HEADER    PEROXIDASE (DONOR:H2O2 OXIDOREDUCTASE)  25-APR-95   1ARU              
TITLE     CRYSTAL STRUCTURES OF CYANIDE-AND TRIIODIDE-BOUND FORMS OF ARTHROMYCES
TITLE    2 RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES. PERTURBATIONS OF ACTIVE   
TITLE    3 SITE RESIDUES AND THEIR IMPLICATION IN ENZYME CATALYSIS              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXIDASE;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.11.1.7;                                                        
COMPND   5 OTHER_DETAILS: PH 7.5                                                
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: 'ARTHROMYCES RAMOSUS';                          
SOURCE   3 ORGANISM_TAXID: 5451                                                 
KEYWDS    PEROXIDASE (DONOR:H2O2 OXIDOREDUCTASE)                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.FUKUYAMA,N.KUNISHIMA,F.AMADA                                        
REVDAT   4   29-JUL-20 1ARU    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE   ATOM                              
REVDAT   3   13-JUL-11 1ARU    1       VERSN                                    
REVDAT   2   24-FEB-09 1ARU    1       VERSN                                    
REVDAT   1   29-JAN-96 1ARU    0                                                
JRNL        AUTH   K.FUKUYAMA,N.KUNISHIMA,F.AMADA,T.KUBOTA,H.MATSUBARA          
JRNL        TITL   CRYSTAL STRUCTURES OF CYANIDE- AND TRIIODIDE-BOUND FORMS OF  
JRNL        TITL 2 ARTHROMYCES RAMOSUS PEROXIDASE AT DIFFERENT PH VALUES.       
JRNL        TITL 3 PERTURBATIONS OF ACTIVE SITE RESIDUES AND THEIR IMPLICATION  
JRNL        TITL 4 IN ENZYME CATALYSIS.                                         
JRNL        REF    J.BIOL.CHEM.                  V. 270 21884 1995              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   7665612                                                      
JRNL        DOI    10.1074/JBC.270.37.21884                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   N.KUNISHIMA,K.FUKUYAMA,H.MATSUBARA,H.HATANAKA,Y.SHIBANO,     
REMARK   1  AUTH 2 T.AMACHI                                                     
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE FUNGAL PEROXIDASE FROM ARTHROMYCES  
REMARK   1  TITL 2 RAMOSUS AT 1.9 ANGSTROMS RESOLUTION: STRUCTURAL COMPARISONS  
REMARK   1  TITL 3 WITH THE LIGNIN AND CYTOCHROME C PEROXIDASES                 
REMARK   1  REF    J.MOL.BIOL.                   V. 235   331 1994              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   N.KUNISHIMA,K.FUKUYAMA,S.WAKABAYASHI,M.SUMIDA,M.TAKAYA,      
REMARK   1  AUTH 2 Y.SHIBANO,T.AMACHI,H.MATSUBARA                               
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF 
REMARK   1  TITL 2 PEROXIDASE FROM A FUNGUS ARTHROMYCES RAMOSUS                 
REMARK   1  REF    PROTEINS                      V.  15   216 1993              
REMARK   1  REFN                   ISSN 0887-3585                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
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            : 2465                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 75                                      
REMARK   3   SOLVENT ATOMS            : 306                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.018                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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  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 1ARU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000171180.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : DIFFRACTOMETER                     
REMARK 200  DETECTOR MANUFACTURER          : WEISSENBERG                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       37.28500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       37.28500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       58.73500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       37.28500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       37.28500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       58.73500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       37.28500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       37.28500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       58.73500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       37.28500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       37.28500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       58.73500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLN A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     GLY A     8                                                      
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    HIS A  56   NE2   HIS A  56   CD2    -0.071                       
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    VAL A  10   CA  -  C   -  N   ANGL. DEV. = -14.3 DEGREES          
REMARK 500    TRP A  26   CD1 -  CG  -  CD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    TRP A  26   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG A  48   NE  -  CZ  -  NH1 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ARG A  48   NE  -  CZ  -  NH2 ANGL. DEV. = -14.3 DEGREES          
REMARK 500    ARG A 141   CG  -  CD  -  NE  ANGL. DEV. = -13.6 DEGREES          
REMARK 500    ARG A 141   CD  -  NE  -  CZ  ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ARG A 141   NE  -  CZ  -  NH1 ANGL. DEV. =  14.7 DEGREES          
REMARK 500    ARG A 141   NE  -  CZ  -  NH2 ANGL. DEV. = -14.7 DEGREES          
REMARK 500    ARG A 166   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    THR A 210   N   -  CA  -  CB  ANGL. DEV. = -17.4 DEGREES          
REMARK 500    THR A 210   OG1 -  CB  -  CG2 ANGL. DEV. =  15.8 DEGREES          
REMARK 500    ARG A 242   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 244   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    TRP A 259   CD1 -  CG  -  CD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    TRP A 259   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    GLN A 271   CA  -  CB  -  CG  ANGL. DEV. =  13.6 DEGREES          
REMARK 500    ARG A 272   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG A 272   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 287   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 287   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 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  36      -70.83    -98.38                                   
REMARK 500    CYS A  43       75.74   -114.56                                   
REMARK 500    GLU A  44     -156.71   -127.00                                   
REMARK 500    THR A 314     -168.47   -127.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 346  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  57   O                                                      
REMARK 620 2 ASP A  57   OD1  80.5                                              
REMARK 620 3 GLY A  75   O    67.2  94.1                                        
REMARK 620 4 ASP A  77   OD1 136.2  86.7  72.2                                  
REMARK 620 5 SER A  79   OG  149.7  94.9 143.0  72.6                            
REMARK 620 6 HOH A 424   O    95.9 174.8  87.9  98.5  86.3                      
REMARK 620 7 HOH A 425   O    74.9  89.6 140.6 147.2  75.2  85.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 345  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 184   NE2                                                    
REMARK 620 2 HEM A 345   NA   95.4                                              
REMARK 620 3 HEM A 345   NB   89.3  89.4                                        
REMARK 620 4 HEM A 345   NC   91.1 173.4  89.6                                  
REMARK 620 5 HEM A 345   ND   89.0  90.4 178.2  90.8                            
REMARK 620 6 CYN A 800   N   171.7  81.3  83.1  92.2  98.6                      
REMARK 620 7 CYN A 800   C   179.4  85.2  90.8  88.3  91.0   8.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 347  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 185   OG                                                     
REMARK 620 2 SER A 185   O    72.1                                              
REMARK 620 3 ASP A 202   OD2  76.3  91.2                                        
REMARK 620 4 ASP A 202   OD1 117.4  80.0  49.1                                  
REMARK 620 5 THR A 204   OG1 141.3 146.3  93.3  78.0                            
REMARK 620 6 THR A 204   O   147.2  80.9 123.3  74.3  68.8                      
REMARK 620 7 VAL A 207   O    82.1  88.5 157.4 152.2  99.4  78.9                
