     39  CD1 PHE A   6      37.615  84.020  23.087  1.00 37.43           C  
ATOM     40  CD2 PHE A   6      38.258  84.111  20.860  1.00 37.61           C  
ATOM     41  CE1 PHE A   6      37.001  82.794  22.889  1.00 37.69           C  
ATOM     42  CE2 PHE A   6      37.650  82.886  20.656  1.00 38.46           C  
ATOM     43  CZ  PHE A   6      37.017  82.225  21.684  1.00 37.34           C  
ATOM     44  N   VAL A   7      36.987  87.489  19.970  1.00 41.64           N  
ATOM     45  CA  VAL A   7      36.882  87.754  18.552  1.00 40.88           C  
ATOM     46  C   VAL A   7      36.740  89.249  18.452  1.00 40.36           C  
ATOM     47  O   VAL A   7      35.698  89.825  18.726  1.00 40.39           O  
ATOM     48  CB  VAL A   7      35.699  87.076  17.950  1.00 41.31           C  
ATOM     49  CG1 VAL A   7      35.466  87.677  16.604  1.00 42.39           C  
ATOM     50  CG2 VAL A   7      35.959  85.575  17.797  1.00 40.14           C  
ATOM     51  N   VAL A   8      37.834  89.831  18.005  1.00 40.22           N  
ATOM     52  CA  VAL A   8      38.095  91.248  17.939  1.00 40.31           C  
ATOM     53  C   VAL A   8      38.553  91.883  16.612  1.00 41.11           C  
ATOM     54  O   VAL A   8      39.190  91.235  15.767  1.00 41.94           O  
ATOM     55  CB  VAL A   8      39.200  91.444  18.921  1.00 40.06           C  
ATOM     56  CG1 VAL A   8      39.834  92.774  18.766  1.00 41.97           C  
ATOM     57  CG2 VAL A   8      38.682  91.205  20.263  1.00 39.91           C  
ATOM     58  N   PRO A   9      38.297  93.182  16.434  1.00 40.81           N  
ATOM     59  CA  PRO A   9      38.707  93.881  15.218  1.00 41.58           C  
ATOM     60  C   PRO A   9      40.207  93.778  15.018  1.00 43.04           C  
ATOM     61  O   PRO A   9      40.956  93.899  15.988  1.00 43.32           O  
ATOM     62  CB  PRO A   9      38.301  95.291  15.504  1.00 40.68           C  
ATOM     63  CG  PRO A   9      37.083  95.098  16.307  1.00 40.38           C  
ATOM     64  CD  PRO A   9      37.421  94.025  17.242  1.00 40.23           C  
ATOM     65  N   GLY A  10      40.637  93.571  13.776  1.00 44.49           N  
ATOM     66  CA  GLY A  10      42.051  93.463  13.474  1.00 47.40           C  
ATOM     67  C   GLY A  10      42.478  92.269  12.626  1.00 50.03           C  
ATOM     68  O   GLY A  10      41.694  91.345  12.381  1.00 50.85           O  
ATOM     69  N   LYS A  11      43.733  92.289  12.167  1.00 51.71           N  
ATOM     70  CA  LYS A  11      44.308  91.221  11.346  1.00 52.63           C  
ATOM     71  C   LYS A  11      45.324  90.472  12.184  1.00 52.54           C  
ATOM     72  O   LYS A  11      45.818  90.998  13.198  1.00 52.70           O  
ATOM     73  CB  LYS A  11      45.111  91.797  10.189  1.00 54.80           C  
ATOM     74  CG  LYS A  11      44.391  92.579   9.116  1.00 58.64           C  
ATOM     75  CD  LYS A  11      45.389  93.515   8.263  1.00 61.86           C  
ATOM     76  CE  LYS A  11      46.595  92.802   7.492  1.00 63.38           C  
ATOM     77  NZ  LYS A  11      46.230  91.616   6.566  1.00 63.49           N  
ATOM     78  N   CYS A  12      45.672  89.259  11.760  1.00 51.87           N  
ATOM     79  CA  CYS A  12      46.711  88.557  12.475  1.00 51.46           C  
ATOM     80  C   CYS A  12      47.950  89.179  11.927  1.00 52.66           C  
ATOM     81  O   CYS A  12      47.918  89.852  10.910  1.00 52.69           O  
ATOM     82  CB  CYS A  12      46.772  87.117  12.140  1.00 49.65           C  
ATOM     83  SG  CYS A  12      45.425  86.083  12.767  1.00 48.90           S  
ATOM     84  N   ALA A  13      49.067  88.931  12.577  1.00 54.23           N  
ATOM     85  CA  ALA A  13      50.292  89.558  12.136  1.00 55.41           C  
ATOM     86  C   ALA A  13      51.017  88.700  11.163  1.00 56.01           C  
ATOM     87  O   ALA A  13      50.808  87.490  11.127  1.00 56.19           O  
ATOM     88  CB  ALA A  13      51.160  89.855  13.318  1.00 55.89           C  
ATOM     89  N   SER A  14      51.865  89.327  10.359  1.00 56.75           N  
ATOM     90  CA  SER A  14      52.614  88.559   9.385  1.00 58.24           C  
ATOM     91  C   SER A  14      53.871  87.977  10.033  1.00 57.87           C  
ATOM     92  O   SER A  14      54.839  88.696  10.265  1.00 58.89           O  
ATOM     93  CB  SER A  14      53.003  89.443   8.179  1.00 60.26           C  
ATOM     94  OG  SER A  14      52.362  89.040   6.954  1.00 63.24           O  
ATOM     95  N   VAL A  15      53.865  86.689  10.357  1.00 56.43           N  
ATOM     96  CA  VAL A  15      55.064  86.097  10.929  1.00 54.85           C  
ATOM     97  C   VAL A  15      55.656  85.349   9.732  1.00 54.50           C  
ATOM     98  O   VAL A  15      54.925  85.047   8.787  1.00 54.58           O  
ATOM     99  CB  VAL A  15      54.696  85.193  12.098  1.00 54.16           C  
ATOM    100  CG1 VAL A  15      53.236  85.334  12.360  1.00 53.59           C  
ATOM    101  CG2 VAL A  15      55.045  83.758  11.823  1.00 53.58           C  
ATOM    102  N   ASP A  16      56.964  85.111   9.727  1.00 53.85           N  
ATOM    103  CA  ASP A  16      57.612  84.432   8.597  1.00 53.20           C  
ATOM    104  C   ASP A  16      57.530  82.936   8.934  1.00 51.56           C  
ATOM    105  O   ASP A  16      58.466  82.382   9.494  1.00 51.72           O  
ATOM    106  CB  ASP A  16      59.083  84.928   8.491  1.00 55.05           C  
ATOM    107  CG  ASP A  16      59.823  84.455   7.187  1.00 56.86           C  
ATOM    108  OD1 ASP A  16      60.839  85.117   6.864  1.00 58.09           O  
ATOM    109  OD2 ASP A  16      59.447  83.448   6.501  1.00 57.57           O  
ATOM    110  N   ARG A  17      56.432  82.274   8.575  1.00 48.94           N  
ATOM    111  CA  ARG A  17      56.287  80.893   8.976  1.00 46.86           C  
ATOM    112  C   ARG A  17      57.104  79.941   8.264  1.00 45.91           C  
ATOM    113  O   ARG A  17      57.360  78.875   8.806  1.00 46.48           O  
ATOM    114  CB  ARG A  17      54.892  80.376   8.812  1.00 46.65           C  
ATOM    115  CG  ARG A  17      53.853  81.194   9.366  1.00 46.57           C  
ATOM    116  CD  ARG A  17      52.631  80.442   9.116  1.00 48.52           C  
ATOM    117  NE  ARG A  17      51.794  81.010   8.077  1.00 51.05           N  
ATOM    118  CZ  ARG A  17      50.833  80.304   7.491  1.00 53.24           C  
ATOM    119  NH1 ARG A  17      50.649  79.030   7.844  1.00 53.92           N  
ATOM    120  NH2 ARG A  17      49.998  80.870   6.623  1.00 53.76           N  
ATOM    121  N   ASN A  18      57.468  80.295   7.040  1.00 44.81           N  
ATOM    122  CA  ASN A  18      58.233  79.392   6.200  1.00 43.99           C  
ATOM    123  C   ASN A  18      59.599  79.170   6.706  1.00 42.76           C  
ATOM    124  O   ASN A  18      60.089  78.053   6.724  1.00 41.03           O  
ATOM    125  CB  ASN A  18      58.310  79.897   4.766  1.00 45.30           C  
ATOM    126  CG  ASN A  18      57.082  79.519   3.950  1.00 45.97           C  
ATOM    127  OD1 ASN A  18      56.250  80.352   3.684  1.00 47.88           O  
ATOM    128  ND2 ASN A  18      56.963  78.258   3.569  1.00 47.46           N  
ATOM    129  N   LYS A  19      60.206  80.278   7.092  1.00 43.08           N  
ATOM    130  CA  LYS A  19      61.556  80.297   7.645  1.00 43.47           C  
ATOM    131  C   LYS A  19      61.552  79.420   8.864  1.00 41.72           C  
ATOM    132  O   LYS A  19      62.363  78.511   8.946  1.00 43.02           O  
ATOM    133  CB  LYS A  19      61.944  81.721   8.049  1.00 45.82           C  
ATOM    134  CG  LYS A  19      63.326  81.913   8.656  1.00 49.19           C  
ATOM    135  CD  LYS A  19      63.632  83.443   8.701  1.00 52.63           C  
ATOM    136  CE  LYS A  19      65.056  83.758   9.208  1.00 55.21           C  
ATOM    137  NZ  LYS A  19      65.302  83.424  10.702  1.00 58.43           N  
ATOM    138  N   LEU A  20      60.626  79.700   9.789  1.00 38.61           N  
ATOM    139  CA  LEU A  20      60.480  78.976  11.036  1.00 34.72           C  
ATOM    140  C   LEU A  20      60.298  77.551  10.750  1.00 33.81           C  
ATOM    141  O   LEU A  20      60.956  76.716  11.311  1.00 33.16           O  
ATOM    142  CB  LEU A  20      59.280  79.479  11.827  1.00 33.69           C  
ATOM    143  CG  LEU A  20      59.497  80.907  12.338  1.00 32.58           C  
ATOM    144  CD1 LEU A  20      58.434  81.407  13.218  1.00 31.31           C  
ATOM    145  CD2 LEU A  20      60.743  80.899  13.105  1.00 33.55           C  
ATOM    146  N   TRP A  21      59.414  77.263   9.818  1.00 33.95           N  
ATOM    147  CA  TRP A  21      59.089  75.880   9.501  1.00 33.47           C  
ATOM    148  C   TRP A  21      60.258  75.058   8.986  1.00 34.69           C  
ATOM    149  O   TRP A  21      60.336  73.849   9.212  1.00 34.43           O  
ATOM    150  CB  TRP A  21      57.906  75.880   8.540  1.00 30.67           C  
ATOM    151  CG  TRP A  21      57.494  74.569   8.098  1.00 28.57           C  
ATOM    152  CD1 TRP A  21      57.954  73.874   7.032  1.00 28.39           C  
ATOM    153  CD2 TRP A  21      56.593  73.741   8.741  1.00 27.98           C  
ATOM    154  NE1 TRP A  21      57.386  72.643   6.971  1.00 26.30           N  
ATOM    155  CE2 TRP A  21      56.545  72.534   8.026  1.00 26.91           C  
ATOM    156  CE3 TRP A  21      55.817  73.888   9.866  1.00 28.32           C  
ATOM    157  CZ2 TRP A  21      55.779  71.500   8.399  1.00 26.62           C  
ATOM    158  CZ3 TRP A  21      55.047  72.858  10.235  1.00 27.97           C  
ATOM    159  CH2 TRP A  21      55.033  71.668   9.504  1.00 27.81           C  
ATOM    160  N   ALA A  22      61.191  75.721   8.324  1.00 36.58           N  
ATOM    161  CA  ALA A  22      62.327  75.023   7.765  1.00 38.52           C  
ATOM    162  C   ALA A  22      63.437  74.816   8.765  1.00 40.75           C  
ATOM    163  O   ALA A  22      64.182  73.808   8.642  1.00 41.94           O  
ATOM    164  CB  ALA A  22      62.830  75.758   6.606  1.00 38.30           C  
ATOM    165  N   GLU A  23      63.563  75.774   9.710  1.00 41.54           N  
ATOM    166  CA  GLU A  23      64.546  75.708  10.771  1.00 42.04           C  
ATOM    167  C   GLU A  23      63.967  74.621  11.616  1.00 41.98           C  
ATOM    168  O   GLU A  23      64.680  73.728  12.012  1.00 44.55           O  
ATOM    169  CB  GLU A  23      64.548  76.890  11.738  1.00 43.35           C  
ATOM    170  CG  GLU A  23      64.799  78.298  11.232  1.00 48.96           C  
ATOM    171  CD  GLU A  23      64.698  79.409  12.385  1.00 53.27           C  
ATOM    172  OE1 GLU A  23      63.964  79.227  13.449  1.00 54.27           O  
ATOM    173  OE2 GLU A  23      65.357  80.492  12.201  1.00 55.90           O  
ATOM    174  N   GLN A  24      62.657  74.655  11.853  1.00 39.82           N  
ATOM    175  CA  GLN A  24      62.058  73.728  12.810  1.00 37.94           C  
ATOM    176  C   GLN A  24      61.717  72.323  12.504  1.00 37.41           C  
ATOM    177  O   GLN A  24      61.578  71.521  13.395  1.00 37.55           O  
ATOM    178  CB  GLN A  24      60.791  74.346  13.436  1.00 36.71           C  
ATOM    179  CG  GLN A  24      60.962  75.724  14.064  1.00 36.63           C  
ATOM    180  CD  GLN A  24      59.642  76.339  14.448  1.00 36.40           C  
ATOM    181  OE1 GLN A  24      58.674  75.640  14.691  1.00 37.29           O  
ATOM    182  NE2 GLN A  24      59.602  77.642  14.515  1.00 35.96           N  
ATOM    183  N   THR A  25      61.569  71.994  11.259  1.00 37.89           N  
ATOM    184  CA  THR A  25      61.093  70.668  10.978  1.00 39.19           C  
ATOM    185  C   THR A  25      62.026  69.525  11.165  1.00 40.58           C  
ATOM    186  O   THR A  25      61.636  68.380  11.424  1.00 40.02           O  
ATOM    187  CB  THR A  25      60.592  70.658   9.611  1.00 39.16           C  
ATOM    188  OG1 THR A  25      59.440  71.501   9.582  1.00 39.22           O  
ATOM    189  CG2 THR A  25      60.246  69.262   9.209  1.00 39.53           C  
ATOM    190  N   PRO A  26      63.297  69.814  10.972  1.00 42.50           N  
ATOM    191  CA  PRO A  26      64.360  68.829  11.106  1.00 43.32           C  
ATOM    192  C   PRO A  26      64.621  68.412  12.568  1.00 44.11           C  
ATOM    193  O   PRO A  26      65.025  67.263  12.815  1.00 44.21           O  
ATOM    194  CB  PRO A  26      65.536  69.555  10.463  1.00 43.22           C  
ATOM    195  CG  PRO A  26      64.840  70.468   9.437  1.00 43.04           C  
ATOM    196  CD  PRO A  26      63.780  71.024  10.274  1.00 42.74           C  
ATOM    197  N   ASN A  27      64.390  69.350  13.503  1.00 44.52           N  
ATOM    198  CA  ASN A  27      64.595  69.150  14.938  1.00 45.69           C  
ATOM    199  C   ASN A  27      63.292  69.092  15.672  1.00 45.87           C  
ATOM    200  O   ASN A  27      63.012  69.912  16.531  1.00 46.27           O  
ATOM    201  CB  ASN A  27      65.341  70.308  15.497  1.00 47.35           C  
ATOM    202  CG  ASN A  27      66.460  70.714  14.633  1.00 49.94           C  
ATOM    203  OD1 ASN A  27      67.369  69.898  14.299  1.00 51.13           O  
ATOM    204  ND2 ASN A  27      66.438  71.987  14.240  1.00 50.64           N  
ATOM    205  N   ARG A  28      62.489  68.103  15.375  1.00 45.67           N  
ATOM    206  CA  ARG A  28      61.212  68.097  15.992  1.00 44.70           C  
ATOM    207  C   ARG A  28      61.260  67.212  17.166  1.00 44.11           C  
ATOM    208  O   ARG A  28      60.347  67.182  17.938  1.00 45.27           O  
ATOM    209  CB  ARG A  28      60.202  67.617  14.992  1.00 45.00           C  
ATOM    210  CG  ARG A  28      58.835  67.785  15.435  1.00 46.64           C  
ATOM    211  CD  ARG A  28      57.984  68.134  14.272  1.00 47.84           C  
ATOM    212  NE  ARG A  28      57.889  69.574  14.197  1.00 49.18           N  
ATOM    213  CZ  ARG A  28      57.513  70.192  13.096  1.00 50.26           C  
ATOM    214  NH1 ARG A  28      57.214  69.428  12.008  1.00 51.14           N  
ATOM    215  NH2 ARG A  28      57.454  71.537  13.097  1.00 48.85           N  
ATOM    216  N   ASN A  29      62.322  66.457  17.315  1.00 43.08           N  
ATOM    217  CA  ASN A  29      62.384  65.598  18.469  1.00 41.69           C  
ATOM    218  C   ASN A  29      62.941  66.433  19.618  1.00 40.49           C  
ATOM    219  O   ASN A  29      62.624  66.225  20.751  1.00 40.45           O  
ATOM    220  CB  ASN A  29      63.274  64.444  18.163  1.00 43.24           C  
ATOM    221  CG  ASN A  29      63.238  63.410  19.220  1.00 45.11           C  
ATOM    222  OD1 ASN A  29      62.209  62.775  19.446  1.00 46.10           O  
ATOM    223  ND2 ASN A  29      64.375  63.202  19.884  1.00 46.50           N  
ATOM    224  N   SER A  30      63.755  67.420  19.308  1.00 39.34           N  
ATOM    225  CA  SER A  30      64.319  68.288  20.316  1.00 37.76           C  
ATOM    226  C   SER A  30      63.194  69.052  20.942  1.00 36.67           C  
ATOM    227  O   SER A  30      63.428  69.978  21.680  1.00 37.81           O  
ATOM    228  CB  SER A  30      65.253  69.330  19.690  1.00 38.28           C  
ATOM    229  OG  SER A  30      66.336  68.742  18.992  1.00 40.42           O  
ATOM    230  N   TYR A  31      61.957  68.726  20.654  1.00 34.66           N  
ATOM    231  CA  TYR A  31      60.922  69.542  21.254  1.00 32.44           C  
ATOM    232  C   TYR A  31      60.156  68.713  22.212  1.00 32.53           C  
ATOM    233  O   TYR A  31      59.513  69.294  23.074  1.00 33.15           O  
ATOM    234  CB  TYR A  31      59.955  70.040  20.218  1.00 30.56           C  
ATOM    235  CG  TYR A  31      59.033  71.119  20.658  1.00 28.21           C  
ATOM    236  CD1 TYR A  31      59.499  72.413  20.807  1.00 28.55           C  
ATOM    237  CD2 TYR A  31      57.680  70.870  20.867  1.00 26.82           C  
ATOM    238  CE1 TYR A  31      58.643  73.455  21.165  1.00 27.76           C  
ATOM    239  CE2 TYR A  31      56.825  71.891  21.214  1.00 26.27           C  
ATOM    240  CZ  TYR A  31      57.328  73.174  21.366  1.00 27.46           C  
ATOM    241  OH  TYR A  31      56.539  74.190  21.779  1.00 29.16           O  
ATOM    242  N   ALA A  32      60.198  67.381  22.069  1.00 30.89           N  
ATOM    243  CA  ALA A  32      59.453  66.511  22.958  1.00 30.73           C  
ATOM    244  C   ALA A  32      59.923  66.832  24.342  1.00 31.80           C  
ATOM    245  O   ALA A  32      60.777  67.676  24.534  1.00 32.02           O  
ATOM    246  CB  ALA A  32      59.716  65.067  22.649  1.00 30.00           C  
ATOM    247  N   GLY A  33      59.406  66.160  25.343  1.00 32.67           N  
ATOM    248  CA  GLY A  33      59.872  66.535  26.653  1.00 34.20           C  
ATOM    249  C   GLY A  33      58.760  67.105  27.485  1.00 34.95           C  
ATOM    250  O   GLY A  33      57.599  66.781  27.252  1.00 36.78           O  
ATOM    251  N   VAL A  34      59.059  67.922  28.475  1.00 34.60           N  
ATOM    252  CA  VAL A  34      57.947  68.441  29.254  1.00 35.11           C  
ATOM    253  C   VAL A  34      58.149  69.911  29.171  1.00 35.44           C  
ATOM    254  O   VAL A  34      59.293  70.355  29.161  1.00 37.94           O  
ATOM    255  CB  VAL A  34      58.052  68.071  30.697  1.00 34.35           C  
ATOM    256  CG1 VAL A  34      57.808  66.541  30.932  1.00 33.52           C  
ATOM    257  CG2 VAL A  34      59.415  68.493  31.102  1.00 36.15           C  
ATOM    258  N   TRP A  35      57.076  70.675  29.073  1.00 34.20           N  
ATOM    259  CA  TRP A  35      57.243  72.098  29.017  1.00 33.90           C  
ATOM    260  C   TRP A  35      56.312  72.622  30.080  1.00 34.38           C  
ATOM    261  O   TRP A  35      55.171  72.165  30.162  1.00 35.39           O  
ATOM    262  CB  TRP A  35      56.831  72.660  27.658  1.00 33.21           C  
ATOM    263  CG  TRP A  35      57.774  72.480  26.557  1.00 31.60           C  
ATOM    264  CD1 TRP A  35      57.782  71.483  25.651  1.00 32.58           C  
ATOM    265  CD2 TRP A  35      58.871  73.304  26.249  1.00 30.81           C  
ATOM    266  NE1 TRP A  35      58.837  71.629  24.781  1.00 32.06           N  
ATOM    267  CE2 TRP A  35      59.522  72.747  25.142  1.00 31.35           C  
ATOM    268  CE3 TRP A  35      59.366  74.469  26.787  1.00 31.38           C  
ATOM    269  CZ2 TRP A  35      60.638  73.301  24.590  1.00 31.33           C  
ATOM    270  CZ3 TRP A  35      60.488  75.038  26.218  1.00 31.95           C  
ATOM    271  CH2 TRP A  35      61.112  74.450  25.135  1.00 31.22           C  
ATOM    272  N   TYR A  36      56.797  73.551  30.902  1.00 34.06           N  
ATOM    273  CA  TYR A  36      55.980  74.144  31.941  1.00 34.30           C  
ATOM    274  C   TYR A  36      55.452  75.381  31.251  1.00 34.61           C  
ATOM    275  O   TYR A  36      56.146  75.939  30.371  1.00 34.66           O  
ATOM    276  CB  TYR A  36      56.833  74.538  33.162  1.00 34.64           C  
ATOM    277  CG  TYR A  36      57.221  73.359  34.037  1.00 36.07           C  
ATOM    278  CD1 TYR A  36      58.472  72.766  33.908  1.00 36.47           C  
ATOM    279  CD2 TYR A  36      56.292  72.768  34.935  1.00 36.13           C  
ATOM    280  CE1 TYR A  36      58.806  71.597  34.633  1.00 38.05           C  
ATOM    281  CE2 TYR A  36      56.602  71.607  35.665  1.00 36.82           C  
ATOM    282  CZ  TYR A  36      57.875  71.008  35.505  1.00 38.43           C  
ATOM    283  OH  TYR A  36      58.232  69.788  36.120  1.00 38.79           O  
ATOM    284  N   GLN A  37      54.246  75.812  31.626  1.00 33.80           N  
ATOM    285  CA  GLN A  37      53.686  76.992  31.011  1.00 33.41           C  
ATOM    286  C   GLN A  37      54.151  78.147  31.789  1.00 33.72           C  
ATOM    287  O   GLN A  37      53.812  78.274  32.912  1.00 34.14           O  
ATOM    288  CB  GLN A  37      52.175  76.938  31.084  1.00 33.46           C  
ATOM    289  CG  GLN A  37      51.423  78.167  30.504  1.00 31.68           C  
ATOM    290  CD  GLN A  37      49.973  77.823  30.270  1.00 30.60           C  
ATOM    291  OE1 GLN A  37      49.674  76.934  29.439  1.00 30.53           O  
ATOM    292  NE2 GLN A  37      49.063  78.484  31.001  1.00 29.18           N  
ATOM    293  N   PHE A  38      54.923  79.020  31.226  1.00 35.29           N  
ATOM    294  CA  PHE A  38      55.351  80.156  32.032  1.00 38.69           C  
ATOM    295  C   PHE A  38      54.334  81.277  32.224  1.00 40.12           C  
ATOM    296  O   PHE A  38      54.229  81.847  33.312  1.00 41.38           O  
ATOM    297  CB  PHE A  38      56.578  80.791  31.440  1.00 40.04           C  
ATOM    298  CG  PHE A  38      56.971  82.048  32.116  1.00 41.58           C  
ATOM    299  CD1 PHE A  38      57.714  82.012  33.289  1.00 41.53           C  
ATOM    300  CD2 PHE A  38      56.623  83.274  31.573  1.00 42.47           C  
ATOM    301  CE1 PHE A  38      58.100  83.167  33.883  1.00 41.16           C  
ATOM    302  CE2 PHE A  38      57.020  84.454  32.183  1.00 42.13           C  
ATOM    303  CZ  PHE A  38      57.751  84.391  33.322  1.00 41.38           C  
ATOM    304  N   ALA A  39      53.642  81.621  31.139  1.00 41.87           N  
ATOM    305  CA  ALA A  39      52.609  82.662  31.098  1.00 42.03           C  
ATOM    306  C   ALA A  39      51.907  82.612  29.723  1.00 42.18           C  
ATOM    307  O   ALA A  39      52.546  82.253  28.722  1.00 41.54           O  
ATOM    308  CB  ALA A  39      53.253  84.033  31.331  1.00 40.61           C  
ATOM    309  N   LEU A  40      50.613  82.960  29.696  1.00 42.33           N  
ATOM    310  CA  LEU A  40      49.784  82.976  28.479  1.00 42.81           C  
ATOM    311  C   LEU A  40      48.846  84.159  28.398  1.00 43.75           C  
ATOM    312  O   LEU A  40      48.343  84.573  29.417  1.00 45.99           O  
ATOM    313  CB  LEU A  40      48.895  81.758  28.439  1.00 41.65           C  
ATOM    314  CG  LEU A  40      47.996  81.646  29.648  1.00 40.83           C  
ATOM    315  CD1 LEU A  40      46.828  82.616  29.578  1.00 41.26           C  
ATOM    316  CD2 LEU A  40      47.444  80.231  29.691  1.00 42.29           C  
ATOM    317  N   THR A  41      48.556  84.688  27.208  1.00 43.84           N  
ATOM    318  CA  THR A  41      47.593  85.800  27.088  1.00 43.26           C  
ATOM    319  C   THR A  41      46.214  85.161  27.268  1.00 43.56           C  
ATOM    320  O   THR A  41      45.994  84.051  26.768  1.00 43.96           O  
ATOM    321  CB  THR A  41      47.671  86.456  25.705  1.00 42.76           C  
ATOM    322  OG1 THR A  41      47.327  85.501  24.709  1.00 43.76           O  
ATOM    323  CG2 THR A  41      49.055  86.926  25.421  1.00 41.05           C  
ATOM    324  N   ASN A  42      45.298  85.833  27.971  1.00 43.78           N  
ATOM    325  CA  ASN A  42      43.952  85.270  28.244  1.00 43.95           C  
ATOM    326  C   ASN A  42      43.501  84.213  27.219  1.00 42.25           C  
ATOM    327  O   ASN A  42      43.455  84.515  26.035  1.00 43.89           O  
ATOM    328  CB  ASN A  42      42.896  86.387  28.288  1.00 45.93           C  
ATOM    329  CG  ASN A  42      41.455  85.833  28.527  1.00 48.83           C  
ATOM    330  OD1 ASN A  42      41.059  85.577  29.699  1.00 49.72           O  
ATOM    331  ND2 ASN A  42      40.671  85.635  27.413  1.00 48.81           N  
ATOM    332  N   ASN A  43      43.104  83.022  27.637  1.00 38.93           N  
ATOM    333  CA  ASN A  43      42.752  82.042  26.648  1.00 37.23           C  
ATOM    334  C   ASN A  43      41.764  81.020  27.125  1.00 36.43           C  
ATOM    335  O   ASN A  43      42.090  79.966  27.639  1.00 36.43           O  
ATOM    336  CB  ASN A  43      44.046  81.383  26.213  1.00 39.23           C  
ATOM    337  CG  ASN A  43      43.841  80.208  25.265  1.00 40.19           C  
ATOM    338  OD1 ASN A  43      42.711  79.658  25.127  1.00 40.57           O  
ATOM    339  ND2 ASN A  43      44.943  79.796  24.623  1.00 38.01           N  
ATOM    340  N   PRO A  44      40.521  81.282  26.906  1.00 35.58           N  
ATOM    341  CA  PRO A  44      39.495  80.360  27.350  1.00 35.36           C  
ATOM    342  C   PRO A  44      39.627  78.900  27.138  1.00 36.22           C  
ATOM    343  O   PRO A  44      38.825  78.136  27.696  1.00 37.16           O  
ATOM    344  CB  PRO A  44      38.249  80.886  26.728  1.00 34.24           C  
ATOM    345  CG  PRO A  44      38.723  81.909  25.788  1.00 36.02           C  
ATOM    346  CD  PRO A  44      39.954  82.464  26.290  1.00 35.82           C  
ATOM    347  N   TYR A  45      40.608  78.446  26.375  1.00 36.29           N  
ATOM    348  CA  TYR A  45      40.659  77.004  26.212  1.00 36.75           C  
ATOM    349  C   TYR A  45      41.558  76.235  27.190  1.00 38.83           C  
ATOM    350  O   TYR A  45      41.618  74.953  27.216  1.00 38.53           O  
ATOM    351  CB  TYR A  45      40.991  76.714  24.799  1.00 34.37           C  
ATOM    352  CG  TYR A  45      39.957  77.322  23.933  1.00 32.17           C  
ATOM    353  CD1 TYR A  45      39.985  78.656  23.636  1.00 30.75           C  
ATOM    354  CD2 TYR A  45      38.932  76.560  23.403  1.00 31.43           C  
ATOM    355  CE1 TYR A  45      39.016  79.222  22.811  1.00 30.00           C  
ATOM    356  CE2 TYR A  45      37.959  77.140  22.596  1.00 30.20           C  
ATOM    357  CZ  TYR A  45      38.016  78.464  22.307  1.00 29.63           C  
ATOM    358  OH  TYR A  45      37.051  79.043  21.539  1.00 30.28           O  
ATOM    359  N   GLN A  46      42.244  77.045  28.013  1.00 40.43           N  
ATOM    360  CA  GLN A  46      43.123  76.554  29.072  1.00 41.07           C  
ATOM    361  C   GLN A  46      42.237  76.285  30.285  1.00 40.42           C  
ATOM    362  O   GLN A  46      41.854  77.208  30.996  1.00 41.05           O  
ATOM    363  CB  GLN A  46      44.169  77.609  29.441  1.00 42.09           C  
ATOM    364  CG  GLN A  46      45.089  77.082  30.496  1.00 43.98           C  
ATOM    365  CD  GLN A  46      45.688  75.733  30.074  1.00 44.93           C  
ATOM    366  OE1 GLN A  46      45.038  74.649  30.126  1.00 46.03           O  
ATOM    367  NE2 GLN A  46      46.940  75.796  29.622  1.00 45.26           N  
ATOM    368  N   LEU A  47      41.883  75.037  30.500  1.00 39.69           N  
ATOM    369  CA  LEU A  47      41.043  74.752  31.616  1.00 39.81           C  
ATOM    370  C   LEU A  47      41.846  74.483  32.874  1.00 41.74           C  
ATOM    371  O   LEU A  47      41.242  74.278  33.943  1.00 43.29           O  
ATOM    372  CB  LEU A  47      40.169  73.573  31.312  1.00 37.14           C  
ATOM    373  CG  LEU A  47      39.310  73.720  30.093  1.00 34.47           C  
ATOM    374  CD1 LEU A  47      38.436  72.540  30.065  1.00 33.34           C  
ATOM    375  CD2 LEU A  47      38.509  74.986  30.105  1.00 34.45           C  
ATOM    376  N   ILE A  48      43.178  74.515  32.734  1.00 42.14           N  
ATOM    377  CA  ILE A  48      44.158  74.310  33.796  1.00 42.94           C  
ATOM    378  C   ILE A  48      44.743  75.665  34.285  1.00 45.75           C  
ATOM    379  O   ILE A  48      45.562  76.307  33.594  1.00 44.86           O  
ATOM    380  CB  ILE A  48      45.257  73.472  33.259  1.00 41.42           C  
ATOM    381  CG1 ILE A  48      44.847  72.033  33.286  1.00 40.38           C  
ATOM    382  CG2 ILE A  48      46.507  73.669  34.031  1.00 42.28           C  
ATOM    383  CD1 ILE A  48      45.943  71.097  32.751  1.00 38.82           C  
ATOM    384  N   GLU A  49      44.360  76.083  35.496  1.00 48.74           N  
ATOM    385  CA  GLU A  49      44.799  77.382  36.002  1.00 52.01           C  
ATOM    386  C   GLU A  49      46.201  77.544  36.505  1.00 52.60           C  
ATOM    387  O   GLU A  49      46.815  78.607  36.323  1.00 52.59           O  
ATOM    388  CB  GLU A  49      43.875  77.875  37.107  1.00 55.48           C  
ATOM    389  CG  GLU A  49      44.252  79.310  37.597  1.00 59.45           C  
ATOM    390  CD  GLU A  49      43.301  79.895  38.679  1.00 62.29           C  
ATOM    391  OE1 GLU A  49      43.423  81.144  38.919  1.00 63.09           O  
ATOM    392  OE2 GLU A  49      42.460  79.116  39.263  1.00 62.95           O  
ATOM    393  N   LYS A  50      46.687  76.532  37.218  1.00 53.41           N  
ATOM    394  CA  LYS A  50      48.041  76.606  37.735  1.00 54.36           C  
ATOM    395  C   LYS A  50      48.739  75.277  37.768  1.00 54.34           C  
ATOM    396  O   LYS A  50      48.093  74.203  37.781  1.00 54.63           O  
ATOM    397  CB  LYS A  50      48.091  77.272  39.120  1.00 56.53           C  
ATOM    398  CG  LYS A  50      46.857  77.126  40.039  1.00 59.18           C  
ATOM    399  CD  LYS A  50      46.744  78.351  41.015  1.00 61.06           C  
ATOM    400  CE  LYS A  50      45.451  78.340  41.905  1.00 62.47           C  
ATOM    401  NZ  LYS A  50      45.387  79.502  42.894  1.00 62.79           N  
ATOM    402  N   CYS A  51      50.069  75.360  37.728  1.00 54.04           N  
ATOM    403  CA  CYS A  51      50.924  74.170  37.738  1.00 54.47           C  
ATOM    404  C   CYS A  51      50.899  73.407  36.408  1.00 52.91           C  
ATOM    405  O   CYS A  51      51.178  72.219  36.338  1.00 53.46           O  
ATOM    406  CB  CYS A  51      50.520  73.238  38.913  1.00 55.88           C  
ATOM    407  SG  CYS A  51      50.711  74.019  40.569  1.00 57.45           S  
ATOM    408  N   VAL A  52      50.568  74.142  35.364  1.00 50.86           N  
ATOM    409  CA  VAL A  52      50.453  73.676  33.999  1.00 47.92           C  
ATOM    410  C   VAL A  52      51.745  72.975  33.552  1.00 45.98           C  
ATOM    411  O   VAL A  52      52.762  73.653  33.263  1.00 45.71           O  
ATOM    412  CB  VAL A  52      50.182  74.909  33.107  1.00 48.07           C  
ATOM    413  CG1 VAL A  52      49.948  74.501  31.771  1.00 49.17           C  
ATOM    414  CG2 VAL A  52      48.948  75.624  33.531  1.00 48.07           C  
ATOM    415  N   ARG A  53      51.699  71.636  33.492  1.00 43.35           N  
ATOM    416  CA  ARG A  53      52.841  70.794  33.076  1.00 41.10           C  
ATOM    417  C   ARG A  53      52.422  70.005  31.851  1.00 40.03           C  
ATOM    418  O   ARG A  53      51.691  68.992  31.925  1.00 39.88           O  
ATOM    419  CB  ARG A  53      53.244  69.805  34.189  1.00 41.97           C  
ATOM    420  CG  ARG A  53      54.652  69.234  34.060  1.00 40.97           C  
ATOM    421  CD  ARG A  53      55.160  68.553  35.298  1.00 39.60           C  
ATOM    422  NE  ARG A  53      55.818  67.317  34.921  1.00 39.91           N  
ATOM    423  CZ  ARG A  53      55.201  66.355  34.234  1.00 40.72           C  
ATOM    424  NH1 ARG A  53      53.910  66.511  33.866  1.00 39.36           N  
ATOM    425  NH2 ARG A  53      55.870  65.242  33.892  1.00 41.12           N  