REMARK 620 8 ASP A 209   OD1  69.6 141.0  86.7 124.6  72.6 131.5  79.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CA1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CA2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GL1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
DBREF  1ARU A    1   344  UNP    P28313   PER_ARTRA       21    364             
SEQRES   1 A  344  GLN GLY PRO GLY GLY GLY GLY GLY SER VAL THR CYS PRO          
SEQRES   2 A  344  GLY GLY GLN SER THR SER ASN SER GLN CYS CYS VAL TRP          
SEQRES   3 A  344  PHE ASP VAL LEU ASP ASP LEU GLN THR ASN PHE TYR GLN          
SEQRES   4 A  344  GLY SER LYS CYS GLU SER PRO VAL ARG LYS ILE LEU ARG          
SEQRES   5 A  344  ILE VAL PHE HIS ASP ALA ILE GLY PHE SER PRO ALA LEU          
SEQRES   6 A  344  THR ALA ALA GLY GLN PHE GLY GLY GLY GLY ALA ASP GLY          
SEQRES   7 A  344  SER ILE ILE ALA HIS SER ASN ILE GLU LEU ALA PHE PRO          
SEQRES   8 A  344  ALA ASN GLY GLY LEU THR ASP THR ILE GLU ALA LEU ARG          
SEQRES   9 A  344  ALA VAL GLY ILE ASN HIS GLY VAL SER PHE GLY ASP LEU          
SEQRES  10 A  344  ILE GLN PHE ALA THR ALA VAL GLY MET SER ASN CYS PRO          
SEQRES  11 A  344  GLY SER PRO ARG LEU GLU PHE LEU THR GLY ARG SER ASN          
SEQRES  12 A  344  SER SER GLN PRO SER PRO PRO SER LEU ILE PRO GLY PRO          
SEQRES  13 A  344  GLY ASN THR VAL THR ALA ILE LEU ASP ARG MET GLY ASP          
SEQRES  14 A  344  ALA GLY PHE SER PRO ASP GLU VAL VAL ASP LEU LEU ALA          
SEQRES  15 A  344  ALA HIS SER LEU ALA SER GLN GLU GLY LEU ASN SER ALA          
SEQRES  16 A  344  ILE PHE ARG SER PRO LEU ASP SER THR PRO GLN VAL PHE          
SEQRES  17 A  344  ASP THR GLN PHE TYR ILE GLU THR LEU LEU LYS GLY THR          
SEQRES  18 A  344  THR GLN PRO GLY PRO SER LEU GLY PHE ALA GLU GLU LEU          
SEQRES  19 A  344  SER PRO PHE PRO GLY GLU PHE ARG MET ARG SER ASP ALA          
SEQRES  20 A  344  LEU LEU ALA ARG ASP SER ARG THR ALA CYS ARG TRP GLN          
SEQRES  21 A  344  SER MET THR SER SER ASN GLU VAL MET GLY GLN ARG TYR          
SEQRES  22 A  344  ARG ALA ALA MET ALA LYS MET SER VAL LEU GLY PHE ASP          
SEQRES  23 A  344  ARG ASN ALA LEU THR ASP CYS SER ASP VAL ILE PRO SER          
SEQRES  24 A  344  ALA VAL SER ASN ASN ALA ALA PRO VAL ILE PRO GLY GLY          
SEQRES  25 A  344  LEU THR VAL ASP ASP ILE GLU VAL SER CYS PRO SER GLU          
SEQRES  26 A  344  PRO PHE PRO GLU ILE ALA THR ALA SER GLY PRO LEU PRO          
SEQRES  27 A  344  SER LEU ALA PRO ALA PRO                                      
MODRES 1ARU ASN A  143  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET    CYN  A 800       2                                                       
HET     CA  A 346       1                                                       
HET     CA  A 347       1                                                       
HET    HEM  A 345      43                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     CYN CYANIDE ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     HEM HEME                                                             
FORMUL   2  NAG    2(C8 H15 N O6)                                               
FORMUL   3  CYN    C N 1-                                                       
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   6  HEM    C34 H32 FE N4 O4                                             
FORMUL   7  HOH   *306(H2 O)                                                    
HELIX    1   A VAL A   25  ASN A   36  1                                  12    
HELIX    2   B SER A   45  ILE A   59  1                                  15    
HELIX    3  B1 SER A   62  ALA A   68  1                                   7    
HELIX    4  B2 HIS A   83  LEU A   88  1                                   6    
HELIX    5   C LEU A   96  HIS A  110  1                                  15    
HELIX    6   D SER A  113  SER A  127  1                                  15    
HELIX    7   E THR A  159  GLY A  171  1                                  13    
HELIX    8   F SER A  173  LEU A  186  1INCLUDES 3/10 HELIX               14    
HELIX    9   G GLN A  211  THR A  216  1                                   6    
HELIX   10   H MET A  243  ASP A  252  1                                  10    
HELIX   11   I THR A  255  MET A  262  1                                   8    
HELIX   12   J SER A  265  SER A  281  1                                  17    
SHEET    1   A 2 LEU A 138  THR A 139  0                                        
SHEET    2   A 2 THR A 291  ASP A 292 -1  N  THR A 291   O  THR A 139           
SHEET    1   B 2 SER A 188  GLN A 189  0                                        
SHEET    2   B 2 SER A 199  PRO A 200 -1  O  SER A 199   N  GLN A 189           
SHEET    1   C 2 GLU A 232  GLU A 233  0                                        
SHEET    2   C 2 ARG A 242  MET A 243 -1  O  ARG A 242   N  GLU A 233           
SHEET    1   D 2 VAL A 308  ILE A 309  0                                        
SHEET    2   D 2 ALA A 331  THR A 332  1  O  ALA A 331   N  ILE A 309           
SSBOND   1 CYS A   12    CYS A   24                          1555   1555  2.02  
SSBOND   2 CYS A   23    CYS A  293                          1555   1555  2.03  
SSBOND   3 CYS A   43    CYS A  129                          1555   1555  2.02  
SSBOND   4 CYS A  257    CYS A  322                          1555   1555  2.01  
LINK         ND2 ASN A 143                 C1  NAG B   1     1555   1555  1.46  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.41  
LINK         O   ASP A  57                CA    CA A 346     1555   1555  2.56  
LINK         OD1 ASP A  57                CA    CA A 346     1555   1555  2.30  
LINK         O   GLY A  75                CA    CA A 346     1555   1555  2.54  
LINK         OD1 ASP A  77                CA    CA A 346     1555   1555  2.44  
LINK         OG  SER A  79                CA    CA A 346     1555   1555  2.50  
LINK         NE2 HIS A 184                FE   HEM A 345     1555   1555  2.13  
LINK         OG  SER A 185                CA    CA A 347     1555   1555  2.46  
LINK         O   SER A 185                CA    CA A 347     1555   1555  2.48  
LINK         OD2 ASP A 202                CA    CA A 347     1555   1555  2.42  
LINK         OD1 ASP A 202                CA    CA A 347     1555   1555  2.69  
LINK         OG1 THR A 204                CA    CA A 347     1555   1555  2.55  
LINK         O   THR A 204                CA    CA A 347     1555   1555  2.42  
LINK         O   VAL A 207                CA    CA A 347     1555   1555  2.52  
LINK         OD1 ASP A 209                CA    CA A 347     1555   1555  2.47  
LINK        FE   HEM A 345                 N   CYN A 800     1555   1555  3.04  
LINK        FE   HEM A 345                 C   CYN A 800     1555   1555  1.96  
LINK        CA    CA A 346                 O   HOH A 424     1555   1555  2.44  
LINK        CA    CA A 346                 O   HOH A 425     1555   1555  2.54  
SITE     1 CA1  7  CA A 346  ASP A  57  GLY A  75  ASP A  77                    
SITE     2 CA1  7 SER A  79  HOH A 424  HOH A 425                               
SITE     1 CA2  6  CA A 347  SER A 185  ASP A 202  THR A 204                    
SITE     2 CA2  6 VAL A 207  ASP A 209                                          
SITE     1 GL1  3 NAG B   1  NAG B   2  ASN A 143                               
CRYST1   74.570   74.570  117.470  90.00  90.00  90.00 P 42 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013410  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013410  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008513        0.00000                         
ATOM      1  N   SER A   9      50.571  28.066  58.200  1.00 42.39           N  
ATOM      2  CA  SER A   9      49.339  28.744  57.857  1.00 43.26           C  
ATOM      3  C   SER A   9      48.297  27.725  57.393  1.00 42.29           C  
ATOM      4  O   SER A   9      48.640  26.540  57.530  1.00 43.41           O  
ATOM      5  CB  SER A   9      49.702  29.791  56.808  1.00 44.11           C  
ATOM      6  OG  SER A   9      50.732  30.573  57.426  1.00 49.05           O  
ATOM      7  N   VAL A  10      47.081  28.024  56.864  1.00 40.56           N  
ATOM      8  CA  VAL A  10      46.075  26.976  56.605  1.00 37.36           C  
ATOM      9  C   VAL A  10      46.316  25.944  55.503  1.00 36.56           C  
ATOM     10  O   VAL A  10      46.293  26.106  54.277  1.00 35.41           O  
ATOM     11  CB  VAL A  10      44.637  27.584  56.357  1.00 37.56           C  
ATOM     12  CG1 VAL A  10      43.615  26.516  56.733  1.00 33.58           C  
ATOM     13  CG2 VAL A  10      44.315  28.781  57.245  1.00 34.81           C  
ATOM     14  N   THR A  11      46.659  24.870  56.177  1.00 35.76           N  
ATOM     15  CA  THR A  11      46.937  23.587  55.597  1.00 35.85           C  
ATOM     16  C   THR A  11      45.839  22.679  56.108  1.00 35.57           C  
ATOM     17  O   THR A  11      45.540  22.662  57.324  1.00 34.38           O  
ATOM     18  CB  THR A  11      48.300  23.060  56.078  1.00 36.53           C  
ATOM     19  OG1 THR A  11      48.518  23.614  57.406  1.00 37.92           O  
ATOM     20  CG2 THR A  11      49.395  23.348  55.055  1.00 35.94           C  
ATOM     21  N   CYS A  12      45.244  21.980  55.149  1.00 34.60           N  
ATOM     22  CA  CYS A  12      44.199  21.036  55.471  1.00 34.16           C  
ATOM     23  C   CYS A  12      44.862  19.719  55.832  1.00 34.93           C  
ATOM     24  O   CYS A  12      46.010  19.515  55.402  1.00 35.59           O  
ATOM     25  CB  CYS A  12      43.303  20.858  54.271  1.00 31.62           C  
ATOM     26  SG  CYS A  12      42.444  22.407  53.947  1.00 29.17           S  
ATOM     27  N   PRO A  13      44.226  18.808  56.599  1.00 35.09           N  
ATOM     28  CA  PRO A  13      44.763  17.492  56.943  1.00 34.84           C  
ATOM     29  C   PRO A  13      45.406  16.716  55.802  1.00 35.05           C  
ATOM     30  O   PRO A  13      46.354  15.971  56.037  1.00 36.03           O  
ATOM     31  CB  PRO A  13      43.584  16.769  57.554  1.00 33.43           C  
ATOM     32  CG  PRO A  13      42.940  17.895  58.339  1.00 34.33           C  
ATOM     33  CD  PRO A  13      42.987  19.062  57.345  1.00 34.16           C  
ATOM     34  N   GLY A  14      44.955  16.851  54.560  1.00 35.09           N  
ATOM     35  CA  GLY A  14      45.576  16.135  53.456  1.00 34.63           C  
ATOM     36  C   GLY A  14      46.840  16.827  52.945  1.00 34.44           C  
ATOM     37  O   GLY A  14      47.477  16.314  52.014  1.00 34.94           O  
ATOM     38  N   GLY A  15      47.145  18.024  53.472  1.00 33.22           N  
ATOM     39  CA  GLY A  15      48.343  18.772  53.131  1.00 33.45           C  
ATOM     40  C   GLY A  15      48.190  19.827  52.039  1.00 33.75           C  
ATOM     41  O   GLY A  15      49.161  20.473  51.604  1.00 33.98           O  
ATOM     42  N   GLN A  16      46.963  20.077  51.602  1.00 33.24           N  
ATOM     43  CA  GLN A  16      46.768  21.072  50.556  1.00 32.67           C  
ATOM     44  C   GLN A  16      46.703  22.380  51.331  1.00 32.78           C  
ATOM     45  O   GLN A  16      46.461  22.396  52.564  1.00 31.34           O  
ATOM     46  CB  GLN A  16      45.436  20.891  49.788  1.00 34.00           C  
ATOM     47  CG  GLN A  16      44.955  19.460  49.481  1.00 34.12           C  
ATOM     48  CD  GLN A  16      44.426  18.670  50.695  1.00 35.06           C  
ATOM     49  OE1 GLN A  16      44.386  19.098  51.862  1.00 33.78           O  
ATOM     50  NE2 GLN A  16      43.994  17.447  50.460  1.00 36.01           N  
ATOM     51  N   SER A  17      46.942  23.467  50.600  1.00 32.82           N  
ATOM     52  CA  SER A  17      46.878  24.778  51.196  1.00 33.17           C  
ATOM     53  C   SER A  17      45.612  25.488  50.718  1.00 32.58           C  
ATOM     54  O   SER A  17      45.203  25.389  49.543  1.00 32.21           O  
ATOM     55  CB  SER A  17      48.160  25.548  50.818  1.00 33.52           C  
ATOM     56  OG  SER A  17      48.562  25.408  49.456  1.00 37.38           O  
ATOM     57  N   THR A  18      44.933  26.173  51.639  1.00 31.39           N  
ATOM     58  CA  THR A  18      43.722  26.886  51.280  1.00 29.49           C  
ATOM     59  C   THR A  18      43.681  28.231  52.005  1.00 30.31           C  
ATOM     60  O   THR A  18      44.427  28.484  52.964  1.00 29.83           O  
ATOM     61  CB  THR A  18      42.501  25.995  51.630  1.00 27.89           C  
ATOM     62  OG1 THR A  18      41.425  26.673  50.982  1.00 26.51           O  
ATOM     63  CG2 THR A  18      42.257  25.743  53.101  1.00 22.36           C  
ATOM     64  N   SER A  19      42.786  29.092  51.524  1.00 30.36           N  
ATOM     65  CA  SER A  19      42.638  30.421  52.078  1.00 30.33           C  
ATOM     66  C   SER A  19      41.946  30.463  53.430  1.00 29.84           C  
ATOM     67  O   SER A  19      42.219  31.329  54.266  1.00 31.83           O  
ATOM     68  CB  SER A  19      41.868  31.256  51.070  1.00 30.38           C  
ATOM     69  OG  SER A  19      40.660  30.636  50.619  1.00 32.90           O  
ATOM     70  N   ASN A  20      41.103  29.484  53.724  1.00 28.22           N  
ATOM     71  CA  ASN A  20      40.307  29.542  54.936  1.00 25.28           C  
ATOM     72  C   ASN A  20      40.025  28.158  55.469  1.00 23.96           C  
ATOM     73  O   ASN A  20      39.906  27.223  54.684  1.00 22.51           O  
ATOM     74  CB  ASN A  20      39.013  30.269  54.559  1.00 25.35           C  
ATOM     75  CG  ASN A  20      38.156  30.615  55.752  1.00 25.88           C  
ATOM     76  OD1 ASN A  20      37.586  29.766  56.436  1.00 25.58           O  
ATOM     77  ND2 ASN A  20      38.043  31.885  56.060  1.00 28.06           N  
ATOM     78  N   SER A  21      39.848  28.004  56.776  1.00 23.77           N  
ATOM     79  CA  SER A  21      39.557  26.747  57.455  1.00 24.20           C  
ATOM     80  C   SER A  21      38.267  26.077  56.975  1.00 23.64           C  
ATOM     81  O   SER A  21      38.151  24.843  56.878  1.00 24.52           O  
ATOM     82  CB  SER A  21      39.537  27.092  58.950  1.00 24.17           C  
ATOM     83  OG  SER A  21      38.885  26.171  59.806  1.00 27.09           O  
ATOM     84  N   GLN A  22      37.274  26.884  56.606  1.00 23.06           N  
ATOM     85  CA  GLN A  22      35.994  26.408  56.083  1.00 23.36           C  
ATOM     86  C   GLN A  22      36.114  25.649  54.777  1.00 20.21           C  
ATOM     87  O   GLN A  22      35.168  24.968  54.396  1.00 20.26           O  
ATOM     88  CB  GLN A  22      35.029  27.543  55.809  1.00 25.70           C  
ATOM     89  CG  GLN A  22      34.537  28.213  57.076  1.00 32.45           C  
ATOM     90  CD  GLN A  22      33.373  29.188  56.877  1.00 34.71           C  
ATOM     91  OE1 GLN A  22      33.150  30.013  57.770  1.00 40.13           O  
ATOM     92  NE2 GLN A  22      32.513  29.154  55.844  1.00 36.27           N  
ATOM     93  N   CYS A  23      37.227  25.760  54.068  1.00 17.26           N  
ATOM     94  CA  CYS A  23      37.397  25.068  52.802  1.00 16.37           C  
ATOM     95  C   CYS A  23      37.860  23.634  52.973  1.00 16.31           C  
ATOM     96  O   CYS A  23      37.632  22.817  52.079  1.00 15.43           O  
ATOM     97  CB  CYS A  23      38.420  25.789  51.937  1.00 13.90           C  
ATOM     98  SG  CYS A  23      38.037  27.541  51.696  1.00 14.42           S  
ATOM     99  N   CYS A  24      38.420  23.251  54.128  1.00 17.02           N  
ATOM    100  CA  CYS A  24      38.976  21.931  54.217  1.00 16.64           C  
ATOM    101  C   CYS A  24      38.018  20.784  54.027  1.00 16.31           C  
ATOM    102  O   CYS A  24      38.431  19.840  53.335  1.00 15.84           O  
ATOM    103  CB  CYS A  24      39.734  21.806  55.546  1.00 20.38           C  
ATOM    104  SG  CYS A  24      41.274  22.785  55.552  1.00 23.64           S  
ATOM    105  N   VAL A  25      36.761  20.805  54.501  1.00 14.93           N  
ATOM    106  CA  VAL A  25      35.848  19.679  54.289  1.00 14.86           C  
ATOM    107  C   VAL A  25      35.607  19.473  52.782  1.00 13.26           C  
ATOM    108  O   VAL A  25      35.479  18.331  52.333  1.00 11.58           O  
ATOM    109  CB  VAL A  25      34.482  19.932  55.043  1.00 15.91           C  
ATOM    110  CG1 VAL A  25      33.781  21.186  54.494  1.00 16.55           C  
ATOM    111  CG2 VAL A  25      33.552  18.712  54.895  1.00 16.97           C  
ATOM    112  N   TRP A  26      35.641  20.536  51.964  1.00 13.22           N  
ATOM    113  CA  TRP A  26      35.397  20.408  50.537  1.00 12.49           C  
ATOM    114  C   TRP A  26      36.425  19.545  49.816  1.00 13.31           C  
ATOM    115  O   TRP A  26      36.090  18.930  48.803  1.00 12.79           O  
ATOM    116  CB  TRP A  26      35.260  21.839  49.971  1.00 10.84           C  
ATOM    117  CG  TRP A  26      33.959  22.456  50.524  1.00 11.23           C  
ATOM    118  CD1 TRP A  26      33.983  23.461  51.469  1.00 10.57           C  
ATOM    119  CD2 TRP A  26      32.658  22.081  50.204  1.00  9.49           C  
ATOM    120  NE1 TRP A  26      32.719  23.713  51.736  1.00 11.53           N  
ATOM    121  CE2 TRP A  26      31.913  22.914  51.014  1.00 10.57           C  
ATOM    122  CE3 TRP A  26      31.997  21.191  49.375  1.00  9.98           C  
ATOM    123  CZ2 TRP A  26      30.530  22.869  51.002  1.00  9.18           C  
ATOM    124  CZ3 TRP A  26      30.610  21.132  49.350  1.00  7.60           C  