ATOM    426  N   ASN A  54      52.915  70.494  30.719  1.00 38.02           N  
ATOM    427  CA  ASN A  54      52.638  69.977  29.404  1.00 36.09           C  
ATOM    428  C   ASN A  54      53.706  69.002  29.001  1.00 36.92           C  
ATOM    429  O   ASN A  54      54.827  69.430  28.762  1.00 36.60           O  
ATOM    430  CB  ASN A  54      52.647  71.156  28.484  1.00 33.49           C  
ATOM    431  CG  ASN A  54      51.478  72.049  28.711  1.00 33.03           C  
ATOM    432  OD1 ASN A  54      50.399  71.546  29.000  1.00 31.61           O  
ATOM    433  ND2 ASN A  54      51.654  73.387  28.550  1.00 32.75           N  
ATOM    434  N   GLU A  55      53.382  67.713  28.897  1.00 38.03           N  
ATOM    435  CA  GLU A  55      54.399  66.720  28.549  1.00 40.26           C  
ATOM    436  C   GLU A  55      54.263  66.152  27.146  1.00 39.85           C  
ATOM    437  O   GLU A  55      53.439  65.280  26.878  1.00 40.92           O  
ATOM    438  CB  GLU A  55      54.353  65.595  29.581  1.00 44.98           C  
ATOM    439  CG  GLU A  55      55.220  64.342  29.336  1.00 53.37           C  
ATOM    440  CD  GLU A  55      55.290  63.343  30.583  1.00 59.52           C  
ATOM    441  OE1 GLU A  55      56.001  62.283  30.419  1.00 62.53           O  
ATOM    442  OE2 GLU A  55      54.661  63.601  31.701  1.00 61.16           O  
ATOM    443  N   TYR A  56      55.103  66.620  26.247  1.00 38.53           N  
ATOM    444  CA  TYR A  56      55.068  66.176  24.865  1.00 38.19           C  
ATOM    445  C   TYR A  56      55.798  64.880  24.501  1.00 38.26           C  
ATOM    446  O   TYR A  56      56.949  64.695  24.834  1.00 38.89           O  
ATOM    447  CB  TYR A  56      55.637  67.277  24.020  1.00 37.78           C  
ATOM    448  CG  TYR A  56      54.740  68.470  23.860  1.00 37.77           C  
ATOM    449  CD1 TYR A  56      54.185  69.113  24.932  1.00 37.13           C  
ATOM    450  CD2 TYR A  56      54.521  68.996  22.622  1.00 38.34           C  
ATOM    451  CE1 TYR A  56      53.455  70.240  24.772  1.00 37.23           C  
ATOM    452  CE2 TYR A  56      53.791  70.121  22.463  1.00 38.94           C  
ATOM    453  CZ  TYR A  56      53.270  70.741  23.534  1.00 38.31           C  
ATOM    454  OH  TYR A  56      52.632  71.926  23.290  1.00 40.31           O  
ATOM    455  N   SER A  57      55.150  63.991  23.779  1.00 38.17           N  
ATOM    456  CA  SER A  57      55.818  62.782  23.393  1.00 39.71           C  
ATOM    457  C   SER A  57      55.812  62.620  21.876  1.00 41.34           C  
ATOM    458  O   SER A  57      54.769  62.313  21.283  1.00 43.08           O  
ATOM    459  CB  SER A  57      55.120  61.608  24.021  1.00 40.70           C  
ATOM    460  OG  SER A  57      54.733  60.655  23.031  1.00 41.97           O  
ATOM    461  N   PHE A  58      56.971  62.787  21.237  1.00 41.32           N  
ATOM    462  CA  PHE A  58      57.074  62.690  19.782  1.00 40.62           C  
ATOM    463  C   PHE A  58      57.065  61.277  19.309  1.00 41.16           C  
ATOM    464  O   PHE A  58      57.547  60.416  20.015  1.00 42.39           O  
ATOM    465  CB  PHE A  58      58.365  63.241  19.369  1.00 40.56           C  
ATOM    466  CG  PHE A  58      58.412  63.641  17.990  1.00 40.97           C  
ATOM    467  CD1 PHE A  58      59.422  63.231  17.196  1.00 41.03           C  
ATOM    468  CD2 PHE A  58      57.484  64.518  17.492  1.00 42.27           C  
ATOM    469  CE1 PHE A  58      59.511  63.691  15.931  1.00 41.98           C  
ATOM    470  CE2 PHE A  58      57.574  64.979  16.235  1.00 41.62           C  
ATOM    471  CZ  PHE A  58      58.588  64.567  15.454  1.00 41.71           C  
ATOM    472  N   ASP A  59      56.544  61.019  18.118  1.00 42.04           N  
ATOM    473  CA  ASP A  59      56.524  59.649  17.604  1.00 42.18           C  
ATOM    474  C   ASP A  59      57.104  59.535  16.237  1.00 41.24           C  
ATOM    475  O   ASP A  59      57.102  58.463  15.673  1.00 40.82           O  
ATOM    476  CB  ASP A  59      55.119  59.042  17.616  1.00 44.12           C  
ATOM    477  CG  ASP A  59      54.224  59.507  16.449  1.00 46.80           C  
ATOM    478  OD1 ASP A  59      54.527  60.542  15.763  1.00 46.52           O  
ATOM    479  OD2 ASP A  59      53.166  58.814  16.260  1.00 48.59           O  
ATOM    480  N   GLY A  60      57.626  60.653  15.731  1.00 40.99           N  
ATOM    481  CA  GLY A  60      58.255  60.703  14.425  1.00 40.00           C  
ATOM    482  C   GLY A  60      57.650  61.798  13.572  1.00 39.88           C  
ATOM    483  O   GLY A  60      58.395  62.597  13.015  1.00 40.36           O  
ATOM    484  N   LYS A  61      56.305  61.815  13.503  1.00 39.54           N  
ATOM    485  CA  LYS A  61      55.437  62.729  12.722  1.00 37.72           C  
ATOM    486  C   LYS A  61      54.850  63.813  13.541  1.00 36.92           C  
ATOM    487  O   LYS A  61      55.126  64.993  13.305  1.00 36.40           O  
ATOM    488  CB  LYS A  61      54.222  61.992  12.112  1.00 37.72           C  
ATOM    489  CG  LYS A  61      54.416  61.344  10.702  1.00 37.14           C  
ATOM    490  CD  LYS A  61      53.186  60.622  10.144  1.00 34.75           C  
ATOM    491  CE  LYS A  61      51.919  61.383  10.415  1.00 32.99           C  
ATOM    492  NZ  LYS A  61      52.008  62.794  10.045  1.00 32.45           N  
ATOM    493  N   GLN A  62      54.002  63.396  14.476  1.00 36.58           N  
ATOM    494  CA  GLN A  62      53.320  64.335  15.363  1.00 36.99           C  
ATOM    495  C   GLN A  62      53.548  64.020  16.858  1.00 35.06           C  
ATOM    496  O   GLN A  62      53.968  62.907  17.169  1.00 35.89           O  
ATOM    497  CB  GLN A  62      51.835  64.278  15.073  1.00 39.29           C  
ATOM    498  CG  GLN A  62      51.115  63.314  15.983  1.00 44.37           C  
ATOM    499  CD  GLN A  62      50.038  62.519  15.279  1.00 48.09           C  
ATOM    500  OE1 GLN A  62      48.811  62.711  15.496  1.00 49.53           O  
ATOM    501  NE2 GLN A  62      50.487  61.591  14.417  1.00 51.13           N  
ATOM    502  N   PHE A  63      53.282  64.973  17.767  1.00 31.17           N  
ATOM    503  CA  PHE A  63      53.404  64.717  19.203  1.00 27.92           C  
ATOM    504  C   PHE A  63      52.082  64.424  19.860  1.00 28.37           C  
ATOM    505  O   PHE A  63      51.051  64.870  19.419  1.00 28.45           O  
ATOM    506  CB  PHE A  63      53.815  65.896  19.966  1.00 23.95           C  
ATOM    507  CG  PHE A  63      54.918  66.555  19.447  1.00 20.78           C  
ATOM    508  CD1 PHE A  63      54.745  67.706  18.735  1.00 20.33           C  
ATOM    509  CD2 PHE A  63      56.153  66.144  19.763  1.00 19.18           C  
ATOM    510  CE1 PHE A  63      55.831  68.469  18.339  1.00 19.23           C  
ATOM    511  CE2 PHE A  63      57.238  66.897  19.382  1.00 19.59           C  
ATOM    512  CZ  PHE A  63      57.072  68.075  18.664  1.00 18.88           C  
ATOM    513  N   VAL A  64      52.134  63.764  21.001  1.00 29.08           N  
ATOM    514  CA  VAL A  64      50.942  63.471  21.758  1.00 30.39           C  
ATOM    515  C   VAL A  64      51.037  64.123  23.085  1.00 32.29           C  
ATOM    516  O   VAL A  64      51.823  63.680  23.872  1.00 33.43           O  
ATOM    517  CB  VAL A  64      50.857  62.112  22.092  1.00 29.00           C  
ATOM    518  CG1 VAL A  64      49.620  61.896  22.783  1.00 30.25           C  
ATOM    519  CG2 VAL A  64      50.936  61.334  20.896  1.00 31.52           C  
ATOM    520  N   ILE A  65      50.214  65.120  23.381  1.00 34.43           N  
ATOM    521  CA  ILE A  65      50.333  65.791  24.655  1.00 36.78           C  
ATOM    522  C   ILE A  65      49.558  65.216  25.870  1.00 39.24           C  
ATOM    523  O   ILE A  65      48.557  64.513  25.707  1.00 41.85           O  
ATOM    524  CB  ILE A  65      49.991  67.218  24.457  1.00 36.32           C  
ATOM    525  CG1 ILE A  65      50.765  67.769  23.252  1.00 36.93           C  
ATOM    526  CG2 ILE A  65      50.493  67.977  25.582  1.00 37.36           C  
ATOM    527  CD1 ILE A  65      50.764  69.314  23.102  1.00 33.74           C  
ATOM    528  N   LYS A  66      50.068  65.449  27.086  1.00 40.40           N  
ATOM    529  CA  LYS A  66      49.435  65.034  28.332  1.00 40.05           C  
ATOM    530  C   LYS A  66      49.678  66.283  29.159  1.00 39.76           C  
ATOM    531  O   LYS A  66      50.827  66.706  29.383  1.00 38.54           O  
ATOM    532  CB  LYS A  66      50.157  63.887  28.889  1.00 42.17           C  
ATOM    533  CG  LYS A  66      49.285  63.108  29.691  1.00 48.09           C  
ATOM    534  CD  LYS A  66      48.724  61.909  28.857  1.00 55.12           C  
ATOM    535  CE  LYS A  66      48.072  60.679  29.805  1.00 59.42           C  
ATOM    536  NZ  LYS A  66      47.168  59.470  29.243  1.00 59.67           N  
ATOM    537  N   SER A  67      48.590  66.941  29.542  1.00 39.73           N  
ATOM    538  CA  SER A  67      48.683  68.196  30.281  1.00 39.59           C  
ATOM    539  C   SER A  67      48.024  68.099  31.649  1.00 41.48           C  
ATOM    540  O   SER A  67      46.914  67.554  31.792  1.00 42.14           O  
ATOM    541  CB  SER A  67      48.050  69.283  29.463  1.00 38.23           C  
ATOM    542  OG  SER A  67      49.016  69.872  28.640  1.00 36.68           O  
ATOM    543  N   THR A  68      48.718  68.628  32.664  1.00 42.96           N  
ATOM    544  CA  THR A  68      48.288  68.526  34.073  1.00 43.42           C  
ATOM    545  C   THR A  68      48.510  69.770  34.887  1.00 44.07           C  
ATOM    546  O   THR A  68      49.394  70.584  34.614  1.00 43.48           O  
ATOM    547  CB  THR A  68      49.056  67.375  34.786  1.00 43.48           C  
ATOM    548  OG1 THR A  68      50.395  67.307  34.269  1.00 45.12           O  
ATOM    549  CG2 THR A  68      48.419  66.027  34.539  1.00 42.92           C  
ATOM    550  N   GLY A  69      47.695  69.887  35.920  1.00 46.19           N  
ATOM    551  CA  GLY A  69      47.752  71.030  36.837  1.00 48.52           C  
ATOM    552  C   GLY A  69      46.434  71.087  37.618  1.00 50.17           C  
ATOM    553  O   GLY A  69      45.690  70.065  37.758  1.00 50.09           O  
ATOM    554  N   ILE A  70      46.107  72.260  38.148  1.00 51.03           N  
ATOM    555  CA  ILE A  70      44.843  72.321  38.844  1.00 51.90           C  
ATOM    556  C   ILE A  70      43.933  73.264  38.156  1.00 53.72           C  
ATOM    557  O   ILE A  70      44.354  74.377  37.740  1.00 52.66           O  
ATOM    558  CB  ILE A  70      44.982  72.685  40.309  1.00 51.01           C  
ATOM    559  CG1 ILE A  70      46.054  73.747  40.521  1.00 50.07           C  
ATOM    560  CG2 ILE A  70      45.350  71.430  41.058  1.00 50.62           C  
ATOM    561  CD1 ILE A  70      47.325  73.159  41.144  1.00 48.62           C  
ATOM    562  N   ALA A  71      42.699  72.758  38.002  1.00 56.00           N  
ATOM    563  CA  ALA A  71      41.594  73.444  37.348  1.00 58.82           C  
ATOM    564  C   ALA A  71      41.344  74.771  38.006  1.00 61.27           C  
ATOM    565  O   ALA A  71      42.104  75.221  38.875  1.00 63.01           O  
ATOM    566  CB  ALA A  71      40.334  72.604  37.396  1.00 58.02           C  
ATOM    567  N   TYR A  72      40.285  75.437  37.595  1.00 63.47           N  
ATOM    568  CA  TYR A  72      40.037  76.716  38.216  1.00 64.74           C  
ATOM    569  C   TYR A  72      39.196  76.397  39.428  1.00 65.21           C  
ATOM    570  O   TYR A  72      39.231  77.101  40.470  1.00 65.09           O  
ATOM    571  CB  TYR A  72      39.300  77.614  37.244  1.00 65.34           C  
ATOM    572  CG  TYR A  72      40.214  78.396  36.334  1.00 66.42           C  
ATOM    573  CD1 TYR A  72      40.550  77.925  35.078  1.00 67.05           C  
ATOM    574  CD2 TYR A  72      40.669  79.666  36.705  1.00 67.17           C  
ATOM    575  CE1 TYR A  72      41.305  78.717  34.203  1.00 68.22           C  
ATOM    576  CE2 TYR A  72      41.424  80.464  35.840  1.00 67.68           C  
ATOM    577  CZ  TYR A  72      41.731  79.990  34.590  1.00 68.26           C  
ATOM    578  OH  TYR A  72      42.403  80.809  33.699  1.00 69.79           O  
ATOM    579  N   ASP A  73      38.470  75.290  39.275  1.00 65.29           N  
ATOM    580  CA  ASP A  73      37.580  74.833  40.309  1.00 65.68           C  
ATOM    581  C   ASP A  73      38.348  74.554  41.613  1.00 65.49           C  
ATOM    582  O   ASP A  73      37.825  74.799  42.725  1.00 66.83           O  
ATOM    583  CB  ASP A  73      36.723  73.630  39.774  1.00 66.52           C  
ATOM    584  CG  ASP A  73      37.312  72.214  40.076  1.00 67.15           C  
ATOM    585  OD1 ASP A  73      38.184  72.085  40.971  1.00 66.87           O  
ATOM    586  OD2 ASP A  73      36.856  71.216  39.422  1.00 67.41           O  
ATOM    587  N   GLY A  74      39.605  74.125  41.471  1.00 63.89           N  
ATOM    588  CA  GLY A  74      40.427  73.796  42.619  1.00 61.39           C  
ATOM    589  C   GLY A  74      41.069  72.423  42.483  1.00 59.89           C  
ATOM    590  O   GLY A  74      42.143  72.196  43.011  1.00 59.60           O  
ATOM    591  N   ASN A  75      40.416  71.516  41.766  1.00 58.48           N  
ATOM    592  CA  ASN A  75      40.922  70.173  41.531  1.00 57.52           C  
ATOM    593  C   ASN A  75      42.080  69.937  40.528  1.00 56.46           C  
ATOM    594  O   ASN A  75      42.517  70.793  39.755  1.00 56.40           O  
ATOM    595  CB  ASN A  75      39.802  69.284  41.060  1.00 59.62           C  
ATOM    596  CG  ASN A  75      38.639  69.201  42.039  1.00 61.72           C  
ATOM    597  OD1 ASN A  75      38.822  69.150  43.278  1.00 61.78           O  
ATOM    598  ND2 ASN A  75      37.403  69.141  41.472  1.00 62.42           N  
ATOM    599  N   LEU A  76      42.545  68.699  40.568  1.00 54.82           N  
ATOM    600  CA  LEU A  76      43.597  68.168  39.734  1.00 52.25           C  
ATOM    601  C   LEU A  76      42.945  67.809  38.433  1.00 52.41           C  
ATOM    602  O   LEU A  76      41.921  67.076  38.414  1.00 50.78           O  
ATOM    603  CB  LEU A  76      44.098  66.882  40.334  1.00 50.91           C  
ATOM    604  CG  LEU A  76      45.490  66.895  40.899  1.00 49.57           C  
ATOM    605  CD1 LEU A  76      45.862  68.293  41.190  1.00 49.15           C  
ATOM    606  CD2 LEU A  76      45.564  65.976  42.087  1.00 48.48           C  
ATOM    607  N   LEU A  77      43.557  68.297  37.341  1.00 52.73           N  
ATOM    608  CA  LEU A  77      43.049  68.036  35.975  1.00 51.68           C  
ATOM    609  C   LEU A  77      44.060  67.457  34.951  1.00 51.13           C  
ATOM    610  O   LEU A  77      45.198  67.947  34.831  1.00 51.12           O  
ATOM    611  CB  LEU A  77      42.406  69.327  35.439  1.00 50.15           C  
ATOM    612  CG  LEU A  77      41.632  69.222  34.124  1.00 50.68           C  
ATOM    613  CD1 LEU A  77      40.936  67.877  33.855  1.00 51.11           C  
ATOM    614  CD2 LEU A  77      40.641  70.304  34.184  1.00 51.49           C  
ATOM    615  N   LYS A  78      43.677  66.388  34.256  1.00 50.35           N  
ATOM    616  CA  LYS A  78      44.576  65.880  33.234  1.00 50.70           C  
ATOM    617  C   LYS A  78      43.856  66.033  31.920  1.00 51.10           C  
ATOM    618  O   LYS A  78      42.750  65.489  31.764  1.00 51.28           O  
ATOM    619  CB  LYS A  78      44.884  64.395  33.390  1.00 51.56           C  
ATOM    620  CG  LYS A  78      45.894  63.859  32.329  1.00 52.06           C  
ATOM    621  CD  LYS A  78      45.933  62.321  32.164  1.00 52.46           C  
ATOM    622  CE  LYS A  78      44.588  61.759  31.623  1.00 54.99           C  
ATOM    623  NZ  LYS A  78      44.513  60.210  31.525  1.00 57.47           N  
ATOM    624  N   ARG A  79      44.496  66.745  30.978  1.00 51.39           N  
ATOM    625  CA  ARG A  79      43.989  66.998  29.603  1.00 50.75           C  
ATOM    626  C   ARG A  79      44.876  66.422  28.523  1.00 49.15           C  
ATOM    627  O   ARG A  79      46.066  66.706  28.521  1.00 48.43           O  
ATOM    628  CB  ARG A  79      43.866  68.492  29.376  1.00 52.18           C  
ATOM    629  CG  ARG A  79      42.829  69.056  30.290  1.00 55.47           C  
ATOM    630  CD  ARG A  79      41.534  69.155  29.564  1.00 58.14           C  
ATOM    631  NE  ARG A  79      41.651  70.356  28.765  1.00 61.04           N  
ATOM    632  CZ  ARG A  79      40.924  70.597  27.690  1.00 62.78           C  
ATOM    633  NH1 ARG A  79      40.029  69.674  27.305  1.00 63.45           N  
ATOM    634  NH2 ARG A  79      41.085  71.758  27.025  1.00 62.41           N  
ATOM    635  N   ASN A  80      44.281  65.626  27.628  1.00 47.83           N  
ATOM    636  CA  ASN A  80      44.966  64.990  26.489  1.00 47.13           C  
ATOM    637  C   ASN A  80      44.934  65.788  25.162  1.00 45.54           C  
ATOM    638  O   ASN A  80      43.931  66.328  24.803  1.00 45.61           O  
ATOM    639  CB  ASN A  80      44.312  63.660  26.200  1.00 49.62           C  
ATOM    640  CG  ASN A  80      44.453  62.686  27.326  1.00 51.97           C  
ATOM    641  OD1 ASN A  80      45.573  62.416  27.778  1.00 52.31           O  
ATOM    642  ND2 ASN A  80      43.317  62.116  27.782  1.00 53.33           N  
ATOM    643  N   GLY A  81      46.020  65.820  24.405  1.00 44.73           N  
ATOM    644  CA  GLY A  81      46.045  66.561  23.134  1.00 42.87           C  
ATOM    645  C   GLY A  81      46.992  65.981  22.070  1.00 40.74           C  
ATOM    646  O   GLY A  81      47.544  64.888  22.261  1.00 41.51           O  
ATOM    647  N   LYS A  82      47.138  66.654  20.934  1.00 37.36           N  
ATOM    648  CA  LYS A  82      48.057  66.199  19.909  1.00 34.66           C  
ATOM    649  C   LYS A  82      48.444  67.472  19.205  1.00 31.60           C  
ATOM    650  O   LYS A  82      47.630  68.374  19.133  1.00 31.41           O  
ATOM    651  CB  LYS A  82      47.379  65.259  18.923  1.00 37.37           C  
ATOM    652  CG  LYS A  82      46.246  64.397  19.482  1.00 42.82           C  
ATOM    653  CD  LYS A  82      45.383  63.626  18.379  1.00 47.11           C  
ATOM    654  CE  LYS A  82      45.981  62.203  17.929  1.00 51.33           C  
ATOM    655  NZ  LYS A  82      45.992  61.003  18.956  1.00 52.17           N  
ATOM    656  N   LEU A  83      49.692  67.572  18.743  1.00 28.50           N  
ATOM    657  CA  LEU A  83      50.236  68.739  18.007  1.00 25.62           C  
ATOM    658  C   LEU A  83      50.828  68.030  16.850  1.00 26.29           C  
ATOM    659  O   LEU A  83      51.861  67.422  17.060  1.00 27.47           O  
ATOM    660  CB  LEU A  83      51.415  69.322  18.709  1.00 22.74           C  
ATOM    661  CG  LEU A  83      51.993  70.532  18.063  1.00 21.23           C  
ATOM    662  CD1 LEU A  83      51.009  71.592  18.219  1.00 21.64           C  
ATOM    663  CD2 LEU A  83      53.253  70.957  18.701  1.00 19.94           C  
ATOM    664  N   TYR A  84      50.196  68.057  15.670  1.00 25.94           N  
ATOM    665  CA  TYR A  84      50.656  67.365  14.469  1.00 24.98           C  
ATOM    666  C   TYR A  84      50.856  68.449  13.509  1.00 25.15           C  
ATOM    667  O   TYR A  84      50.444  69.542  13.806  1.00 26.49           O  
ATOM    668  CB  TYR A  84      49.593  66.466  13.952  1.00 25.34           C  
ATOM    669  CG  TYR A  84      48.225  67.011  14.093  1.00 26.94           C  
ATOM    670  CD1 TYR A  84      47.876  68.192  13.545  1.00 29.33           C  
ATOM    671  CD2 TYR A  84      47.247  66.293  14.704  1.00 28.55           C  
ATOM    672  CE1 TYR A  84      46.556  68.645  13.596  1.00 31.16           C  
ATOM    673  CE2 TYR A  84      45.926  66.729  14.758  1.00 30.18           C  
ATOM    674  CZ  TYR A  84      45.583  67.893  14.197  1.00 31.11           C  
ATOM    675  OH  TYR A  84      44.249  68.258  14.120  1.00 33.65           O  
ATOM    676  N   PRO A  85      51.489  68.199  12.351  1.00 25.09           N  
ATOM    677  CA  PRO A  85      51.728  69.240  11.353  1.00 25.08           C  
ATOM    678  C   PRO A  85      50.413  69.542  10.680  1.00 25.70           C  
ATOM    679  O   PRO A  85      49.615  68.616  10.529  1.00 26.20           O  
ATOM    680  CB  PRO A  85      52.718  68.570  10.424  1.00 24.32           C  
ATOM    681  CG  PRO A  85      52.246  67.287  10.382  1.00 24.62           C  
ATOM    682  CD  PRO A  85      52.027  66.940  11.840  1.00 25.26           C  
ATOM    683  N   ASN A  86      50.182  70.810  10.293  1.00 26.51           N  
ATOM    684  CA  ASN A  86      48.912  71.242   9.647  1.00 26.70           C  
ATOM    685  C   ASN A  86      48.475  70.321   8.579  1.00 26.59           C  
ATOM    686  O   ASN A  86      49.263  69.957   7.729  1.00 28.32           O  
ATOM    687  CB  ASN A  86      49.033  72.577   9.015  1.00 26.90           C  
ATOM    688  CG  ASN A  86      47.750  72.999   8.400  1.00 27.65           C  
ATOM    689  OD1 ASN A  86      46.787  73.315   9.094  1.00 27.46           O  
ATOM    690  ND2 ASN A  86      47.717  73.022   7.089  1.00 28.82           N  
ATOM    691  N   PRO A  87      47.206  70.009   8.516  1.00 26.24           N  
ATOM    692  CA  PRO A  87      46.875  69.056   7.463  1.00 27.69           C  
ATOM    693  C   PRO A  87      46.466  69.497   6.111  1.00 28.76           C  
ATOM    694  O   PRO A  87      46.017  68.672   5.340  1.00 29.90           O  
ATOM    695  CB  PRO A  87      45.787  68.237   8.093  1.00 26.26           C  
ATOM    696  CG  PRO A  87      45.019  69.281   8.766  1.00 27.08           C  
ATOM    697  CD  PRO A  87      46.093  70.155   9.441  1.00 26.99           C  
ATOM    698  N   PHE A  88      46.596  70.780   5.825  1.00 29.31           N  
ATOM    699  CA  PHE A  88      46.216  71.337   4.547  1.00 29.65           C  
ATOM    700  C   PHE A  88      47.506  71.857   3.982  1.00 30.07           C  
ATOM    701  O   PHE A  88      47.556  72.773   3.145  1.00 31.44           O  
ATOM    702  CB  PHE A  88      45.255  72.486   4.756  1.00 29.72           C  
ATOM    703  CG  PHE A  88      43.928  72.078   5.256  1.00 31.75           C  
ATOM    704  CD1 PHE A  88      43.000  73.043   5.639  1.00 32.44           C  
ATOM    705  CD2 PHE A  88      43.564  70.749   5.294  1.00 33.21           C  
ATOM    706  CE1 PHE A  88      41.724  72.713   6.047  1.00 32.54           C  
ATOM    707  CE2 PHE A  88      42.278  70.392   5.705  1.00 35.39           C  
ATOM    708  CZ  PHE A  88      41.349  71.396   6.083  1.00 33.94           C  
ATOM    709  N   GLY A  89      48.571  71.291   4.501  1.00 29.49           N  
ATOM    710  CA  GLY A  89      49.885  71.675   4.066  1.00 29.00           C  
ATOM    711  C   GLY A  89      50.418  73.020   4.472  1.00 28.99           C  
ATOM    712  O   GLY A  89      51.447  73.367   3.927  1.00 30.50           O  
ATOM    713  N   GLU A  90      49.799  73.789   5.361  1.00 28.43           N  
ATOM    714  CA  GLU A  90      50.372  75.086   5.702  1.00 28.77           C  
ATOM    715  C   GLU A  90      51.649  74.857   6.474  1.00 26.83           C  
ATOM    716  O   GLU A  90      51.811  73.783   7.014  1.00 29.22           O  
ATOM    717  CB  GLU A  90      49.376  75.836   6.558  1.00 32.25           C  
ATOM    718  CG  GLU A  90      48.039  75.962   5.899  1.00 39.77           C  
ATOM    719  CD  GLU A  90      47.811  77.340   5.203  1.00 45.58           C  
ATOM    720  OE1 GLU A  90      48.847  77.991   4.808  1.00 47.52           O  
ATOM    721  OE2 GLU A  90      46.587  77.757   5.044  1.00 48.23           O  
ATOM    722  N   PRO A  91      52.582  75.820   6.532  1.00 24.33           N  
ATOM    723  CA  PRO A  91      53.842  75.680   7.283  1.00 24.28           C  
ATOM    724  C   PRO A  91      53.734  75.968   8.861  1.00 25.04           C  
ATOM    725  O   PRO A  91      54.375  76.895   9.449  1.00 25.58           O  
ATOM    726  CB  PRO A  91      54.734  76.696   6.596  1.00 22.98           C  
ATOM    727  CG  PRO A  91      53.838  77.783   6.396  1.00 21.86           C  
ATOM    728  CD  PRO A  91      52.628  77.063   5.771  1.00 23.55           C  
ATOM    729  N   HIS A  92      52.936  75.182   9.554  1.00 24.05           N  
ATOM    730  CA  HIS A  92      52.822  75.383  10.967  1.00 24.79           C  
ATOM    731  C   HIS A  92      52.093  74.201  11.534  1.00 25.17           C  
ATOM    732  O   HIS A  92      51.404  73.489  10.773  1.00 25.57           O  
ATOM    733  CB  HIS A  92      52.055  76.646  11.194  1.00 26.40           C  
ATOM    734  CG  HIS A  92      50.610  76.598  10.755  1.00 28.82           C  
ATOM    735  ND1 HIS A  92      50.032  77.612  10.009  1.00 29.44           N  
ATOM    736  CD2 HIS A  92      49.586  75.793  11.141  1.00 29.04           C  
ATOM    737  CE1 HIS A  92      48.722  77.436   9.975  1.00 29.63           C  
ATOM    738  NE2 HIS A  92      48.424  76.343  10.655  1.00 28.65           N  
ATOM    739  N   LEU A  93      52.193  73.921  12.824  1.00 23.64           N  
ATOM    740  CA  LEU A  93      51.406  72.762  13.178  1.00 23.24           C  
ATOM    741  C   LEU A  93      50.059  73.176  13.711  1.00 23.74           C  
ATOM    742  O   LEU A  93      49.816  74.334  13.955  1.00 24.68           O  
ATOM    743  CB  LEU A  93      52.117  71.869  14.177  1.00 23.03           C  
ATOM    744  CG  LEU A  93      53.628  71.908  14.262  1.00 22.14           C  
ATOM    745  CD1 LEU A  93      53.886  73.096  15.084  1.00 21.55           C  
ATOM    746  CD2 LEU A  93      54.267  70.731  14.882  1.00 18.61           C  
ATOM    747  N   SER A  94      49.163  72.228  13.878  1.00 23.87           N  
ATOM    748  CA  SER A  94      47.832  72.516  14.394  1.00 24.12           C  
ATOM    749  C   SER A  94      47.796  71.816  15.732  1.00 24.30           C  
ATOM    750  O   SER A  94      48.261  70.706  15.803  1.00 23.49           O  
ATOM    751  CB  SER A  94      46.791  71.865  13.501  1.00 24.65           C  
ATOM    752  OG  SER A  94      46.709  72.466  12.241  1.00 25.78           O  
ATOM    753  N   ILE A  95      47.243  72.441  16.772  1.00 25.45           N  
ATOM    754  CA  ILE A  95      47.197  71.822  18.102  1.00 27.21           C  
ATOM    755  C   ILE A  95      45.795  71.445  18.411  1.00 27.49           C  
ATOM    756  O   ILE A  95      44.907  72.226  18.230  1.00 27.30           O  
ATOM    757  CB  ILE A  95      47.766  72.751  19.153  1.00 28.04           C  
ATOM    758  CG1 ILE A  95      47.957  71.992  20.440  1.00 28.62           C  
ATOM    759  CG2 ILE A  95      46.892  73.912  19.374  1.00 27.59           C  
ATOM    760  CD1 ILE A  95      48.603  72.880  21.477  1.00 29.42           C  
ATOM    761  N   ASP A  96      45.592  70.274  18.953  1.00 28.93           N  
ATOM    762  CA  ASP A  96      44.242  69.825  19.050  1.00 32.17           C  
ATOM    763  C   ASP A  96      43.929  68.921  20.257  1.00 35.56           C  
ATOM    764  O   ASP A  96      44.165  67.671  20.234  1.00 35.13           O  
ATOM    765  CB  ASP A  96      44.071  69.202  17.660  1.00 31.92           C  
ATOM    766  CG  ASP A  96      43.050  68.082  17.552  1.00 33.61           C  
ATOM    767  OD1 ASP A  96      43.236  67.283  16.549  1.00 31.24           O  
ATOM    768  OD2 ASP A  96      42.086  68.006  18.390  1.00 35.24           O  
ATOM    769  N   TYR A  97      43.410  69.557  21.326  1.00 38.73           N  
ATOM    770  CA  TYR A  97      43.069  68.813  22.537  1.00 42.99           C  
ATOM    771  C   TYR A  97      41.700  68.232  22.486  1.00 46.60           C  
ATOM    772  O   TYR A  97      40.804  68.860  21.952  1.00 46.58           O  
ATOM    773  CB  TYR A  97      43.178  69.656  23.772  1.00 42.85           C  
ATOM    774  CG  TYR A  97      44.585  69.776  24.258  1.00 43.97           C  
ATOM    775  CD1 TYR A  97      45.474  70.579  23.608  1.00 45.09           C  
ATOM    776  CD2 TYR A  97      45.001  69.172  25.409  1.00 44.23           C  
ATOM    777  CE1 TYR A  97      46.746  70.809  24.092  1.00 45.70           C  
ATOM    778  CE2 TYR A  97      46.279  69.401  25.906  1.00 45.68           C  
ATOM    779  CZ  TYR A  97      47.145  70.235  25.235  1.00 45.54           C  
ATOM    780  OH  TYR A  97      48.393  70.569  25.721  1.00 45.38           O  
ATOM    781  N   GLU A  98      41.504  67.040  23.058  1.00 51.74           N  
ATOM    782  CA  GLU A  98      40.187  66.482  22.918  1.00 56.64           C  
ATOM    783  C   GLU A  98      39.160  67.276  23.602  1.00 58.15           C  
ATOM    784  O   GLU A  98      39.435  68.010  24.578  1.00 58.66           O  
ATOM    785  CB  GLU A  98      40.045  65.002  23.257  1.00 59.79           C  
ATOM    786  CG  GLU A  98      38.775  64.364  22.412  1.00 66.54           C  
ATOM    787  CD  GLU A  98      38.695  64.628  20.787  1.00 69.71           C  
ATOM    788  OE1 GLU A  98      38.889  63.622  20.007  1.00 70.10           O  
ATOM    789  OE2 GLU A  98      38.413  65.806  20.311  1.00 70.98           O  
ATOM    790  N   ASN A  99      37.975  67.145  22.997  1.00 59.75           N  
ATOM    791  CA  ASN A  99      36.766  67.873  23.331  1.00 60.68           C  
ATOM    792  C   ASN A  99      37.005  69.335  22.838  1.00 58.93           C  
ATOM    793  O   ASN A  99      36.614  70.333  23.510  1.00 58.51           O  
ATOM    794  CB  ASN A  99      36.452  67.808  24.831  1.00 64.50           C  
ATOM    795  CG  ASN A  99      34.967  67.893  25.082  1.00 67.87           C  
ATOM    796  OD1 ASN A  99      34.196  67.039  24.555  1.00 69.51           O  
ATOM    797  ND2 ASN A  99      34.527  68.930  25.849  1.00 68.72           N  
ATOM    798  N   SER A 100      37.702  69.402  21.671  1.00 56.54           N  
ATOM    799  CA  SER A 100      38.030  70.639  20.910  1.00 52.44           C  
ATOM    800  C   SER A 100      38.516  70.503  19.449  1.00 48.04           C  
ATOM    801  O   SER A 100      39.175  69.502  19.045  1.00 46.43           O  
ATOM    802  CB  SER A 100      39.031  71.522  21.655  1.00 54.66           C  
ATOM    803  OG  SER A 100      39.214  72.734  20.919  1.00 58.14           O  
ATOM    804  N   PHE A 101      38.158  71.547  18.684  1.00 43.24           N  
ATOM    805  CA  PHE A 101      38.527  71.672  17.254  1.00 38.87           C  
ATOM    806  C   PHE A 101      39.916  72.254  17.241  1.00 36.54           C  
ATOM    807  O   PHE A 101      40.166  73.222  17.971  1.00 38.66           O  
ATOM    808  CB  PHE A 101      37.668  72.694  16.483  1.00 35.92           C  
ATOM    809  CG  PHE A 101      36.266  72.263  16.193  1.00 32.24           C  
ATOM    810  CD1 PHE A 101      36.000  71.053  15.587  1.00 31.55           C  
ATOM    811  CD2 PHE A 101      35.221  73.095  16.484  1.00 30.34           C  
ATOM    812  CE1 PHE A 101      34.720  70.680  15.275  1.00 30.31           C  