ATOM    125  CH2 TRP A  26      29.884  21.966  50.161  1.00  9.93           C  
ATOM    126  N   PHE A  27      37.647  19.342  50.340  1.00 13.12           N  
ATOM    127  CA  PHE A  27      38.598  18.429  49.718  1.00 13.61           C  
ATOM    128  C   PHE A  27      38.037  17.007  49.882  1.00 13.84           C  
ATOM    129  O   PHE A  27      38.138  16.178  48.985  1.00 14.42           O  
ATOM    130  CB  PHE A  27      39.970  18.578  50.404  1.00 14.95           C  
ATOM    131  CG  PHE A  27      40.704  19.861  49.978  1.00 17.67           C  
ATOM    132  CD1 PHE A  27      41.168  20.006  48.694  1.00 16.77           C  
ATOM    133  CD2 PHE A  27      40.872  20.899  50.879  1.00 17.56           C  
ATOM    134  CE1 PHE A  27      41.791  21.178  48.307  1.00 19.22           C  
ATOM    135  CE2 PHE A  27      41.494  22.061  50.480  1.00 18.87           C  
ATOM    136  CZ  PHE A  27      41.956  22.208  49.197  1.00 16.20           C  
ATOM    137  N   ASP A  28      37.341  16.681  50.962  1.00 14.27           N  
ATOM    138  CA  ASP A  28      36.778  15.345  51.123  1.00 15.97           C  
ATOM    139  C   ASP A  28      35.579  15.112  50.229  1.00 15.13           C  
ATOM    140  O   ASP A  28      35.433  14.023  49.659  1.00 16.03           O  
ATOM    141  CB  ASP A  28      36.291  15.056  52.555  1.00 18.84           C  
ATOM    142  CG  ASP A  28      37.340  15.079  53.661  1.00 20.78           C  
ATOM    143  OD1 ASP A  28      38.525  14.824  53.415  1.00 22.44           O  
ATOM    144  OD2 ASP A  28      36.934  15.355  54.785  1.00 23.32           O  
ATOM    145  N   VAL A  29      34.690  16.097  50.079  1.00 13.81           N  
ATOM    146  CA  VAL A  29      33.548  15.840  49.225  1.00 13.73           C  
ATOM    147  C   VAL A  29      34.036  15.872  47.772  1.00 13.15           C  
ATOM    148  O   VAL A  29      33.473  15.126  46.959  1.00 13.37           O  
ATOM    149  CB  VAL A  29      32.298  16.824  49.591  1.00 15.83           C  
ATOM    150  CG1 VAL A  29      32.696  17.862  50.591  1.00 15.06           C  
ATOM    151  CG2 VAL A  29      31.667  17.424  48.367  1.00 12.85           C  
ATOM    152  N   LEU A  30      35.146  16.554  47.446  1.00 12.71           N  
ATOM    153  CA  LEU A  30      35.723  16.490  46.100  1.00 11.95           C  
ATOM    154  C   LEU A  30      36.105  15.046  45.777  1.00 11.99           C  
ATOM    155  O   LEU A  30      35.721  14.523  44.735  1.00  9.80           O  
ATOM    156  CB  LEU A  30      36.991  17.334  45.982  1.00 13.02           C  
ATOM    157  CG  LEU A  30      37.825  17.327  44.689  1.00 14.86           C  
ATOM    158  CD1 LEU A  30      37.045  17.918  43.546  1.00 15.92           C  
ATOM    159  CD2 LEU A  30      39.059  18.188  44.870  1.00 16.58           C  
ATOM    160  N   ASP A  31      36.841  14.352  46.652  1.00 13.73           N  
ATOM    161  CA  ASP A  31      37.256  12.978  46.386  1.00 15.18           C  
ATOM    162  C   ASP A  31      36.091  12.029  46.222  1.00 14.58           C  
ATOM    163  O   ASP A  31      36.075  11.215  45.303  1.00 14.49           O  
ATOM    164  CB  ASP A  31      38.153  12.452  47.517  1.00 19.89           C  
ATOM    165  CG  ASP A  31      39.444  13.252  47.707  1.00 24.82           C  
ATOM    166  OD1 ASP A  31      39.955  13.882  46.746  1.00 28.34           O  
ATOM    167  OD2 ASP A  31      39.934  13.235  48.846  1.00 28.61           O  
ATOM    168  N   ASP A  32      35.090  12.176  47.065  1.00 13.51           N  
ATOM    169  CA  ASP A  32      33.920  11.342  47.007  1.00 13.64           C  
ATOM    170  C   ASP A  32      33.185  11.556  45.676  1.00 14.27           C  
ATOM    171  O   ASP A  32      32.795  10.602  45.007  1.00 13.29           O  
ATOM    172  CB  ASP A  32      33.019  11.701  48.190  1.00 15.90           C  
ATOM    173  CG  ASP A  32      31.717  10.915  48.355  1.00 14.91           C  
ATOM    174  OD1 ASP A  32      31.292  10.159  47.490  1.00 19.98           O  
ATOM    175  OD2 ASP A  32      31.080  11.065  49.381  1.00 19.90           O  
ATOM    176  N   LEU A  33      32.899  12.810  45.303  1.00 13.07           N  
ATOM    177  CA  LEU A  33      32.192  13.099  44.071  1.00 13.31           C  
ATOM    178  C   LEU A  33      32.968  12.595  42.878  1.00 11.96           C  
ATOM    179  O   LEU A  33      32.380  11.934  42.024  1.00 11.24           O  
ATOM    180  CB  LEU A  33      31.976  14.601  43.919  1.00 13.12           C  
ATOM    181  CG  LEU A  33      30.938  15.289  44.785  1.00 14.57           C  
ATOM    182  CD1 LEU A  33      30.995  16.795  44.522  1.00 14.13           C  
ATOM    183  CD2 LEU A  33      29.541  14.749  44.443  1.00 14.32           C  
ATOM    184  N   GLN A  34      34.283  12.856  42.775  1.00 11.85           N  
ATOM    185  CA  GLN A  34      35.061  12.384  41.629  1.00 12.14           C  
ATOM    186  C   GLN A  34      35.108  10.859  41.511  1.00 12.37           C  
ATOM    187  O   GLN A  34      34.950  10.336  40.410  1.00 12.88           O  
ATOM    188  CB  GLN A  34      36.499  12.910  41.681  1.00 10.79           C  
ATOM    189  CG  GLN A  34      36.695  14.411  41.426  1.00 10.83           C  
ATOM    190  CD  GLN A  34      36.262  14.921  40.047  1.00 12.26           C  
ATOM    191  OE1 GLN A  34      36.977  15.682  39.396  1.00 13.74           O  
ATOM    192  NE2 GLN A  34      35.100  14.612  39.507  1.00 10.62           N  
ATOM    193  N   THR A  35      35.216  10.143  42.630  1.00 14.11           N  
ATOM    194  CA  THR A  35      35.290   8.694  42.612  1.00 14.80           C  
ATOM    195  C   THR A  35      33.952   8.032  42.357  1.00 16.11           C  
ATOM    196  O   THR A  35      33.842   7.104  41.548  1.00 16.39           O  
ATOM    197  CB  THR A  35      35.832   8.164  43.952  1.00 13.93           C  
ATOM    198  OG1 THR A  35      37.094   8.775  44.133  1.00 17.47           O  
ATOM    199  CG2 THR A  35      35.967   6.653  43.982  1.00 15.86           C  
ATOM    200  N   ASN A  36      32.928   8.527  43.048  1.00 15.53           N  
ATOM    201  CA  ASN A  36      31.637   7.892  42.989  1.00 15.53           C  
ATOM    202  C   ASN A  36      30.645   8.502  42.048  1.00 14.58           C  
ATOM    203  O   ASN A  36      30.410   7.922  40.994  1.00 14.77           O  
ATOM    204  CB  ASN A  36      31.080   7.846  44.417  1.00 16.73           C  
ATOM    205  CG  ASN A  36      32.060   7.147  45.341  1.00 20.54           C  
ATOM    206  OD1 ASN A  36      32.565   7.740  46.299  1.00 22.25           O  
ATOM    207  ND2 ASN A  36      32.450   5.907  45.062  1.00 19.79           N  
ATOM    208  N   PHE A  37      30.129   9.692  42.374  1.00 14.18           N  
ATOM    209  CA  PHE A  37      29.138  10.386  41.566  1.00 12.53           C  
ATOM    210  C   PHE A  37      29.598  10.554  40.129  1.00 11.44           C  
ATOM    211  O   PHE A  37      28.844  10.258  39.197  1.00 12.04           O  
ATOM    212  CB  PHE A  37      28.856  11.759  42.204  1.00 12.92           C  
ATOM    213  CG  PHE A  37      27.722  12.543  41.551  1.00 14.14           C  
ATOM    214  CD1 PHE A  37      26.410  12.110  41.672  1.00 15.71           C  
ATOM    215  CD2 PHE A  37      27.993  13.692  40.848  1.00 13.38           C  
ATOM    216  CE1 PHE A  37      25.386  12.836  41.087  1.00 16.27           C  
ATOM    217  CE2 PHE A  37      26.961  14.398  40.272  1.00 13.96           C  
ATOM    218  CZ  PHE A  37      25.660  13.987  40.382  1.00 14.10           C  
ATOM    219  N   TYR A  38      30.840  10.989  39.909  1.00 10.94           N  
ATOM    220  CA  TYR A  38      31.328  11.204  38.573  1.00 10.66           C  
ATOM    221  C   TYR A  38      32.067  10.009  37.983  1.00 11.71           C  
ATOM    222  O   TYR A  38      32.694  10.134  36.926  1.00 10.61           O  
ATOM    223  CB  TYR A  38      32.213  12.464  38.529  1.00  9.44           C  
ATOM    224  CG  TYR A  38      31.357  13.726  38.664  1.00  9.24           C  
ATOM    225  CD1 TYR A  38      30.245  13.918  37.850  1.00  8.63           C  
ATOM    226  CD2 TYR A  38      31.676  14.660  39.630  1.00 10.10           C  
ATOM    227  CE1 TYR A  38      29.451  15.034  38.006  1.00  9.18           C  
ATOM    228  CE2 TYR A  38      30.884  15.787  39.800  1.00  9.67           C  
ATOM    229  CZ  TYR A  38      29.773  15.961  38.983  1.00 11.52           C  
ATOM    230  OH  TYR A  38      28.957  17.071  39.156  1.00 11.10           O  
ATOM    231  N   GLN A  39      32.009   8.852  38.664  1.00 14.10           N  
ATOM    232  CA  GLN A  39      32.556   7.596  38.138  1.00 15.73           C  
ATOM    233  C   GLN A  39      33.997   7.679  37.622  1.00 14.89           C  
ATOM    234  O   GLN A  39      34.335   7.197  36.543  1.00 15.30           O  