ATOM    813  CE2 PHE A 101      33.968  72.726  16.173  1.00 29.83           C  
ATOM    814  CZ  PHE A 101      33.719  71.516  15.571  1.00 29.80           C  
ATOM    815  N   ALA A 102      40.781  71.735  16.387  1.00 31.85           N  
ATOM    816  CA  ALA A 102      42.157  72.189  16.282  1.00 27.13           C  
ATOM    817  C   ALA A 102      42.448  73.663  16.060  1.00 24.19           C  
ATOM    818  O   ALA A 102      41.608  74.363  15.608  1.00 24.33           O  
ATOM    819  CB  ALA A 102      42.751  71.439  15.194  1.00 27.42           C  
ATOM    820  N   ALA A 103      43.622  74.152  16.409  1.00 21.19           N  
ATOM    821  CA  ALA A 103      43.956  75.526  16.040  1.00 20.69           C  
ATOM    822  C   ALA A 103      45.376  75.566  15.483  1.00 20.92           C  
ATOM    823  O   ALA A 103      46.203  74.677  15.643  1.00 22.01           O  
ATOM    824  CB  ALA A 103      43.849  76.481  17.155  1.00 17.59           C  
ATOM    825  N   PRO A 104      45.674  76.585  14.762  1.00 20.35           N  
ATOM    826  CA  PRO A 104      47.023  76.655  14.228  1.00 21.65           C  
ATOM    827  C   PRO A 104      47.954  77.060  15.383  1.00 22.78           C  
ATOM    828  O   PRO A 104      47.466  77.695  16.291  1.00 24.77           O  
ATOM    829  CB  PRO A 104      46.891  77.769  13.215  1.00 21.32           C  
ATOM    830  CG  PRO A 104      45.898  78.663  13.915  1.00 21.10           C  
ATOM    831  CD  PRO A 104      44.854  77.693  14.313  1.00 20.34           C  
ATOM    832  N   LEU A 105      49.263  76.762  15.350  1.00 23.03           N  
ATOM    833  CA  LEU A 105      50.180  77.145  16.437  1.00 23.13           C  
ATOM    834  C   LEU A 105      51.554  77.261  15.941  1.00 23.29           C  
ATOM    835  O   LEU A 105      52.175  76.275  15.779  1.00 24.70           O  
ATOM    836  CB  LEU A 105      50.248  76.065  17.477  1.00 24.11           C  
ATOM    837  CG  LEU A 105      51.118  76.190  18.694  1.00 23.30           C  
ATOM    838  CD1 LEU A 105      50.433  76.968  19.711  1.00 21.80           C  
ATOM    839  CD2 LEU A 105      51.259  74.811  19.216  1.00 24.16           C  
ATOM    840  N   VAL A 106      52.046  78.457  15.751  1.00 23.45           N  
ATOM    841  CA  VAL A 106      53.382  78.687  15.253  1.00 23.51           C  
ATOM    842  C   VAL A 106      54.374  78.723  16.402  1.00 25.16           C  
ATOM    843  O   VAL A 106      54.083  79.352  17.396  1.00 27.05           O  
ATOM    844  CB  VAL A 106      53.458  80.042  14.671  1.00 22.25           C  
ATOM    845  CG1 VAL A 106      54.847  80.386  14.348  1.00 22.72           C  
ATOM    846  CG2 VAL A 106      52.638  80.127  13.536  1.00 22.25           C  
ATOM    847  N   ILE A 107      55.535  78.086  16.300  1.00 25.55           N  
ATOM    848  CA  ILE A 107      56.508  78.220  17.372  1.00 26.05           C  
ATOM    849  C   ILE A 107      57.318  79.393  16.857  1.00 27.72           C  
ATOM    850  O   ILE A 107      58.087  79.281  15.912  1.00 28.31           O  
ATOM    851  CB  ILE A 107      57.373  77.013  17.480  1.00 24.66           C  
ATOM    852  CG1 ILE A 107      56.620  75.931  18.178  1.00 23.64           C  
ATOM    853  CG2 ILE A 107      58.516  77.281  18.318  1.00 24.55           C  
ATOM    854  CD1 ILE A 107      57.113  74.622  17.768  1.00 23.01           C  
ATOM    855  N   LEU A 108      57.099  80.534  17.471  1.00 29.16           N  
ATOM    856  CA  LEU A 108      57.728  81.797  17.118  1.00 30.81           C  
ATOM    857  C   LEU A 108      59.234  81.934  17.222  1.00 33.54           C  
ATOM    858  O   LEU A 108      59.857  82.709  16.430  1.00 33.80           O  
ATOM    859  CB  LEU A 108      57.115  82.873  17.964  1.00 27.95           C  
ATOM    860  CG  LEU A 108      56.435  83.796  17.066  1.00 25.80           C  
ATOM    861  CD1 LEU A 108      55.658  84.733  17.859  1.00 27.43           C  
ATOM    862  CD2 LEU A 108      57.514  84.465  16.313  1.00 27.31           C  
ATOM    863  N   GLU A 109      59.776  81.246  18.242  1.00 36.53           N  
ATOM    864  CA  GLU A 109      61.212  81.198  18.595  1.00 40.10           C  
ATOM    865  C   GLU A 109      61.341  80.191  19.713  1.00 40.18           C  
ATOM    866  O   GLU A 109      60.549  80.197  20.621  1.00 40.83           O  
ATOM    867  CB  GLU A 109      61.679  82.550  19.105  1.00 43.25           C  
ATOM    868  CG  GLU A 109      63.055  82.597  19.731  1.00 49.62           C  
ATOM    869  CD  GLU A 109      63.498  84.074  20.065  1.00 54.44           C  
ATOM    870  OE1 GLU A 109      63.193  85.019  19.252  1.00 55.93           O  
ATOM    871  OE2 GLU A 109      64.166  84.296  21.129  1.00 56.24           O  
ATOM    872  N   THR A 110      62.291  79.288  19.630  1.00 40.22           N  
ATOM    873  CA  THR A 110      62.470  78.341  20.713  1.00 41.67           C  
ATOM    874  C   THR A 110      63.905  77.922  20.666  1.00 44.11           C  
ATOM    875  O   THR A 110      64.504  78.006  19.585  1.00 45.52           O  
ATOM    876  CB  THR A 110      61.700  77.039  20.591  1.00 40.68           C  
ATOM    877  OG1 THR A 110      61.858  76.338  21.822  1.00 40.94           O  
ATOM    878  CG2 THR A 110      62.293  76.114  19.566  1.00 39.07           C  
ATOM    879  N   ASP A 111      64.477  77.502  21.805  1.00 45.03           N  
ATOM    880  CA  ASP A 111      65.845  77.036  21.803  1.00 44.98           C  
ATOM    881  C   ASP A 111      65.832  75.602  22.279  1.00 44.72           C  
ATOM    882  O   ASP A 111      66.816  75.044  22.687  1.00 45.15           O  
ATOM    883  CB  ASP A 111      66.747  77.942  22.627  1.00 46.88           C  
ATOM    884  CG  ASP A 111      66.585  77.779  24.112  1.00 49.29           C  
ATOM    885  OD1 ASP A 111      67.269  78.553  24.825  1.00 51.30           O  
ATOM    886  OD2 ASP A 111      65.820  76.914  24.582  1.00 49.68           O  
ATOM    887  N   TYR A 112      64.668  75.007  22.189  1.00 43.78           N  
ATOM    888  CA  TYR A 112      64.510  73.643  22.537  1.00 44.26           C  
ATOM    889  C   TYR A 112      64.811  73.241  23.937  1.00 46.24           C  
ATOM    890  O   TYR A 112      64.256  72.253  24.439  1.00 46.64           O  
ATOM    891  CB  TYR A 112      65.286  72.797  21.560  1.00 42.73           C  
ATOM    892  CG  TYR A 112      64.702  72.910  20.164  1.00 43.58           C  
ATOM    893  CD1 TYR A 112      65.228  73.818  19.241  1.00 43.57           C  
ATOM    894  CD2 TYR A 112      63.568  72.194  19.785  1.00 42.47           C  
ATOM    895  CE1 TYR A 112      64.654  74.009  17.997  1.00 41.95           C  
ATOM    896  CE2 TYR A 112      62.997  72.397  18.540  1.00 41.75           C  
ATOM    897  CZ  TYR A 112      63.556  73.300  17.664  1.00 41.35           C  
ATOM    898  OH  TYR A 112      63.067  73.479  16.417  1.00 41.44           O  
ATOM    899  N   SER A 113      65.654  73.987  24.626  1.00 48.86           N  
ATOM    900  CA  SER A 113      65.962  73.560  25.988  1.00 51.34           C  
ATOM    901  C   SER A 113      65.878  74.599  27.059  1.00 52.01           C  
ATOM    902  O   SER A 113      66.363  74.379  28.165  1.00 53.56           O  
ATOM    903  CB  SER A 113      67.323  72.888  26.043  1.00 52.67           C  
ATOM    904  OG  SER A 113      68.284  73.635  25.286  1.00 56.07           O  
ATOM    905  N   ASN A 114      65.258  75.724  26.742  1.00 52.02           N  
ATOM    906  CA  ASN A 114      65.066  76.735  27.730  1.00 52.06           C  
ATOM    907  C   ASN A 114      63.698  77.422  27.741  1.00 51.30           C  
ATOM    908  O   ASN A 114      63.052  77.515  28.786  1.00 52.38           O  
ATOM    909  CB  ASN A 114      66.227  77.688  27.659  1.00 53.27           C  
ATOM    910  CG  ASN A 114      67.350  77.217  28.550  1.00 56.03           C  
ATOM    911  OD1 ASN A 114      67.116  76.382  29.444  1.00 57.69           O  
ATOM    912  ND2 ASN A 114      68.563  77.736  28.348  1.00 57.83           N  
ATOM    913  N   TYR A 115      63.227  77.855  26.582  1.00 49.23           N  
ATOM    914  CA  TYR A 115      61.934  78.497  26.482  1.00 46.22           C  
ATOM    915  C   TYR A 115      61.441  78.229  25.066  1.00 45.68           C  
ATOM    916  O   TYR A 115      62.191  77.720  24.232  1.00 46.46           O  
ATOM    917  CB  TYR A 115      62.140  79.961  26.633  1.00 44.64           C  
ATOM    918  CG  TYR A 115      62.994  80.476  25.539  1.00 43.71           C  
ATOM    919  CD1 TYR A 115      62.485  81.327  24.597  1.00 44.24           C  
ATOM    920  CD2 TYR A 115      64.326  80.128  25.455  1.00 43.52           C  
ATOM    921  CE1 TYR A 115      63.300  81.849  23.579  1.00 45.35           C  
ATOM    922  CE2 TYR A 115      65.144  80.627  24.457  1.00 44.22           C  
ATOM    923  CZ  TYR A 115      64.630  81.496  23.516  1.00 45.05           C  
ATOM    924  OH  TYR A 115      65.430  82.026  22.522  1.00 44.80           O  
ATOM    925  N   ALA A 116      60.191  78.585  24.789  1.00 43.96           N  
ATOM    926  CA  ALA A 116      59.598  78.443  23.474  1.00 40.94           C  
ATOM    927  C   ALA A 116      58.497  79.454  23.523  1.00 40.11           C  
ATOM    928  O   ALA A 116      57.770  79.505  24.483  1.00 39.44           O  
ATOM    929  CB  ALA A 116      59.046  77.088  23.314  1.00 39.87           C  
ATOM    930  N   CYS A 117      58.396  80.316  22.531  1.00 40.62           N  
ATOM    931  CA  CYS A 117      57.308  81.284  22.523  1.00 41.38           C  
ATOM    932  C   CYS A 117      56.290  80.784  21.498  1.00 39.72           C  
ATOM    933  O   CYS A 117      56.658  80.562  20.359  1.00 41.21           O  
ATOM    934  CB  CYS A 117      57.838  82.654  22.150  1.00 44.14           C  
ATOM    935  SG  CYS A 117      59.491  82.974  22.884  1.00 52.86           S  
ATOM    936  N   LEU A 118      55.044  80.536  21.909  1.00 36.60           N  
ATOM    937  CA  LEU A 118      54.004  80.069  21.014  1.00 34.15           C  
ATOM    938  C   LEU A 118      52.999  81.165  20.584  1.00 35.10           C  
ATOM    939  O   LEU A 118      52.608  82.027  21.358  1.00 37.51           O  
ATOM    940  CB  LEU A 118      53.302  78.942  21.701  1.00 31.62           C  
ATOM    941  CG  LEU A 118      54.298  77.892  22.154  1.00 30.22           C  
ATOM    942  CD1 LEU A 118      53.651  76.551  22.399  1.00 27.73           C  
ATOM    943  CD2 LEU A 118      55.327  77.746  21.101  1.00 30.12           C  
ATOM    944  N   TYR A 119      52.574  81.176  19.334  1.00 34.49           N  
ATOM    945  CA  TYR A 119      51.616  82.201  18.889  1.00 32.93           C  
ATOM    946  C   TYR A 119      50.586  81.473  18.067  1.00 32.75           C  
ATOM    947  O   TYR A 119      50.926  80.562  17.318  1.00 33.56           O  
ATOM    948  CB  TYR A 119      52.326  83.213  18.025  1.00 32.04           C  
ATOM    949  CG  TYR A 119      51.446  84.218  17.392  1.00 31.31           C  
ATOM    950  CD1 TYR A 119      50.563  84.920  18.114  1.00 32.23           C  
ATOM    951  CD2 TYR A 119      51.531  84.490  16.076  1.00 31.22           C  
ATOM    952  CE1 TYR A 119      49.777  85.885  17.537  1.00 32.73           C  
ATOM    953  CE2 TYR A 119      50.741  85.442  15.484  1.00 31.32           C  
ATOM    954  CZ  TYR A 119      49.868  86.135  16.221  1.00 32.37           C  
ATOM    955  OH  TYR A 119      49.059  87.093  15.650  1.00 34.01           O  
ATOM    956  N   SER A 120      49.323  81.810  18.221  1.00 31.12           N  
ATOM    957  CA  SER A 120      48.342  81.129  17.412  1.00 29.87           C  
ATOM    958  C   SER A 120      47.206  82.063  17.118  1.00 30.70           C  
ATOM    959  O   SER A 120      46.475  82.382  17.978  1.00 31.36           O  
ATOM    960  CB  SER A 120      47.816  79.945  18.115  1.00 27.32           C  
ATOM    961  OG  SER A 120      46.449  79.905  17.806  1.00 26.44           O  
ATOM    962  N   CYS A 121      47.033  82.460  15.875  1.00 32.50           N  
ATOM    963  CA  CYS A 121      46.016  83.423  15.480  1.00 33.33           C  
ATOM    964  C   CYS A 121      45.144  83.069  14.252  1.00 32.56           C  
ATOM    965  O   CYS A 121      45.643  82.402  13.305  1.00 34.40           O  
ATOM    966  CB  CYS A 121      46.754  84.636  15.151  1.00 36.75           C  
ATOM    967  SG  CYS A 121      45.580  85.896  14.791  1.00 43.27           S  
ATOM    968  N   ILE A 122      43.879  83.507  14.201  1.00 29.31           N  
ATOM    969  CA  ILE A 122      43.055  83.164  13.017  1.00 27.47           C  
ATOM    970  C   ILE A 122      42.391  84.432  12.475  1.00 28.98           C  
ATOM    971  O   ILE A 122      41.968  85.212  13.292  1.00 31.55           O  
ATOM    972  CB  ILE A 122      41.989  82.199  13.410  1.00 23.87           C  
ATOM    973  CG1 ILE A 122      42.576  80.873  13.629  1.00 22.13           C  
ATOM    974  CG2 ILE A 122      41.175  81.848  12.342  1.00 22.49           C  
ATOM    975  CD1 ILE A 122      41.550  79.952  14.094  1.00 21.40           C  
ATOM    976  N   ASP A 123      42.303  84.687  11.155  1.00 28.70           N  
ATOM    977  CA  ASP A 123      41.588  85.893  10.642  1.00 29.47           C  
ATOM    978  C   ASP A 123      40.159  85.551  10.277  1.00 28.82           C  
ATOM    979  O   ASP A 123      39.959  84.524   9.769  1.00 28.40           O  
ATOM    980  CB  ASP A 123      42.204  86.413   9.365  1.00 32.41           C  
ATOM    981  CG  ASP A 123      43.454  87.140   9.616  1.00 35.38           C  
ATOM    982  OD1 ASP A 123      43.335  88.208  10.253  1.00 39.10           O  
ATOM    983  OD2 ASP A 123      44.547  86.658   9.212  1.00 36.58           O  
ATOM    984  N   TYR A 124      39.153  86.375  10.502  1.00 28.76           N  
ATOM    985  CA  TYR A 124      37.819  85.959  10.082  1.00 28.20           C  
ATOM    986  C   TYR A 124      37.313  87.021   9.126  1.00 29.12           C  
ATOM    987  O   TYR A 124      38.077  87.937   8.760  1.00 28.38           O  
ATOM    988  CB  TYR A 124      36.915  85.934  11.251  1.00 28.23           C  
ATOM    989  CG  TYR A 124      37.447  85.191  12.428  1.00 29.87           C  
ATOM    990  CD1 TYR A 124      38.087  85.841  13.476  1.00 29.50           C  
ATOM    991  CD2 TYR A 124      37.221  83.831  12.545  1.00 30.92           C  
ATOM    992  CE1 TYR A 124      38.473  85.141  14.595  1.00 30.19           C  
ATOM    993  CE2 TYR A 124      37.596  83.140  13.652  1.00 31.45           C  
ATOM    994  CZ  TYR A 124      38.216  83.788  14.661  1.00 31.54           C  
ATOM    995  OH  TYR A 124      38.617  83.000  15.700  1.00 33.92           O  
ATOM    996  N   ASN A 125      36.050  86.940   8.698  1.00 29.73           N  
ATOM    997  CA  ASN A 125      35.550  88.004   7.807  1.00 30.34           C  
ATOM    998  C   ASN A 125      35.108  89.260   8.550  1.00 31.32           C  
ATOM    999  O   ASN A 125      35.134  89.315   9.782  1.00 31.84           O  
ATOM   1000  CB  ASN A 125      34.424  87.554   6.879  1.00 28.58           C  
ATOM   1001  CG  ASN A 125      33.699  86.387   7.377  1.00 28.84           C  
ATOM   1002  OD1 ASN A 125      34.186  85.632   8.201  1.00 29.02           O  
ATOM   1003  ND2 ASN A 125      32.511  86.187   6.846  1.00 30.13           N  
ATOM   1004  N   PHE A 126      34.730  90.291   7.803  1.00 32.19           N  
ATOM   1005  CA  PHE A 126      34.303  91.537   8.437  1.00 32.51           C  
ATOM   1006  C   PHE A 126      35.357  92.176   9.321  1.00 33.62           C  
ATOM   1007  O   PHE A 126      35.066  92.968  10.209  1.00 33.50           O  
ATOM   1008  CB  PHE A 126      33.064  91.289   9.245  1.00 32.13           C  
ATOM   1009  CG  PHE A 126      31.968  90.724   8.452  1.00 31.63           C  
ATOM   1010  CD1 PHE A 126      31.563  89.429   8.648  1.00 31.51           C  
ATOM   1011  CD2 PHE A 126      31.399  91.452   7.453  1.00 30.51           C  
ATOM   1012  CE1 PHE A 126      30.614  88.879   7.849  1.00 31.49           C  
ATOM   1013  CE2 PHE A 126      30.465  90.887   6.673  1.00 30.43           C  
ATOM   1014  CZ  PHE A 126      30.073  89.601   6.865  1.00 30.02           C  
ATOM   1015  N   GLY A 127      36.599  91.807   9.090  1.00 35.22           N  
ATOM   1016  CA  GLY A 127      37.625  92.449   9.839  1.00 36.50           C  
ATOM   1017  C   GLY A 127      37.964  91.895  11.173  1.00 37.79           C  
ATOM   1018  O   GLY A 127      38.839  92.457  11.779  1.00 40.04           O  
ATOM   1019  N   TYR A 128      37.324  90.844  11.663  1.00 38.42           N  
ATOM   1020  CA  TYR A 128      37.748  90.303  12.950  1.00 38.70           C  
ATOM   1021  C   TYR A 128      38.940  89.324  12.942  1.00 38.50           C  
ATOM   1022  O   TYR A 128      39.497  88.962  11.896  1.00 39.12           O  
ATOM   1023  CB  TYR A 128      36.567  89.667  13.618  1.00 39.98           C  
ATOM   1024  CG  TYR A 128      35.526  90.695  13.888  1.00 42.70           C  
ATOM   1025  CD1 TYR A 128      34.792  91.250  12.854  1.00 43.92           C  
ATOM   1026  CD2 TYR A 128      35.298  91.157  15.173  1.00 43.83           C  
ATOM   1027  CE1 TYR A 128      33.841  92.256  13.098  1.00 45.85           C  
ATOM   1028  CE2 TYR A 128      34.346  92.162  15.430  1.00 45.65           C  
ATOM   1029  CZ  TYR A 128      33.621  92.709  14.391  1.00 46.19           C  
ATOM   1030  OH  TYR A 128      32.689  93.703  14.641  1.00 48.71           O  
ATOM   1031  N   HIS A 129      39.372  88.942  14.133  1.00 37.99           N  
ATOM   1032  CA  HIS A 129      40.465  87.983  14.303  1.00 36.85           C  
ATOM   1033  C   HIS A 129      40.603  87.655  15.774  1.00 35.55           C  
ATOM   1034  O   HIS A 129      39.843  88.109  16.600  1.00 35.75           O  
ATOM   1035  CB  HIS A 129      41.779  88.547  13.837  1.00 37.30           C  
ATOM   1036  CG  HIS A 129      42.377  89.502  14.802  1.00 38.94           C  
ATOM   1037  ND1 HIS A 129      43.730  89.572  15.040  1.00 40.06           N  
ATOM   1038  CD2 HIS A 129      41.813  90.455  15.575  1.00 40.04           C  
ATOM   1039  CE1 HIS A 129      43.983  90.526  15.918  1.00 39.97           C  
ATOM   1040  NE2 HIS A 129      42.834  91.078  16.259  1.00 41.31           N  
ATOM   1041  N   SER A 130      41.571  86.847  16.110  1.00 33.91           N  
ATOM   1042  CA  SER A 130      41.766  86.525  17.484  1.00 33.15           C  
ATOM   1043  C   SER A 130      43.054  85.765  17.587  1.00 34.26           C  
ATOM   1044  O   SER A 130      43.335  84.892  16.770  1.00 34.68           O  
ATOM   1045  CB  SER A 130      40.616  85.709  17.989  1.00 29.58           C  
ATOM   1046  OG  SER A 130      40.519  84.621  17.172  1.00 27.10           O  
ATOM   1047  N   ASP A 131      43.869  86.147  18.559  1.00 35.19           N  
ATOM   1048  CA  ASP A 131      45.103  85.479  18.766  1.00 36.38           C  
ATOM   1049  C   ASP A 131      45.230  85.004  20.181  1.00 36.44           C  
ATOM   1050  O   ASP A 131      44.589  85.523  21.057  1.00 38.04           O  
ATOM   1051  CB  ASP A 131      46.297  86.368  18.366  1.00 39.01           C  
ATOM   1052  CG  ASP A 131      46.234  87.820  18.911  1.00 42.41           C  
ATOM   1053  OD1 ASP A 131      45.386  88.075  19.823  1.00 42.94           O  
ATOM   1054  OD2 ASP A 131      47.069  88.686  18.399  1.00 43.45           O  
ATOM   1055  N   PHE A 132      46.046  83.980  20.377  1.00 36.03           N  
ATOM   1056  CA  PHE A 132      46.346  83.380  21.660  1.00 35.66           C  
ATOM   1057  C   PHE A 132      47.819  83.139  21.668  1.00 35.74           C  
ATOM   1058  O   PHE A 132      48.308  82.443  20.783  1.00 36.54           O  
ATOM   1059  CB  PHE A 132      45.632  82.071  21.773  1.00 35.87           C  
ATOM   1060  CG  PHE A 132      44.179  82.234  21.789  1.00 36.78           C  
ATOM   1061  CD1 PHE A 132      43.568  82.830  22.861  1.00 37.32           C  
ATOM   1062  CD2 PHE A 132      43.417  81.857  20.721  1.00 37.32           C  
ATOM   1063  CE1 PHE A 132      42.215  83.040  22.862  1.00 38.26           C  
ATOM   1064  CE2 PHE A 132      42.064  82.066  20.710  1.00 36.97           C  
ATOM   1065  CZ  PHE A 132      41.457  82.652  21.772  1.00 37.74           C  
ATOM   1066  N   SER A 133      48.535  83.709  22.644  1.00 35.35           N  
ATOM   1067  CA  SER A 133      49.988  83.545  22.740  1.00 34.00           C  
ATOM   1068  C   SER A 133      50.327  82.785  24.029  1.00 33.41           C  
ATOM   1069  O   SER A 133      49.484  82.630  24.885  1.00 33.52           O  
ATOM   1070  CB  SER A 133      50.582  84.923  22.649  1.00 33.34           C  
ATOM   1071  OG  SER A 133      49.628  85.767  21.946  1.00 33.59           O  
ATOM   1072  N   PHE A 134      51.518  82.220  24.110  1.00 33.24           N  
ATOM   1073  CA  PHE A 134      51.972  81.447  25.267  1.00 33.60           C  
ATOM   1074  C   PHE A 134      53.472  81.569  25.403  1.00 35.12           C  
ATOM   1075  O   PHE A 134      54.123  82.069  24.489  1.00 36.30           O  
ATOM   1076  CB  PHE A 134      51.795  80.006  25.051  1.00 32.59           C  
ATOM   1077  CG  PHE A 134      50.432  79.594  24.975  1.00 33.70           C  
ATOM   1078  CD1 PHE A 134      49.871  78.887  26.009  1.00 34.13           C  
ATOM   1079  CD2 PHE A 134      49.727  79.742  23.820  1.00 33.74           C  
ATOM   1080  CE1 PHE A 134      48.618  78.308  25.883  1.00 34.71           C  
ATOM   1081  CE2 PHE A 134      48.483  79.167  23.695  1.00 34.96           C  
ATOM   1082  CZ  PHE A 134      47.932  78.445  24.729  1.00 34.80           C  
ATOM   1083  N   ILE A 135      54.027  81.141  26.551  1.00 35.67           N  
ATOM   1084  CA  ILE A 135      55.490  81.093  26.751  1.00 34.81           C  
ATOM   1085  C   ILE A 135      55.820  79.794  27.435  1.00 35.50           C  
ATOM   1086  O   ILE A 135      55.324  79.492  28.481  1.00 36.96           O  
ATOM   1087  CB  ILE A 135      55.995  82.140  27.577  1.00 33.34           C  
ATOM   1088  CG1 ILE A 135      55.659  83.478  26.955  1.00 32.54           C  
ATOM   1089  CG2 ILE A 135      57.434  81.923  27.651  1.00 33.82           C  
ATOM   1090  CD1 ILE A 135      56.659  84.526  27.209  1.00 31.51           C  
ATOM   1091  N   PHE A 136      56.640  78.976  26.856  1.00 36.10           N  
ATOM   1092  CA  PHE A 136      56.859  77.714  27.520  1.00 37.61           C  
ATOM   1093  C   PHE A 136      58.277  77.730  28.136  1.00 40.02           C  
ATOM   1094  O   PHE A 136      59.237  78.218  27.514  1.00 40.58           O  
ATOM   1095  CB  PHE A 136      56.691  76.559  26.497  1.00 35.86           C  
ATOM   1096  CG  PHE A 136      55.265  76.056  26.311  1.00 33.47           C  
ATOM   1097  CD1 PHE A 136      55.038  74.846  25.643  1.00 32.80           C  
ATOM   1098  CD2 PHE A 136      54.177  76.725  26.838  1.00 32.75           C  
ATOM   1099  CE1 PHE A 136      53.742  74.294  25.512  1.00 32.42           C  
ATOM   1100  CE2 PHE A 136      52.872  76.176  26.711  1.00 33.36           C  
ATOM   1101  CZ  PHE A 136      52.669  74.954  26.047  1.00 32.87           C  
ATOM   1102  N   SER A 137      58.431  77.197  29.348  1.00 42.01           N  
ATOM   1103  CA  SER A 137      59.753  77.210  29.986  1.00 44.19           C  
ATOM   1104  C   SER A 137      60.020  75.808  30.140  1.00 44.00           C  
ATOM   1105  O   SER A 137      59.080  75.039  30.224  1.00 42.26           O  
ATOM   1106  CB  SER A 137      59.732  77.765  31.391  1.00 46.97           C  
ATOM   1107  OG  SER A 137      59.052  76.823  32.246  1.00 51.59           O  
ATOM   1108  N   ARG A 138      61.296  75.503  30.259  1.00 45.99           N  
ATOM   1109  CA  ARG A 138      61.730  74.134  30.359  1.00 49.58           C  
ATOM   1110  C   ARG A 138      61.796  73.667  31.796  1.00 52.00           C  
ATOM   1111  O   ARG A 138      61.828  72.451  32.072  1.00 50.76           O  
ATOM   1112  CB  ARG A 138      63.094  74.001  29.668  1.00 49.78           C  
ATOM   1113  CG  ARG A 138      63.061  73.492  28.221  1.00 49.88           C  
ATOM   1114  CD  ARG A 138      62.266  72.140  28.036  1.00 49.21           C  
ATOM   1115  NE  ARG A 138      62.388  71.665  26.660  1.00 46.17           N  
ATOM   1116  CZ  ARG A 138      61.816  70.580  26.167  1.00 45.64           C  
ATOM   1117  NH1 ARG A 138      61.028  69.784  26.893  1.00 43.91           N  
ATOM   1118  NH2 ARG A 138      62.096  70.265  24.924  1.00 46.23           N  
ATOM   1119  N   SER A 139      61.827  74.661  32.686  1.00 55.70           N  
ATOM   1120  CA  SER A 139      61.891  74.451  34.130  1.00 60.54           C  
ATOM   1121  C   SER A 139      60.897  75.407  34.869  1.00 62.10           C  
ATOM   1122  O   SER A 139      60.907  76.629  34.676  1.00 63.14           O  
ATOM   1123  CB  SER A 139      63.367  74.666  34.650  1.00 63.09           C  
ATOM   1124  OG  SER A 139      63.904  73.567  35.471  1.00 66.49           O  
ATOM   1125  N   ALA A 140      60.058  74.846  35.730  1.00 63.00           N  
ATOM   1126  CA  ALA A 140      59.088  75.624  36.468  1.00 64.03           C  
ATOM   1127  C   ALA A 140      59.319  77.135  36.584  1.00 65.00           C  
ATOM   1128  O   ALA A 140      58.445  77.938  36.368  1.00 65.06           O  
ATOM   1129  CB  ALA A 140      58.933  75.008  37.805  1.00 63.67           C  
ATOM   1130  N   ASN A 141      60.505  77.550  36.917  1.00 68.01           N  
ATOM   1131  CA  ASN A 141      60.732  78.983  37.037  1.00 71.65           C  
ATOM   1132  C   ASN A 141      61.615  79.394  35.832  1.00 70.68           C  
ATOM   1133  O   ASN A 141      62.632  78.756  35.551  1.00 70.59           O  
ATOM   1134  CB  ASN A 141      61.371  79.267  38.452  1.00 76.43           C  
ATOM   1135  CG  ASN A 141      61.754  80.784  38.687  1.00 81.13           C  
ATOM   1136  OD1 ASN A 141      60.946  81.739  38.402  1.00 83.13           O  
ATOM   1137  ND2 ASN A 141      62.997  81.003  39.218  1.00 82.33           N  
ATOM   1138  N   LEU A 142      61.235  80.445  35.113  1.00 69.77           N  
ATOM   1139  CA  LEU A 142      62.017  80.817  33.931  1.00 69.51           C  
ATOM   1140  C   LEU A 142      62.954  81.982  34.091  1.00 69.87           C  
ATOM   1141  O   LEU A 142      62.547  83.090  34.429  1.00 69.72           O  
ATOM   1142  CB  LEU A 142      61.095  81.107  32.723  1.00 68.64           C  
ATOM   1143  CG  LEU A 142      61.691  81.340  31.331  1.00 66.69           C  
ATOM   1144  CD1 LEU A 142      61.728  80.048  30.569  1.00 66.04           C  
ATOM   1145  CD2 LEU A 142      60.882  82.335  30.601  1.00 65.65           C  
ATOM   1146  N   ALA A 143      64.218  81.719  33.810  1.00 70.69           N  
ATOM   1147  CA  ALA A 143      65.241  82.744  33.882  1.00 72.20           C  
ATOM   1148  C   ALA A 143      64.834  84.082  33.207  1.00 73.03           C  
ATOM   1149  O   ALA A 143      64.792  84.184  32.003  1.00 73.20           O  
ATOM   1150  CB  ALA A 143      66.497  82.192  33.247  1.00 72.76           C  
ATOM   1151  N   ASP A 144      64.555  85.125  33.958  1.00 74.49           N  
ATOM   1152  CA  ASP A 144      64.146  86.356  33.301  1.00 76.00           C  
ATOM   1153  C   ASP A 144      65.153  86.935  32.302  1.00 75.32           C  
ATOM   1154  O   ASP A 144      65.226  88.141  32.089  1.00 75.19           O  
ATOM   1155  CB  ASP A 144      63.679  87.397  34.349  1.00 78.69           C  
ATOM   1156  CG  ASP A 144      62.147  87.208  34.755  1.00 81.61           C  
ATOM   1157  OD1 ASP A 144      61.742  86.143  35.338  1.00 82.17           O  
ATOM   1158  OD2 ASP A 144      61.332  88.139  34.476  1.00 82.73           O  
ATOM   1159  N   GLN A 145      65.928  86.051  31.689  1.00 74.48           N  
ATOM   1160  CA  GLN A 145      66.882  86.439  30.652  1.00 74.77           C  
ATOM   1161  C   GLN A 145      66.245  85.937  29.344  1.00 73.58           C  
ATOM   1162  O   GLN A 145      66.477  86.496  28.263  1.00 73.73           O  
ATOM   1163  CB  GLN A 145      68.306  85.801  30.861  1.00 76.29           C  
ATOM   1164  CG  GLN A 145      68.567  84.347  30.296  1.00 76.89           C  
ATOM   1165  CD  GLN A 145      70.036  84.046  29.838  1.00 77.46           C  
ATOM   1166  OE1 GLN A 145      70.531  84.619  28.837  1.00 77.42           O  
ATOM   1167  NE2 GLN A 145      70.718  83.126  30.563  1.00 76.84           N  
ATOM   1168  N   TYR A 146      65.451  84.866  29.479  1.00 72.11           N  
ATOM   1169  CA  TYR A 146      64.697  84.223  28.397  1.00 70.43           C  
ATOM   1170  C   TYR A 146      63.360  84.957  28.296  1.00 69.83           C  
ATOM   1171  O   TYR A 146      62.974  85.432  27.229  1.00 70.15           O  
ATOM   1172  CB  TYR A 146      64.447  82.773  28.735  1.00 69.33           C  
ATOM   1173  CG  TYR A 146      65.721  82.031  28.874  1.00 69.27           C  
ATOM   1174  CD1 TYR A 146      65.935  81.170  29.938  1.00 69.85           C  
ATOM   1175  CD2 TYR A 146      66.710  82.153  27.925  1.00 69.56           C  
ATOM   1176  CE1 TYR A 146      67.118  80.436  30.065  1.00 70.39           C  
ATOM   1177  CE2 TYR A 146      67.902  81.417  28.023  1.00 70.34           C  
ATOM   1178  CZ  TYR A 146      68.105  80.558  29.099  1.00 70.76           C  
ATOM   1179  OH  TYR A 146      69.293  79.830  29.204  1.00 71.81           O  
ATOM   1180  N   VAL A 147      62.645  85.069  29.404  1.00 68.53           N  
ATOM   1181  CA  VAL A 147      61.416  85.795  29.342  1.00 67.32           C  
ATOM   1182  C   VAL A 147      61.601  87.080  28.543  1.00 68.04           C  
ATOM   1183  O   VAL A 147      60.654  87.607  28.009  1.00 68.40           O  
ATOM   1184  CB  VAL A 147      60.912  86.125  30.711  1.00 65.93           C  
ATOM   1185  CG1 VAL A 147      60.120  87.383  30.663  1.00 65.67           C  
ATOM   1186  CG2 VAL A 147      60.022  85.026  31.179  1.00 65.09           C  
ATOM   1187  N   LYS A 148      62.819  87.581  28.423  1.00 69.48           N  
ATOM   1188  CA  LYS A 148      63.041  88.818  27.667  1.00 70.58           C  
ATOM   1189  C   LYS A 148      63.289  88.591  26.192  1.00 69.76           C  
ATOM   1190  O   LYS A 148      63.132  89.509  25.406  1.00 70.17           O  
ATOM   1191  CB  LYS A 148      64.218  89.622  28.246  1.00 72.90           C  
ATOM   1192  CG  LYS A 148      63.928  90.435  29.529  1.00 75.88           C  
ATOM   1193  CD  LYS A 148      65.263  90.733  30.303  1.00 79.33           C  
ATOM   1194  CE  LYS A 148      66.467  91.268  29.394  1.00 80.92           C  
ATOM   1195  NZ  LYS A 148      67.843  91.357  30.095  1.00 80.65           N  
ATOM   1196  N   LYS A 149      63.703  87.388  25.820  1.00 68.80           N  
ATOM   1197  CA  LYS A 149      63.954  87.075  24.412  1.00 68.49           C  
ATOM   1198  C   LYS A 149      62.598  86.807  23.714  1.00 67.02           C  
ATOM   1199  O   LYS A 149      62.487  86.967  22.471  1.00 66.54           O  