ATOM    235  CB  GLN A  39      31.576   7.094  37.024  1.00 17.59           C  
ATOM    236  CG  GLN A  39      30.141   6.797  37.533  1.00 25.30           C  
ATOM    237  CD  GLN A  39      29.045   6.493  36.491  1.00 28.53           C  
ATOM    238  OE1 GLN A  39      28.696   5.332  36.217  1.00 31.87           O  
ATOM    239  NE2 GLN A  39      28.443   7.477  35.841  1.00 28.91           N  
ATOM    240  N   GLY A  40      34.875   8.311  38.385  1.00 14.04           N  
ATOM    241  CA  GLY A  40      36.243   8.431  37.972  1.00 13.55           C  
ATOM    242  C   GLY A  40      36.494   9.704  37.200  1.00 13.32           C  
ATOM    243  O   GLY A  40      37.196   9.690  36.186  1.00 12.72           O  
ATOM    244  N   SER A  41      35.949  10.813  37.703  1.00 12.36           N  
ATOM    245  CA  SER A  41      36.131  12.132  37.093  1.00 13.80           C  
ATOM    246  C   SER A  41      35.720  12.245  35.611  1.00 12.81           C  
ATOM    247  O   SER A  41      36.402  12.899  34.807  1.00 13.97           O  
ATOM    248  CB  SER A  41      37.601  12.559  37.233  1.00 14.09           C  
ATOM    249  OG  SER A  41      38.083  12.430  38.572  1.00 14.90           O  
ATOM    250  N   LYS A  42      34.609  11.607  35.212  1.00 13.87           N  
ATOM    251  CA  LYS A  42      34.089  11.635  33.831  1.00 12.97           C  
ATOM    252  C   LYS A  42      33.197  12.837  33.593  1.00 11.68           C  
ATOM    253  O   LYS A  42      32.624  13.388  34.544  1.00 11.46           O  
ATOM    254  CB  LYS A  42      33.212  10.440  33.495  1.00 12.54           C  
ATOM    255  CG  LYS A  42      33.769   9.057  33.721  1.00 17.77           C  
ATOM    256  CD  LYS A  42      34.992   8.948  32.888  1.00 21.56           C  
ATOM    257  CE  LYS A  42      35.287   7.478  32.681  1.00 24.18           C  
ATOM    258  NZ  LYS A  42      36.344   7.380  31.685  1.00 29.03           N  
ATOM    259  N   CYS A  43      32.994  13.186  32.319  1.00 11.25           N  
ATOM    260  CA  CYS A  43      32.109  14.285  31.931  1.00 11.06           C  
ATOM    261  C   CYS A  43      30.976  13.616  31.171  1.00 11.17           C  
ATOM    262  O   CYS A  43      30.948  13.600  29.931  1.00 12.31           O  
ATOM    263  CB  CYS A  43      32.879  15.232  31.049  1.00 10.73           C  
ATOM    264  SG  CYS A  43      31.808  16.520  30.369  1.00 13.43           S  
ATOM    265  N   GLU A  44      30.046  12.954  31.870  1.00 10.74           N  
ATOM    266  CA  GLU A  44      28.963  12.216  31.217  1.00  9.60           C  
ATOM    267  C   GLU A  44      27.623  12.654  31.769  1.00  8.75           C  
ATOM    268  O   GLU A  44      27.558  13.745  32.342  1.00  8.83           O  
ATOM    269  CB  GLU A  44      29.181  10.730  31.456  1.00  9.55           C  
ATOM    270  CG  GLU A  44      30.469  10.265  30.770  1.00 12.71           C  
ATOM    271  CD  GLU A  44      30.765   8.767  30.833  1.00 15.38           C  
ATOM    272  OE1 GLU A  44      30.192   8.042  31.646  1.00 17.13           O  
ATOM    273  OE2 GLU A  44      31.605   8.321  30.056  1.00 16.29           O  
ATOM    274  N   SER A  45      26.556  11.874  31.705  1.00  7.30           N  
ATOM    275  CA  SER A  45      25.256  12.291  32.215  1.00  7.95           C  
ATOM    276  C   SER A  45      25.224  12.902  33.631  1.00  8.12           C  
ATOM    277  O   SER A  45      24.522  13.922  33.755  1.00  6.23           O  
ATOM    278  CB  SER A  45      24.323  11.070  32.095  1.00  6.69           C  
ATOM    279  OG  SER A  45      23.002  11.356  32.507  1.00 13.66           O  
ATOM    280  N   PRO A  46      25.936  12.462  34.709  1.00  8.46           N  
ATOM    281  CA  PRO A  46      25.916  13.084  36.035  1.00  8.95           C  
ATOM    282  C   PRO A  46      26.244  14.568  35.976  1.00  8.20           C  
ATOM    283  O   PRO A  46      25.548  15.359  36.597  1.00  8.74           O  
ATOM    284  CB  PRO A  46      26.912  12.273  36.844  1.00  8.12           C  
ATOM    285  CG  PRO A  46      26.649  10.889  36.303  1.00  8.28           C  
ATOM    286  CD  PRO A  46      26.664  11.183  34.803  1.00  8.33           C  
ATOM    287  N   VAL A  47      27.213  14.989  35.170  1.00  9.61           N  
ATOM    288  CA  VAL A  47      27.521  16.414  35.041  1.00  9.83           C  
ATOM    289  C   VAL A  47      26.325  17.158  34.417  1.00  9.42           C  
ATOM    290  O   VAL A  47      25.920  18.219  34.894  1.00  8.84           O  
ATOM    291  CB  VAL A  47      28.758  16.636  34.133  1.00  9.74           C  
ATOM    292  CG1 VAL A  47      29.079  18.129  34.095  1.00 10.11           C  
ATOM    293  CG2 VAL A  47      29.977  15.891  34.652  1.00 11.06           C  
ATOM    294  N   ARG A  48      25.741  16.624  33.339  1.00  9.38           N  
ATOM    295  CA  ARG A  48      24.656  17.305  32.633  1.00  8.86           C  
ATOM    296  C   ARG A  48      23.418  17.433  33.499  1.00  7.94           C  
ATOM    297  O   ARG A  48      22.765  18.480  33.532  1.00  7.67           O  
ATOM    298  CB  ARG A  48      24.311  16.556  31.367  1.00  8.42           C  
ATOM    299  CG  ARG A  48      25.475  16.396  30.407  1.00  9.04           C  
ATOM    300  CD  ARG A  48      24.837  15.896  29.134  1.00 10.83           C  
ATOM    301  NE  ARG A  48      25.653  14.825  28.767  1.00 17.99           N  
ATOM    302  CZ  ARG A  48      25.389  13.542  28.691  1.00 11.28           C  
ATOM    303  NH1 ARG A  48      24.253  12.861  28.913  1.00 13.10           N  
ATOM    304  NH2 ARG A  48      26.523  12.957  28.449  1.00 13.72           N  
ATOM    305  N   LYS A  49      23.095  16.404  34.282  1.00  8.42           N  
ATOM    306  CA  LYS A  49      21.964  16.439  35.199  1.00  7.89           C  
ATOM    307  C   LYS A  49      22.304  17.458  36.296  1.00  8.34           C  
ATOM    308  O   LYS A  49      21.398  18.184  36.702  1.00  8.37           O  
ATOM    309  CB  LYS A  49      21.727  15.074  35.871  1.00  9.56           C  
ATOM    310  CG  LYS A  49      21.403  13.857  34.998  1.00  8.64           C  
ATOM    311  CD  LYS A  49      20.027  14.070  34.421  1.00  8.66           C  
ATOM    312  CE  LYS A  49      19.568  12.810  33.729  1.00  9.13           C  
ATOM    313  NZ  LYS A  49      18.257  13.027  33.138  1.00 10.16           N  
ATOM    314  N   ILE A  50      23.526  17.581  36.855  1.00  7.34           N  
ATOM    315  CA  ILE A  50      23.792  18.565  37.882  1.00  7.27           C  
ATOM    316  C   ILE A  50      23.650  19.971  37.322  1.00  6.24           C  
ATOM    317  O   ILE A  50      23.142  20.832  38.031  1.00  6.01           O  
ATOM    318  CB  ILE A  50      25.207  18.266  38.512  1.00  9.41           C  
ATOM    319  CG1 ILE A  50      24.986  18.062  40.029  1.00 10.57           C  
ATOM    320  CG2 ILE A  50      26.245  19.363  38.231  1.00  8.47           C  
ATOM    321  CD1 ILE A  50      24.583  19.300  40.894  1.00  9.89           C  
ATOM    322  N   LEU A  51      23.985  20.227  36.053  1.00  7.46           N  
ATOM    323  CA  LEU A  51      23.814  21.564  35.502  1.00  7.01           C  
ATOM    324  C   LEU A  51      22.334  21.923  35.400  1.00  7.83           C  
ATOM    325  O   LEU A  51      21.962  23.077  35.630  1.00  7.78           O  
ATOM    326  CB  LEU A  51      24.511  21.640  34.152  1.00  7.52           C  
ATOM    327  CG  LEU A  51      26.050  21.706  34.168  1.00 10.22           C  
ATOM    328  CD1 LEU A  51      26.596  21.413  32.760  1.00 10.15           C  
ATOM    329  CD2 LEU A  51      26.494  23.076  34.663  1.00 12.23           C  
ATOM    330  N   ARG A  52      21.443  20.968  35.059  1.00  6.83           N  
ATOM    331  CA  ARG A  52      20.017  21.242  35.097  1.00  7.86           C  
ATOM    332  C   ARG A  52      19.612  21.533  36.554  1.00  7.91           C  
ATOM    333  O   ARG A  52      18.871  22.485  36.834  1.00  7.72           O  
ATOM    334  CB  ARG A  52      19.189  20.054  34.642  1.00  7.78           C  
ATOM    335  CG  ARG A  52      19.033  19.956  33.163  1.00 10.16           C  
ATOM    336  CD  ARG A  52      18.197  18.742  32.758  1.00 10.97           C  
ATOM    337  NE  ARG A  52      16.789  18.903  33.068  1.00 11.68           N  
ATOM    338  CZ  ARG A  52      16.001  17.849  33.350  1.00 11.81           C  
ATOM    339  NH1 ARG A  52      16.449  16.593  33.359  1.00 13.70           N  
ATOM    340  NH2 ARG A  52      14.731  18.060  33.662  1.00 12.42           N  
ATOM    341  N   ILE A  53      20.078  20.723  37.525  1.00  7.54           N  
ATOM    342  CA  ILE A  53      19.749  20.916  38.928  1.00  8.03           C  
ATOM    343  C   ILE A  53      20.204  22.282  39.462  1.00  7.47           C  