ATOM   1200  CB  LYS A 149      64.897  85.845  24.279  1.00 70.09           C  
ATOM   1201  CG  LYS A 149      66.216  86.081  23.463  1.00 72.05           C  
ATOM   1202  CD  LYS A 149      67.254  84.929  23.718  1.00 73.51           C  
ATOM   1203  CE  LYS A 149      68.712  85.225  23.202  1.00 74.91           C  
ATOM   1204  NZ  LYS A 149      69.043  85.033  21.710  1.00 76.17           N  
ATOM   1205  N   CYS A 150      61.600  86.397  24.519  1.00 64.71           N  
ATOM   1206  CA  CYS A 150      60.261  86.131  24.039  1.00 62.77           C  
ATOM   1207  C   CYS A 150      59.645  87.461  23.940  1.00 64.40           C  
ATOM   1208  O   CYS A 150      59.250  87.868  22.868  1.00 65.20           O  
ATOM   1209  CB  CYS A 150      59.406  85.393  25.018  1.00 59.06           C  
ATOM   1210  SG  CYS A 150      59.331  83.594  24.864  1.00 56.11           S  
ATOM   1211  N   GLU A 151      59.542  88.154  25.068  1.00 65.88           N  
ATOM   1212  CA  GLU A 151      58.920  89.476  25.044  1.00 67.77           C  
ATOM   1213  C   GLU A 151      59.405  90.283  23.885  1.00 66.89           C  
ATOM   1214  O   GLU A 151      58.709  91.160  23.414  1.00 67.24           O  
ATOM   1215  CB  GLU A 151      59.176  90.284  26.322  1.00 71.13           C  
ATOM   1216  CG  GLU A 151      58.294  89.838  27.525  1.00 76.24           C  
ATOM   1217  CD  GLU A 151      58.224  90.878  28.689  1.00 79.38           C  
ATOM   1218  OE1 GLU A 151      57.635  90.510  29.788  1.00 80.88           O  
ATOM   1219  OE2 GLU A 151      58.748  92.038  28.475  1.00 79.90           O  
ATOM   1220  N   ALA A 152      60.598  89.966  23.419  1.00 66.28           N  
ATOM   1221  CA  ALA A 152      61.213  90.687  22.318  1.00 66.01           C  
ATOM   1222  C   ALA A 152      60.683  90.254  21.018  1.00 65.27           C  
ATOM   1223  O   ALA A 152      60.654  91.020  20.082  1.00 65.85           O  
ATOM   1224  CB  ALA A 152      62.700  90.461  22.309  1.00 67.41           C  
ATOM   1225  N   ALA A 153      60.313  88.991  20.970  1.00 64.56           N  
ATOM   1226  CA  ALA A 153      59.793  88.343  19.773  1.00 63.21           C  
ATOM   1227  C   ALA A 153      58.359  88.693  19.492  1.00 61.51           C  
ATOM   1228  O   ALA A 153      57.990  88.839  18.329  1.00 61.52           O  
ATOM   1229  CB  ALA A 153      59.917  86.839  19.911  1.00 63.85           C  
ATOM   1230  N   PHE A 154      57.561  88.778  20.555  1.00 59.29           N  
ATOM   1231  CA  PHE A 154      56.175  89.121  20.426  1.00 56.90           C  
ATOM   1232  C   PHE A 154      56.061  90.571  20.098  1.00 58.18           C  
ATOM   1233  O   PHE A 154      55.073  90.960  19.510  1.00 58.93           O  
ATOM   1234  CB  PHE A 154      55.424  88.889  21.696  1.00 52.37           C  
ATOM   1235  CG  PHE A 154      55.116  87.499  21.942  1.00 47.99           C  
ATOM   1236  CD1 PHE A 154      55.957  86.727  22.642  1.00 46.65           C  
ATOM   1237  CD2 PHE A 154      53.943  86.971  21.515  1.00 47.19           C  
ATOM   1238  CE1 PHE A 154      55.618  85.433  22.921  1.00 47.39           C  
ATOM   1239  CE2 PHE A 154      53.592  85.680  21.784  1.00 47.07           C  
ATOM   1240  CZ  PHE A 154      54.420  84.908  22.485  1.00 47.21           C  
ATOM   1241  N   LYS A 155      57.044  91.389  20.476  1.00 59.96           N  
ATOM   1242  CA  LYS A 155      56.960  92.833  20.172  1.00 61.92           C  
ATOM   1243  C   LYS A 155      57.183  93.068  18.656  1.00 61.75           C  
ATOM   1244  O   LYS A 155      56.870  94.162  18.111  1.00 62.30           O  
ATOM   1245  CB  LYS A 155      57.980  93.659  21.007  1.00 64.11           C  
ATOM   1246  CG  LYS A 155      57.413  94.434  22.251  1.00 68.47           C  
ATOM   1247  CD  LYS A 155      58.337  95.700  22.636  1.00 72.74           C  
ATOM   1248  CE  LYS A 155      57.887  96.588  23.940  1.00 74.94           C  
ATOM   1249  NZ  LYS A 155      58.640  97.938  24.265  1.00 74.34           N  
ATOM   1250  N   ASN A 156      57.710  92.041  17.979  1.00 60.84           N  
ATOM   1251  CA  ASN A 156      57.970  92.130  16.544  1.00 60.22           C  
ATOM   1252  C   ASN A 156      56.720  91.795  15.736  1.00 59.37           C  
ATOM   1253  O   ASN A 156      56.629  92.151  14.556  1.00 60.18           O  
ATOM   1254  CB  ASN A 156      59.097  91.184  16.103  1.00 61.01           C  
ATOM   1255  CG  ASN A 156      59.643  91.551  14.727  1.00 62.14           C  
ATOM   1256  OD1 ASN A 156      60.108  92.683  14.540  1.00 63.23           O  
ATOM   1257  ND2 ASN A 156      59.575  90.619  13.756  1.00 62.13           N  
ATOM   1258  N   ILE A 157      55.770  91.096  16.349  1.00 57.35           N  
ATOM   1259  CA  ILE A 157      54.570  90.758  15.647  1.00 55.39           C  
ATOM   1260  C   ILE A 157      53.422  91.480  16.339  1.00 56.24           C  
ATOM   1261  O   ILE A 157      52.245  91.114  16.248  1.00 56.21           O  
ATOM   1262  CB  ILE A 157      54.401  89.247  15.572  1.00 53.19           C  
ATOM   1263  CG1 ILE A 157      54.085  88.652  16.913  1.00 52.48           C  
ATOM   1264  CG2 ILE A 157      55.671  88.637  15.169  1.00 52.72           C  
ATOM   1265  CD1 ILE A 157      53.837  87.147  16.853  1.00 51.60           C  
ATOM   1266  N   ASN A 158      53.811  92.553  17.011  1.00 56.79           N  
ATOM   1267  CA  ASN A 158      52.928  93.453  17.725  1.00 58.21           C  
ATOM   1268  C   ASN A 158      51.921  92.957  18.700  1.00 58.78           C  
ATOM   1269  O   ASN A 158      50.810  93.504  18.728  1.00 59.35           O  
ATOM   1270  CB  ASN A 158      52.178  94.322  16.760  1.00 60.02           C  
ATOM   1271  CG  ASN A 158      53.084  94.971  15.771  1.00 62.94           C  
ATOM   1272  OD1 ASN A 158      54.095  95.614  16.135  1.00 65.51           O  
ATOM   1273  ND2 ASN A 158      52.746  94.820  14.494  1.00 64.60           N  
ATOM   1274  N   VAL A 159      52.286  91.968  19.516  1.00 58.98           N  
ATOM   1275  CA  VAL A 159      51.376  91.435  20.516  1.00 59.58           C  
ATOM   1276  C   VAL A 159      51.563  92.261  21.776  1.00 60.89           C  
ATOM   1277  O   VAL A 159      52.683  92.446  22.253  1.00 61.45           O  
ATOM   1278  CB  VAL A 159      51.694  89.984  20.790  1.00 58.64           C  
ATOM   1279  CG1 VAL A 159      50.568  89.320  21.521  1.00 58.80           C  
ATOM   1280  CG2 VAL A 159      51.876  89.286  19.504  1.00 59.15           C  
ATOM   1281  N   ASP A 160      50.480  92.798  22.313  1.00 61.87           N  
ATOM   1282  CA  ASP A 160      50.640  93.610  23.503  1.00 62.48           C  
ATOM   1283  C   ASP A 160      51.109  92.786  24.661  1.00 61.63           C  
ATOM   1284  O   ASP A 160      50.299  92.207  25.354  1.00 61.39           O  
ATOM   1285  CB  ASP A 160      49.329  94.303  23.887  1.00 65.31           C  
ATOM   1286  CG  ASP A 160      49.545  95.439  24.898  1.00 67.26           C  
ATOM   1287  OD1 ASP A 160      48.633  96.301  25.068  1.00 67.64           O  
ATOM   1288  OD2 ASP A 160      50.646  95.457  25.515  1.00 69.31           O  
ATOM   1289  N   THR A 161      52.421  92.768  24.869  1.00 61.57           N  
ATOM   1290  CA  THR A 161      53.069  92.029  25.961  1.00 61.11           C  
ATOM   1291  C   THR A 161      52.348  92.095  27.293  1.00 60.32           C  
ATOM   1292  O   THR A 161      52.329  91.125  28.045  1.00 59.84           O  
ATOM   1293  CB  THR A 161      54.472  92.544  26.272  1.00 61.36           C  
ATOM   1294  OG1 THR A 161      54.898  93.511  25.292  1.00 62.19           O  
ATOM   1295  CG2 THR A 161      55.411  91.384  26.319  1.00 61.86           C  
ATOM   1296  N   THR A 162      51.775  93.255  27.583  1.00 59.44           N  
ATOM   1297  CA  THR A 162      51.060  93.464  28.830  1.00 59.07           C  
ATOM   1298  C   THR A 162      49.951  92.437  28.981  1.00 58.65           C  
ATOM   1299  O   THR A 162      49.366  92.279  30.071  1.00 59.84           O  
ATOM   1300  CB  THR A 162      50.389  94.842  28.866  1.00 59.33           C  
ATOM   1301  OG1 THR A 162      49.096  94.754  28.242  1.00 59.24           O  
ATOM   1302  CG2 THR A 162      51.252  95.878  28.129  1.00 59.53           C  
ATOM   1303  N   ARG A 163      49.663  91.739  27.891  1.00 56.81           N  
ATOM   1304  CA  ARG A 163      48.592  90.778  27.894  1.00 55.13           C  
ATOM   1305  C   ARG A 163      48.881  89.451  28.547  1.00 53.22           C  
ATOM   1306  O   ARG A 163      47.950  88.742  28.937  1.00 52.46           O  
ATOM   1307  CB  ARG A 163      48.089  90.583  26.463  1.00 56.98           C  
ATOM   1308  CG  ARG A 163      46.694  91.159  26.203  1.00 59.47           C  
ATOM   1309  CD  ARG A 163      46.398  91.180  24.713  1.00 61.41           C  
ATOM   1310  NE  ARG A 163      46.157  89.849  24.136  1.00 63.26           N  
ATOM   1311  CZ  ARG A 163      46.407  89.550  22.853  1.00 64.69           C  
ATOM   1312  NH1 ARG A 163      46.898  90.497  22.031  1.00 64.33           N  
ATOM   1313  NH2 ARG A 163      46.207  88.304  22.393  1.00 64.87           N  
ATOM   1314  N   PHE A 164      50.146  89.097  28.688  1.00 51.35           N  
ATOM   1315  CA  PHE A 164      50.415  87.826  29.306  1.00 50.93           C  
ATOM   1316  C   PHE A 164      50.153  87.878  30.765  1.00 52.02           C  
ATOM   1317  O   PHE A 164      50.036  88.954  31.348  1.00 52.85           O  
ATOM   1318  CB  PHE A 164      51.819  87.434  29.125  1.00 49.32           C  
ATOM   1319  CG  PHE A 164      52.174  87.137  27.735  1.00 48.98           C  
ATOM   1320  CD1 PHE A 164      52.214  85.836  27.287  1.00 48.38           C  
ATOM   1321  CD2 PHE A 164      52.589  88.152  26.886  1.00 48.57           C  
ATOM   1322  CE1 PHE A 164      52.688  85.555  26.003  1.00 48.83           C  
ATOM   1323  CE2 PHE A 164      53.055  87.867  25.603  1.00 48.28           C  
ATOM   1324  CZ  PHE A 164      53.109  86.569  25.165  1.00 48.01           C  
ATOM   1325  N   VAL A 165      50.085  86.704  31.369  1.00 52.86           N  
ATOM   1326  CA  VAL A 165      49.816  86.591  32.787  1.00 54.31           C  
ATOM   1327  C   VAL A 165      50.590  85.396  33.351  1.00 56.67           C  
ATOM   1328  O   VAL A 165      50.219  84.269  33.065  1.00 57.71           O  
ATOM   1329  CB  VAL A 165      48.294  86.449  32.981  1.00 52.65           C  
ATOM   1330  CG1 VAL A 165      47.941  85.456  34.092  1.00 52.07           C  
ATOM   1331  CG2 VAL A 165      47.732  87.820  33.269  1.00 52.42           C  
ATOM   1332  N   LYS A 166      51.662  85.609  34.134  1.00 58.58           N  
ATOM   1333  CA  LYS A 166      52.413  84.453  34.651  1.00 60.60           C  
ATOM   1334  C   LYS A 166      51.441  83.431  35.229  1.00 60.54           C  
ATOM   1335  O   LYS A 166      50.541  83.771  35.989  1.00 60.31           O  
ATOM   1336  CB  LYS A 166      53.401  84.856  35.742  1.00 62.90           C  
ATOM   1337  CG  LYS A 166      54.660  85.624  35.341  1.00 66.66           C  
ATOM   1338  CD  LYS A 166      55.624  85.680  36.609  1.00 70.90           C  
ATOM   1339  CE  LYS A 166      57.168  86.050  36.366  1.00 73.14           C  
ATOM   1340  NZ  LYS A 166      57.509  87.416  35.713  1.00 74.26           N  
ATOM   1341  N   THR A 167      51.552  82.178  34.836  1.00 61.50           N  
ATOM   1342  CA  THR A 167      50.630  81.214  35.441  1.00 63.33           C  
ATOM   1343  C   THR A 167      51.453  80.867  36.632  1.00 63.20           C  
ATOM   1344  O   THR A 167      52.594  81.339  36.739  1.00 63.06           O  
ATOM   1345  CB  THR A 167      50.339  79.909  34.577  1.00 64.04           C  
ATOM   1346  OG1 THR A 167      51.442  79.651  33.691  1.00 63.99           O  
ATOM   1347  CG2 THR A 167      48.967  80.056  33.757  1.00 64.70           C  
ATOM   1348  N   VAL A 168      50.916  80.043  37.512  1.00 63.02           N  
ATOM   1349  CA  VAL A 168      51.678  79.737  38.691  1.00 63.05           C  
ATOM   1350  C   VAL A 168      52.355  78.400  38.744  1.00 63.27           C  
ATOM   1351  O   VAL A 168      51.740  77.335  38.887  1.00 62.58           O  
ATOM   1352  CB  VAL A 168      50.815  79.966  39.949  1.00 63.46           C  
ATOM   1353  CG1 VAL A 168      50.657  78.676  40.778  1.00 62.66           C  
ATOM   1354  CG2 VAL A 168      51.435  81.100  40.757  1.00 64.42           C  
ATOM   1355  N   GLN A 169      53.663  78.473  38.594  1.00 64.40           N  
ATOM   1356  CA  GLN A 169      54.476  77.280  38.681  1.00 65.55           C  
ATOM   1357  C   GLN A 169      55.291  77.448  39.958  1.00 67.30           C  
ATOM   1358  O   GLN A 169      55.611  78.600  40.399  1.00 66.84           O  
ATOM   1359  CB  GLN A 169      55.400  77.121  37.470  1.00 63.53           C  
ATOM   1360  CG  GLN A 169      54.716  76.909  36.121  1.00 61.43           C  
ATOM   1361  CD  GLN A 169      53.740  75.735  36.067  1.00 60.71           C  
ATOM   1362  OE1 GLN A 169      53.601  74.990  37.022  1.00 59.58           O  
ATOM   1363  NE2 GLN A 169      53.054  75.578  34.923  1.00 60.50           N  
ATOM   1364  N   GLY A 170      55.573  76.296  40.570  1.00 69.15           N  
ATOM   1365  CA  GLY A 170      56.352  76.297  41.793  1.00 72.42           C  
ATOM   1366  C   GLY A 170      56.497  75.047  42.665  1.00 74.14           C  
ATOM   1367  O   GLY A 170      56.190  73.900  42.273  1.00 74.98           O  
ATOM   1368  N   SER A 171      57.013  75.319  43.867  1.00 74.80           N  
ATOM   1369  CA  SER A 171      57.266  74.354  44.947  1.00 74.84           C  
ATOM   1370  C   SER A 171      55.918  73.789  45.455  1.00 73.61           C  
ATOM   1371  O   SER A 171      55.807  72.590  45.859  1.00 73.46           O  
ATOM   1372  CB  SER A 171      57.970  75.131  46.062  1.00 76.47           C  
ATOM   1373  OG  SER A 171      57.520  76.509  46.040  1.00 78.41           O  
ATOM   1374  N   SER A 172      54.938  74.712  45.420  1.00 71.43           N  
ATOM   1375  CA  SER A 172      53.525  74.558  45.807  1.00 69.70           C  
ATOM   1376  C   SER A 172      52.889  73.354  45.088  1.00 67.60           C  
ATOM   1377  O   SER A 172      52.323  72.387  45.693  1.00 67.84           O  
ATOM   1378  CB  SER A 172      52.762  75.845  45.392  1.00 70.91           C  
ATOM   1379  OG  SER A 172      53.661  76.867  44.916  1.00 72.89           O  
ATOM   1380  N   CYS A 173      53.019  73.486  43.766  1.00 63.89           N  
ATOM   1381  CA  CYS A 173      52.570  72.589  42.714  1.00 58.93           C  
ATOM   1382  C   CYS A 173      52.720  71.131  42.967  1.00 55.42           C  
ATOM   1383  O   CYS A 173      53.788  70.672  43.327  1.00 55.01           O  
ATOM   1384  CB  CYS A 173      53.324  72.963  41.455  1.00 58.87           C  
ATOM   1385  SG  CYS A 173      52.694  74.514  40.760  1.00 58.96           S  
ATOM   1386  N   PRO A 174      51.648  70.379  42.791  1.00 52.33           N  
ATOM   1387  CA  PRO A 174      51.751  68.949  43.018  1.00 51.74           C  
ATOM   1388  C   PRO A 174      52.365  68.130  41.864  1.00 51.97           C  
ATOM   1389  O   PRO A 174      51.939  66.974  41.641  1.00 52.17           O  
ATOM   1390  CB  PRO A 174      50.325  68.557  43.321  1.00 50.22           C  
ATOM   1391  CG  PRO A 174      49.596  69.518  42.613  1.00 50.09           C  
ATOM   1392  CD  PRO A 174      50.259  70.790  42.879  1.00 50.82           C  
ATOM   1393  N   TYR A 175      53.381  68.697  41.179  1.00 50.93           N  
ATOM   1394  CA  TYR A 175      54.024  68.036  40.057  1.00 50.23           C  
ATOM   1395  C   TYR A 175      54.053  66.565  40.303  1.00 52.61           C  
ATOM   1396  O   TYR A 175      53.430  65.792  39.604  1.00 53.36           O  
ATOM   1397  CB  TYR A 175      55.430  68.535  39.839  1.00 45.77           C  
ATOM   1398  CG  TYR A 175      55.457  69.973  39.454  1.00 42.86           C  
ATOM   1399  CD1 TYR A 175      56.606  70.739  39.618  1.00 42.91           C  
ATOM   1400  CD2 TYR A 175      54.340  70.594  38.938  1.00 42.34           C  
ATOM   1401  CE1 TYR A 175      56.645  72.089  39.288  1.00 41.86           C  
ATOM   1402  CE2 TYR A 175      54.365  71.951  38.587  1.00 41.87           C  
ATOM   1403  CZ  TYR A 175      55.525  72.685  38.774  1.00 41.93           C  
ATOM   1404  OH  TYR A 175      55.573  74.011  38.455  1.00 42.39           O  
ATOM   1405  N   ASP A 176      54.730  66.164  41.345  1.00 55.47           N  
ATOM   1406  CA  ASP A 176      54.821  64.741  41.631  1.00 57.89           C  
ATOM   1407  C   ASP A 176      53.480  63.985  41.542  1.00 57.00           C  
ATOM   1408  O   ASP A 176      53.460  62.802  41.121  1.00 57.02           O  
ATOM   1409  CB  ASP A 176      55.528  64.560  43.003  1.00 62.36           C  
ATOM   1410  CG  ASP A 176      56.922  65.313  43.056  1.00 67.26           C  
ATOM   1411  OD1 ASP A 176      56.983  66.542  43.478  1.00 68.42           O  
ATOM   1412  OD2 ASP A 176      57.939  64.656  42.627  1.00 68.84           O  
ATOM   1413  N   THR A 177      52.369  64.648  41.894  1.00 55.46           N  
ATOM   1414  CA  THR A 177      51.073  63.966  41.840  1.00 54.39           C  
ATOM   1415  C   THR A 177      50.589  63.867  40.398  1.00 54.13           C  
ATOM   1416  O   THR A 177      50.069  62.813  39.990  1.00 54.42           O  
ATOM   1417  CB  THR A 177      49.961  64.660  42.666  1.00 53.57           C  
ATOM   1418  OG1 THR A 177      50.471  65.078  43.930  1.00 54.16           O  
ATOM   1419  CG2 THR A 177      48.834  63.680  42.910  1.00 51.95           C  
ATOM   1420  N   GLN A 178      50.763  64.969  39.646  1.00 52.89           N  
ATOM   1421  CA  GLN A 178      50.380  65.072  38.243  1.00 50.85           C  
ATOM   1422  C   GLN A 178      51.104  64.004  37.434  1.00 51.28           C  
ATOM   1423  O   GLN A 178      50.477  63.333  36.633  1.00 52.12           O  
ATOM   1424  CB  GLN A 178      50.736  66.427  37.723  1.00 48.84           C  
ATOM   1425  CG  GLN A 178      50.235  67.537  38.589  1.00 48.59           C  
ATOM   1426  CD  GLN A 178      50.729  68.902  38.118  1.00 48.73           C  
ATOM   1427  OE1 GLN A 178      51.143  69.746  38.898  1.00 47.82           O  
ATOM   1428  NE2 GLN A 178      50.678  69.119  36.816  1.00 50.68           N  
ATOM   1429  N   LYS A 179      52.407  63.820  37.641  1.00 51.13           N  
ATOM   1430  CA  LYS A 179      53.130  62.791  36.914  1.00 51.38           C  
ATOM   1431  C   LYS A 179      52.476  61.414  36.970  1.00 52.69           C  
ATOM   1432  O   LYS A 179      52.976  60.500  36.314  1.00 53.59           O  
ATOM   1433  CB  LYS A 179      54.558  62.651  37.407  1.00 50.98           C  
ATOM   1434  CG  LYS A 179      55.370  63.885  37.304  1.00 52.16           C  
ATOM   1435  CD  LYS A 179      56.864  63.581  37.571  1.00 54.75           C  
ATOM   1436  CE  LYS A 179      57.738  64.803  37.117  1.00 57.01           C  
ATOM   1437  NZ  LYS A 179      59.282  64.724  37.174  1.00 57.90           N  
ATOM   1438  N   THR A 180      51.393  61.235  37.741  1.00 53.97           N  
ATOM   1439  CA  THR A 180      50.699  59.915  37.824  1.00 56.23           C  
ATOM   1440  C   THR A 180      49.302  60.027  37.187  1.00 56.73           C  
ATOM   1441  O   THR A 180      48.564  58.984  37.016  1.00 56.64           O  
ATOM   1442  CB  THR A 180      50.549  59.377  39.305  1.00 57.49           C  
ATOM   1443  OG1 THR A 180      49.563  60.147  40.023  1.00 58.92           O  
ATOM   1444  CG2 THR A 180      51.917  59.443  40.051  1.00 58.43           C  
ATOM   1445  N   VAL A 181      49.011  61.314  36.854  1.00 56.62           N  
ATOM   1446  CA  VAL A 181      47.824  61.870  36.175  1.00 56.49           C  
ATOM   1447  C   VAL A 181      46.908  62.859  37.036  1.00 56.00           C  
ATOM   1448  O   VAL A 181      47.207  64.064  37.187  1.00 54.60           O  
ATOM   1449  CB  VAL A 181      47.066  60.641  35.458  1.00 57.65           C  
ATOM   1450  CG1 VAL A 181      45.555  60.893  35.325  1.00 59.06           C  
ATOM   1451  CG2 VAL A 181      47.724  60.352  34.038  1.00 57.73           C  
ATOM   1452  OXT VAL A 181      45.880  62.479  37.607  1.00 56.29           O  
TER    1453      VAL A 181                                                      
ATOM   1454  N   ASP B   1      37.898  67.429  18.463  1.00 67.55           N  
ATOM   1455  CA  ASP B   1      39.160  67.272  17.590  1.00 69.03           C  
ATOM   1456  C   ASP B   1      39.107  67.300  15.940  1.00 66.74           C  
ATOM   1457  O   ASP B   1      38.215  66.700  15.222  1.00 67.85           O  
ATOM   1458  CB  ASP B   1      39.960  66.018  18.124  1.00 73.01           C  
ATOM   1459  CG  ASP B   1      40.616  65.112  16.963  1.00 77.57           C  
ATOM   1460  OD1 ASP B   1      41.861  65.277  16.685  1.00 79.57           O  
ATOM   1461  OD2 ASP B   1      39.892  64.234  16.340  1.00 78.88           O  
ATOM   1462  N   GLY B   2      40.086  68.009  15.357  1.00 62.50           N  
ATOM   1463  CA  GLY B   2      40.175  68.138  13.918  1.00 56.47           C  
ATOM   1464  C   GLY B   2      39.538  69.449  13.519  1.00 52.43           C  
ATOM   1465  O   GLY B   2      39.272  70.327  14.338  1.00 51.27           O  
ATOM   1466  N   ILE B   3      39.332  69.581  12.222  1.00 48.75           N  
ATOM   1467  CA  ILE B   3      38.690  70.730  11.654  1.00 44.42           C  
ATOM   1468  C   ILE B   3      37.315  70.193  11.349  1.00 41.80           C  
ATOM   1469  O   ILE B   3      37.187  69.101  10.783  1.00 41.64           O  
ATOM   1470  CB  ILE B   3      39.328  71.137  10.343  1.00 44.55           C  
ATOM   1471  CG1 ILE B   3      40.710  71.734  10.582  1.00 45.37           C  
ATOM   1472  CG2 ILE B   3      38.434  72.107   9.618  1.00 44.61           C  
ATOM   1473  CD1 ILE B   3      41.824  70.672  10.616  1.00 47.67           C  
ATOM   1474  N   PRO B   4      36.271  70.935  11.722  1.00 39.03           N  
ATOM   1475  CA  PRO B   4      34.908  70.496  11.466  1.00 37.56           C  
ATOM   1476  C   PRO B   4      34.940  70.011  10.041  1.00 37.43           C  
ATOM   1477  O   PRO B   4      35.805  70.411   9.262  1.00 38.09           O  
ATOM   1478  CB  PRO B   4      34.122  71.760  11.585  1.00 37.83           C  
ATOM   1479  CG  PRO B   4      34.976  72.641  12.439  1.00 38.08           C  
ATOM   1480  CD  PRO B   4      36.319  72.374  11.992  1.00 38.14           C  
ATOM   1481  N   SER B   5      33.996  69.164   9.666  1.00 36.96           N  
ATOM   1482  CA  SER B   5      34.008  68.592   8.317  1.00 34.85           C  
ATOM   1483  C   SER B   5      33.447  69.484   7.227  1.00 33.24           C  
ATOM   1484  O   SER B   5      33.750  69.259   6.032  1.00 35.28           O  
ATOM   1485  CB  SER B   5      33.235  67.299   8.316  1.00 35.16           C  
ATOM   1486  OG  SER B   5      31.927  67.651   7.982  1.00 37.21           O  
ATOM   1487  N   PHE B   6      32.642  70.480   7.612  1.00 30.20           N  
ATOM   1488  CA  PHE B   6      32.041  71.403   6.655  1.00 26.89           C  
ATOM   1489  C   PHE B   6      32.952  72.541   6.222  1.00 26.17           C  
ATOM   1490  O   PHE B   6      32.604  73.343   5.347  1.00 27.68           O  
ATOM   1491  CB  PHE B   6      30.730  71.970   7.196  1.00 25.33           C  
ATOM   1492  CG  PHE B   6      30.848  72.614   8.510  1.00 22.43           C  
ATOM   1493  CD1 PHE B   6      31.436  73.833   8.632  1.00 21.68           C  
ATOM   1494  CD2 PHE B   6      30.444  71.946   9.648  1.00 22.42           C  
ATOM   1495  CE1 PHE B   6      31.645  74.394   9.865  1.00 22.11           C  
ATOM   1496  CE2 PHE B   6      30.642  72.498  10.905  1.00 22.36           C  
ATOM   1497  CZ  PHE B   6      31.246  73.721  11.018  1.00 22.35           C  
ATOM   1498  N   VAL B   7      34.124  72.664   6.820  1.00 24.58           N  
ATOM   1499  CA  VAL B   7      35.001  73.720   6.361  1.00 22.42           C  
ATOM   1500  C   VAL B   7      35.445  73.290   4.974  1.00 22.08           C  
ATOM   1501  O   VAL B   7      35.651  72.066   4.701  1.00 21.91           O  
ATOM   1502  CB  VAL B   7      36.202  73.809   7.207  1.00 21.89           C  
ATOM   1503  CG1 VAL B   7      37.103  74.886   6.683  1.00 21.45           C  
ATOM   1504  CG2 VAL B   7      35.794  74.033   8.595  1.00 21.76           C  
ATOM   1505  N   THR B   8      35.577  74.280   4.091  1.00 20.82           N  
ATOM   1506  CA  THR B   8      36.000  74.035   2.707  1.00 19.58           C  
ATOM   1507  C   THR B   8      36.951  75.130   2.324  1.00 20.16           C  
ATOM   1508  O   THR B   8      37.111  76.105   3.040  1.00 20.82           O  
ATOM   1509  CB  THR B   8      34.876  74.139   1.769  1.00 18.28           C  
ATOM   1510  OG1 THR B   8      34.312  75.428   1.921  1.00 19.18           O  
ATOM   1511  CG2 THR B   8      33.840  73.147   2.074  1.00 16.95           C  
ATOM   1512  N   ALA B   9      37.557  74.991   1.161  1.00 19.91           N  
ATOM   1513  CA  ALA B   9      38.533  75.965   0.727  1.00 19.36           C  
ATOM   1514  C   ALA B   9      37.983  77.243   0.330  1.00 19.75           C  
ATOM   1515  O   ALA B   9      36.899  77.302  -0.210  1.00 20.31           O  
ATOM   1516  CB  ALA B   9      39.232  75.455  -0.400  1.00 19.98           C  
ATOM   1517  N   GLY B  10      38.740  78.285   0.570  1.00 20.18           N  
ATOM   1518  CA  GLY B  10      38.304  79.595   0.097  1.00 21.77           C  
ATOM   1519  C   GLY B  10      37.598  80.503   1.044  1.00 21.68           C  
ATOM   1520  O   GLY B  10      36.910  80.046   1.915  1.00 21.78           O  
ATOM   1521  N   LYS B  11      37.708  81.801   0.890  1.00 22.48           N  
ATOM   1522  CA  LYS B  11      37.006  82.552   1.905  1.00 23.16           C  
ATOM   1523  C   LYS B  11      35.547  82.712   1.586  1.00 23.07           C  
ATOM   1524  O   LYS B  11      35.132  82.410   0.477  1.00 22.46           O  
ATOM   1525  CB  LYS B  11      37.668  83.888   2.093  1.00 23.04           C  
ATOM   1526  CG  LYS B  11      39.111  83.766   1.848  1.00 26.40           C  
ATOM   1527  CD  LYS B  11      39.923  84.743   2.638  1.00 30.09           C  
ATOM   1528  CE  LYS B  11      41.187  85.108   1.851  1.00 33.82           C  
ATOM   1529  NZ  LYS B  11      42.326  85.604   2.729  1.00 37.86           N  
ATOM   1530  N   CYS B  12      34.758  83.150   2.568  1.00 22.99           N  
ATOM   1531  CA  CYS B  12      33.358  83.407   2.274  1.00 22.27           C  
ATOM   1532  C   CYS B  12      33.268  84.445   1.212  1.00 20.98           C  
ATOM   1533  O   CYS B  12      34.095  85.383   1.085  1.00 18.72           O  
ATOM   1534  CB  CYS B  12      32.594  84.010   3.394  1.00 23.14           C  
ATOM   1535  SG  CYS B  12      32.624  83.025   4.849  1.00 25.69           S  
ATOM   1536  N   ALA B  13      32.147  84.310   0.541  1.00 20.54           N  
ATOM   1537  CA  ALA B  13      31.837  85.156  -0.540  1.00 21.67           C  
ATOM   1538  C   ALA B  13      31.547  86.485   0.009  1.00 23.02           C  
ATOM   1539  O   ALA B  13      31.052  86.612   1.113  1.00 24.41           O  
ATOM   1540  CB  ALA B  13      30.668  84.645  -1.180  1.00 21.56           C  
ATOM   1541  N   SER B  14      31.842  87.526  -0.720  1.00 24.25           N  
ATOM   1542  CA  SER B  14      31.421  88.779  -0.129  1.00 26.09           C  
ATOM   1543  C   SER B  14      30.071  89.284  -0.745  1.00 25.52           C  
ATOM   1544  O   SER B  14      30.064  90.129  -1.600  1.00 25.63           O  
ATOM   1545  CB  SER B  14      32.535  89.750  -0.331  1.00 27.81           C  
ATOM   1546  OG  SER B  14      32.084  90.992   0.123  1.00 33.59           O  
ATOM   1547  N   VAL B  15      28.941  88.743  -0.306  1.00 26.22           N  
ATOM   1548  CA  VAL B  15      27.590  89.031  -0.855  1.00 26.69           C  
ATOM   1549  C   VAL B  15      27.063  90.392  -0.451  1.00 27.37           C  
ATOM   1550  O   VAL B  15      27.520  90.929   0.557  1.00 27.26           O  
ATOM   1551  CB  VAL B  15      26.527  88.036  -0.289  1.00 26.96           C  
ATOM   1552  CG1 VAL B  15      26.886  86.597  -0.558  1.00 26.24           C  
ATOM   1553  CG2 VAL B  15      26.420  88.242   1.230  1.00 25.81           C  
ATOM   1554  N   ALA B  16      26.058  90.894  -1.184  1.00 27.57           N  
ATOM   1555  CA  ALA B  16      25.430  92.192  -0.870  1.00 29.56           C  
ATOM   1556  C   ALA B  16      24.336  92.082   0.171  1.00 30.60           C  
ATOM   1557  O   ALA B  16      23.736  91.024   0.277  1.00 32.28           O  
ATOM   1558  CB  ALA B  16      24.838  92.757  -2.060  1.00 30.22           C  
ATOM   1559  N   ASN B  17      24.034  93.145   0.912  1.00 30.11           N  
ATOM   1560  CA  ASN B  17      22.977  93.059   1.908  1.00 30.76           C  
ATOM   1561  C   ASN B  17      21.736  93.789   1.364  1.00 32.21           C  
ATOM   1562  O   ASN B  17      21.931  94.814   0.731  1.00 32.95           O  
ATOM   1563  CB  ASN B  17      23.414  93.769   3.184  1.00 31.73           C  
ATOM   1564  CG  ASN B  17      24.571  93.097   3.914  1.00 32.87           C  
ATOM   1565  OD1 ASN B  17      24.822  91.915   3.740  1.00 33.74           O  
ATOM   1566  ND2 ASN B  17      25.262  93.864   4.780  1.00 33.72           N  
ATOM   1567  N   GLN B  18      20.496  93.311   1.602  1.00 33.26           N  
ATOM   1568  CA  GLN B  18      19.248  93.997   1.113  1.00 36.01           C  
ATOM   1569  C   GLN B  18      19.258  95.441   1.471  1.00 38.49           C  
ATOM   1570  O   GLN B  18      19.623  95.775   2.590  1.00 38.89           O  
ATOM   1571  CB  GLN B  18      17.978  93.485   1.743  1.00 35.80           C  
ATOM   1572  CG  GLN B  18      16.933  92.934   0.760  1.00 37.14           C  
ATOM   1573  CD  GLN B  18      16.249  93.994   0.021  1.00 37.03           C  
ATOM   1574  OE1 GLN B  18      16.212  95.105   0.488  1.00 38.33           O  
ATOM   1575  NE2 GLN B  18      15.677  93.673  -1.129  1.00 38.12           N  
ATOM   1576  N   ASP B  19      18.795  96.311   0.572  1.00 41.11           N  
ATOM   1577  CA  ASP B  19      18.890  97.731   0.879  1.00 42.53           C  
ATOM   1578  C   ASP B  19      18.079  98.300   2.050  1.00 41.88           C  
ATOM   1579  O   ASP B  19      18.666  98.694   3.048  1.00 43.84           O  
ATOM   1580  CB  ASP B  19      18.804  98.576  -0.413  1.00 45.94           C  
ATOM   1581  CG  ASP B  19      20.263  98.968  -1.004  1.00 50.16           C  
ATOM   1582  OD1 ASP B  19      21.207  99.243  -0.169  1.00 50.97           O  
ATOM   1583  OD2 ASP B  19      20.450  99.025  -2.290  1.00 51.77           O  
ATOM   1584  N   ASN B  20      16.785  98.402   2.080  1.00 40.57           N  
ATOM   1585  CA  ASN B  20      16.408  98.950   3.384  1.00 39.91           C  
ATOM   1586  C   ASN B  20      15.682  97.907   4.137  1.00 37.66           C  
ATOM   1587  O   ASN B  20      14.484  97.706   3.918  1.00 37.71           O  
ATOM   1588  CB  ASN B  20      15.612 100.178   3.164  1.00 43.87           C  
ATOM   1589  CG  ASN B  20      16.442 101.238   2.535  1.00 47.31           C  
ATOM   1590  OD1 ASN B  20      17.445 101.702   3.169  1.00 48.00           O  
ATOM   1591  ND2 ASN B  20      16.085 101.629   1.255  1.00 48.60           N  
ATOM   1592  N   PHE B  21      16.380  97.243   5.048  1.00 34.44           N  
ATOM   1593  CA  PHE B  21      15.749  96.072   5.635  1.00 31.92           C  
ATOM   1594  C   PHE B  21      14.681  96.343   6.636  1.00 31.72           C  
ATOM   1595  O   PHE B  21      14.911  97.016   7.630  1.00 33.48           O  
ATOM   1596  CB  PHE B  21      16.830  95.122   6.143  1.00 28.68           C  
ATOM   1597  CG  PHE B  21      16.349  93.767   6.391  1.00 25.95           C  
ATOM   1598  CD1 PHE B  21      15.718  93.073   5.406  1.00 25.38           C  
ATOM   1599  CD2 PHE B  21      16.479  93.187   7.662  1.00 25.32           C  
ATOM   1600  CE1 PHE B  21      15.200  91.784   5.688  1.00 26.32           C  
ATOM   1601  CE2 PHE B  21      15.974  91.908   7.976  1.00 23.69           C  
ATOM   1602  CZ  PHE B  21      15.333  91.204   6.993  1.00 24.80           C  
ATOM   1603  N   ASP B  22      13.498  95.797   6.404  1.00 30.73           N  
ATOM   1604  CA  ASP B  22      12.382  96.080   7.312  1.00 30.40           C  
ATOM   1605  C   ASP B  22      11.988  94.900   8.162  1.00 29.36           C  
ATOM   1606  O   ASP B  22      11.101  94.110   7.765  1.00 28.90           O  
ATOM   1607  CB  ASP B  22      11.153  96.550   6.516  1.00 30.93           C  
ATOM   1608  CG  ASP B  22      10.184  97.342   7.356  1.00 30.78           C  
ATOM   1609  OD1 ASP B  22       9.969  96.914   8.525  1.00 30.85           O  
ATOM   1610  OD2 ASP B  22       9.654  98.361   6.838  1.00 29.20           O  
ATOM   1611  N   LEU B  23      12.569  94.804   9.360  1.00 27.81           N  
ATOM   1612  CA  LEU B  23      12.259  93.603  10.102  1.00 26.58           C  
ATOM   1613  C   LEU B  23      10.840  93.209  10.118  1.00 26.55           C  
ATOM   1614  O   LEU B  23      10.529  92.039   9.892  1.00 25.45           O  
ATOM   1615  CB  LEU B  23      12.768  93.634  11.514  1.00 24.83           C  
ATOM   1616  CG  LEU B  23      14.219  93.341  11.330  1.00 23.06           C  
ATOM   1617  CD1 LEU B  23      14.796  94.681  10.811  1.00 23.45           C  
ATOM   1618  CD2 LEU B  23      14.856  92.833  12.586  1.00 21.69           C  
ATOM   1619  N   ARG B  24       9.998  94.209  10.343  1.00 26.72           N  
ATOM   1620  CA  ARG B  24       8.581  94.007  10.461  1.00 26.65           C  
ATOM   1621  C   ARG B  24       7.907  93.419   9.262  1.00 25.52           C  
ATOM   1622  O   ARG B  24       6.951  92.657   9.407  1.00 25.72           O  
ATOM   1623  CB  ARG B  24       7.931  95.290  10.824  1.00 28.66           C  
ATOM   1624  CG  ARG B  24       6.479  95.174  10.728  1.00 32.41           C  
ATOM   1625  CD  ARG B  24       5.804  96.331  11.396  1.00 34.84           C  
ATOM   1626  NE  ARG B  24       5.332  95.840  12.674  1.00 35.88           N  
ATOM   1627  CZ  ARG B  24       5.609  96.460  13.804  1.00 35.50           C  
ATOM   1628  NH1 ARG B  24       6.349  97.583  13.790  1.00 33.46           N  
ATOM   1629  NH2 ARG B  24       5.131  95.939  14.923  1.00 35.95           N  
ATOM   1630  N   ARG B  25       8.380  93.769   8.083  1.00 23.74           N  
ATOM   1631  CA  ARG B  25       7.811  93.170   6.920  1.00 23.73           C  
ATOM   1632  C   ARG B  25       8.404  91.763   6.792  1.00 23.65           C  
ATOM   1633  O   ARG B  25       7.835  90.891   6.172  1.00 25.28           O  
ATOM   1634  CB  ARG B  25       8.165  93.959   5.660  1.00 25.04           C  
ATOM   1635  CG  ARG B  25       7.344  95.197   5.411  1.00 26.23           C  
ATOM   1636  CD  ARG B  25       7.560  95.883   4.109  1.00 26.20           C  
ATOM   1637  NE  ARG B  25       7.073  95.142   2.960  1.00 27.50           N  
ATOM   1638  CZ  ARG B  25       7.649  95.314   1.780  1.00 29.39           C  
ATOM   1639  NH1 ARG B  25       8.658  96.178   1.714  1.00 31.20           N  
ATOM   1640  NH2 ARG B  25       7.285  94.636   0.694  1.00 30.66           N  
ATOM   1641  N   TYR B  26       9.556  91.500   7.370  1.00 22.17           N  
ATOM   1642  CA  TYR B  26      10.110  90.163   7.184  1.00 20.45           C  
ATOM   1643  C   TYR B  26       9.486  89.107   8.038  1.00 19.58           C  
ATOM   1644  O   TYR B  26       9.827  87.980   7.892  1.00 17.86           O  
ATOM   1645  CB  TYR B  26      11.602  90.185   7.495  1.00 19.94           C  
ATOM   1646  CG  TYR B  26      12.445  89.014   7.028  1.00 18.59           C  
ATOM   1647  CD1 TYR B  26      12.797  88.849   5.695  1.00 17.52           C  
ATOM   1648  CD2 TYR B  26      12.970  88.111   7.958  1.00 19.03           C  
ATOM   1649  CE1 TYR B  26      13.671  87.815   5.305  1.00 17.06           C  
ATOM   1650  CE2 TYR B  26      13.845  87.060   7.568  1.00 18.22           C  
ATOM   1651  CZ  TYR B  26      14.196  86.939   6.258  1.00 17.51           C  
ATOM   1652  OH  TYR B  26      15.166  86.037   5.965  1.00 16.80           O  
ATOM   1653  N   ALA B  27       8.563  89.451   8.925  1.00 20.56           N  
ATOM   1654  CA  ALA B  27       8.015  88.456   9.866  1.00 20.95           C  
ATOM   1655  C   ALA B  27       7.091  87.477   9.301  1.00 21.82           C  
ATOM   1656  O   ALA B  27       6.603  87.605   8.172  1.00 23.44           O  
ATOM   1657  CB  ALA B  27       7.338  89.110  10.955  1.00 20.50           C  
ATOM   1658  N   GLY B  28       6.798  86.475  10.080  1.00 21.09           N  
ATOM   1659  CA  GLY B  28       5.886  85.535   9.488  1.00 23.18           C  
ATOM   1660  C   GLY B  28       6.389  84.121   9.299  1.00 23.22           C  
ATOM   1661  O   GLY B  28       7.271  83.679  10.043  1.00 23.64           O  
ATOM   1662  N   ARG B  29       5.789  83.398   8.353  1.00 22.88           N  
ATOM   1663  CA  ARG B  29       6.183  82.015   8.107  1.00 22.32           C  
ATOM   1664  C   ARG B  29       6.986  82.091   6.877  1.00 21.57           C  
ATOM   1665  O   ARG B  29       6.603  82.817   5.938  1.00 22.13           O  
ATOM   1666  CB  ARG B  29       4.965  81.112   7.839  1.00 23.01           C  
ATOM   1667  CG  ARG B  29       5.124  80.016   6.765  1.00 23.21           C  
ATOM   1668  CD  ARG B  29       4.714  78.698   7.343  1.00 23.77           C  
ATOM   1669  NE  ARG B  29       5.197  78.662   8.713  1.00 27.11           N  
ATOM   1670  CZ  ARG B  29       4.496  78.238   9.759  1.00 28.33           C  
ATOM   1671  NH1 ARG B  29       3.278  77.784   9.591  1.00 28.68           N  
ATOM   1672  NH2 ARG B  29       4.969  78.351  10.991  1.00 29.89           N  
ATOM   1673  N   TRP B  30       8.078  81.344   6.887  1.00 19.52           N  
ATOM   1674  CA  TRP B  30       8.943  81.275   5.757  1.00 19.32           C  
ATOM   1675  C   TRP B  30       9.246  79.829   5.673  1.00 19.62           C  
ATOM   1676  O   TRP B  30       9.453  79.281   6.741  1.00 21.35           O  
ATOM   1677  CB  TRP B  30      10.220  81.982   6.048  1.00 18.88           C  
ATOM   1678  CG  TRP B  30      10.210  83.462   5.855  1.00 19.36           C  
ATOM   1679  CD1 TRP B  30      10.343  84.386   6.816  1.00 20.62           C  
ATOM   1680  CD2 TRP B  30      10.240  84.174   4.628  1.00 17.42           C  
ATOM   1681  NE1 TRP B  30      10.470  85.634   6.265  1.00 20.32           N  
ATOM   1682  CE2 TRP B  30      10.393  85.516   4.923  1.00 16.94           C  
ATOM   1683  CE3 TRP B  30      10.158  83.801   3.326  1.00 18.37           C  
ATOM   1684  CZ2 TRP B  30      10.452  86.452   4.004  1.00 17.30           C  
ATOM   1685  CZ3 TRP B  30      10.221  84.735   2.404  1.00 19.83           C  
ATOM   1686  CH2 TRP B  30      10.358  86.060   2.737  1.00 19.37           C  
ATOM   1687  N   TYR B  31       9.244  79.187   4.476  1.00 19.31           N  
ATOM   1688  CA  TYR B  31       9.622  77.746   4.353  1.00 18.94           C  
ATOM   1689  C   TYR B  31      10.998  77.682   3.779  1.00 20.19           C  
ATOM   1690  O   TYR B  31      11.355  78.542   2.983  1.00 21.78           O  
ATOM   1691  CB  TYR B  31       8.758  77.001   3.411  1.00 17.31           C  
ATOM   1692  CG  TYR B  31       7.300  77.073   3.741  1.00 18.92           C  
ATOM   1693  CD1 TYR B  31       6.500  78.074   3.205  1.00 18.35           C  
ATOM   1694  CD2 TYR B  31       6.688  76.102   4.585  1.00 19.25           C  
ATOM   1695  CE1 TYR B  31       5.121  78.111   3.494  1.00 20.83           C  
ATOM   1696  CE2 TYR B  31       5.309  76.124   4.890  1.00 19.67           C  
ATOM   1697  CZ  TYR B  31       4.516  77.134   4.344  1.00 21.76           C  
ATOM   1698  OH  TYR B  31       3.132  77.214   4.621  1.00 23.48           O  
ATOM   1699  N   GLN B  32      11.809  76.721   4.193  1.00 21.08           N  
ATOM   1700  CA  GLN B  32      13.158  76.600   3.628  1.00 21.72           C  
ATOM   1701  C   GLN B  32      12.967  75.695   2.381  1.00 23.12           C  
ATOM   1702  O   GLN B  32      12.456  74.584   2.485  1.00 23.77           O  
ATOM   1703  CB  GLN B  32      14.107  75.980   4.660  1.00 19.81           C  
ATOM   1704  CG  GLN B  32      14.816  77.019   5.522  1.00 21.06           C  
ATOM   1705  CD  GLN B  32      15.733  76.424   6.617  1.00 21.71           C  
ATOM   1706  OE1 GLN B  32      16.414  75.416   6.412  1.00 21.16           O  
ATOM   1707  NE2 GLN B  32      15.745  77.068   7.787  1.00 21.28           N  
ATOM   1708  N   THR B  33      13.318  76.145   1.187  1.00 23.53           N  
ATOM   1709  CA  THR B  33      13.052  75.252   0.100  1.00 24.37           C  
ATOM   1710  C   THR B  33      14.298  74.736  -0.538  1.00 26.63           C  
ATOM   1711  O   THR B  33      14.243  73.719  -1.203  1.00 27.72           O  
ATOM   1712  CB  THR B  33      12.197  75.880  -0.949  1.00 23.73           C  
ATOM   1713  OG1 THR B  33      12.939  76.911  -1.628  1.00 24.00           O  
ATOM   1714  CG2 THR B  33      10.970  76.376  -0.342  1.00 20.79           C  
ATOM   1715  N   HIS B  34      15.417  75.448  -0.405  1.00 28.42           N  
ATOM   1716  CA  HIS B  34      16.734  74.951  -0.901  1.00 28.69           C  
ATOM   1717  C   HIS B  34      17.773  75.403   0.092  1.00 27.94           C  
ATOM   1718  O   HIS B  34      17.819  76.585   0.477  1.00 28.33           O  
ATOM   1719  CB  HIS B  34      17.077  75.522  -2.256  1.00 30.99           C  
ATOM   1720  CG  HIS B  34      16.178  75.043  -3.340  1.00 32.81           C  
ATOM   1721  ND1 HIS B  34      16.592  74.152  -4.314  1.00 34.15           N  
ATOM   1722  CD2 HIS B  34      14.861  75.243  -3.539  1.00 32.66           C  
ATOM   1723  CE1 HIS B  34      15.563  73.815  -5.058  1.00 34.88           C  
ATOM   1724  NE2 HIS B  34      14.500  74.463  -4.606  1.00 34.86           N  
ATOM   1725  N   ILE B  35      18.595  74.498   0.550  1.00 26.08           N  
ATOM   1726  CA  ILE B  35      19.555  74.960   1.517  1.00 26.16           C  
ATOM   1727  C   ILE B  35      20.918  74.383   1.199  1.00 27.62           C  
ATOM   1728  O   ILE B  35      21.013  73.414   0.478  1.00 28.60           O  
ATOM   1729  CB  ILE B  35      19.176  74.490   2.919  1.00 23.97           C  
ATOM   1730  CG1 ILE B  35      19.594  73.043   3.076  1.00 22.23           C  
ATOM   1731  CG2 ILE B  35      17.731  74.555   3.140  1.00 21.65           C  
ATOM   1732  CD1 ILE B  35      19.193  72.468   4.295  1.00 20.41           C  
ATOM   1733  N   ILE B  36      21.987  74.985   1.687  1.00 28.80           N  
ATOM   1734  CA  ILE B  36      23.290  74.356   1.504  1.00 30.33           C  
ATOM   1735  C   ILE B  36      23.340  73.447   2.743  1.00 32.44           C  
ATOM   1736  O   ILE B  36      23.249  73.960   3.839  1.00 31.89           O  
ATOM   1737  CB  ILE B  36      24.362  75.336   1.600  1.00 28.06           C  
ATOM   1738  CG1 ILE B  36      24.467  76.096   0.299  1.00 26.90           C  
ATOM   1739  CG2 ILE B  36      25.558  74.641   1.980  1.00 27.26           C  
ATOM   1740  CD1 ILE B  36      25.698  76.936   0.173  1.00 26.09           C  
ATOM   1741  N   GLU B  37      23.505  72.126   2.606  1.00 35.57           N  
ATOM   1742  CA  GLU B  37      23.388  71.297   3.815  1.00 37.90           C  
ATOM   1743  C   GLU B  37      24.199  71.799   4.891  1.00 36.73           C  
ATOM   1744  O   GLU B  37      25.414  71.895   4.778  1.00 36.31           O  
ATOM   1745  CB  GLU B  37      23.705  69.837   3.632  1.00 42.36           C  
ATOM   1746  CG  GLU B  37      24.374  69.441   2.336  1.00 51.85           C  
ATOM   1747  CD  GLU B  37      24.547  67.902   2.299  1.00 57.02           C  
ATOM   1748  OE1 GLU B  37      25.078  67.412   3.382  1.00 59.28           O  
ATOM   1749  OE2 GLU B  37      24.163  67.237   1.245  1.00 58.24           O  
ATOM   1750  N   ASN B  38      23.483  72.047   5.970  1.00 35.79           N  
ATOM   1751  CA  ASN B  38      24.010  72.645   7.162  1.00 35.27           C  
ATOM   1752  C   ASN B  38      23.906  71.753   8.415  1.00 36.01           C  
ATOM   1753  O   ASN B  38      22.816  71.381   8.884  1.00 36.95           O  
ATOM   1754  CB  ASN B  38      23.260  73.942   7.244  1.00 35.30           C  
ATOM   1755  CG  ASN B  38      23.237  74.524   8.561  1.00 35.79           C  
ATOM   1756  OD1 ASN B  38      22.898  75.709   8.698  1.00 37.33           O  
ATOM   1757  ND2 ASN B  38      23.560  73.741   9.568  1.00 35.36           N  
ATOM   1758  N   ALA B  39      25.074  71.400   8.955  1.00 35.79           N  
ATOM   1759  CA  ALA B  39      25.171  70.510  10.103  1.00 33.89           C  
ATOM   1760  C   ALA B  39      24.528  70.882  11.397  1.00 32.42           C  
ATOM   1761  O   ALA B  39      24.144  69.996  12.133  1.00 32.74           O  
ATOM   1762  CB  ALA B  39      26.557  70.214  10.342  1.00 34.38           C  
ATOM   1763  N   TYR B  40      24.429  72.164  11.696  1.00 31.04           N  
ATOM   1764  CA  TYR B  40      23.810  72.568  12.920  1.00 30.79           C  
ATOM   1765  C   TYR B  40      22.310  72.496  12.870  1.00 32.26           C  
ATOM   1766  O   TYR B  40      21.649  72.807  13.882  1.00 32.35           O  
ATOM   1767  CB  TYR B  40      24.184  73.959  13.274  1.00 29.49           C  
ATOM   1768  CG  TYR B  40      25.628  74.160  13.422  1.00 30.65           C  
ATOM   1769  CD1 TYR B  40      26.404  74.542  12.363  1.00 33.36           C  
ATOM   1770  CD2 TYR B  40      26.246  73.937  14.610  1.00 31.52           C  
ATOM   1771  CE1 TYR B  40      27.801  74.693  12.509  1.00 34.38           C  
ATOM   1772  CE2 TYR B  40      27.623  74.082  14.769  1.00 32.76           C  
ATOM   1773  CZ  TYR B  40      28.382  74.461  13.723  1.00 33.55           C  
ATOM   1774  OH  TYR B  40      29.710  74.649  13.903  1.00 35.03           O  
ATOM   1775  N   GLN B  41      21.752  72.096  11.712  1.00 34.42           N  
ATOM   1776  CA  GLN B  41      20.259  71.970  11.526  1.00 35.79           C  
ATOM   1777  C   GLN B  41      19.804  70.521  11.454  1.00 36.70           C  
ATOM   1778  O   GLN B  41      19.978  69.870  10.411  1.00 37.93           O  
ATOM   1779  CB  GLN B  41      19.732  72.689  10.258  1.00 34.69           C  
ATOM   1780  CG  GLN B  41      18.241  72.974  10.375  1.00 34.08           C  
ATOM   1781  CD  GLN B  41      17.690  73.945   9.341  1.00 33.73           C  
ATOM   1782  OE1 GLN B  41      17.061  74.958   9.707  1.00 32.36           O  
ATOM   1783  NE2 GLN B  41      17.895  73.635   8.054  1.00 30.84           N  
ATOM   1784  N   PRO B  42      19.230  69.997  12.560  1.00 36.85           N  
ATOM   1785  CA  PRO B  42      18.757  68.620  12.642  1.00 36.86           C  
ATOM   1786  C   PRO B  42      17.665  68.302  11.693  1.00 37.57           C  
ATOM   1787  O   PRO B  42      17.743  67.266  11.097  1.00 39.20           O  
ATOM   1788  CB  PRO B  42      18.292  68.484  14.061  1.00 36.41           C  
ATOM   1789  CG  PRO B  42      17.747  69.836  14.314  1.00 37.75           C  
ATOM   1790  CD  PRO B  42      18.847  70.728  13.771  1.00 37.45           C  
ATOM   1791  N   VAL B  43      16.661  69.167  11.535  1.00 37.65           N  
ATOM   1792  CA  VAL B  43      15.543  68.888  10.635  1.00 37.55           C  
ATOM   1793  C   VAL B  43      16.033  68.969   9.198  1.00 39.54           C  
ATOM   1794  O   VAL B  43      16.869  69.823   8.905  1.00 39.76           O  
ATOM   1795  CB  VAL B  43      14.435  69.903  10.807  1.00 35.66           C  
ATOM   1796  CG1 VAL B  43      14.013  69.982  12.215  1.00 35.65           C  
ATOM   1797  CG2 VAL B  43      14.904  71.199  10.383  1.00 35.17           C  
ATOM   1798  N   THR B  44      15.520  68.106   8.302  1.00 41.35           N  
ATOM   1799  CA  THR B  44      15.965  68.118   6.903  1.00 42.66           C  
ATOM   1800  C   THR B  44      14.893  68.099   5.878  1.00 43.25           C  
ATOM   1801  O   THR B  44      15.196  68.172   4.684  1.00 42.84           O  
ATOM   1802  CB  THR B  44      16.863  66.972   6.594  1.00 43.46           C  
ATOM   1803  OG1 THR B  44      16.109  65.770   6.349  1.00 45.04           O  
ATOM   1804  CG2 THR B  44      17.699  66.728   7.767  1.00 45.42           C  
ATOM   1805  N   ARG B  45      13.654  67.921   6.322  1.00 44.35           N  
ATOM   1806  CA  ARG B  45      12.541  68.008   5.383  1.00 46.28           C  
ATOM   1807  C   ARG B  45      11.280  68.645   6.046  1.00 45.18           C  
ATOM   1808  O   ARG B  45      11.103  68.565   7.259  1.00 45.69           O  
ATOM   1809  CB  ARG B  45      12.300  66.653   4.677  1.00 50.13           C  
ATOM   1810  CG  ARG B  45      11.755  65.519   5.516  1.00 55.38           C  
ATOM   1811  CD  ARG B  45      11.168  64.341   4.706  1.00 59.27           C  
ATOM   1812  NE  ARG B  45      10.329  63.606   5.660  1.00 64.05           N  
ATOM   1813  CZ  ARG B  45       9.007  63.422   5.561  1.00 66.94           C  
ATOM   1814  NH1 ARG B  45       8.310  63.917   4.499  1.00 67.47           N  
ATOM   1815  NH2 ARG B  45       8.381  62.760   6.557  1.00 67.42           N  
ATOM   1816  N   CYS B  46      10.455  69.330   5.265  1.00 43.66           N  
ATOM   1817  CA  CYS B  46       9.290  70.052   5.793  1.00 43.60           C  
ATOM   1818  C   CYS B  46       9.717  71.210   6.632  1.00 40.55           C  
ATOM   1819  O   CYS B  46       8.947  71.777   7.397  1.00 40.59           O  
ATOM   1820  CB  CYS B  46       8.380  69.176   6.638  1.00 48.00           C  
ATOM   1821  SG  CYS B  46       7.566  67.933   5.591  1.00 56.36           S  
ATOM   1822  N   ILE B  47      10.970  71.565   6.473  1.00 37.39           N  
ATOM   1823  CA  ILE B  47      11.562  72.642   7.236  1.00 33.93           C  
ATOM   1824  C   ILE B  47      10.713  73.877   7.076  1.00 32.10           C  
ATOM   1825  O   ILE B  47      10.555  74.369   5.998  1.00 33.16           O  
ATOM   1826  CB  ILE B  47      13.054  72.889   6.748  1.00 33.44           C  
ATOM   1827  CG1 ILE B  47      13.889  71.611   6.916  1.00 32.17           C  
ATOM   1828  CG2 ILE B  47      13.708  74.013   7.497  1.00 32.23           C  
ATOM   1829  CD1 ILE B  47      15.348  71.852   7.016  1.00 31.73           C  
ATOM   1830  N   HIS B  48      10.116  74.362   8.136  1.00 29.85           N  
ATOM   1831  CA  HIS B  48       9.349  75.590   8.027  1.00 28.36           C  
ATOM   1832  C   HIS B  48       9.550  76.418   9.327  1.00 28.83           C  
ATOM   1833  O   HIS B  48       9.997  75.903  10.385  1.00 28.94           O  
ATOM   1834  CB  HIS B  48       7.907  75.252   7.887  1.00 26.20           C  
ATOM   1835  CG  HIS B  48       7.364  74.597   9.097  1.00 24.99           C  
ATOM   1836  ND1 HIS B  48       7.763  73.345   9.489  1.00 24.80           N  
ATOM   1837  CD2 HIS B  48       6.557  75.062  10.079  1.00 25.32           C  
ATOM   1838  CE1 HIS B  48       7.231  73.063  10.668  1.00 25.75           C  
ATOM   1839  NE2 HIS B  48       6.494  74.089  11.050  1.00 26.03           N  
ATOM   1840  N   SER B  49       9.251  77.705   9.291  1.00 27.96           N  
ATOM   1841  CA  SER B  49       9.435  78.443  10.524  1.00 26.93           C  
ATOM   1842  C   SER B  49       8.638  79.701  10.644  1.00 26.71           C  
ATOM   1843  O   SER B  49       7.925  80.109   9.728  1.00 26.52           O  
ATOM   1844  CB  SER B  49      10.891  78.736  10.743  1.00 25.61           C  
ATOM   1845  OG  SER B  49      11.411  79.245   9.564  1.00 24.01           O  
ATOM   1846  N   ASN B  50       8.723  80.290  11.818  1.00 26.67           N  
ATOM   1847  CA  ASN B  50       7.993  81.501  12.057  1.00 27.43           C  
ATOM   1848  C   ASN B  50       8.903  82.512  12.704  1.00 26.90           C  
ATOM   1849  O   ASN B  50       9.538  82.235  13.724  1.00 27.23           O  
ATOM   1850  CB  ASN B  50       6.782  81.245  12.947  1.00 28.81           C  
ATOM   1851  CG  ASN B  50       6.118  82.518  13.348  1.00 29.14           C  
ATOM   1852  OD1 ASN B  50       5.525  83.175  12.533  1.00 31.40           O  
ATOM   1853  ND2 ASN B  50       6.241  82.893  14.589  1.00 28.94           N  
ATOM   1854  N   TYR B  51       8.989  83.668  12.076  1.00 26.02           N  
ATOM   1855  CA  TYR B  51       9.827  84.700  12.574  1.00 27.43           C  
ATOM   1856  C   TYR B  51       8.892  85.705  13.221  1.00 30.62           C  
ATOM   1857  O   TYR B  51       8.230  86.471  12.502  1.00 32.11           O  
ATOM   1858  CB  TYR B  51      10.597  85.384  11.441  1.00 23.47           C  
ATOM   1859  CG  TYR B  51      11.770  84.656  10.852  1.00 19.70           C  
ATOM   1860  CD1 TYR B  51      11.606  83.473  10.226  1.00 19.51           C  
ATOM   1861  CD2 TYR B  51      13.034  85.194  10.866  1.00 18.74           C  
ATOM   1862  CE1 TYR B  51      12.670  82.815   9.629  1.00 18.96           C  
ATOM   1863  CE2 TYR B  51      14.113  84.553  10.256  1.00 17.52           C  
ATOM   1864  CZ  TYR B  51      13.935  83.344   9.645  1.00 17.77           C  
ATOM   1865  OH  TYR B  51      14.981  82.558   9.157  1.00 14.15           O  
ATOM   1866  N   GLU B  52       8.852  85.707  14.556  1.00 33.14           N  
ATOM   1867  CA  GLU B  52       8.030  86.616  15.339  1.00 36.85           C  
ATOM   1868  C   GLU B  52       8.738  87.925  15.604  1.00 37.20           C  
ATOM   1869  O   GLU B  52       9.752  87.938  16.270  1.00 37.98           O  
ATOM   1870  CB  GLU B  52       7.730  85.975  16.664  1.00 40.83           C  
ATOM   1871  CG  GLU B  52       6.992  86.841  17.675  1.00 47.75           C  
ATOM   1872  CD  GLU B  52       6.232  85.947  18.658  1.00 52.63           C  
ATOM   1873  OE1 GLU B  52       6.404  86.046  19.952  1.00 54.38           O  
ATOM   1874  OE2 GLU B  52       5.453  85.114  18.072  1.00 55.13           O  
ATOM   1875  N   TYR B  53       8.196  89.043  15.155  1.00 37.58           N  
ATOM   1876  CA  TYR B  53       8.909  90.268  15.388  1.00 38.86           C  
ATOM   1877  C   TYR B  53       8.630  90.967  16.661  1.00 42.85           C  
ATOM   1878  O   TYR B  53       7.497  91.329  16.921  1.00 44.70           O  
ATOM   1879  CB  TYR B  53       8.620  91.261  14.321  1.00 35.29           C  
ATOM   1880  CG  TYR B  53       9.288  92.573  14.523  1.00 32.14           C  
ATOM   1881  CD1 TYR B  53      10.624  92.715  14.377  1.00 33.30           C  
ATOM   1882  CD2 TYR B  53       8.577  93.677  14.729  1.00 31.97           C  
ATOM   1883  CE1 TYR B  53      11.224  93.948  14.407  1.00 32.72           C  
ATOM   1884  CE2 TYR B  53       9.148  94.889  14.758  1.00 32.76           C  
ATOM   1885  CZ  TYR B  53      10.465  95.022  14.577  1.00 32.81           C  
ATOM   1886  OH  TYR B  53      10.968  96.258  14.384  1.00 34.32           O  
ATOM   1887  N   SER B  54       9.667  91.186  17.459  1.00 47.10           N  
ATOM   1888  CA  SER B  54       9.540  91.948  18.701  1.00 50.78           C  
ATOM   1889  C   SER B  54       9.968  93.377  18.371  1.00 52.32           C  
ATOM   1890  O   SER B  54      10.664  93.595  17.380  1.00 53.13           O  
ATOM   1891  CB  SER B  54      10.453  91.389  19.790  1.00 51.97           C  
ATOM   1892  OG  SER B  54      10.633  92.407  20.769  1.00 54.45           O  
ATOM   1893  N   THR B  55       9.573  94.380  19.136  1.00 54.29           N  
ATOM   1894  CA  THR B  55      10.077  95.661  18.686  1.00 56.85           C  
ATOM   1895  C   THR B  55      10.802  96.479  19.745  1.00 58.60           C  
ATOM   1896  O   THR B  55      11.305  97.556  19.474  1.00 59.50           O  
ATOM   1897  CB  THR B  55       8.978  96.467  18.010  1.00 56.79           C  
ATOM   1898  OG1 THR B  55       9.560  97.514  17.209  1.00 55.36           O  
ATOM   1899  CG2 THR B  55       8.033  97.004  19.062  1.00 57.47           C  
ATOM   1900  N   ASN B  56      10.915  95.931  20.941  1.00 60.31           N  
ATOM   1901  CA  ASN B  56      11.608  96.608  22.030  1.00 61.44           C  
ATOM   1902  C   ASN B  56      12.951  95.952  22.023  1.00 60.02           C  
ATOM   1903  O   ASN B  56      13.923  96.417  22.649  1.00 60.89           O  
ATOM   1904  CB  ASN B  56      10.842  96.329  23.312  1.00 65.18           C  
ATOM   1905  CG  ASN B  56       9.372  96.731  23.169  1.00 68.99           C  
ATOM   1906  OD1 ASN B  56       9.020  97.919  23.413  1.00 70.71           O  
ATOM   1907  ND2 ASN B  56       8.499  95.763  22.703  1.00 70.26           N  
ATOM   1908  N   ASP B  57      12.965  94.843  21.295  1.00 57.71           N  
ATOM   1909  CA  ASP B  57      14.156  94.047  21.090  1.00 55.56           C  
ATOM   1910  C   ASP B  57      14.695  94.362  19.688  1.00 52.35           C  
ATOM   1911  O   ASP B  57      15.914  94.390  19.490  1.00 52.22           O  
ATOM   1912  CB  ASP B  57      13.837  92.549  21.234  1.00 57.98           C  
ATOM   1913  CG  ASP B  57      13.274  92.189  22.630  1.00 60.10           C  
ATOM   1914  OD1 ASP B  57      13.633  92.880  23.640  1.00 61.66           O  
ATOM   1915  OD2 ASP B  57      12.483  91.197  22.710  1.00 61.01           O  
ATOM   1916  N   TYR B  58      13.780  94.623  18.745  1.00 48.31           N  
ATOM   1917  CA  TYR B  58      14.120  94.962  17.371  1.00 43.92           C  
ATOM   1918  C   TYR B  58      14.896  93.771  16.901  1.00 42.57           C  
ATOM   1919  O   TYR B  58      16.086  93.854  16.588  1.00 42.64           O  
ATOM   1920  CB  TYR B  58      14.982  96.219  17.341  1.00 41.71           C  
ATOM   1921  CG  TYR B  58      15.464  96.643  15.983  1.00 40.01           C  
ATOM   1922  CD1 TYR B  58      14.638  96.569  14.887  1.00 40.02           C  
ATOM   1923  CD2 TYR B  58      16.725  97.162  15.800  1.00 39.55           C  
ATOM   1924  CE1 TYR B  58      15.048  97.013  13.612  1.00 39.38           C  
ATOM   1925  CE2 TYR B  58      17.157  97.599  14.536  1.00 39.42           C  
ATOM   1926  CZ  TYR B  58      16.300  97.528  13.436  1.00 39.42           C  
ATOM   1927  OH  TYR B  58      16.649  98.034  12.180  1.00 39.50           O  
ATOM   1928  N   GLY B  59      14.218  92.636  16.892  1.00 40.28           N  
ATOM   1929  CA  GLY B  59      14.855  91.411  16.471  1.00 38.33           C  
ATOM   1930  C   GLY B  59      13.726  90.421  16.303  1.00 37.13           C  
ATOM   1931  O   GLY B  59      12.594  90.791  16.475  1.00 37.35           O  
ATOM   1932  N   PHE B  60      14.016  89.173  15.970  1.00 35.23           N  
ATOM   1933  CA  PHE B  60      12.990  88.194  15.782  1.00 33.04           C  
ATOM   1934  C   PHE B  60      13.212  87.128  16.831  1.00 34.27           C  
ATOM   1935  O   PHE B  60      14.327  86.976  17.286  1.00 35.21           O  
ATOM   1936  CB  PHE B  60      13.159  87.558  14.435  1.00 29.91           C  
ATOM   1937  CG  PHE B  60      12.957  88.471  13.302  1.00 27.40           C  
ATOM   1938  CD1 PHE B  60      14.022  89.098  12.702  1.00 26.99           C  
ATOM   1939  CD2 PHE B  60      11.719  88.706  12.818  1.00 26.00           C  
ATOM   1940  CE1 PHE B  60      13.846  89.947  11.646  1.00 25.66           C  
ATOM   1941  CE2 PHE B  60      11.549  89.557  11.749  1.00 25.80           C  
ATOM   1942  CZ  PHE B  60      12.606  90.173  11.173  1.00 25.50           C  
ATOM   1943  N   LYS B  61      12.144  86.414  17.207  1.00 35.21           N  
ATOM   1944  CA  LYS B  61      12.140  85.283  18.142  1.00 35.68           C  
ATOM   1945  C   LYS B  61      11.680  84.208  17.123  1.00 34.23           C  
ATOM   1946  O   LYS B  61      10.495  84.011  16.851  1.00 34.64           O  
ATOM   1947  CB  LYS B  61      11.091  85.551  19.235  1.00 39.77           C  
ATOM   1948  CG  LYS B  61      11.517  85.238  20.727  1.00 45.14           C  
ATOM   1949  CD  LYS B  61      10.681  86.057  21.878  1.00 48.16           C  
ATOM   1950  CE  LYS B  61      11.553  86.270  23.221  1.00 50.98           C  
ATOM   1951  NZ  LYS B  61      11.004  86.981  24.513  1.00 52.43           N  
ATOM   1952  N   VAL B  62      12.641  83.546  16.511  1.00 31.72           N  
ATOM   1953  CA  VAL B  62      12.354  82.585  15.462  1.00 29.54           C  
ATOM   1954  C   VAL B  62      12.133  81.217  15.977  1.00 28.32           C  
ATOM   1955  O   VAL B  62      12.880  80.816  16.828  1.00 28.61           O  
ATOM   1956  CB  VAL B  62      13.566  82.461  14.489  1.00 29.88           C  
ATOM   1957  CG1 VAL B  62      13.327  81.386  13.494  1.00 30.11           C  
ATOM   1958  CG2 VAL B  62      13.805  83.737  13.745  1.00 29.87           C  
ATOM   1959  N   THR B  63      11.149  80.485  15.454  1.00 27.36           N  
ATOM   1960  CA  THR B  63      10.958  79.066  15.837  1.00 27.04           C  
ATOM   1961  C   THR B  63      11.016  78.242  14.571  1.00 25.99           C  
ATOM   1962  O   THR B  63      10.334  78.588  13.627  1.00 25.86           O  
ATOM   1963  CB  THR B  63       9.610  78.778  16.313  1.00 28.42           C  
ATOM   1964  OG1 THR B  63       9.280  79.654  17.381  1.00 31.00           O  
ATOM   1965  CG2 THR B  63       9.539  77.364  16.745  1.00 29.09           C  
ATOM   1966  N   THR B  64      11.784  77.168  14.511  1.00 25.22           N  
ATOM   1967  CA  THR B  64      11.806  76.398  13.253  1.00 26.33           C  
ATOM   1968  C   THR B  64      11.438  74.954  13.560  1.00 28.31           C  
ATOM   1969  O   THR B  64      11.717  74.471  14.643  1.00 28.45           O  
ATOM   1970  CB  THR B  64      13.172  76.358  12.562  1.00 24.84           C  
ATOM   1971  OG1 THR B  64      13.374  77.505  11.750  1.00 22.35           O  
ATOM   1972  CG2 THR B  64      13.246  75.171  11.696  1.00 23.87           C  