ATOM    344  O   ILE A  53      19.420  22.946  40.140  1.00  7.59           O  
ATOM    345  CB  ILE A  53      20.378  19.753  39.757  1.00  7.84           C  
ATOM    346  CG1 ILE A  53      19.563  18.483  39.497  1.00  7.14           C  
ATOM    347  CG2 ILE A  53      20.313  20.016  41.249  1.00  8.99           C  
ATOM    348  CD1 ILE A  53      20.283  17.209  39.981  1.00  7.13           C  
ATOM    349  N   VAL A  54      21.394  22.789  39.161  1.00  7.85           N  
ATOM    350  CA  VAL A  54      21.822  24.052  39.732  1.00  7.89           C  
ATOM    351  C   VAL A  54      20.962  25.195  39.205  1.00  8.06           C  
ATOM    352  O   VAL A  54      20.595  26.067  39.995  1.00  6.81           O  
ATOM    353  CB  VAL A  54      23.349  24.229  39.442  1.00  8.46           C  
ATOM    354  CG1 VAL A  54      23.659  24.520  37.997  1.00  7.61           C  
ATOM    355  CG2 VAL A  54      23.847  25.343  40.333  1.00  9.97           C  
ATOM    356  N   PHE A  55      20.557  25.141  37.921  1.00  9.05           N  
ATOM    357  CA  PHE A  55      19.679  26.129  37.297  1.00  8.76           C  
ATOM    358  C   PHE A  55      18.305  26.034  37.968  1.00  8.92           C  
ATOM    359  O   PHE A  55      17.793  27.036  38.483  1.00  9.05           O  
ATOM    360  CB  PHE A  55      19.557  25.837  35.782  1.00  8.24           C  
ATOM    361  CG  PHE A  55      18.567  26.711  35.007  1.00  8.59           C  
ATOM    362  CD1 PHE A  55      18.380  28.050  35.328  1.00 11.30           C  
ATOM    363  CD2 PHE A  55      17.843  26.156  33.968  1.00  9.89           C  
ATOM    364  CE1 PHE A  55      17.472  28.816  34.617  1.00 11.14           C  
ATOM    365  CE2 PHE A  55      16.936  26.920  33.253  1.00  9.93           C  
ATOM    366  CZ  PHE A  55      16.749  28.250  33.581  1.00 12.26           C  
ATOM    367  N   HIS A  56      17.715  24.837  38.054  1.00  8.77           N  
ATOM    368  CA  HIS A  56      16.379  24.708  38.632  1.00  8.43           C  
ATOM    369  C   HIS A  56      16.319  25.013  40.109  1.00  9.17           C  
ATOM    370  O   HIS A  56      15.268  25.401  40.624  1.00  9.83           O  
ATOM    371  CB  HIS A  56      15.843  23.302  38.358  1.00  9.05           C  
ATOM    372  CG  HIS A  56      15.556  23.035  36.880  1.00  8.59           C  
ATOM    373  ND1 HIS A  56      14.888  21.996  36.389  1.00  9.35           N  
ATOM    374  CD2 HIS A  56      15.996  23.777  35.803  1.00  8.27           C  
ATOM    375  CE1 HIS A  56      14.918  22.084  35.079  1.00 10.64           C  
ATOM    376  NE2 HIS A  56      15.590  23.157  34.732  1.00 11.00           N  
ATOM    377  N   ASP A  57      17.425  24.845  40.802  1.00  8.49           N  
ATOM    378  CA  ASP A  57      17.457  25.218  42.186  1.00 10.57           C  
ATOM    379  C   ASP A  57      17.558  26.747  42.316  1.00 10.03           C  
ATOM    380  O   ASP A  57      16.731  27.335  43.024  1.00  9.66           O  
ATOM    381  CB  ASP A  57      18.660  24.592  42.950  1.00  9.63           C  
ATOM    382  CG  ASP A  57      18.661  24.921  44.440  1.00 11.17           C  
ATOM    383  OD1 ASP A  57      17.582  25.064  45.032  1.00  9.31           O  
ATOM    384  OD2 ASP A  57      19.745  25.060  44.991  1.00 11.33           O  
ATOM    385  N   ALA A  58      18.488  27.385  41.609  1.00  9.26           N  
ATOM    386  CA  ALA A  58      18.707  28.798  41.794  1.00  9.31           C  
ATOM    387  C   ALA A  58      17.627  29.675  41.225  1.00  9.64           C  
ATOM    388  O   ALA A  58      17.300  30.696  41.837  1.00 11.62           O  
ATOM    389  CB  ALA A  58      20.052  29.181  41.177  1.00  8.11           C  
ATOM    390  N   ILE A  59      17.009  29.271  40.109  1.00  9.99           N  
ATOM    391  CA  ILE A  59      15.962  30.069  39.502  1.00 10.85           C  
ATOM    392  C   ILE A  59      14.646  30.134  40.303  1.00 10.99           C  
ATOM    393  O   ILE A  59      13.791  30.966  39.968  1.00 11.34           O  
ATOM    394  CB  ILE A  59      15.752  29.549  38.029  1.00 10.15           C  
ATOM    395  CG1 ILE A  59      15.282  30.738  37.179  1.00 10.83           C  
ATOM    396  CG2 ILE A  59      14.715  28.437  37.920  1.00 10.68           C  
ATOM    397  CD1 ILE A  59      16.312  31.862  37.067  1.00 11.28           C  
ATOM    398  N   GLY A  60      14.426  29.322  41.349  1.00  7.94           N  
ATOM    399  CA  GLY A  60      13.231  29.461  42.155  1.00  9.84           C  
ATOM    400  C   GLY A  60      13.461  30.652  43.087  1.00  9.98           C  
ATOM    401  O   GLY A  60      13.742  30.504  44.293  1.00 10.20           O  
ATOM    402  N   PHE A  61      13.378  31.854  42.520  1.00 10.98           N  
ATOM    403  CA  PHE A  61      13.615  33.103  43.231  1.00 12.56           C  
ATOM    404  C   PHE A  61      12.868  34.165  42.425  1.00 12.97           C  
ATOM    405  O   PHE A  61      13.164  34.402  41.242  1.00 12.88           O  
ATOM    406  CB  PHE A  61      15.112  33.356  43.252  1.00 11.38           C  
ATOM    407  CG  PHE A  61      15.524  34.650  43.920  1.00 11.24           C  
ATOM    408  CD1 PHE A  61      15.443  34.774  45.278  1.00 11.26           C  
ATOM    409  CD2 PHE A  61      15.989  35.692  43.132  1.00 12.57           C  
ATOM    410  CE1 PHE A  61      15.826  35.957  45.864  1.00 13.13           C  
ATOM    411  CE2 PHE A  61      16.371  36.875  43.736  1.00 13.69           C  
ATOM    412  CZ  PHE A  61      16.287  37.008  45.104  1.00 12.22           C  
ATOM    413  N   SER A  62      11.867  34.804  43.041  1.00 12.97           N  
ATOM    414  CA  SER A  62      11.073  35.793  42.348  1.00 13.06           C  
ATOM    415  C   SER A  62      10.842  37.060  43.170  1.00 14.25           C  
ATOM    416  O   SER A  62       9.963  37.099  44.061  1.00 14.57           O  
ATOM    417  CB  SER A  62       9.739  35.153  41.958  1.00 11.01           C  
ATOM    418  OG  SER A  62       8.929  36.118  41.276  1.00 11.22           O  
ATOM    419  N   PRO A  63      11.583  38.156  42.889  1.00 14.07           N  
ATOM    420  CA  PRO A  63      11.376  39.439  43.545  1.00 14.05           C  
ATOM    421  C   PRO A  63       9.941  39.903  43.346  1.00 14.26           C  
ATOM    422  O   PRO A  63       9.352  40.447  44.284  1.00 13.56           O  
ATOM    423  CB  PRO A  63      12.399  40.349  42.910  1.00 14.84           C  
ATOM    424  CG  PRO A  63      13.582  39.411  42.699  1.00 13.67           C  
ATOM    425  CD  PRO A  63      12.854  38.179  42.147  1.00 14.33           C  
ATOM    426  N   ALA A  64       9.342  39.656  42.185  1.00 13.92           N  
ATOM    427  CA  ALA A  64       7.980  40.093  41.931  1.00 16.38           C  
ATOM    428  C   ALA A  64       6.973  39.399  42.863  1.00 17.59           C  
ATOM    429  O   ALA A  64       6.038  40.053  43.361  1.00 18.45           O  
ATOM    430  CB  ALA A  64       7.619  39.808  40.481  1.00 13.96           C  
ATOM    431  N   LEU A  65       7.143  38.120  43.200  1.00 17.24           N  
ATOM    432  CA  LEU A  65       6.257  37.425  44.121  1.00 18.54           C  
ATOM    433  C   LEU A  65       6.442  38.040  45.481  1.00 19.83           C  
ATOM    434  O   LEU A  65       5.441  38.272  46.158  1.00 20.48           O  
ATOM    435  CB  LEU A  65       6.600  35.958  44.218  1.00 18.87           C  
ATOM    436  CG  LEU A  65       5.642  34.932  43.621  1.00 20.75           C  
ATOM    437  CD1 LEU A  65       5.311  35.255  42.191  1.00 21.75           C  
ATOM    438  CD2 LEU A  65       6.299  33.580  43.685  1.00 20.82           C  
ATOM    439  N   THR A  66       7.695  38.312  45.888  1.00 20.04           N  
ATOM    440  CA  THR A  66       7.971  38.940  47.164  1.00 20.80           C  
ATOM    441  C   THR A  66       7.220  40.269  47.240  1.00 22.58           C  
ATOM    442  O   THR A  66       6.490  40.538  48.213  1.00 22.14           O  
ATOM    443  CB  THR A  66       9.495  39.140  47.298  1.00 21.35           C  
ATOM    444  OG1 THR A  66      10.046  37.826  47.277  1.00 22.08           O  
ATOM    445  CG2 THR A  66       9.957  39.783  48.600  1.00 22.29           C  
ATOM    446  N   ALA A  67       7.299  41.029  46.140  1.00 21.21           N  
ATOM    447  CA  ALA A  67       6.657  42.321  46.081  1.00 22.89           C  
ATOM    448  C   ALA A  67       5.162  42.184  46.250  1.00 23.68           C  
ATOM    449  O   ALA A  67       4.563  43.036  46.889  1.00 26.67           O  
ATOM    450  CB  ALA A  67       6.904  43.010  44.758  1.00 20.58           C  
ATOM    451  N   ALA A  68       4.538  41.118  45.763  1.00 25.03           N  
ATOM    452  CA  ALA A  68       3.104  40.931  45.905  1.00 26.03           C  
ATOM    453  C   ALA A  68       2.700  40.313  47.247  1.00 27.61           C  