ATOM   1973  N   ALA B  65      10.853  74.253  12.594  1.00 29.62           N  
ATOM   1974  CA  ALA B  65      10.398  72.907  12.851  1.00 30.68           C  
ATOM   1975  C   ALA B  65      10.278  72.126  11.617  1.00 31.96           C  
ATOM   1976  O   ALA B  65      10.112  72.686  10.564  1.00 33.00           O  
ATOM   1977  CB  ALA B  65       9.096  72.960  13.462  1.00 29.93           C  
ATOM   1978  N   GLY B  66      10.301  70.815  11.760  1.00 33.61           N  
ATOM   1979  CA  GLY B  66      10.203  69.940  10.607  1.00 36.23           C  
ATOM   1980  C   GLY B  66      10.615  68.545  11.015  1.00 38.52           C  
ATOM   1981  O   GLY B  66      10.619  68.197  12.196  1.00 38.55           O  
ATOM   1982  N   PHE B  67      11.002  67.746  10.048  1.00 40.74           N  
ATOM   1983  CA  PHE B  67      11.388  66.408  10.363  1.00 44.08           C  
ATOM   1984  C   PHE B  67      12.871  66.117  10.223  1.00 47.08           C  
ATOM   1985  O   PHE B  67      13.607  66.727   9.428  1.00 46.34           O  
ATOM   1986  CB  PHE B  67      10.667  65.422   9.448  1.00 45.23           C  
ATOM   1987  CG  PHE B  67       9.202  65.261   9.699  1.00 45.27           C  
ATOM   1988  CD1 PHE B  67       8.327  65.206   8.629  1.00 46.57           C  
ATOM   1989  CD2 PHE B  67       8.704  65.109  10.967  1.00 44.79           C  
ATOM   1990  CE1 PHE B  67       6.978  65.002   8.843  1.00 47.46           C  
ATOM   1991  CE2 PHE B  67       7.377  64.908  11.179  1.00 44.88           C  
ATOM   1992  CZ  PHE B  67       6.508  64.853  10.129  1.00 46.58           C  
ATOM   1993  N   ASN B  68      13.237  65.089  10.978  1.00 51.13           N  
ATOM   1994  CA  ASN B  68      14.544  64.487  11.062  1.00 55.56           C  
ATOM   1995  C   ASN B  68      14.822  63.788   9.756  1.00 58.81           C  
ATOM   1996  O   ASN B  68      13.945  63.679   8.920  1.00 59.48           O  
ATOM   1997  CB  ASN B  68      14.466  63.420  12.104  1.00 56.75           C  
ATOM   1998  CG  ASN B  68      15.352  63.697  13.241  1.00 59.67           C  
ATOM   1999  OD1 ASN B  68      16.443  64.234  13.053  1.00 61.14           O  
ATOM   2000  ND2 ASN B  68      14.920  63.327  14.451  1.00 60.65           N  
ATOM   2001  N   PRO B  69      16.040  63.274   9.555  1.00 61.86           N  
ATOM   2002  CA  PRO B  69      16.333  62.565   8.291  1.00 64.47           C  
ATOM   2003  C   PRO B  69      15.844  61.122   8.539  1.00 66.44           C  
ATOM   2004  O   PRO B  69      15.627  60.323   7.626  1.00 66.51           O  
ATOM   2005  CB  PRO B  69      17.840  62.717   8.155  1.00 64.24           C  
ATOM   2006  CG  PRO B  69      18.298  62.648   9.612  1.00 64.25           C  
ATOM   2007  CD  PRO B  69      17.238  63.409  10.395  1.00 62.94           C  
ATOM   2008  N   ASN B  70      15.687  60.851   9.837  1.00 69.27           N  
ATOM   2009  CA  ASN B  70      15.106  59.630  10.420  1.00 71.65           C  
ATOM   2010  C   ASN B  70      13.693  60.273  10.577  1.00 71.59           C  
ATOM   2011  O   ASN B  70      13.492  61.346   9.999  1.00 72.67           O  
ATOM   2012  CB  ASN B  70      15.738  59.339  11.795  1.00 74.00           C  
ATOM   2013  CG  ASN B  70      15.171  58.087  12.449  1.00 75.87           C  
ATOM   2014  OD1 ASN B  70      15.524  56.958  12.055  1.00 77.07           O  
ATOM   2015  ND2 ASN B  70      14.279  58.274  13.449  1.00 76.53           N  
ATOM   2016  N   ASP B  71      12.722  59.771  11.338  1.00 70.19           N  
ATOM   2017  CA  ASP B  71      11.494  60.543  11.212  1.00 68.87           C  
ATOM   2018  C   ASP B  71      10.841  61.318  12.333  1.00 67.62           C  
ATOM   2019  O   ASP B  71       9.639  61.601  12.275  1.00 67.14           O  
ATOM   2020  CB  ASP B  71      10.449  59.702  10.464  1.00 69.97           C  
ATOM   2021  CG  ASP B  71      10.780  59.544   8.945  1.00 71.49           C  
ATOM   2022  OD1 ASP B  71      10.963  60.577   8.245  1.00 72.16           O  
ATOM   2023  OD2 ASP B  71      10.853  58.390   8.440  1.00 72.51           O  
ATOM   2024  N   GLU B  72      11.628  61.741  13.315  1.00 66.21           N  
ATOM   2025  CA  GLU B  72      11.055  62.510  14.431  1.00 64.72           C  
ATOM   2026  C   GLU B  72      10.792  63.936  13.990  1.00 60.95           C  
ATOM   2027  O   GLU B  72      11.425  64.404  13.049  1.00 60.43           O  
ATOM   2028  CB  GLU B  72      12.011  62.551  15.639  1.00 68.36           C  
ATOM   2029  CG  GLU B  72      13.043  61.410  15.687  1.00 74.07           C  
ATOM   2030  CD  GLU B  72      13.931  61.417  16.962  1.00 77.86           C  
ATOM   2031  OE1 GLU B  72      14.908  60.601  16.964  1.00 79.84           O  
ATOM   2032  OE2 GLU B  72      13.654  62.205  17.940  1.00 79.37           O  
ATOM   2033  N   TYR B  73       9.884  64.619  14.681  1.00 56.73           N  
ATOM   2034  CA  TYR B  73       9.552  66.011  14.385  1.00 53.48           C  
ATOM   2035  C   TYR B  73      10.208  66.909  15.387  1.00 52.64           C  
ATOM   2036  O   TYR B  73       9.762  66.947  16.527  1.00 52.81           O  
ATOM   2037  CB  TYR B  73       8.074  66.202  14.515  1.00 52.32           C  
ATOM   2038  CG  TYR B  73       7.543  67.610  14.357  1.00 50.81           C  
ATOM   2039  CD1 TYR B  73       7.198  68.121  13.121  1.00 49.95           C  
ATOM   2040  CD2 TYR B  73       7.300  68.387  15.460  1.00 50.99           C  
ATOM   2041  CE1 TYR B  73       6.632  69.348  13.010  1.00 49.51           C  
ATOM   2042  CE2 TYR B  73       6.738  69.618  15.353  1.00 50.22           C  
ATOM   2043  CZ  TYR B  73       6.419  70.086  14.136  1.00 49.94           C  
ATOM   2044  OH  TYR B  73       5.960  71.360  14.073  1.00 51.94           O  
ATOM   2045  N   LEU B  74      11.237  67.654  14.989  1.00 51.46           N  
ATOM   2046  CA  LEU B  74      11.939  68.504  15.939  1.00 49.90           C  
ATOM   2047  C   LEU B  74      11.524  69.927  15.852  1.00 48.95           C  
ATOM   2048  O   LEU B  74      11.038  70.349  14.838  1.00 48.85           O  
ATOM   2049  CB  LEU B  74      13.427  68.412  15.733  1.00 50.25           C  
ATOM   2050  CG  LEU B  74      14.007  67.052  16.098  1.00 50.52           C  
ATOM   2051  CD1 LEU B  74      13.733  66.211  14.938  1.00 51.20           C  
ATOM   2052  CD2 LEU B  74      15.578  67.057  16.373  1.00 53.05           C  
ATOM   2053  N   LYS B  75      11.734  70.658  16.928  1.00 48.45           N  
ATOM   2054  CA  LYS B  75      11.358  72.049  17.016  1.00 49.13           C  
ATOM   2055  C   LYS B  75      12.538  72.834  17.634  1.00 48.55           C  
ATOM   2056  O   LYS B  75      12.925  72.571  18.756  1.00 49.97           O  
ATOM   2057  CB  LYS B  75      10.103  72.111  17.880  1.00 51.65           C  
ATOM   2058  CG  LYS B  75       9.677  73.475  18.405  1.00 55.61           C  
ATOM   2059  CD  LYS B  75       8.386  73.341  19.297  1.00 58.84           C  
ATOM   2060  CE  LYS B  75       7.780  74.745  19.705  1.00 60.92           C  
ATOM   2061  NZ  LYS B  75       8.656  75.710  20.535  1.00 61.20           N  
ATOM   2062  N   ILE B  76      13.134  73.776  16.903  1.00 46.91           N  
ATOM   2063  CA  ILE B  76      14.274  74.527  17.405  1.00 44.35           C  
ATOM   2064  C   ILE B  76      13.774  75.843  17.790  1.00 43.11           C  
ATOM   2065  O   ILE B  76      12.881  76.338  17.170  1.00 43.25           O  
ATOM   2066  CB  ILE B  76      15.292  74.810  16.360  1.00 44.46           C  
ATOM   2067  CG1 ILE B  76      16.111  73.572  15.976  1.00 45.68           C  
ATOM   2068  CG2 ILE B  76      16.226  75.750  16.925  1.00 44.42           C  
ATOM   2069  CD1 ILE B  76      15.402  72.468  15.164  1.00 46.16           C  
ATOM   2070  N   ASP B  77      14.409  76.474  18.742  1.00 42.50           N  
ATOM   2071  CA  ASP B  77      13.894  77.737  19.191  1.00 42.86           C  
ATOM   2072  C   ASP B  77      14.910  78.872  19.316  1.00 40.85           C  
ATOM   2073  O   ASP B  77      15.230  79.253  20.411  1.00 42.58           O  
ATOM   2074  CB  ASP B  77      13.245  77.483  20.556  1.00 47.57           C  
ATOM   2075  CG  ASP B  77      11.695  77.652  20.555  1.00 52.14           C  
ATOM   2076  OD1 ASP B  77      11.000  77.265  21.587  1.00 53.90           O  
ATOM   2077  OD2 ASP B  77      11.195  78.193  19.521  1.00 54.00           O  
ATOM   2078  N   PHE B  78      15.389  79.489  18.252  1.00 37.08           N  
ATOM   2079  CA  PHE B  78      16.383  80.531  18.470  1.00 33.66           C  
ATOM   2080  C   PHE B  78      15.931  81.972  18.388  1.00 32.18           C  
ATOM   2081  O   PHE B  78      14.750  82.221  18.215  1.00 32.58           O  
ATOM   2082  CB  PHE B  78      17.483  80.328  17.488  1.00 32.68           C  
ATOM   2083  CG  PHE B  78      17.004  80.289  16.062  1.00 31.63           C  
ATOM   2084  CD1 PHE B  78      17.309  81.315  15.175  1.00 30.79           C  
ATOM   2085  CD2 PHE B  78      16.271  79.241  15.602  1.00 30.59           C  
ATOM   2086  CE1 PHE B  78      16.901  81.283  13.906  1.00 28.92           C  
ATOM   2087  CE2 PHE B  78      15.874  79.225  14.319  1.00 30.89           C  
ATOM   2088  CZ  PHE B  78      16.191  80.248  13.474  1.00 30.04           C  
ATOM   2089  N   LYS B  79      16.886  82.907  18.499  1.00 30.15           N  
ATOM   2090  CA  LYS B  79      16.663  84.363  18.414  1.00 29.55           C  
ATOM   2091  C   LYS B  79      17.500  84.836  17.228  1.00 28.10           C  
ATOM   2092  O   LYS B  79      18.528  84.262  17.002  1.00 28.40           O  
ATOM   2093  CB  LYS B  79      17.177  85.047  19.696  1.00 31.66           C  
ATOM   2094  CG  LYS B  79      16.133  85.694  20.625  1.00 35.89           C  
ATOM   2095  CD  LYS B  79      16.701  86.105  22.033  1.00 42.13           C  
ATOM   2096  CE  LYS B  79      16.501  85.028  23.240  1.00 47.60           C  
ATOM   2097  NZ  LYS B  79      16.888  83.460  23.111  1.00 50.44           N  
ATOM   2098  N   VAL B  80      17.096  85.841  16.465  1.00 26.83           N  
ATOM   2099  CA  VAL B  80      17.906  86.325  15.330  1.00 27.16           C  
ATOM   2100  C   VAL B  80      17.740  87.815  15.339  1.00 28.45           C  
ATOM   2101  O   VAL B  80      16.614  88.252  15.332  1.00 29.47           O  
ATOM   2102  CB  VAL B  80      17.375  85.876  13.983  1.00 26.36           C  
ATOM   2103  CG1 VAL B  80      17.905  86.772  12.878  1.00 25.37           C  
ATOM   2104  CG2 VAL B  80      17.782  84.518  13.721  1.00 26.16           C  
ATOM   2105  N   TYR B  81      18.802  88.614  15.276  1.00 29.21           N  
ATOM   2106  CA  TYR B  81      18.605  90.056  15.384  1.00 30.41           C  
ATOM   2107  C   TYR B  81      19.613  90.943  14.732  1.00 32.57           C  
ATOM   2108  O   TYR B  81      20.718  90.550  14.574  1.00 33.59           O  
ATOM   2109  CB  TYR B  81      18.590  90.407  16.846  1.00 28.98           C  
ATOM   2110  CG  TYR B  81      19.678  89.733  17.685  1.00 27.82           C  
ATOM   2111  CD1 TYR B  81      20.942  90.294  17.818  1.00 27.78           C  
ATOM   2112  CD2 TYR B  81      19.384  88.604  18.466  1.00 27.95           C  
ATOM   2113  CE1 TYR B  81      21.884  89.757  18.721  1.00 28.71           C  
ATOM   2114  CE2 TYR B  81      20.306  88.061  19.375  1.00 27.78           C  
ATOM   2115  CZ  TYR B  81      21.550  88.637  19.497  1.00 29.09           C  
ATOM   2116  OH  TYR B  81      22.478  88.071  20.363  1.00 30.79           O  
ATOM   2117  N   PRO B  82      19.249  92.167  14.358  1.00 34.30           N  
ATOM   2118  CA  PRO B  82      20.233  93.030  13.737  1.00 36.39           C  
ATOM   2119  C   PRO B  82      21.120  93.439  14.838  1.00 39.15           C  
ATOM   2120  O   PRO B  82      20.813  93.173  15.994  1.00 38.92           O  
ATOM   2121  CB  PRO B  82      19.417  94.178  13.202  1.00 36.03           C  
ATOM   2122  CG  PRO B  82      18.323  94.241  14.101  1.00 36.34           C  
ATOM   2123  CD  PRO B  82      17.943  92.813  14.350  1.00 35.62           C  
ATOM   2124  N   THR B  83      22.226  94.093  14.491  1.00 43.64           N  
ATOM   2125  CA  THR B  83      23.222  94.493  15.494  1.00 47.13           C  
ATOM   2126  C   THR B  83      23.771  95.818  15.191  1.00 49.24           C  
ATOM   2127  O   THR B  83      23.715  96.265  14.054  1.00 51.06           O  
ATOM   2128  CB  THR B  83      24.366  93.485  15.536  1.00 48.02           C  
ATOM   2129  OG1 THR B  83      24.238  92.757  16.744  1.00 49.68           O  
ATOM   2130  CG2 THR B  83      25.742  94.121  15.480  1.00 48.01           C  
ATOM   2131  N   LYS B  84      24.319  96.428  16.222  1.00 52.05           N  
ATOM   2132  CA  LYS B  84      24.901  97.775  16.176  1.00 55.08           C  
ATOM   2133  C   LYS B  84      25.940  98.049  15.063  1.00 55.05           C  
ATOM   2134  O   LYS B  84      25.908  99.088  14.429  1.00 55.27           O  
ATOM   2135  CB  LYS B  84      25.494  98.039  17.580  1.00 57.81           C  
ATOM   2136  CG  LYS B  84      25.702  99.502  18.047  1.00 60.91           C  
ATOM   2137  CD  LYS B  84      27.201  99.787  18.625  1.00 63.48           C  
ATOM   2138  CE  LYS B  84      27.955  98.595  19.416  1.00 64.26           C  
ATOM   2139  NZ  LYS B  84      27.565  98.242  20.856  1.00 64.78           N  
ATOM   2140  N   GLU B  85      26.824  97.089  14.824  1.00 56.00           N  
ATOM   2141  CA  GLU B  85      27.934  97.179  13.862  1.00 57.59           C  
ATOM   2142  C   GLU B  85      27.651  97.247  12.378  1.00 55.69           C  
ATOM   2143  O   GLU B  85      28.478  97.789  11.633  1.00 56.18           O  
ATOM   2144  CB  GLU B  85      28.951  96.010  14.087  1.00 61.93           C  
ATOM   2145  CG  GLU B  85      30.214  96.320  14.955  1.00 69.24           C  
ATOM   2146  CD  GLU B  85      29.944  96.513  16.542  1.00 74.51           C  
ATOM   2147  OE1 GLU B  85      30.713  97.344  17.191  1.00 76.20           O  
ATOM   2148  OE2 GLU B  85      28.999  95.831  17.120  1.00 75.70           O  
ATOM   2149  N   PHE B  86      26.545  96.640  11.936  1.00 53.59           N  
ATOM   2150  CA  PHE B  86      26.170  96.629  10.507  1.00 50.67           C  
ATOM   2151  C   PHE B  86      24.689  96.860  10.239  1.00 48.80           C  
ATOM   2152  O   PHE B  86      23.811  96.696  11.126  1.00 48.93           O  
ATOM   2153  CB  PHE B  86      26.470  95.295   9.794  1.00 49.49           C  
ATOM   2154  CG  PHE B  86      27.694  94.574  10.255  1.00 48.92           C  
ATOM   2155  CD1 PHE B  86      27.603  93.583  11.236  1.00 48.94           C  
ATOM   2156  CD2 PHE B  86      28.926  94.803   9.651  1.00 48.79           C  
ATOM   2157  CE1 PHE B  86      28.734  92.807  11.617  1.00 48.15           C  
ATOM   2158  CE2 PHE B  86      30.046  94.053  10.009  1.00 47.96           C  
ATOM   2159  CZ  PHE B  86      29.944  93.046  11.002  1.00 48.03           C  
ATOM   2160  N   PRO B  87      24.391  97.212   8.981  1.00 46.58           N  
ATOM   2161  CA  PRO B  87      23.061  97.474   8.429  1.00 45.39           C  
ATOM   2162  C   PRO B  87      22.101  96.337   8.807  1.00 43.62           C  
ATOM   2163  O   PRO B  87      22.479  95.160   8.919  1.00 44.03           O  
ATOM   2164  CB  PRO B  87      23.308  97.573   6.911  1.00 46.23           C  
ATOM   2165  CG  PRO B  87      24.708  97.104   6.709  1.00 46.93           C  
ATOM   2166  CD  PRO B  87      25.400  97.580   7.998  1.00 46.62           C  
ATOM   2167  N   ALA B  88      20.843  96.660   8.999  1.00 40.60           N  
ATOM   2168  CA  ALA B  88      20.014  95.587   9.442  1.00 37.44           C  
ATOM   2169  C   ALA B  88      19.968  94.324   8.592  1.00 35.37           C  
ATOM   2170  O   ALA B  88      19.652  93.258   9.086  1.00 34.43           O  
ATOM   2171  CB  ALA B  88      18.665  96.101   9.688  1.00 37.86           C  
ATOM   2172  N   ALA B  89      20.307  94.371   7.327  1.00 33.52           N  
ATOM   2173  CA  ALA B  89      20.147  93.105   6.672  1.00 32.51           C  
ATOM   2174  C   ALA B  89      21.201  92.114   7.038  1.00 32.08           C  
ATOM   2175  O   ALA B  89      21.161  90.979   6.561  1.00 32.59           O  
ATOM   2176  CB  ALA B  89      20.099  93.258   5.238  1.00 33.23           C  
ATOM   2177  N   HIS B  90      22.149  92.516   7.877  1.00 30.60           N  
ATOM   2178  CA  HIS B  90      23.205  91.602   8.290  1.00 29.01           C  
ATOM   2179  C   HIS B  90      22.913  91.355   9.724  1.00 28.57           C  
ATOM   2180  O   HIS B  90      23.360  92.114  10.578  1.00 29.50           O  
ATOM   2181  CB  HIS B  90      24.560  92.268   8.124  1.00 28.54           C  
ATOM   2182  CG  HIS B  90      25.720  91.459   8.622  1.00 27.94           C  
ATOM   2183  ND1 HIS B  90      26.999  91.634   8.134  1.00 27.39           N  
ATOM   2184  CD2 HIS B  90      25.810  90.517   9.593  1.00 26.66           C  
ATOM   2185  CE1 HIS B  90      27.823  90.831   8.790  1.00 26.59           C  
ATOM   2186  NE2 HIS B  90      27.130  90.144   9.679  1.00 25.82           N  
ATOM   2187  N   MET B  91      22.121  90.327   9.994  1.00 27.85           N  
ATOM   2188  CA  MET B  91      21.761  90.025  11.363  1.00 27.50           C  
ATOM   2189  C   MET B  91      22.651  88.942  11.961  1.00 27.65           C  
ATOM   2190  O   MET B  91      23.529  88.445  11.295  1.00 28.79           O  
ATOM   2191  CB  MET B  91      20.294  89.643  11.440  1.00 26.99           C  
ATOM   2192  CG  MET B  91      19.398  90.780  11.045  1.00 27.15           C  
ATOM   2193  SD  MET B  91      17.643  90.336  11.032  1.00 30.66           S  
ATOM   2194  CE  MET B  91      17.492  89.246   9.607  1.00 27.59           C  
ATOM   2195  N   LEU B  92      22.419  88.570  13.210  1.00 26.78           N  
ATOM   2196  CA  LEU B  92      23.220  87.575  13.886  1.00 25.56           C  
ATOM   2197  C   LEU B  92      22.286  86.457  14.409  1.00 25.50           C  
ATOM   2198  O   LEU B  92      21.190  86.741  14.776  1.00 25.72           O  
ATOM   2199  CB  LEU B  92      23.911  88.346  14.972  1.00 25.28           C  
ATOM   2200  CG  LEU B  92      24.857  87.820  16.011  1.00 25.48           C  
ATOM   2201  CD1 LEU B  92      25.328  89.031  16.619  1.00 26.43           C  
ATOM   2202  CD2 LEU B  92      24.264  86.916  17.065  1.00 25.15           C  
ATOM   2203  N   ILE B  93      22.685  85.195  14.404  1.00 25.78           N  
ATOM   2204  CA  ILE B  93      21.840  84.124  14.847  1.00 27.41           C  
ATOM   2205  C   ILE B  93      22.241  83.655  16.242  1.00 31.58           C  
ATOM   2206  O   ILE B  93      23.314  83.115  16.438  1.00 32.20           O  
ATOM   2207  CB  ILE B  93      22.006  82.995  13.935  1.00 25.57           C  
ATOM   2208  CG1 ILE B  93      21.507  83.361  12.590  1.00 25.67           C  
ATOM   2209  CG2 ILE B  93      21.206  81.849  14.357  1.00 25.16           C  
ATOM   2210  CD1 ILE B  93      21.496  82.176  11.680  1.00 26.07           C  
ATOM   2211  N   ASP B  94      21.359  83.796  17.219  1.00 35.57           N  
ATOM   2212  CA  ASP B  94      21.682  83.397  18.565  1.00 39.92           C  
ATOM   2213  C   ASP B  94      20.939  82.137  18.989  1.00 42.94           C  
ATOM   2214  O   ASP B  94      20.069  82.222  19.836  1.00 43.21           O  
ATOM   2215  CB  ASP B  94      21.316  84.565  19.464  1.00 41.96           C  
ATOM   2216  CG  ASP B  94      21.865  84.437  20.899  1.00 45.56           C  
ATOM   2217  OD1 ASP B  94      21.479  85.312  21.758  1.00 46.25           O  
ATOM   2218  OD2 ASP B  94      22.672  83.488  21.161  1.00 46.42           O  
ATOM   2219  N   ALA B  95      21.267  80.966  18.431  1.00 46.74           N  
ATOM   2220  CA  ALA B  95      20.563  79.710  18.809  1.00 50.33           C  
ATOM   2221  C   ALA B  95      21.369  79.014  19.844  1.00 53.95           C  
ATOM   2222  O   ALA B  95      22.571  79.001  19.711  1.00 55.01           O  
ATOM   2223  CB  ALA B  95      20.459  78.825  17.690  1.00 49.76           C  
ATOM   2224  N   PRO B  96      20.729  78.321  20.814  1.00 57.40           N  
ATOM   2225  CA  PRO B  96      21.299  77.579  21.950  1.00 60.06           C  
ATOM   2226  C   PRO B  96      22.678  76.827  21.776  1.00 62.76           C  
ATOM   2227  O   PRO B  96      23.758  77.272  22.333  1.00 64.39           O  
ATOM   2228  CB  PRO B  96      20.151  76.649  22.327  1.00 59.05           C  
ATOM   2229  CG  PRO B  96      19.696  76.237  21.045  1.00 59.37           C  
ATOM   2230  CD  PRO B  96      19.518  77.606  20.386  1.00 58.86           C  
ATOM   2231  N   SER B  97      22.671  75.711  21.040  1.00 63.35           N  
ATOM   2232  CA  SER B  97      23.925  74.980  20.858  1.00 64.18           C  
ATOM   2233  C   SER B  97      24.911  75.704  19.864  1.00 62.69           C  
ATOM   2234  O   SER B  97      26.059  76.018  20.224  1.00 63.80           O  
ATOM   2235  CB  SER B  97      23.587  73.546  20.409  1.00 66.47           C  
ATOM   2236  OG  SER B  97      24.748  72.776  20.077  1.00 69.46           O  
ATOM   2237  N   VAL B  98      24.439  75.948  18.641  1.00 60.08           N  
ATOM   2238  CA  VAL B  98      25.113  76.649  17.520  1.00 57.60           C  
ATOM   2239  C   VAL B  98      25.991  77.942  17.707  1.00 56.90           C  
ATOM   2240  O   VAL B  98      25.622  78.849  18.465  1.00 58.51           O  
ATOM   2241  CB  VAL B  98      24.007  77.043  16.552  1.00 56.17           C  
ATOM   2242  CG1 VAL B  98      24.548  77.781  15.346  1.00 54.02           C  
ATOM   2243  CG2 VAL B  98      23.192  75.810  16.265  1.00 55.66           C  
ATOM   2244  N   PHE B  99      27.118  78.068  17.005  1.00 54.15           N  
ATOM   2245  CA  PHE B  99      27.954  79.315  17.062  1.00 52.32           C  
ATOM   2246  C   PHE B  99      27.254  80.648  16.782  1.00 49.24           C  
ATOM   2247  O   PHE B  99      26.410  80.695  15.886  1.00 49.96           O  
ATOM   2248  CB  PHE B  99      29.042  79.274  15.994  1.00 53.91           C  
ATOM   2249  CG  PHE B  99      30.132  78.476  16.382  1.00 56.06           C  
ATOM   2250  CD1 PHE B  99      29.905  77.129  16.690  1.00 58.60           C  
ATOM   2251  CD2 PHE B  99      31.329  79.057  16.651  1.00 56.17           C  
ATOM   2252  CE1 PHE B  99      30.862  76.390  17.285  1.00 59.51           C  
ATOM   2253  CE2 PHE B  99      32.303  78.351  17.246  1.00 57.93           C  
ATOM   2254  CZ  PHE B  99      32.095  77.017  17.573  1.00 59.69           C  
ATOM   2255  N   ALA B 100      27.573  81.752  17.453  1.00 44.81           N  
ATOM   2256  CA  ALA B 100      26.865  82.934  16.955  1.00 40.58           C  
ATOM   2257  C   ALA B 100      27.278  82.931  15.481  1.00 37.09           C  
ATOM   2258  O   ALA B 100      28.429  82.738  15.176  1.00 37.34           O  
ATOM   2259  CB  ALA B 100      27.317  84.187  17.624  1.00 41.32           C  
ATOM   2260  N   ALA B 101      26.339  83.103  14.571  1.00 33.03           N  
ATOM   2261  CA  ALA B 101      26.664  83.080  13.164  1.00 29.90           C  
ATOM   2262  C   ALA B 101      25.969  84.203  12.454  1.00 27.38           C  
ATOM   2263  O   ALA B 101      24.972  84.687  12.910  1.00 28.24           O  
ATOM   2264  CB  ALA B 101      26.247  81.754  12.558  1.00 30.39           C  
ATOM   2265  N   PRO B 102      26.461  84.608  11.293  1.00 24.54           N  
ATOM   2266  CA  PRO B 102      25.708  85.693  10.722  1.00 22.75           C  
ATOM   2267  C   PRO B 102      24.557  85.201   9.843  1.00 21.50           C  
ATOM   2268  O   PRO B 102      24.573  84.076   9.413  1.00 21.95           O  
ATOM   2269  CB  PRO B 102      26.791  86.463   9.987  1.00 21.70           C  
ATOM   2270  CG  PRO B 102      27.594  85.449   9.496  1.00 22.26           C  
ATOM   2271  CD  PRO B 102      27.754  84.503  10.624  1.00 23.56           C  
ATOM   2272  N   TYR B 103      23.557  86.063   9.644  1.00 19.71           N  
ATOM   2273  CA  TYR B 103      22.367  85.859   8.832  1.00 17.24           C  
ATOM   2274  C   TYR B 103      22.340  87.111   7.915  1.00 17.94           C  
ATOM   2275  O   TYR B 103      21.805  88.167   8.265  1.00 17.44           O  
ATOM   2276  CB  TYR B 103      21.167  85.873   9.751  1.00 15.05           C  
ATOM   2277  CG  TYR B 103      19.830  85.428   9.196  1.00 12.79           C  
ATOM   2278  CD1 TYR B 103      19.328  84.167   9.461  1.00 10.91           C  
ATOM   2279  CD2 TYR B 103      19.061  86.269   8.438  1.00 11.44           C  
ATOM   2280  CE1 TYR B 103      18.122  83.784   8.985  1.00  9.44           C  
ATOM   2281  CE2 TYR B 103      17.866  85.871   7.962  1.00  9.60           C  
ATOM   2282  CZ  TYR B 103      17.405  84.636   8.243  1.00  9.55           C  
ATOM   2283  OH  TYR B 103      16.160  84.289   7.819  1.00 11.81           O  
ATOM   2284  N   GLU B 104      22.968  87.011   6.752  1.00 18.75           N  
ATOM   2285  CA  GLU B 104      23.006  88.113   5.799  1.00 19.08           C  
ATOM   2286  C   GLU B 104      21.812  88.020   4.831  1.00 18.81           C  
ATOM   2287  O   GLU B 104      21.704  87.016   4.151  1.00 20.95           O  
ATOM   2288  CB  GLU B 104      24.323  88.027   5.046  1.00 19.21           C  
ATOM   2289  CG  GLU B 104      25.429  88.692   5.779  1.00 23.21           C  
ATOM   2290  CD  GLU B 104      26.751  88.663   5.042  1.00 27.58           C  
ATOM   2291  OE1 GLU B 104      27.104  89.672   4.363  1.00 30.67           O  
ATOM   2292  OE2 GLU B 104      27.471  87.624   5.124  1.00 29.67           O  
ATOM   2293  N   VAL B 105      20.899  89.000   4.770  1.00 17.19           N  
ATOM   2294  CA  VAL B 105      19.781  88.904   3.825  1.00 15.33           C  
ATOM   2295  C   VAL B 105      20.262  89.584   2.607  1.00 15.19           C  
ATOM   2296  O   VAL B 105      20.291  90.809   2.568  1.00 14.10           O  
ATOM   2297  CB  VAL B 105      18.526  89.618   4.285  1.00 14.19           C  
ATOM   2298  CG1 VAL B 105      17.512  89.623   3.242  1.00 13.11           C  
ATOM   2299  CG2 VAL B 105      17.915  88.847   5.336  1.00 14.74           C  
ATOM   2300  N   ILE B 106      20.665  88.770   1.629  1.00 15.44           N  
ATOM   2301  CA  ILE B 106      21.190  89.257   0.365  1.00 16.70           C  
ATOM   2302  C   ILE B 106      20.112  90.023  -0.311  1.00 18.52           C  
ATOM   2303  O   ILE B 106      20.293  91.159  -0.570  1.00 19.97           O  
ATOM   2304  CB  ILE B 106      21.666  88.137  -0.580  1.00 15.47           C  
ATOM   2305  CG1 ILE B 106      23.085  87.749  -0.268  1.00 15.55           C  
ATOM   2306  CG2 ILE B 106      21.755  88.617  -1.963  1.00 13.91           C  
ATOM   2307  CD1 ILE B 106      23.417  86.324  -0.569  1.00 15.27           C  
ATOM   2308  N   GLU B 107      18.977  89.430  -0.608  1.00 20.44           N  
ATOM   2309  CA  GLU B 107      17.946  90.201  -1.249  1.00 22.35           C  
ATOM   2310  C   GLU B 107      16.575  89.659  -0.832  1.00 23.91           C  
ATOM   2311  O   GLU B 107      16.436  88.430  -0.604  1.00 25.14           O  
ATOM   2312  CB  GLU B 107      18.149  90.066  -2.724  1.00 23.33           C  
ATOM   2313  CG  GLU B 107      17.224  90.854  -3.541  1.00 27.12           C  
ATOM   2314  CD  GLU B 107      17.341  90.567  -5.080  1.00 30.77           C  
ATOM   2315  OE1 GLU B 107      18.437  90.908  -5.697  1.00 30.94           O  
ATOM   2316  OE2 GLU B 107      16.321  90.013  -5.652  1.00 29.99           O  
ATOM   2317  N   THR B 108      15.573  90.527  -0.636  1.00 22.92           N  
ATOM   2318  CA  THR B 108      14.236  89.974  -0.368  1.00 22.66           C  
ATOM   2319  C   THR B 108      13.100  90.837  -0.873  1.00 22.48           C  
ATOM   2320  O   THR B 108      13.241  92.074  -0.998  1.00 23.29           O  
ATOM   2321  CB  THR B 108      13.952  89.684   1.107  1.00 23.09           C  
ATOM   2322  OG1 THR B 108      12.821  88.791   1.177  1.00 22.67           O  
ATOM   2323  CG2 THR B 108      13.637  90.989   1.870  1.00 22.53           C  
ATOM   2324  N   ASP B 109      11.974  90.198  -1.179  1.00 20.99           N  
ATOM   2325  CA  ASP B 109      10.846  90.956  -1.654  1.00 20.11           C  
ATOM   2326  C   ASP B 109       9.820  90.957  -0.564  1.00 20.10           C  
ATOM   2327  O   ASP B 109       8.799  91.628  -0.657  1.00 20.96           O  
ATOM   2328  CB  ASP B 109      10.333  90.396  -2.994  1.00 21.28           C  
ATOM   2329  CG  ASP B 109       9.293  89.298  -2.853  1.00 23.05           C  
ATOM   2330  OD1 ASP B 109       9.284  88.685  -1.801  1.00 24.41           O  
ATOM   2331  OD2 ASP B 109       8.485  89.041  -3.799  1.00 24.33           O  
ATOM   2332  N   TYR B 110      10.169  90.277   0.513  1.00 19.46           N  
ATOM   2333  CA  TYR B 110       9.327  90.140   1.674  1.00 20.64           C  
ATOM   2334  C   TYR B 110       8.070  89.378   1.449  1.00 22.15           C  
ATOM   2335  O   TYR B 110       7.691  88.600   2.312  1.00 23.24           O  
ATOM   2336  CB  TYR B 110       8.894  91.457   2.277  1.00 20.10           C  
ATOM   2337  CG  TYR B 110       9.955  92.376   2.653  1.00 21.02           C  
ATOM   2338  CD1 TYR B 110      10.403  93.328   1.754  1.00 21.36           C  
ATOM   2339  CD2 TYR B 110      10.558  92.293   3.912  1.00 22.74           C  
ATOM   2340  CE1 TYR B 110      11.451  94.211   2.093  1.00 23.82           C  
ATOM   2341  CE2 TYR B 110      11.642  93.155   4.279  1.00 24.06           C  
ATOM   2342  CZ  TYR B 110      12.069  94.104   3.354  1.00 24.36           C  
ATOM   2343  OH  TYR B 110      13.122  94.904   3.634  1.00 24.62           O  
ATOM   2344  N   GLU B 111       7.401  89.610   0.329  1.00 23.14           N  
ATOM   2345  CA  GLU B 111       6.152  88.924   0.030  1.00 26.13           C  
ATOM   2346  C   GLU B 111       6.354  87.530  -0.617  1.00 24.37           C  
ATOM   2347  O   GLU B 111       5.516  86.657  -0.578  1.00 22.89           O  
ATOM   2348  CB  GLU B 111       5.310  89.749  -0.975  1.00 34.33           C  
ATOM   2349  CG  GLU B 111       5.013  91.266  -0.748  1.00 41.90           C  
ATOM   2350  CD  GLU B 111       4.363  91.475   0.606  1.00 47.60           C  
ATOM   2351  OE1 GLU B 111       3.585  90.508   0.980  1.00 50.99           O  
ATOM   2352  OE2 GLU B 111       4.627  92.564   1.278  1.00 50.10           O  
ATOM   2353  N   THR B 112       7.484  87.343  -1.238  1.00 23.76           N  
ATOM   2354  CA  THR B 112       7.728  86.107  -1.920  1.00 24.61           C  
ATOM   2355  C   THR B 112       8.962  85.194  -1.644  1.00 24.53           C  
ATOM   2356  O   THR B 112       8.772  83.982  -1.326  1.00 24.97           O  
ATOM   2357  CB  THR B 112       7.539  86.430  -3.374  1.00 25.22           C  
ATOM   2358  OG1 THR B 112       6.327  85.809  -3.707  1.00 28.11           O  
ATOM   2359  CG2 THR B 112       8.647  85.971  -4.307  1.00 23.02           C  