ATOM    454  O   ALA A  68       1.572  39.849  47.435  1.00 29.24           O  
ATOM    455  CB  ALA A  68       2.611  40.043  44.782  1.00 26.15           C  
ATOM    456  N   GLY A  69       3.602  40.306  48.226  1.00 27.81           N  
ATOM    457  CA  GLY A  69       3.345  39.749  49.532  1.00 28.18           C  
ATOM    458  C   GLY A  69       3.488  38.231  49.584  1.00 29.08           C  
ATOM    459  O   GLY A  69       3.209  37.649  50.638  1.00 30.87           O  
ATOM    460  N   GLN A  70       3.937  37.536  48.537  1.00 27.00           N  
ATOM    461  CA  GLN A  70       4.012  36.089  48.594  1.00 26.37           C  
ATOM    462  C   GLN A  70       5.465  35.671  48.833  1.00 24.86           C  
ATOM    463  O   GLN A  70       6.388  36.489  48.722  1.00 23.68           O  
ATOM    464  CB  GLN A  70       3.499  35.487  47.276  1.00 27.32           C  
ATOM    465  CG  GLN A  70       2.146  35.989  46.756  1.00 31.66           C  
ATOM    466  CD  GLN A  70       1.554  35.192  45.585  1.00 32.99           C  
ATOM    467  OE1 GLN A  70       1.166  35.724  44.546  1.00 34.41           O  
ATOM    468  NE2 GLN A  70       1.458  33.873  45.624  1.00 34.73           N  
ATOM    469  N   PHE A  71       5.710  34.403  49.205  1.00 22.18           N  
ATOM    470  CA  PHE A  71       7.070  33.897  49.361  1.00 20.52           C  
ATOM    471  C   PHE A  71       7.574  33.761  47.920  1.00 18.94           C  
ATOM    472  O   PHE A  71       6.923  33.125  47.083  1.00 20.29           O  
ATOM    473  CB  PHE A  71       7.060  32.535  50.059  1.00 17.69           C  
ATOM    474  CG  PHE A  71       8.443  31.895  50.147  1.00 17.53           C  
ATOM    475  CD1 PHE A  71       9.492  32.556  50.773  1.00 17.05           C  
ATOM    476  CD2 PHE A  71       8.658  30.658  49.562  1.00 16.60           C  
ATOM    477  CE1 PHE A  71      10.743  31.970  50.792  1.00 16.22           C  
ATOM    478  CE2 PHE A  71       9.915  30.098  49.597  1.00 15.74           C  
ATOM    479  CZ  PHE A  71      10.950  30.748  50.206  1.00 14.47           C  
ATOM    480  N   GLY A  72       8.701  34.361  47.586  1.00 17.91           N  
ATOM    481  CA  GLY A  72       9.191  34.305  46.230  1.00 15.85           C  
ATOM    482  C   GLY A  72      10.214  33.216  45.975  1.00 15.30           C  
ATOM    483  O   GLY A  72      10.642  33.113  44.836  1.00 13.41           O  
ATOM    484  N   GLY A  73      10.641  32.398  46.937  1.00 13.24           N  
ATOM    485  CA  GLY A  73      11.650  31.371  46.695  1.00 13.57           C  
ATOM    486  C   GLY A  73      12.971  31.787  47.327  1.00 12.21           C  
ATOM    487  O   GLY A  73      13.243  32.974  47.444  1.00 12.30           O  
ATOM    488  N   GLY A  74      13.788  30.864  47.797  1.00 11.70           N  
ATOM    489  CA  GLY A  74      15.046  31.226  48.426  1.00 12.52           C  
ATOM    490  C   GLY A  74      16.235  31.178  47.474  1.00 13.28           C  
ATOM    491  O   GLY A  74      17.379  31.293  47.944  1.00 13.60           O  
ATOM    492  N   GLY A  75      16.045  30.970  46.173  1.00 11.73           N  
ATOM    493  CA  GLY A  75      17.177  30.957  45.259  1.00 11.57           C  
ATOM    494  C   GLY A  75      18.021  29.696  45.363  1.00 11.65           C  
ATOM    495  O   GLY A  75      17.463  28.586  45.451  1.00 11.25           O  
ATOM    496  N   ALA A  76      19.348  29.865  45.403  1.00  9.81           N  
ATOM    497  CA  ALA A  76      20.305  28.770  45.422  1.00 10.22           C  
ATOM    498  C   ALA A  76      20.451  28.193  46.819  1.00 10.61           C  
ATOM    499  O   ALA A  76      21.546  28.051  47.367  1.00 11.58           O  
ATOM    500  CB  ALA A  76      21.652  29.290  44.917  1.00  8.61           C  
ATOM    501  N   ASP A  77      19.320  27.720  47.366  1.00 10.91           N  
ATOM    502  CA  ASP A  77      19.218  27.206  48.733  1.00 10.80           C  
ATOM    503  C   ASP A  77      19.178  25.691  48.920  1.00  9.76           C  
ATOM    504  O   ASP A  77      18.976  25.192  50.031  1.00 10.90           O  
ATOM    505  CB  ASP A  77      17.969  27.834  49.368  1.00  9.59           C  
ATOM    506  CG  ASP A  77      16.665  27.536  48.633  1.00 11.84           C  
ATOM    507  OD1 ASP A  77      16.663  26.791  47.637  1.00 11.09           O  
ATOM    508  OD2 ASP A  77      15.636  28.058  49.059  1.00 11.43           O  
ATOM    509  N   GLY A  78      19.305  24.923  47.848  1.00  7.96           N  
ATOM    510  CA  GLY A  78      19.215  23.469  47.954  1.00  9.84           C  
ATOM    511  C   GLY A  78      17.797  22.951  48.189  1.00 10.08           C  
ATOM    512  O   GLY A  78      17.615  21.760  48.511  1.00 10.47           O  
ATOM    513  N   SER A  79      16.764  23.780  47.948  1.00 10.29           N  
ATOM    514  CA  SER A  79      15.388  23.372  48.211  1.00  9.72           C  
ATOM    515  C   SER A  79      14.975  22.278  47.238  1.00 10.33           C  
ATOM    516  O   SER A  79      14.074  21.517  47.592  1.00 11.86           O  
ATOM    517  CB  SER A  79      14.440  24.542  48.073  1.00  8.32           C  
ATOM    518  OG  SER A  79      14.472  25.072  46.727  1.00  9.30           O  
ATOM    519  N   ILE A  80      15.586  22.137  46.044  1.00  8.69           N  
ATOM    520  CA  ILE A  80      15.209  21.041  45.161  1.00  8.00           C  
ATOM    521  C   ILE A  80      15.542  19.674  45.781  1.00  9.06           C  
ATOM    522  O   ILE A  80      14.913  18.659  45.454  1.00  8.81           O  
ATOM    523  CB  ILE A  80      15.899  21.314  43.760  1.00  8.53           C  
ATOM    524  CG1 ILE A  80      15.306  20.367  42.672  1.00  7.13           C  
ATOM    525  CG2 ILE A  80      17.419  21.186  43.903  1.00  7.52           C  
ATOM    526  CD1 ILE A  80      15.655  20.711  41.206  1.00  9.15           C  
ATOM    527  N   ILE A  81      16.503  19.622  46.713  1.00  9.51           N  
ATOM    528  CA  ILE A  81      16.839  18.378  47.412  1.00  9.44           C  
ATOM    529  C   ILE A  81      16.012  18.313  48.704  1.00  9.48           C  
ATOM    530  O   ILE A  81      15.236  17.375  48.879  1.00  8.99           O  
ATOM    531  CB  ILE A  81      18.357  18.302  47.773  1.00 10.66           C  
ATOM    532  CG1 ILE A  81      19.206  18.356  46.500  1.00 10.03           C  
ATOM    533  CG2 ILE A  81      18.632  17.003  48.560  1.00 10.04           C  
ATOM    534  CD1 ILE A  81      20.713  18.203  46.721  1.00 11.31           C  
ATOM    535  N   ALA A  82      16.109  19.315  49.591  1.00 10.59           N  
ATOM    536  CA  ALA A  82      15.388  19.303  50.852  1.00 10.78           C  
ATOM    537  C   ALA A  82      13.891  19.171  50.637  1.00 10.33           C  
ATOM    538  O   ALA A  82      13.217  18.524  51.431  1.00 12.29           O  
ATOM    539  CB  ALA A  82      15.640  20.594  51.644  1.00 10.50           C  
ATOM    540  N   HIS A  83      13.331  19.696  49.546  1.00  9.84           N  
ATOM    541  CA  HIS A  83      11.904  19.606  49.288  1.00 11.00           C  
ATOM    542  C   HIS A  83      11.665  18.937  47.960  1.00 11.85           C  
ATOM    543  O   HIS A  83      10.779  19.347  47.211  1.00 12.66           O  
ATOM    544  CB  HIS A  83      11.272  20.986  49.277  1.00  9.21           C  
ATOM    545  CG  HIS A  83      11.478  21.635  50.629  1.00 13.22           C  
ATOM    546  ND1 HIS A  83      10.816  21.283  51.808  1.00 13.81           N  
ATOM    547  CD2 HIS A  83      12.399  22.662  50.862  1.00 13.23           C  
ATOM    548  CE1 HIS A  83      11.323  22.116  52.747  1.00 14.31           C  
ATOM    549  NE2 HIS A  83      12.215  22.912  52.230  1.00 16.61           N  
ATOM    550  N   SER A  84      12.414  17.879  47.651  1.00 12.41           N  
ATOM    551  CA  SER A  84      12.275  17.184  46.387  1.00 12.44           C  
ATOM    552  C   SER A  84      10.881  16.628  46.198  1.00 13.85           C  
ATOM    553  O   SER A  84      10.362  16.578  45.080  1.00 13.42           O  
ATOM    554  CB  SER A  84      13.280  16.046  46.296  1.00 12.39           C  
ATOM    555  OG  SER A  84      13.229  15.221  47.451  1.00 14.12           O  
ATOM    556  N   ASN A  85      10.274  16.187  47.294  1.00 14.08           N  
ATOM    557  CA  ASN A  85       8.900  15.698  47.236  1.00 16.22           C  
ATOM    558  C   ASN A  85       7.939  16.712  46.589  1.00 15.62           C  
ATOM    559  O   ASN A  85       7.039  16.314  45.844  1.00 15.28           O  
ATOM    560  CB  ASN A  85       8.450  15.360  48.665  1.00 20.69           C  
ATOM    561  CG  ASN A  85       8.563  16.559  49.595  1.00 20.39           C  
ATOM    562  OD1 ASN A  85       7.563  17.118  50.012  1.00 27.09           O  