ATOM   2360  N   TYR B 113      10.191  85.737  -1.751  1.00 22.20           N  
ATOM   2361  CA  TYR B 113      11.381  84.963  -1.459  1.00 20.25           C  
ATOM   2362  C   TYR B 113      12.370  85.721  -0.569  1.00 19.75           C  
ATOM   2363  O   TYR B 113      12.296  86.914  -0.432  1.00 20.50           O  
ATOM   2364  CB  TYR B 113      12.033  84.699  -2.750  1.00 19.33           C  
ATOM   2365  CG  TYR B 113      12.488  85.977  -3.368  1.00 18.90           C  
ATOM   2366  CD1 TYR B 113      13.831  86.330  -3.385  1.00 17.95           C  
ATOM   2367  CD2 TYR B 113      11.584  86.827  -3.985  1.00 19.19           C  
ATOM   2368  CE1 TYR B 113      14.282  87.531  -4.025  1.00 18.36           C  
ATOM   2369  CE2 TYR B 113      12.024  88.035  -4.645  1.00 19.94           C  
ATOM   2370  CZ  TYR B 113      13.383  88.385  -4.654  1.00 19.29           C  
ATOM   2371  OH  TYR B 113      13.798  89.583  -5.244  1.00 18.20           O  
ATOM   2372  N   SER B 114      13.286  85.033   0.074  1.00 19.38           N  
ATOM   2373  CA  SER B 114      14.347  85.724   0.827  1.00 19.96           C  
ATOM   2374  C   SER B 114      15.673  84.934   0.649  1.00 20.33           C  
ATOM   2375  O   SER B 114      15.711  83.716   0.815  1.00 22.18           O  
ATOM   2376  CB  SER B 114      13.997  85.837   2.284  1.00 19.98           C  
ATOM   2377  OG  SER B 114      15.154  86.138   3.052  1.00 19.48           O  
ATOM   2378  N   CYS B 115      16.759  85.592   0.291  1.00 18.92           N  
ATOM   2379  CA  CYS B 115      17.962  84.827   0.053  1.00 18.95           C  
ATOM   2380  C   CYS B 115      18.942  85.065   1.166  1.00 19.55           C  
ATOM   2381  O   CYS B 115      19.534  86.134   1.314  1.00 21.20           O  
ATOM   2382  CB  CYS B 115      18.512  85.215  -1.309  1.00 18.90           C  
ATOM   2383  SG  CYS B 115      17.303  84.952  -2.616  1.00 19.46           S  
ATOM   2384  N   VAL B 116      19.163  84.054   1.966  1.00 19.04           N  
ATOM   2385  CA  VAL B 116      20.030  84.259   3.103  1.00 18.78           C  
ATOM   2386  C   VAL B 116      21.352  83.579   3.034  1.00 18.15           C  
ATOM   2387  O   VAL B 116      21.426  82.417   2.681  1.00 19.20           O  
ATOM   2388  CB  VAL B 116      19.285  83.854   4.329  1.00 19.14           C  
ATOM   2389  CG1 VAL B 116      20.160  83.880   5.495  1.00 19.33           C  
ATOM   2390  CG2 VAL B 116      18.118  84.804   4.494  1.00 20.67           C  
ATOM   2391  N   TYR B 117      22.401  84.315   3.356  1.00 16.80           N  
ATOM   2392  CA  TYR B 117      23.724  83.757   3.295  1.00 16.99           C  
ATOM   2393  C   TYR B 117      24.229  83.788   4.672  1.00 18.05           C  
ATOM   2394  O   TYR B 117      23.905  84.714   5.384  1.00 19.00           O  
ATOM   2395  CB  TYR B 117      24.642  84.628   2.451  1.00 15.75           C  
ATOM   2396  CG  TYR B 117      25.998  84.010   2.144  1.00 13.12           C  
ATOM   2397  CD1 TYR B 117      26.138  82.720   1.622  1.00 11.68           C  
ATOM   2398  CD2 TYR B 117      27.119  84.740   2.294  1.00 11.41           C  
ATOM   2399  CE1 TYR B 117      27.425  82.211   1.240  1.00  9.82           C  
ATOM   2400  CE2 TYR B 117      28.367  84.234   1.943  1.00 10.45           C  
ATOM   2401  CZ  TYR B 117      28.533  82.997   1.421  1.00  9.42           C  
ATOM   2402  OH  TYR B 117      29.835  82.635   1.141  1.00  6.18           O  
ATOM   2403  N   SER B 118      25.040  82.797   5.028  1.00 18.14           N  
ATOM   2404  CA  SER B 118      25.649  82.728   6.326  1.00 18.70           C  
ATOM   2405  C   SER B 118      26.924  81.920   6.315  1.00 18.88           C  
ATOM   2406  O   SER B 118      26.918  80.700   6.218  1.00 18.52           O  
ATOM   2407  CB  SER B 118      24.727  82.110   7.288  1.00 20.34           C  
ATOM   2408  OG  SER B 118      25.514  81.791   8.410  1.00 25.63           O  
ATOM   2409  N   CYS B 119      28.024  82.612   6.516  1.00 19.92           N  
ATOM   2410  CA  CYS B 119      29.339  82.021   6.409  1.00 21.06           C  
ATOM   2411  C   CYS B 119      30.438  82.770   7.162  1.00 21.95           C  
ATOM   2412  O   CYS B 119      30.607  84.001   7.000  1.00 22.48           O  
ATOM   2413  CB  CYS B 119      29.679  82.065   4.948  1.00 22.53           C  
ATOM   2414  SG  CYS B 119      31.314  81.540   4.414  1.00 25.76           S  
ATOM   2415  N   ILE B 120      31.212  82.042   7.957  1.00 22.14           N  
ATOM   2416  CA  ILE B 120      32.308  82.662   8.681  1.00 22.34           C  
ATOM   2417  C   ILE B 120      33.622  82.252   8.021  1.00 23.20           C  
ATOM   2418  O   ILE B 120      33.896  81.050   7.900  1.00 24.25           O  
ATOM   2419  CB  ILE B 120      32.327  82.162  10.068  1.00 21.63           C  
ATOM   2420  CG1 ILE B 120      31.199  82.807  10.833  1.00 22.04           C  
ATOM   2421  CG2 ILE B 120      33.666  82.408  10.668  1.00 19.60           C  
ATOM   2422  CD1 ILE B 120      30.827  82.034  12.053  1.00 23.92           C  
ATOM   2423  N   THR B 121      34.431  83.217   7.586  1.00 22.71           N  
ATOM   2424  CA  THR B 121      35.691  82.862   6.964  1.00 22.69           C  
ATOM   2425  C   THR B 121      36.619  82.452   8.044  1.00 22.42           C  
ATOM   2426  O   THR B 121      36.614  83.052   9.091  1.00 22.83           O  
ATOM   2427  CB  THR B 121      36.404  84.020   6.292  1.00 23.88           C  
ATOM   2428  OG1 THR B 121      35.764  84.404   5.048  1.00 24.81           O  
ATOM   2429  CG2 THR B 121      37.861  83.579   6.022  1.00 24.98           C  
ATOM   2430  N   THR B 122      37.448  81.451   7.798  1.00 22.75           N  
ATOM   2431  CA  THR B 122      38.380  81.062   8.823  1.00 23.38           C  
ATOM   2432  C   THR B 122      39.804  81.453   8.469  1.00 26.93           C  
ATOM   2433  O   THR B 122      40.312  82.291   9.133  1.00 31.53           O  
ATOM   2434  CB  THR B 122      38.218  79.717   9.182  1.00 20.37           C  
ATOM   2435  OG1 THR B 122      37.886  79.726  10.520  1.00 17.74           O  
ATOM   2436  CG2 THR B 122      39.364  79.047   9.099  1.00 19.39           C  
ATOM   2437  N   ASP B 123      40.564  80.948   7.543  1.00 28.31           N  
ATOM   2438  CA  ASP B 123      41.792  81.731   7.387  1.00 30.50           C  
ATOM   2439  C   ASP B 123      41.641  81.955   5.919  1.00 31.39           C  
ATOM   2440  O   ASP B 123      41.288  83.024   5.466  1.00 32.33           O  
ATOM   2441  CB  ASP B 123      43.068  80.962   7.704  1.00 34.81           C  
ATOM   2442  CG  ASP B 123      43.871  81.566   8.902  1.00 39.44           C  
ATOM   2443  OD1 ASP B 123      43.710  82.770   9.208  1.00 41.41           O  
ATOM   2444  OD2 ASP B 123      44.703  80.831   9.539  1.00 42.86           O  
ATOM   2445  N   ASN B 124      41.812  80.861   5.211  1.00 31.72           N  
ATOM   2446  CA  ASN B 124      41.700  80.758   3.820  1.00 32.08           C  
ATOM   2447  C   ASN B 124      40.774  79.610   3.478  1.00 31.18           C  
ATOM   2448  O   ASN B 124      40.882  79.005   2.432  1.00 32.17           O  
ATOM   2449  CB  ASN B 124      43.063  80.521   3.305  1.00 37.29           C  
ATOM   2450  CG  ASN B 124      43.626  81.758   2.694  1.00 43.77           C  
ATOM   2451  OD1 ASN B 124      43.082  82.242   1.646  1.00 47.12           O  
ATOM   2452  ND2 ASN B 124      44.699  82.334   3.323  1.00 45.83           N  
ATOM   2453  N   TYR B 125      39.874  79.296   4.394  1.00 29.41           N  
ATOM   2454  CA  TYR B 125      38.866  78.255   4.254  1.00 27.22           C  
ATOM   2455  C   TYR B 125      37.554  78.876   4.807  1.00 25.58           C  
ATOM   2456  O   TYR B 125      37.559  79.957   5.369  1.00 25.35           O  
ATOM   2457  CB  TYR B 125      39.252  77.047   5.089  1.00 26.71           C  
ATOM   2458  CG  TYR B 125      40.574  76.566   4.740  1.00 28.14           C  
ATOM   2459  CD1 TYR B 125      40.754  75.523   3.815  1.00 29.41           C  
ATOM   2460  CD2 TYR B 125      41.679  77.189   5.272  1.00 29.95           C  
ATOM   2461  CE1 TYR B 125      42.050  75.100   3.398  1.00 31.22           C  
ATOM   2462  CE2 TYR B 125      42.995  76.813   4.907  1.00 32.34           C  
ATOM   2463  CZ  TYR B 125      43.181  75.772   3.957  1.00 33.67           C  
ATOM   2464  OH  TYR B 125      44.504  75.530   3.536  1.00 36.16           O  
ATOM   2465  N   LYS B 126      36.434  78.205   4.671  1.00 23.19           N  
ATOM   2466  CA  LYS B 126      35.264  78.787   5.189  1.00 22.51           C  
ATOM   2467  C   LYS B 126      34.323  77.705   5.629  1.00 24.21           C  
ATOM   2468  O   LYS B 126      34.462  76.486   5.281  1.00 24.68           O  
ATOM   2469  CB  LYS B 126      34.600  79.596   4.108  1.00 22.27           C  
ATOM   2470  CG  LYS B 126      34.129  78.741   2.984  1.00 22.95           C  
ATOM   2471  CD  LYS B 126      33.850  79.564   1.794  1.00 24.19           C  
ATOM   2472  CE  LYS B 126      34.331  78.898   0.487  1.00 25.55           C  
ATOM   2473  NZ  LYS B 126      33.568  77.739  -0.098  1.00 27.22           N  
ATOM   2474  N   SER B 127      33.352  78.153   6.421  1.00 23.41           N  
ATOM   2475  CA  SER B 127      32.304  77.287   6.860  1.00 22.44           C  
ATOM   2476  C   SER B 127      31.193  78.078   6.312  1.00 23.31           C  
ATOM   2477  O   SER B 127      30.832  79.051   6.915  1.00 25.26           O  
ATOM   2478  CB  SER B 127      32.251  77.262   8.342  1.00 20.96           C  
ATOM   2479  OG  SER B 127      33.388  76.583   8.790  1.00 21.41           O  
ATOM   2480  N   GLU B 128      30.678  77.687   5.146  1.00 23.69           N  
ATOM   2481  CA  GLU B 128      29.599  78.424   4.458  1.00 22.88           C  
ATOM   2482  C   GLU B 128      28.264  77.733   4.335  1.00 22.29           C  
ATOM   2483  O   GLU B 128      28.192  76.617   3.785  1.00 22.91           O  
ATOM   2484  CB  GLU B 128      30.075  78.768   3.042  1.00 23.12           C  
ATOM   2485  CG  GLU B 128      29.008  79.226   2.053  1.00 22.21           C  
ATOM   2486  CD  GLU B 128      29.547  79.299   0.632  1.00 22.93           C  
ATOM   2487  OE1 GLU B 128      29.945  78.219   0.107  1.00 22.59           O  
ATOM   2488  OE2 GLU B 128      29.568  80.424   0.063  1.00 21.64           O  
ATOM   2489  N   PHE B 129      27.218  78.404   4.810  1.00 21.05           N  
ATOM   2490  CA  PHE B 129      25.846  77.883   4.716  1.00 20.12           C  
ATOM   2491  C   PHE B 129      24.926  78.902   4.077  1.00 19.49           C  
ATOM   2492  O   PHE B 129      25.174  80.090   4.211  1.00 20.87           O  
ATOM   2493  CB  PHE B 129      25.313  77.558   6.087  1.00 19.57           C  
ATOM   2494  CG  PHE B 129      26.225  76.725   6.876  1.00 20.20           C  
ATOM   2495  CD1 PHE B 129      26.967  77.270   7.899  1.00 21.57           C  
ATOM   2496  CD2 PHE B 129      26.350  75.398   6.610  1.00 19.22           C  
ATOM   2497  CE1 PHE B 129      27.813  76.494   8.647  1.00 21.31           C  
ATOM   2498  CE2 PHE B 129      27.196  74.620   7.346  1.00 20.61           C  
ATOM   2499  CZ  PHE B 129      27.927  75.161   8.369  1.00 21.55           C  
ATOM   2500  N   ALA B 130      23.879  78.477   3.374  1.00 18.53           N  
ATOM   2501  CA  ALA B 130      22.965  79.449   2.780  1.00 18.21           C  
ATOM   2502  C   ALA B 130      21.556  78.946   2.729  1.00 18.40           C  
ATOM   2503  O   ALA B 130      21.322  77.779   2.891  1.00 19.14           O  
ATOM   2504  CB  ALA B 130      23.401  79.823   1.443  1.00 17.22           C  
ATOM   2505  N   PHE B 131      20.598  79.836   2.525  1.00 18.97           N  
ATOM   2506  CA  PHE B 131      19.203  79.412   2.453  1.00 19.61           C  
ATOM   2507  C   PHE B 131      18.462  80.088   1.326  1.00 20.40           C  
ATOM   2508  O   PHE B 131      18.868  81.171   0.887  1.00 22.37           O  
ATOM   2509  CB  PHE B 131      18.482  79.765   3.728  1.00 18.09           C  
ATOM   2510  CG  PHE B 131      19.118  79.215   4.894  1.00 18.69           C  
ATOM   2511  CD1 PHE B 131      18.737  78.007   5.390  1.00 18.48           C  
ATOM   2512  CD2 PHE B 131      20.124  79.910   5.533  1.00 18.07           C  
ATOM   2513  CE1 PHE B 131      19.373  77.496   6.547  1.00 19.76           C  
ATOM   2514  CE2 PHE B 131      20.752  79.407   6.680  1.00 18.18           C  
ATOM   2515  CZ  PHE B 131      20.393  78.209   7.197  1.00 17.71           C  
ATOM   2516  N   VAL B 132      17.407  79.423   0.854  1.00 20.24           N  
ATOM   2517  CA  VAL B 132      16.466  79.949  -0.123  1.00 20.32           C  
ATOM   2518  C   VAL B 132      15.107  79.823   0.595  1.00 21.50           C  
ATOM   2519  O   VAL B 132      14.536  78.710   0.607  1.00 22.12           O  
ATOM   2520  CB  VAL B 132      16.422  79.082  -1.285  1.00 19.38           C  
ATOM   2521  CG1 VAL B 132      15.284  79.477  -2.123  1.00 18.93           C  
ATOM   2522  CG2 VAL B 132      17.719  79.190  -2.014  1.00 18.79           C  
ATOM   2523  N   PHE B 133      14.626  80.907   1.219  1.00 20.89           N  
ATOM   2524  CA  PHE B 133      13.361  80.923   1.982  1.00 22.37           C  
ATOM   2525  C   PHE B 133      12.189  81.354   1.079  1.00 24.64           C  
ATOM   2526  O   PHE B 133      12.299  82.342   0.345  1.00 27.40           O  
ATOM   2527  CB  PHE B 133      13.435  81.960   3.122  1.00 21.64           C  
ATOM   2528  CG  PHE B 133      14.370  81.593   4.315  1.00 21.34           C  
ATOM   2529  CD1 PHE B 133      14.020  80.613   5.243  1.00 20.23           C  
ATOM   2530  CD2 PHE B 133      15.534  82.310   4.553  1.00 19.46           C  
ATOM   2531  CE1 PHE B 133      14.775  80.387   6.328  1.00 17.99           C  
ATOM   2532  CE2 PHE B 133      16.270  82.068   5.633  1.00 18.09           C  
ATOM   2533  CZ  PHE B 133      15.881  81.112   6.514  1.00 18.46           C  
ATOM   2534  N   SER B 134      11.045  80.688   1.110  1.00 24.91           N  
ATOM   2535  CA  SER B 134       9.967  81.145   0.234  1.00 25.54           C  
ATOM   2536  C   SER B 134       8.751  81.253   1.078  1.00 25.78           C  
ATOM   2537  O   SER B 134       8.699  80.597   2.105  1.00 25.31           O  
ATOM   2538  CB  SER B 134       9.712  80.131  -0.858  1.00 27.33           C  
ATOM   2539  OG  SER B 134       8.478  80.336  -1.548  1.00 30.17           O  
ATOM   2540  N   ARG B 135       7.776  82.064   0.665  1.00 26.59           N  
ATOM   2541  CA  ARG B 135       6.566  82.191   1.452  1.00 27.89           C  
ATOM   2542  C   ARG B 135       5.598  81.151   1.104  1.00 29.90           C  
ATOM   2543  O   ARG B 135       4.578  81.094   1.734  1.00 30.74           O  
ATOM   2544  CB  ARG B 135       5.866  83.484   1.257  1.00 28.02           C  
ATOM   2545  CG  ARG B 135       6.600  84.695   1.738  1.00 29.79           C  
ATOM   2546  CD  ARG B 135       6.597  84.814   3.226  1.00 29.03           C  
ATOM   2547  NE  ARG B 135       6.909  86.184   3.577  1.00 27.38           N  
ATOM   2548  CZ  ARG B 135       7.172  86.575   4.808  1.00 28.33           C  
ATOM   2549  NH1 ARG B 135       7.183  85.704   5.816  1.00 28.16           N  
ATOM   2550  NH2 ARG B 135       7.363  87.853   5.051  1.00 29.59           N  
ATOM   2551  N   THR B 136       5.893  80.350   0.087  1.00 32.56           N  
ATOM   2552  CA  THR B 136       5.038  79.222  -0.320  1.00 35.46           C  
ATOM   2553  C   THR B 136       5.892  77.988  -0.102  1.00 36.89           C  
ATOM   2554  O   THR B 136       7.058  78.072  -0.305  1.00 36.71           O  
ATOM   2555  CB  THR B 136       4.664  79.271  -1.812  1.00 35.90           C  
ATOM   2556  OG1 THR B 136       5.808  79.644  -2.598  1.00 37.69           O  
ATOM   2557  CG2 THR B 136       3.577  80.249  -2.023  1.00 36.22           C  
ATOM   2558  N   PRO B 137       5.312  76.830   0.280  1.00 38.79           N  
ATOM   2559  CA  PRO B 137       6.065  75.595   0.522  1.00 40.68           C  
ATOM   2560  C   PRO B 137       6.138  74.829  -0.749  1.00 43.27           C  
ATOM   2561  O   PRO B 137       5.926  73.620  -0.805  1.00 43.40           O  
ATOM   2562  CB  PRO B 137       5.249  74.902   1.579  1.00 39.41           C  
ATOM   2563  CG  PRO B 137       3.821  75.262   1.149  1.00 39.66           C  
ATOM   2564  CD  PRO B 137       3.861  76.574   0.384  1.00 39.73           C  
ATOM   2565  N   GLN B 138       6.441  75.587  -1.780  1.00 47.12           N  
ATOM   2566  CA  GLN B 138       6.571  75.080  -3.114  1.00 52.51           C  
ATOM   2567  C   GLN B 138       8.060  74.997  -3.393  1.00 53.50           C  
ATOM   2568  O   GLN B 138       8.752  76.019  -3.461  1.00 54.35           O  
ATOM   2569  CB  GLN B 138       5.888  76.059  -4.075  1.00 57.18           C  
ATOM   2570  CG  GLN B 138       4.984  75.396  -5.172  1.00 64.66           C  
ATOM   2571  CD  GLN B 138       3.519  75.100  -4.704  1.00 68.90           C  
ATOM   2572  OE1 GLN B 138       3.240  74.134  -3.908  1.00 69.57           O  
ATOM   2573  NE2 GLN B 138       2.569  75.950  -5.195  1.00 70.76           N  
ATOM   2574  N   THR B 139       8.573  73.792  -3.571  1.00 54.77           N  
ATOM   2575  CA  THR B 139      10.009  73.679  -3.789  1.00 55.86           C  
ATOM   2576  C   THR B 139      10.487  73.995  -5.202  1.00 56.95           C  
ATOM   2577  O   THR B 139      11.674  74.119  -5.450  1.00 56.80           O  
ATOM   2578  CB  THR B 139      10.564  72.294  -3.333  1.00 55.45           C  
ATOM   2579  OG1 THR B 139      11.529  71.882  -4.277  1.00 55.70           O  
ATOM   2580  CG2 THR B 139       9.476  71.201  -3.215  1.00 56.10           C  
ATOM   2581  N   SER B 140       9.556  74.143  -6.132  1.00 58.62           N  
ATOM   2582  CA  SER B 140       9.908  74.476  -7.508  1.00 60.09           C  
ATOM   2583  C   SER B 140       9.410  75.898  -7.874  1.00 60.18           C  
ATOM   2584  O   SER B 140       9.674  76.399  -8.995  1.00 60.84           O  
ATOM   2585  CB  SER B 140       9.290  73.447  -8.459  1.00 61.34           C  
ATOM   2586  OG  SER B 140       9.234  73.965  -9.788  1.00 63.99           O  
ATOM   2587  N   GLY B 141       8.706  76.514  -6.904  1.00 59.57           N  
ATOM   2588  CA  GLY B 141       8.108  77.850  -6.991  1.00 58.33           C  
ATOM   2589  C   GLY B 141       8.898  79.050  -7.525  1.00 57.66           C  
ATOM   2590  O   GLY B 141       9.974  78.915  -8.128  1.00 57.92           O  
ATOM   2591  N   PRO B 142       8.398  80.271  -7.298  1.00 56.56           N  
ATOM   2592  CA  PRO B 142       9.206  81.355  -7.865  1.00 54.87           C  
ATOM   2593  C   PRO B 142      10.414  81.746  -7.057  1.00 53.06           C  
ATOM   2594  O   PRO B 142      11.251  82.478  -7.571  1.00 54.48           O  
ATOM   2595  CB  PRO B 142       8.212  82.496  -8.004  1.00 55.72           C  
ATOM   2596  CG  PRO B 142       7.300  82.283  -6.722  1.00 56.48           C  
ATOM   2597  CD  PRO B 142       7.185  80.760  -6.596  1.00 56.54           C  
ATOM   2598  N   ALA B 143      10.510  81.272  -5.811  1.00 49.88           N  
ATOM   2599  CA  ALA B 143      11.635  81.596  -4.924  1.00 46.54           C  
ATOM   2600  C   ALA B 143      12.973  81.110  -5.487  1.00 44.30           C  
ATOM   2601  O   ALA B 143      13.899  81.863  -5.725  1.00 42.12           O  
ATOM   2602  CB  ALA B 143      11.394  80.952  -3.599  1.00 47.09           C  
ATOM   2603  N   VAL B 144      13.052  79.811  -5.678  1.00 42.76           N  
ATOM   2604  CA  VAL B 144      14.226  79.209  -6.226  1.00 41.66           C  
ATOM   2605  C   VAL B 144      14.705  79.913  -7.424  1.00 43.01           C  
ATOM   2606  O   VAL B 144      15.865  80.183  -7.513  1.00 43.98           O  
ATOM   2607  CB  VAL B 144      13.991  77.843  -6.699  1.00 39.05           C  
ATOM   2608  CG1 VAL B 144      15.247  77.222  -6.898  1.00 37.82           C  
ATOM   2609  CG2 VAL B 144      13.203  77.078  -5.716  1.00 39.18           C  
ATOM   2610  N   GLU B 145      13.824  80.207  -8.368  1.00 44.90           N  
ATOM   2611  CA  GLU B 145      14.243  80.858  -9.620  1.00 47.00           C  
ATOM   2612  C   GLU B 145      14.996  82.112  -9.391  1.00 45.32           C  
ATOM   2613  O   GLU B 145      16.095  82.339  -9.912  1.00 45.40           O  
ATOM   2614  CB  GLU B 145      13.046  81.221 -10.517  1.00 52.18           C  
ATOM   2615  CG  GLU B 145      13.228  80.732 -12.010  1.00 59.83           C  
ATOM   2616  CD  GLU B 145      13.375  79.129 -12.127  1.00 65.06           C  
ATOM   2617  OE1 GLU B 145      12.322  78.375 -11.859  1.00 65.69           O  
ATOM   2618  OE2 GLU B 145      14.558  78.667 -12.469  1.00 66.55           O  
ATOM   2619  N   LYS B 146      14.318  82.928  -8.608  1.00 43.05           N  
ATOM   2620  CA  LYS B 146      14.726  84.246  -8.200  1.00 40.12           C  
ATOM   2621  C   LYS B 146      16.027  84.243  -7.431  1.00 36.95           C  
ATOM   2622  O   LYS B 146      16.967  84.915  -7.812  1.00 37.39           O  
ATOM   2623  CB  LYS B 146      13.602  84.829  -7.331  1.00 41.32           C  
ATOM   2624  CG  LYS B 146      13.672  86.289  -7.066  1.00 42.82           C  
ATOM   2625  CD  LYS B 146      13.471  87.098  -8.333  1.00 47.01           C  
ATOM   2626  CE  LYS B 146      12.091  86.855  -9.018  1.00 48.19           C  
ATOM   2627  NZ  LYS B 146      11.603  88.089  -9.788  1.00 49.27           N  
ATOM   2628  N   THR B 147      16.050  83.464  -6.359  1.00 33.04           N  
ATOM   2629  CA  THR B 147      17.138  83.389  -5.417  1.00 28.43           C  
ATOM   2630  C   THR B 147      18.403  82.730  -6.018  1.00 27.93           C  
ATOM   2631  O   THR B 147      19.525  83.184  -5.787  1.00 27.82           O  
ATOM   2632  CB  THR B 147      16.571  82.672  -4.115  1.00 27.03           C  
ATOM   2633  OG1 THR B 147      15.900  83.580  -3.237  1.00 21.05           O  
ATOM   2634  CG2 THR B 147      17.623  82.107  -3.352  1.00 29.06           C  
ATOM   2635  N   ALA B 148      18.249  81.689  -6.829  1.00 26.45           N  
ATOM   2636  CA  ALA B 148      19.431  81.051  -7.395  1.00 25.56           C  
ATOM   2637  C   ALA B 148      20.141  82.075  -8.216  1.00 25.49           C  
ATOM   2638  O   ALA B 148      21.318  82.033  -8.378  1.00 26.19           O  
ATOM   2639  CB  ALA B 148      19.071  79.876  -8.225  1.00 23.74           C  
ATOM   2640  N   ALA B 149      19.405  83.017  -8.750  1.00 26.01           N  
ATOM   2641  CA  ALA B 149      20.016  84.095  -9.511  1.00 26.38           C  
ATOM   2642  C   ALA B 149      20.848  84.902  -8.561  1.00 26.30           C  
ATOM   2643  O   ALA B 149      22.013  85.075  -8.742  1.00 27.87           O  
ATOM   2644  CB  ALA B 149      18.961  85.017 -10.076  1.00 27.85           C  
ATOM   2645  N   VAL B 150      20.220  85.438  -7.542  1.00 26.00           N  
ATOM   2646  CA  VAL B 150      20.911  86.275  -6.604  1.00 24.76           C  
ATOM   2647  C   VAL B 150      22.183  85.660  -6.077  1.00 24.27           C  
ATOM   2648  O   VAL B 150      23.234  86.320  -6.072  1.00 23.04           O  
ATOM   2649  CB  VAL B 150      20.003  86.586  -5.482  1.00 24.70           C  
ATOM   2650  CG1 VAL B 150      20.634  87.553  -4.562  1.00 26.28           C  
ATOM   2651  CG2 VAL B 150      18.819  87.124  -5.991  1.00 23.86           C  
ATOM   2652  N   PHE B 151      22.090  84.411  -5.622  1.00 23.82           N  
ATOM   2653  CA  PHE B 151      23.262  83.742  -5.117  1.00 24.60           C  
ATOM   2654  C   PHE B 151      24.386  83.639  -6.141  1.00 26.36           C  
ATOM   2655  O   PHE B 151      25.545  83.921  -5.829  1.00 27.21           O  
ATOM   2656  CB  PHE B 151      22.912  82.382  -4.657  1.00 23.43           C  
ATOM   2657  CG  PHE B 151      22.409  82.347  -3.283  1.00 22.19           C  
ATOM   2658  CD1 PHE B 151      21.198  81.757  -2.995  1.00 22.39           C  
ATOM   2659  CD2 PHE B 151      23.142  82.869  -2.280  1.00 20.76           C  
ATOM   2660  CE1 PHE B 151      20.741  81.699  -1.733  1.00 21.70           C  
ATOM   2661  CE2 PHE B 151      22.693  82.809  -1.035  1.00 21.69           C  
ATOM   2662  CZ  PHE B 151      21.480  82.221  -0.750  1.00 21.52           C  
ATOM   2663  N   ASN B 152      24.079  83.230  -7.366  1.00 27.54           N  
ATOM   2664  CA  ASN B 152      25.127  83.177  -8.362  1.00 29.00           C  
ATOM   2665  C   ASN B 152      25.749  84.542  -8.567  1.00 30.77           C  
ATOM   2666  O   ASN B 152      26.939  84.670  -8.482  1.00 31.92           O  
ATOM   2667  CB  ASN B 152      24.599  82.644  -9.662  1.00 28.12           C  
ATOM   2668  CG  ASN B 152      24.263  81.221  -9.554  1.00 29.07           C  
ATOM   2669  OD1 ASN B 152      24.977  80.477  -8.907  1.00 30.44           O  
ATOM   2670  ND2 ASN B 152      23.184  80.805 -10.178  1.00 29.72           N  
ATOM   2671  N   LYS B 153      24.958  85.577  -8.800  1.00 32.53           N  
ATOM   2672  CA  LYS B 153      25.502  86.901  -9.034  1.00 33.82           C  
ATOM   2673  C   LYS B 153      26.357  87.396  -7.840  1.00 33.33           C  
ATOM   2674  O   LYS B 153      27.131  88.407  -7.936  1.00 33.51           O  
ATOM   2675  CB  LYS B 153      24.350  87.875  -9.284  1.00 37.10           C  
ATOM   2676  CG  LYS B 153      23.343  87.523 -10.387  1.00 41.97           C  
ATOM   2677  CD  LYS B 153      22.277  88.680 -10.550  1.00 47.75           C  
ATOM   2678  CE  LYS B 153      21.392  88.607 -11.861  1.00 50.43           C  
ATOM   2679  NZ  LYS B 153      21.422  89.972 -12.600  1.00 52.97           N  
ATOM   2680  N   ASN B 154      26.216  86.707  -6.706  1.00 31.18           N  
ATOM   2681  CA  ASN B 154      26.967  87.117  -5.540  1.00 30.00           C  
ATOM   2682  C   ASN B 154      28.175  86.265  -5.178  1.00 29.23           C  
ATOM   2683  O   ASN B 154      29.005  86.617  -4.329  1.00 28.99           O  
ATOM   2684  CB  ASN B 154      26.013  87.267  -4.406  1.00 30.20           C  
ATOM   2685  CG  ASN B 154      25.362  88.591  -4.425  1.00 30.68           C  
ATOM   2686  OD1 ASN B 154      26.002  89.599  -4.134  1.00 31.41           O  
ATOM   2687  ND2 ASN B 154      24.090  88.625  -4.804  1.00 30.91           N  
ATOM   2688  N   GLY B 155      28.270  85.156  -5.879  1.00 27.92           N  
ATOM   2689  CA  GLY B 155      29.388  84.298  -5.713  1.00 26.90           C  
ATOM   2690  C   GLY B 155      29.102  83.043  -4.957  1.00 26.89           C  
ATOM   2691  O   GLY B 155      30.058  82.440  -4.452  1.00 30.13           O  
ATOM   2692  N   VAL B 156      27.866  82.597  -4.847  1.00 23.73           N  
ATOM   2693  CA  VAL B 156      27.678  81.377  -4.098  1.00 21.21           C  
ATOM   2694  C   VAL B 156      27.088  80.468  -5.138  1.00 20.80           C  
ATOM   2695  O   VAL B 156      25.952  80.614  -5.444  1.00 22.00           O  
ATOM   2696  CB  VAL B 156      26.731  81.677  -2.895  1.00 20.99           C  
ATOM   2697  CG1 VAL B 156      26.516  80.471  -2.007  1.00 20.71           C  
ATOM   2698  CG2 VAL B 156      27.294  82.786  -2.087  1.00 18.94           C  
ATOM   2699  N   GLU B 157      27.824  79.537  -5.708  1.00 20.62           N  
ATOM   2700  CA  GLU B 157      27.250  78.706  -6.761  1.00 21.49           C  
ATOM   2701  C   GLU B 157      25.990  78.057  -6.392  1.00 20.40           C  
ATOM   2702  O   GLU B 157      25.956  77.387  -5.387  1.00 19.01           O  
ATOM   2703  CB  GLU B 157      28.180  77.607  -7.118  1.00 25.72           C  
ATOM   2704  CG  GLU B 157      29.471  78.077  -7.704  1.00 34.30           C  
ATOM   2705  CD  GLU B 157      30.649  78.232  -6.711  1.00 39.10           C  
ATOM   2706  OE1 GLU B 157      31.444  77.228  -6.642  1.00 42.90           O  
ATOM   2707  OE2 GLU B 157      30.793  79.333  -6.046  1.00 41.45           O  
ATOM   2708  N   PHE B 158      24.956  78.163  -7.211  1.00 20.66           N  
ATOM   2709  CA  PHE B 158      23.708  77.534  -6.792  1.00 22.06           C  
ATOM   2710  C   PHE B 158      23.747  76.028  -6.761  1.00 23.29           C  
ATOM   2711  O   PHE B 158      22.894  75.362  -6.137  1.00 22.93           O  
ATOM   2712  CB  PHE B 158      22.497  77.972  -7.616  1.00 21.37           C  
ATOM   2713  CG  PHE B 158      21.178  77.697  -6.904  1.00 20.33           C  
ATOM   2714  CD1 PHE B 158      20.909  78.272  -5.687  1.00 19.76           C  
ATOM   2715  CD2 PHE B 158      20.257  76.796  -7.406  1.00 19.76           C  
ATOM   2716  CE1 PHE B 158      19.747  77.946  -4.983  1.00 20.88           C  
ATOM   2717  CE2 PHE B 158      19.090  76.461  -6.707  1.00 19.35           C  
ATOM   2718  CZ  PHE B 158      18.834  77.029  -5.505  1.00 19.63           C  
ATOM   2719  N   SER B 159      24.752  75.487  -7.432  1.00 25.10           N  
ATOM   2720  CA  SER B 159      24.920  74.037  -7.499  1.00 27.16           C  
ATOM   2721  C   SER B 159      25.191  73.444  -6.119  1.00 28.52           C  
ATOM   2722  O   SER B 159      24.852  72.271  -5.855  1.00 30.49           O  
ATOM   2723  CB  SER B 159      26.071  73.684  -8.456  1.00 27.98           C  
ATOM   2724  OG  SER B 159      27.294  74.386  -8.187  1.00 27.92           O  
ATOM   2725  N   LYS B 160      25.803  74.280  -5.259  1.00 28.36           N  
ATOM   2726  CA  LYS B 160      26.190  73.954  -3.900  1.00 26.96           C  
ATOM   2727  C   LYS B 160      24.940  73.606  -3.131  1.00 27.97           C  
ATOM   2728  O   LYS B 160      25.052  72.933  -2.134  1.00 30.44           O  
ATOM   2729  CB  LYS B 160      26.886  75.154  -3.247  1.00 24.56           C  
ATOM   2730  CG  LYS B 160      28.433  75.198  -3.318  1.00 26.00           C  
ATOM   2731  CD  LYS B 160      29.041  76.683  -3.122  1.00 27.02           C  
ATOM   2732  CE  LYS B 160      30.601  76.849  -2.951  1.00 27.98           C  
ATOM   2733  NZ  LYS B 160      31.220  78.306  -2.978  1.00 30.05           N  
ATOM   2734  N   PHE B 161      23.748  74.021  -3.579  1.00 27.48           N  
ATOM   2735  CA  PHE B 161      22.515  73.785  -2.818  1.00 27.26           C  
ATOM   2736  C   PHE B 161      21.726  72.502  -3.087  1.00 28.02           C  
ATOM   2737  O   PHE B 161      21.781  71.966  -4.181  1.00 30.30           O  
ATOM   2738  CB  PHE B 161      21.532  74.914  -3.077  1.00 27.98           C  
ATOM   2739  CG  PHE B 161      21.930  76.263  -2.579  1.00 27.68           C  
ATOM   2740  CD1 PHE B 161      21.239  76.849  -1.552  1.00 27.30           C  
ATOM   2741  CD2 PHE B 161      22.914  76.996  -3.204  1.00 28.27           C  
ATOM   2742  CE1 PHE B 161      21.523  78.151  -1.160  1.00 28.03           C  
ATOM   2743  CE2 PHE B 161      23.203  78.327  -2.798  1.00 28.78           C  
ATOM   2744  CZ  PHE B 161      22.511  78.895  -1.790  1.00 27.61           C  
ATOM   2745  N   VAL B 162      20.979  72.006  -2.110  1.00 27.73           N  
ATOM   2746  CA  VAL B 162      20.122  70.857  -2.357  1.00 29.24           C  
ATOM   2747  C   VAL B 162      18.709  71.283  -2.000  1.00 31.63           C  
ATOM   2748  O   VAL B 162      18.534  72.232  -1.243  1.00 34.46           O  
ATOM   2749  CB  VAL B 162      20.396  69.694  -1.467  1.00 28.14           C  
ATOM   2750  CG1 VAL B 162      21.753  69.154  -1.671  1.00 28.87           C  
ATOM   2751  CG2 VAL B 162      20.203  70.090  -0.131  1.00 28.42           C  
ATOM   2752  N   PRO B 163      17.675  70.612  -2.516  1.00 32.65           N  
ATOM   2753  CA  PRO B 163      16.296  70.991  -2.186  1.00 33.72           C  
ATOM   2754  C   PRO B 163      15.797  70.311  -0.917  1.00 35.12           C  
ATOM   2755  O   PRO B 163      16.192  69.187  -0.637  1.00 37.08           O  
ATOM   2756  CB  PRO B 163      15.535  70.517  -3.365  1.00 33.80           C  
ATOM   2757  CG  PRO B 163      16.273  69.234  -3.681  1.00 34.47           C  
ATOM   2758  CD  PRO B 163      17.688  69.725  -3.676  1.00 33.70           C  
ATOM   2759  N   VAL B 164      14.935  70.992  -0.167  1.00 35.43           N  
ATOM   2760  CA  VAL B 164      14.407  70.517   1.082  1.00 36.81           C  
ATOM   2761  C   VAL B 164      13.158  69.985   0.616  1.00 39.08           C  
ATOM   2762  O   VAL B 164      12.436  70.691  -0.037  1.00 40.03           O  
ATOM   2763  CB  VAL B 164      14.016  71.647   1.990  1.00 36.82           C  
ATOM   2764  CG1 VAL B 164      13.809  71.167   3.376  1.00 37.13           C  
ATOM   2765  CG2 VAL B 164      15.051  72.661   2.005  1.00 37.74           C  
ATOM   2766  N   SER B 165      12.857  68.755   0.957  1.00 42.10           N  
ATOM   2767  CA  SER B 165      11.607  68.181   0.490  1.00 45.30           C  
ATOM   2768  C   SER B 165      10.342  68.630   1.205  1.00 46.17           C  
ATOM   2769  O   SER B 165      10.243  68.550   2.431  1.00 45.56           O  
ATOM   2770  CB  SER B 165      11.667  66.666   0.575  1.00 46.28           C  
ATOM   2771  OG  SER B 165      10.472  66.172   1.189  1.00 49.19           O  
ATOM   2772  N   HIS B 166       9.364  69.075   0.429  1.00 48.27           N  
ATOM   2773  CA  HIS B 166       8.079  69.461   1.011  1.00 50.50           C  
ATOM   2774  C   HIS B 166       7.026  68.633   0.283  1.00 53.54           C  
ATOM   2775  O   HIS B 166       6.700  68.914  -0.871  1.00 55.34           O  
ATOM   2776  CB  HIS B 166       7.803  70.954   0.812  1.00 48.01           C  
ATOM   2777  CG  HIS B 166       8.665  71.855   1.643  1.00 44.28           C  
ATOM   2778  ND1 HIS B 166       8.309  72.264   2.908  1.00 42.82           N  
ATOM   2779  CD2 HIS B 166       9.874  72.406   1.391  1.00 42.42           C  
ATOM   2780  CE1 HIS B 166       9.267  73.024   3.402  1.00 42.19           C  
ATOM   2781  NE2 HIS B 166      10.225  73.128   2.502  1.00 42.02           N  
ATOM   2782  N   THR B 167       6.502  67.614   0.953  1.00 56.33           N  
ATOM   2783  CA  THR B 167       5.534  66.728   0.337  1.00 59.06           C  
ATOM   2784  C   THR B 167       4.244  66.513   1.099  1.00 61.44           C  
ATOM   2785  O   THR B 167       3.788  67.367   1.840  1.00 62.73           O  
ATOM   2786  CB  THR B 167       6.131  65.400   0.142  1.00 58.54           C  
ATOM   2787  OG1 THR B 167       6.745  64.980   1.381  1.00 59.32           O  
ATOM   2788  CG2 THR B 167       7.103  65.470  -0.995  1.00 58.63           C  
ATOM   2789  N   ALA B 168       3.650  65.346   0.890  1.00 63.34           N  
ATOM   2790  CA  ALA B 168       2.395  64.963   1.530  1.00 64.15           C  
ATOM   2791  C   ALA B 168       2.589  64.884   3.045  1.00 64.28           C  
ATOM   2792  O   ALA B 168       1.732  65.278   3.845  1.00 64.45           O  
ATOM   2793  CB  ALA B 168       1.942  63.570   0.966  1.00 64.94           C  
ATOM   2794  N   GLU B 169       3.759  64.411   3.421  1.00 64.28           N  
ATOM   2795  CA  GLU B 169       4.060  64.213   4.802  1.00 64.81           C  
ATOM   2796  C   GLU B 169       4.078  65.446   5.693  1.00 62.42           C  
ATOM   2797  O   GLU B 169       3.850  65.334   6.906  1.00 61.94           O  
ATOM   2798  CB  GLU B 169       5.391  63.456   4.895  1.00 68.99           C  
ATOM   2799  CG  GLU B 169       5.614  62.687   6.257  1.00 76.98           C  
ATOM   2800  CD  GLU B 169       4.325  61.975   6.864  1.00 81.29           C  
ATOM   2801  OE1 GLU B 169       3.757  61.029   6.186  1.00 81.79           O  
ATOM   2802  OE2 GLU B 169       3.913  62.383   8.027  1.00 83.47           O  
ATOM   2803  N   CYS B 170       4.286  66.621   5.103  1.00 59.52           N  
ATOM   2804  CA  CYS B 170       4.430  67.837   5.888  1.00 56.64           C  
ATOM   2805  C   CYS B 170       3.415  68.225   6.879  1.00 54.95           C  
ATOM   2806  O   CYS B 170       2.256  67.997   6.665  1.00 55.55           O  
ATOM   2807  CB  CYS B 170       4.667  69.002   4.985  1.00 56.54           C  
ATOM   2808  SG  CYS B 170       6.327  68.906   4.246  1.00 58.44           S  
ATOM   2809  N   VAL B 171       3.864  68.814   7.979  1.00 53.00           N  
ATOM   2810  CA  VAL B 171       2.963  69.276   9.030  1.00 50.86           C  
ATOM   2811  C   VAL B 171       3.512  70.592   9.473  1.00 49.93           C  
ATOM   2812  O   VAL B 171       4.466  70.615  10.270  1.00 49.97           O  
ATOM   2813  CB  VAL B 171       3.008  68.419  10.320  1.00 50.69           C  
ATOM   2814  CG1 VAL B 171       1.914  68.864  11.289  1.00 50.26           C  
ATOM   2815  CG2 VAL B 171       2.878  66.982  10.000  1.00 50.89           C  
ATOM   2816  N   TYR B 172       2.920  71.686   9.012  1.00 47.77           N  
ATOM   2817  CA  TYR B 172       3.435  72.998   9.416  1.00 46.11           C  
ATOM   2818  C   TYR B 172       2.846  73.594  10.730  1.00 47.73           C  
ATOM   2819  O   TYR B 172       1.936  74.457  10.679  1.00 48.80           O  
ATOM   2820  CB  TYR B 172       3.260  73.991   8.259  1.00 41.07           C  
ATOM   2821  CG  TYR B 172       3.824  73.509   6.954  1.00 36.15           C  
ATOM   2822  CD1 TYR B 172       5.032  72.858   6.900  1.00 35.26           C  
ATOM   2823  CD2 TYR B 172       3.153  73.675   5.779  1.00 34.22           C  
ATOM   2824  CE1 TYR B 172       5.560  72.373   5.676  1.00 33.47           C  
ATOM   2825  CE2 TYR B 172       3.684  73.190   4.565  1.00 32.27           C  
ATOM   2826  CZ  TYR B 172       4.872  72.553   4.535  1.00 31.44           C  
ATOM   2827  OH  TYR B 172       5.401  72.099   3.386  1.00 30.28           O  
ATOM   2828  N   ARG B 173       3.356  73.165  11.897  1.00 48.73           N  
ATOM   2829  CA  ARG B 173       2.836  73.692  13.165  1.00 50.28           C  
ATOM   2830  C   ARG B 173       3.566  74.876  13.696  1.00 50.00           C  
ATOM   2831  O   ARG B 173       2.971  75.638  14.434  1.00 51.08           O  
ATOM   2832  CB  ARG B 173       2.877  72.699  14.306  1.00 52.53           C  
ATOM   2833  CG  ARG B 173       1.890  71.555  14.274  1.00 56.53           C  
ATOM   2834  CD  ARG B 173       1.709  71.099  15.689  1.00 58.90           C  
ATOM   2835  NE  ARG B 173       2.049  72.264  16.504  1.00 62.72           N  
ATOM   2836  CZ  ARG B 173       1.708  72.418  17.778  1.00 64.86           C  
ATOM   2837  NH1 ARG B 173       0.994  71.465  18.419  1.00 65.89           N  
ATOM   2838  NH2 ARG B 173       2.082  73.530  18.401  1.00 64.97           N  
ATOM   2839  N   ALA B 174       4.849  75.020  13.379  1.00 48.85           N  
ATOM   2840  CA  ALA B 174       5.599  76.150  13.892  1.00 48.40           C  
ATOM   2841  C   ALA B 174       4.789  77.434  14.004  1.00 49.56           C  
ATOM   2842  O   ALA B 174       4.079  77.820  13.039  1.00 49.96           O  
ATOM   2843  CB  ALA B 174       6.749  76.393  13.066  1.00 47.59           C  
ATOM   2844  OXT ALA B 174       4.883  78.058  15.091  1.00 51.07           O  
TER    2845      ALA B 174                                                      
HETATM 2846  C1  AXT A1182      45.684  74.744  25.227  1.00 35.26           C  
HETATM 2847  C2  AXT A1182      46.158  74.389  26.637  1.00 36.78           C  
HETATM 2848  C3  AXT A1182      47.309  73.415  26.609  1.00 38.62           C  
HETATM 2849  C4  AXT A1182      48.453  74.088  25.828  1.00 38.88           C  
HETATM 2850  C5  AXT A1182      48.142  74.975  24.705  1.00 37.41           C  
HETATM 2851  C6  AXT A1182      46.847  75.290  24.356  1.00 35.69           C  
HETATM 2852  C7  AXT A1182      46.670  76.134  23.191  1.00 34.10           C  
HETATM 2853  C8  AXT A1182      45.452  76.439  22.611  1.00 31.63           C  
HETATM 2854  C9  AXT A1182      45.339  77.267  21.524  1.00 30.49           C  
HETATM 2855  C10 AXT A1182      44.038  77.552  21.111  1.00 30.66           C  
HETATM 2856  C11 AXT A1182      43.660  78.421  20.051  1.00 30.69           C  
HETATM 2857  C12 AXT A1182      42.291  78.579  19.898  1.00 30.96           C  
HETATM 2858  C13 AXT A1182      41.645  79.410  18.959  1.00 32.52           C  
HETATM 2859  C14 AXT A1182      40.235  79.446  19.035  1.00 34.59           C  
HETATM 2860  C15 AXT A1182      39.400  80.275  18.217  1.00 35.40           C  
HETATM 2861  C16 AXT A1182      44.600  75.764  25.453  1.00 35.32           C  
HETATM 2862  C17 AXT A1182      45.057  73.508  24.618  1.00 34.31           C  
HETATM 2863  C18 AXT A1182      49.242  75.584  23.871  1.00 38.61           C  
HETATM 2864  C19 AXT A1182      46.556  77.874  20.875  1.00 28.56           C  
HETATM 2865  C20 AXT A1182      42.404  80.265  17.944  1.00 30.42           C  
HETATM 2866  O3  AXT A1182      47.726  73.073  27.955  1.00 39.11           O  
HETATM 2867  O4  AXT A1182      49.622  73.840  26.140  1.00 39.94           O  
HETATM 2868  C21 AXT A1182      32.088  87.486  12.660  1.00 26.29           C  
HETATM 2869  C22 AXT A1182      31.483  88.839  12.391  1.00 28.05           C  
HETATM 2870  C23 AXT A1182      30.226  88.754  11.558  1.00 29.82           C  
HETATM 2871  C24 AXT A1182      29.257  87.969  12.246  1.00 29.89           C  
HETATM 2872  C25 AXT A1182      29.678  86.930  13.111  1.00 29.25           C  
HETATM 2873  C26 AXT A1182      31.049  86.651  13.328  1.00 27.49           C  
HETATM 2874  C27 AXT A1182      31.348  85.568  14.170  1.00 28.83           C  
HETATM 2875  C28 AXT A1182      32.590  85.060  14.495  1.00 29.66           C  
HETATM 2876  C29 AXT A1182      32.668  83.996  15.373  1.00 30.20           C  
HETATM 2877  C30 AXT A1182      33.883  83.528  15.700  1.00 31.14           C  
HETATM 2878  C31 AXT A1182      34.057  82.488  16.579  1.00 31.45           C  
HETATM 2879  C32 AXT A1182      35.334  82.183  16.740  1.00 33.68           C  
HETATM 2880  C33 AXT A1182      35.824  81.230  17.582  1.00 33.99           C  
HETATM 2881  C34 AXT A1182      37.238  81.109  17.590  1.00 34.46           C  
HETATM 2882  C35 AXT A1182      38.008  80.244  18.377  1.00 34.59           C  
HETATM 2883  C36 AXT A1182      33.278  87.793  13.508  1.00 25.62           C  
HETATM 2884  C37 AXT A1182      32.544  86.785  11.408  1.00 26.34           C  
HETATM 2885  C38 AXT A1182      28.605  86.088  13.808  1.00 30.63           C  
HETATM 2886  C39 AXT A1182      31.414  83.386  15.953  1.00 30.11           C  
HETATM 2887  C40 AXT A1182      34.901  80.412  18.440  1.00 34.38           C  
HETATM 2888  O24 AXT A1182      28.086  88.223  12.032  1.00 30.64           O  
HETATM 2889  O23 AXT A1182      29.663  90.032  11.375  1.00 34.14           O  
HETATM 2890  C1  D12 A1183      34.375  76.469  21.655  1.00 81.85           C  
HETATM 2891  C2  D12 A1183      34.862  75.459  20.612  1.00 82.84           C  
HETATM 2892  C3  D12 A1183      36.332  75.707  20.382  1.00 82.42           C  
HETATM 2893  C4  D12 A1183      36.781  75.567  18.930  1.00 81.97           C  
HETATM 2894  C5  D12 A1183      38.308  75.923  18.821  1.00 80.99           C  
HETATM 2895  C6  D12 A1183      38.881  75.850  17.384  1.00 79.80           C  
HETATM 2896  C7  D12 A1183      38.624  77.101  16.522  1.00 78.25           C  
HETATM 2897  C8  D12 A1183      37.142  77.322  16.367  1.00 78.38           C  
HETATM 2898  C9  D12 A1183      36.780  78.364  15.370  1.00 79.07           C  
HETATM 2899  C10 D12 A1183      35.260  78.478  15.408  1.00 80.24           C  
HETATM 2900  C11 D12 A1183      34.782  79.553  14.457  1.00 80.97           C  
HETATM 2901  C12 D12 A1183      33.259  79.716  14.485  1.00 81.21           C  
HETATM 2902  C1  AXT B1175      19.585  76.868  12.855  1.00 21.67           C  
HETATM 2903  C2  AXT B1175      18.474  75.911  12.632  1.00 23.10           C  
HETATM 2904  C3  AXT B1175      17.160  76.651  12.624  1.00 25.33           C  
HETATM 2905  C4  AXT B1175      17.120  77.727  11.592  1.00 24.66           C  
HETATM 2906  C5  AXT B1175      18.311  78.312  11.157  1.00 23.41           C  
HETATM 2907  C6  AXT B1175      19.573  77.924  11.691  1.00 22.57           C  
HETATM 2908  C7  AXT B1175      20.748  78.536  11.070  1.00 21.20           C  
HETATM 2909  C8  AXT B1175      22.040  78.226  11.334  1.00 18.54           C  
HETATM 2910  C9  AXT B1175      23.138  78.797  10.706  1.00 18.71           C  
HETATM 2911  C10 AXT B1175      24.413  78.377  11.199  1.00 18.24           C  
HETATM 2912  C11 AXT B1175      25.696  78.831  10.797  1.00 16.82           C  
HETATM 2913  C12 AXT B1175      26.777  78.235  11.418  1.00 15.58           C  
HETATM 2914  C13 AXT B1175      28.122  78.524  11.176  1.00 14.91           C  
HETATM 2915  C14 AXT B1175      29.095  77.776  11.853  1.00 15.81           C  
HETATM 2916  C15 AXT B1175      30.478  77.926  11.636  1.00 15.79           C  
HETATM 2917  C16 AXT B1175      20.764  76.024  12.881  1.00 21.22           C  
HETATM 2918  C17 AXT B1175      19.436  77.557  14.179  1.00 18.75           C  
HETATM 2919  C18 AXT B1175      18.234  79.349  10.088  1.00 22.90           C  
HETATM 2920  C19 AXT B1175      22.967  79.821   9.609  1.00 17.22           C  
HETATM 2921  C20 AXT B1175      28.528  79.556  10.205  1.00 15.22           C  
HETATM 2922  O3  AXT B1175      16.194  75.699  12.327  1.00 29.32           O  
HETATM 2923  O4  AXT B1175      16.027  78.047  11.120  1.00 24.50           O  
HETATM 2924  C21 AXT B1175      42.200  76.536   9.763  1.00 23.16           C  
HETATM 2925  C22 AXT B1175      43.397  76.449   8.870  1.00 24.60           C  
HETATM 2926  C23 AXT B1175      44.613  76.725   9.639  1.00 26.25           C  
HETATM 2927  C24 AXT B1175      44.726  75.603  10.662  1.00 26.71           C  
HETATM 2928  C25 AXT B1175      43.523  75.121  11.346  1.00 26.34           C  
HETATM 2929  C26 AXT B1175      42.252  75.619  10.966  1.00 24.94           C  
HETATM 2930  C27 AXT B1175      41.043  75.236  11.675  1.00 24.15           C  
HETATM 2931  C28 AXT B1175      39.799  75.877  11.456  1.00 23.65           C  
HETATM 2932  C29 AXT B1175      38.629  75.556  12.166  1.00 25.18           C  
HETATM 2933  C30 AXT B1175      37.427  76.212  11.842  1.00 24.87           C  
HETATM 2934  C31 AXT B1175      36.183  75.956  12.486  1.00 22.68           C  
HETATM 2935  C32 AXT B1175      35.060  76.676  12.058  1.00 20.92           C  
HETATM 2936  C33 AXT B1175      33.729  76.513  12.580  1.00 19.16           C  
HETATM 2937  C34 AXT B1175      32.700  77.277  11.978  1.00 16.57           C  
HETATM 2938  C35 AXT B1175      31.360  77.159  12.313  1.00 15.30           C  
HETATM 2939  C36 AXT B1175      41.121  76.133   8.820  1.00 22.84           C  
HETATM 2940  C37 AXT B1175      42.130  77.963  10.220  1.00 22.20           C  
HETATM 2941  C38 AXT B1175      43.620  74.105  12.445  1.00 24.07           C  
HETATM 2942  C39 AXT B1175      38.667  74.500  13.266  1.00 25.88           C  
HETATM 2943  C40 AXT B1175      33.428  75.509  13.696  1.00 17.20           C  
HETATM 2944  O24 AXT B1175      45.823  75.174  10.917  1.00 28.63           O  
HETATM 2945  O23 AXT B1175      45.755  76.723   8.804  1.00 29.41           O  
HETATM 2946  C   TRS B1176      11.804  96.846  -1.203  1.00 70.91           C  
HETATM 2947  C1  TRS B1176      11.641  98.180  -2.124  1.00 70.20           C  
HETATM 2948  C2  TRS B1176      12.452  95.657  -2.279  1.00 71.97           C  
HETATM 2949  C3  TRS B1176      10.340  96.314  -0.723  1.00 70.29           C  
HETATM 2950  N   TRS B1176      12.763  97.352  -0.064  1.00 71.33           N  
HETATM 2951  O1  TRS B1176      10.294  97.886  -2.756  1.00 69.15           O  
HETATM 2952  O2  TRS B1176      13.992  95.892  -2.560  1.00 70.95           O  
HETATM 2953  O3  TRS B1176       9.586  95.384  -1.724  1.00 69.26           O  
HETATM 2954  N1  EPE B1177      37.253  88.714  -0.419  1.00 88.47           N  
HETATM 2955  C2  EPE B1177      36.385  89.045   0.816  1.00 88.61           C  
HETATM 2956  C3  EPE B1177      36.709  90.521   1.151  1.00 89.82           C  
HETATM 2957  N4  EPE B1177      38.114  90.672   1.609  1.00 91.07           N  
HETATM 2958  C5  EPE B1177      39.057  90.195   0.561  1.00 90.10           C  
HETATM 2959  C6  EPE B1177      38.741  88.774   0.036  1.00 89.15           C  
HETATM 2960  C7  EPE B1177      38.598  92.147   1.931  1.00 94.47           C  
HETATM 2961  C8  EPE B1177      37.810  93.048   3.019  1.00 97.18           C  
HETATM 2962  O8  EPE B1177      38.345  94.432   3.333  1.00 97.44           O  
HETATM 2963  C9  EPE B1177      37.075  87.292  -1.033  1.00 87.56           C  
HETATM 2964  C10 EPE B1177      35.848  87.227  -2.089  1.00 87.70           C  
HETATM 2965  S   EPE B1177      35.845  85.520  -2.824  1.00 89.11           S  
HETATM 2966  O1S EPE B1177      34.711  85.148  -3.872  1.00 88.07           O  
HETATM 2967  O2S EPE B1177      35.730  84.469  -1.697  1.00 89.83           O  
HETATM 2968  O3S EPE B1177      37.228  85.661  -3.392  1.00 88.46           O  
HETATM 2969  O   HOH A2001      34.456  84.396  25.929  1.00 36.85           O  
HETATM 2970  O   HOH A2002      53.405  84.560   6.362  1.00 35.49           O  
HETATM 2971  O   HOH A2003      56.400  74.136  14.073  1.00 62.28           O  
HETATM 2972  O   HOH A2004      63.357  61.125  14.967  1.00 23.06           O  
HETATM 2973  O   HOH A2005      60.274  67.812  35.116  1.00 45.41           O  
HETATM 2974  O   HOH A2006      53.910  73.742  22.187  1.00 48.44           O  
HETATM 2975  O   HOH A2007      51.020  71.869  25.173  1.00 52.34           O  
HETATM 2976  O   HOH A2008      54.288  75.710  14.115  1.00 71.65           O  
HETATM 2977  O   HOH A2009      56.009  77.165  13.474  1.00 49.85           O  
HETATM 2978  O   HOH A2010      70.149  74.633  23.111  1.00 36.23           O  
HETATM 2979  O   HOH A2011      59.371  79.009  43.751  1.00 45.29           O  
HETATM 2980  O   HOH B2001      41.871  67.084  10.613  1.00 39.57           O  
HETATM 2981  O   HOH B2002      37.194  72.174  -0.537  1.00 37.32           O  
HETATM 2982  O   HOH B2003      35.432  80.208  -1.759  1.00 26.93           O  
HETATM 2983  O   HOH B2004      22.074  95.912  -1.961  1.00 47.32           O  
HETATM 2984  O   HOH B2005      19.262  70.803   7.386  1.00 23.70           O  
HETATM 2985  O   HOH B2006      48.597  81.107  11.354  1.00 50.87           O  
HETATM 2986  O   HOH B2007      47.884  83.656   8.734  1.00 49.43           O  
HETATM 2987  O   HOH B2008      11.907  62.245   6.293  1.00 58.10           O  
HETATM 2988  O   HOH B2009       2.889  84.509  17.035  1.00 50.34           O  
HETATM 2989  O   HOH B2010      18.301  91.161  21.641  1.00 56.00           O  
HETATM 2990  O   HOH B2011       0.379  89.985   1.897  1.00 84.37           O  
HETATM 2991  O   HOH B2012      27.780  84.977   6.291  1.00 67.14           O  
HETATM 2992  O   HOH B2013      47.470  81.871  10.637  1.00 78.51           O  
HETATM 2993  O   HOH B2014      39.562  79.319   6.640  1.00 45.04           O  
HETATM 2994  O   HOH B2015      35.478  78.489   8.470  1.00 25.22           O  
HETATM 2995  O   HOH B2016      22.421  76.952   5.032  1.00 31.09           O  
HETATM 2996  O   HOH B2017       4.101  70.839  19.258  1.00 53.56           O  
HETATM 2997  O   HOH B2018       2.833  68.672  16.271  1.00 54.93           O  
HETATM 2998  O   HOH B2019      14.535  79.787   9.642  1.00 35.13           O  
CONECT   83  967                                                                
CONECT  407 1385                                                                
CONECT  935 1210                                                                
CONECT  967   83                                                                
CONECT 1210  935                                                                
CONECT 1385  407                                                                
CONECT 1535 2414                                                                
CONECT 1821 2808                                                                
CONECT 2414 1535                                                                
CONECT 2808 1821                                                                
CONECT 2846 2847 2851 2861 2862                                                 
CONECT 2847 2846 2848                                                           
CONECT 2848 2847 2849 2866                                                      
CONECT 2849 2848 2850 2867                                                      
CONECT 2850 2849 2851 2863                                                      
CONECT 2851 2846 2850 2852                                                      
CONECT 2852 2851 2853                                                           
CONECT 2853 2852 2854                                                           
CONECT 2854 2853 2855 2864                                                      
CONECT 2855 2854 2856                                                           
CONECT 2856 2855 2857                                                           
CONECT 2857 2856 2858                                                           
CONECT 2858 2857 2859 2865                                                      
CONECT 2859 2858 2860                                                           
CONECT 2860 2859 2882                                                           
CONECT 2861 2846                                                                
CONECT 2862 2846                                                                
CONECT 2863 2850                                                                
CONECT 2864 2854                                                                
CONECT 2865 2858                                                                
CONECT 2866 2848                                                                
CONECT 2867 2849                                                                
CONECT 2868 2869 2873 2883 2884                                                 
CONECT 2869 2868 2870                                                           
CONECT 2870 2869 2871 2889                                                      
CONECT 2871 2870 2872 2888                                                      
CONECT 2872 2871 2873 2885                                                      
CONECT 2873 2868 2872 2874                                                      
CONECT 2874 2873 2875                                                           
CONECT 2875 2874 2876                                                           
CONECT 2876 2875 2877 2886                                                      
CONECT 2877 2876 2878                                                           
CONECT 2878 2877 2879                                                           
CONECT 2879 2878 2880                                                           
CONECT 2880 2879 2881 2887                                                      
CONECT 2881 2880 2882                                                           
CONECT 2882 2860 2881                                                           
CONECT 2883 2868                                                                
CONECT 2884 2868                                                                
CONECT 2885 2872                                                                
CONECT 2886 2876                                                                
CONECT 2887 2880                                                                
CONECT 2888 2871                                                                
CONECT 2889 2870                                                                
CONECT 2890 2891                                                                
CONECT 2891 2890 2892                                                           
CONECT 2892 2891 2893                                                           
CONECT 2893 2892 2894                                                           
CONECT 2894 2893 2895                                                           
CONECT 2895 2894 2896                                                           
CONECT 2896 2895 2897                                                           
CONECT 2897 2896 2898                                                           
CONECT 2898 2897 2899                                                           
CONECT 2899 2898 2900                                                           
CONECT 2900 2899 2901                                                           
CONECT 2901 2900                                                                
CONECT 2902 2903 2907 2917 2918                                                 
CONECT 2903 2902 2904                                                           
CONECT 2904 2903 2905 2922                                                      
CONECT 2905 2904 2906 2923                                                      
CONECT 2906 2905 2907 2919                                                      
CONECT 2907 2902 2906 2908                                                      
CONECT 2908 2907 2909                                                           
CONECT 2909 2908 2910                                                           
CONECT 2910 2909 2911 2920                                                      
CONECT 2911 2910 2912                                                           
CONECT 2912 2911 2913                                                           
CONECT 2913 2912 2914                                                           
CONECT 2914 2913 2915 2921                                                      
CONECT 2915 2914 2916                                                           
CONECT 2916 2915 2938                                                           
CONECT 2917 2902                                                                
CONECT 2918 2902                                                                
CONECT 2919 2906                                                                
CONECT 2920 2910                                                                
CONECT 2921 2914                                                                
CONECT 2922 2904                                                                
CONECT 2923 2905                                                                
CONECT 2924 2925 2929 2939 2940                                                 
CONECT 2925 2924 2926                                                           
CONECT 2926 2925 2927 2945                                                      
CONECT 2927 2926 2928 2944                                                      
CONECT 2928 2927 2929 2941                                                      
CONECT 2929 2924 2928 2930                                                      
CONECT 2930 2929 2931                                                           
CONECT 2931 2930 2932                                                           
CONECT 2932 2931 2933 2942                                                      
CONECT 2933 2932 2934                                                           
CONECT 2934 2933 2935                                                           
CONECT 2935 2934 2936                                                           
CONECT 2936 2935 2937 2943                                                      
CONECT 2937 2936 2938                                                           
CONECT 2938 2916 2937                                                           
CONECT 2939 2924                                                                
CONECT 2940 2924                                                                
CONECT 2941 2928                                                                
CONECT 2942 2932                                                                
CONECT 2943 2936                                                                
CONECT 2944 2927                                                                
CONECT 2945 2926                                                                
CONECT 2946 2947 2948 2949 2950                                                 
CONECT 2947 2946 2951                                                           
CONECT 2948 2946 2952                                                           
CONECT 2949 2946 2953                                                           
CONECT 2950 2946                                                                
CONECT 2951 2947                                                                
CONECT 2952 2948                                                                
CONECT 2953 2949                                                                
CONECT 2954 2955 2959 2963                                                      
CONECT 2955 2954 2956                                                           
CONECT 2956 2955 2957                                                           
CONECT 2957 2956 2958 2960                                                      
CONECT 2958 2957 2959                                                           
CONECT 2959 2954 2958                                                           
CONECT 2960 2957 2961                                                           
CONECT 2961 2960 2962                                                           
CONECT 2962 2961                                                                
CONECT 2963 2954 2964                                                           
CONECT 2964 2963 2965                                                           
CONECT 2965 2964 2966 2967 2968                                                 
CONECT 2966 2965                                                                
CONECT 2967 2965                                                                
CONECT 2968 2965                                                                
MASTER      429    0    5    7   20    0   18    6 2996    2  133   28          
END                                                                             