ATOM    563  ND2 ASN A  85       9.733  17.049  49.970  1.00 23.34           N  
ATOM    564  N   ILE A  86       8.073  18.032  46.775  1.00 14.42           N  
ATOM    565  CA  ILE A  86       7.151  18.893  46.076  1.00 14.13           C  
ATOM    566  C   ILE A  86       7.827  19.395  44.798  1.00 11.60           C  
ATOM    567  O   ILE A  86       7.203  19.381  43.739  1.00 10.44           O  
ATOM    568  CB  ILE A  86       6.627  20.097  47.010  1.00 17.58           C  
ATOM    569  CG1 ILE A  86       7.411  21.311  46.808  1.00 19.50           C  
ATOM    570  CG2 ILE A  86       6.695  19.776  48.508  1.00 17.99           C  
ATOM    571  CD1 ILE A  86       6.592  22.257  45.953  1.00 19.20           C  
ATOM    572  N   GLU A  87       9.119  19.754  44.783  1.00 10.73           N  
ATOM    573  CA  GLU A  87       9.687  20.320  43.576  1.00  9.62           C  
ATOM    574  C   GLU A  87       9.863  19.365  42.415  1.00  8.59           C  
ATOM    575  O   GLU A  87       9.789  19.785  41.258  1.00  8.77           O  
ATOM    576  CB  GLU A  87      11.030  20.976  43.893  1.00  8.97           C  
ATOM    577  CG  GLU A  87      10.856  22.165  44.812  1.00  8.81           C  
ATOM    578  CD  GLU A  87      12.088  23.073  44.850  1.00 10.77           C  
ATOM    579  OE1 GLU A  87      12.848  23.146  43.869  1.00  8.35           O  
ATOM    580  OE2 GLU A  87      12.262  23.715  45.882  1.00  9.29           O  
ATOM    581  N   LEU A  88      10.045  18.067  42.615  1.00 10.10           N  
ATOM    582  CA  LEU A  88      10.206  17.174  41.476  1.00 11.82           C  
ATOM    583  C   LEU A  88       8.885  16.807  40.815  1.00 12.84           C  
ATOM    584  O   LEU A  88       8.857  16.036  39.862  1.00 13.98           O  
ATOM    585  CB  LEU A  88      10.976  15.931  41.935  1.00 12.25           C  
ATOM    586  CG  LEU A  88      12.445  16.135  42.359  1.00 13.84           C  
ATOM    587  CD1 LEU A  88      13.088  14.763  42.343  1.00 14.56           C  
ATOM    588  CD2 LEU A  88      13.252  17.025  41.406  1.00 12.72           C  
ATOM    589  N   ALA A  89       7.758  17.340  41.292  1.00 14.74           N  
ATOM    590  CA  ALA A  89       6.474  17.130  40.638  1.00 14.41           C  
ATOM    591  C   ALA A  89       6.304  18.228  39.596  1.00 15.19           C  
ATOM    592  O   ALA A  89       5.401  18.169  38.753  1.00 14.96           O  
ATOM    593  CB  ALA A  89       5.307  17.252  41.611  1.00 16.10           C  
ATOM    594  N   PHE A  90       7.119  19.298  39.645  1.00 14.83           N  
ATOM    595  CA  PHE A  90       7.047  20.391  38.667  1.00 13.22           C  
ATOM    596  C   PHE A  90       7.376  19.859  37.269  1.00 13.20           C  
ATOM    597  O   PHE A  90       8.224  18.975  37.121  1.00 10.81           O  
ATOM    598  CB  PHE A  90       8.045  21.531  38.966  1.00 15.20           C  
ATOM    599  CG  PHE A  90       7.898  22.301  40.275  1.00 15.02           C  
ATOM    600  CD1 PHE A  90       6.798  22.134  41.104  1.00 14.24           C  
ATOM    601  CD2 PHE A  90       8.923  23.170  40.648  1.00 14.31           C  
ATOM    602  CE1 PHE A  90       6.748  22.838  42.298  1.00 15.78           C  
ATOM    603  CE2 PHE A  90       8.851  23.861  41.845  1.00 15.22           C  
ATOM    604  CZ  PHE A  90       7.762  23.696  42.673  1.00 14.74           C  
ATOM    605  N   PRO A  91       6.738  20.361  36.206  1.00 13.82           N  
ATOM    606  CA  PRO A  91       6.923  19.908  34.828  1.00 13.87           C  
ATOM    607  C   PRO A  91       8.360  19.877  34.354  1.00 13.60           C  
ATOM    608  O   PRO A  91       8.749  18.968  33.624  1.00 15.56           O  
ATOM    609  CB  PRO A  91       6.070  20.856  34.001  1.00 14.83           C  
ATOM    610  CG  PRO A  91       4.986  21.288  34.964  1.00 14.88           C  
ATOM    611  CD  PRO A  91       5.780  21.472  36.247  1.00 14.10           C  
ATOM    612  N   ALA A  92       9.148  20.885  34.752  1.00 12.49           N  
ATOM    613  CA  ALA A  92      10.526  20.990  34.328  1.00 11.53           C  
ATOM    614  C   ALA A  92      11.491  20.097  35.060  1.00 11.45           C  
ATOM    615  O   ALA A  92      12.640  20.013  34.620  1.00 12.19           O  
ATOM    616  CB  ALA A  92      11.035  22.403  34.521  1.00 12.13           C  
ATOM    617  N   ASN A  93      11.054  19.384  36.103  1.00  9.13           N  
ATOM    618  CA  ASN A  93      11.988  18.657  36.926  1.00  8.33           C  
ATOM    619  C   ASN A  93      11.951  17.176  36.750  1.00  9.00           C  
ATOM    620  O   ASN A  93      12.332  16.433  37.658  1.00 11.47           O  
ATOM    621  CB  ASN A  93      11.756  18.976  38.403  1.00  9.16           C  
ATOM    622  CG  ASN A  93      12.356  20.299  38.824  1.00  9.60           C  
ATOM    623  OD1 ASN A  93      13.405  20.683  38.314  1.00 11.53           O  
ATOM    624  ND2 ASN A  93      11.790  21.072  39.731  1.00  8.76           N  
ATOM    625  N   GLY A  94      11.547  16.696  35.576  1.00  9.43           N  
ATOM    626  CA  GLY A  94      11.539  15.268  35.340  1.00  8.92           C  
ATOM    627  C   GLY A  94      12.948  14.761  35.072  1.00  9.54           C  
ATOM    628  O   GLY A  94      13.852  15.521  34.710  1.00  9.85           O  
ATOM    629  N   GLY A  95      13.183  13.480  35.303  1.00  8.80           N  
ATOM    630  CA  GLY A  95      14.461  12.844  35.032  1.00 10.07           C  
ATOM    631  C   GLY A  95      15.606  13.253  35.954  1.00 11.10           C  
ATOM    632  O   GLY A  95      16.773  13.032  35.624  1.00 10.78           O  
ATOM    633  N   LEU A  96      15.270  13.777  37.129  1.00 11.19           N  
ATOM    634  CA  LEU A  96      16.250  14.260  38.076  1.00 10.94           C  
ATOM    635  C   LEU A  96      16.298  13.476  39.368  1.00 12.61           C  
ATOM    636  O   LEU A  96      17.285  13.582  40.125  1.00 11.10           O  
ATOM    637  CB  LEU A  96      15.961  15.720  38.421  1.00 11.08           C  
ATOM    638  CG  LEU A  96      16.126  16.749  37.314  1.00 10.58           C  
ATOM    639  CD1 LEU A  96      15.789  18.119  37.867  1.00 11.28           C  
ATOM    640  CD2 LEU A  96      17.546  16.695  36.758  1.00 13.17           C  
ATOM    641  N   THR A  97      15.281  12.655  39.667  1.00 12.89           N  
ATOM    642  CA  THR A  97      15.238  11.939  40.930  1.00 13.40           C  
ATOM    643  C   THR A  97      16.476  11.144  41.322  1.00 12.27           C  
ATOM    644  O   THR A  97      16.956  11.267  42.456  1.00 12.60           O  
ATOM    645  CB  THR A  97      14.041  10.972  40.960  1.00 15.15           C  
ATOM    646  OG1 THR A  97      12.937  11.553  40.273  1.00 19.10           O  
ATOM    647  CG2 THR A  97      13.667  10.680  42.394  1.00 16.31           C  
ATOM    648  N   ASP A  98      17.025  10.328  40.435  1.00 11.19           N  
ATOM    649  CA  ASP A  98      18.192   9.549  40.771  1.00 10.78           C  
ATOM    650  C   ASP A  98      19.386  10.415  41.120  1.00 10.22           C  
ATOM    651  O   ASP A  98      20.078  10.098  42.091  1.00  9.04           O  
ATOM    652  CB  ASP A  98      18.531   8.618  39.605  1.00 13.67           C  
ATOM    653  CG  ASP A  98      17.455   7.566  39.335  1.00 14.97           C  
ATOM    654  OD1 ASP A  98      16.623   7.297  40.203  1.00 16.20           O  
ATOM    655  OD2 ASP A  98      17.449   7.013  38.235  1.00 17.34           O  
ATOM    656  N   THR A  99      19.617  11.507  40.409  1.00  9.10           N  
ATOM    657  CA  THR A  99      20.721  12.392  40.708  1.00  9.33           C  
ATOM    658  C   THR A  99      20.496  13.105  42.040  1.00  8.79           C  
ATOM    659  O   THR A  99      21.430  13.205  42.849  1.00 10.37           O  
ATOM    660  CB  THR A  99      20.859  13.414  39.603  1.00  9.18           C  
ATOM    661  OG1 THR A  99      20.927  12.730  38.353  1.00 10.53           O  
ATOM    662  CG2 THR A  99      22.133  14.221  39.787  1.00 11.50           C  
ATOM    663  N   ILE A 100      19.271  13.579  42.306  1.00  9.47           N  
ATOM    664  CA  ILE A 100      18.951  14.254  43.567  1.00  9.07           C  
ATOM    665  C   ILE A 100      19.222  13.338  44.759  1.00 10.33           C  
ATOM    666  O   ILE A 100      19.759  13.801  45.771  1.00  9.67           O  
ATOM    667  CB  ILE A 100      17.451  14.708  43.549  1.00  8.96           C  
ATOM    668  CG1 ILE A 100      17.290  15.886  42.572  1.00 10.02           C  
ATOM    669  CG2 ILE A 100      16.960  15.115  44.952  1.00  7.77           C  
ATOM    670  CD1 ILE A 100      18.026  17.172  42.956  1.00 11.41           C  
ATOM    671  N   GLU A 101      18.889  12.041  44.684  1.00 10.03           N  
ATOM    672  CA  GLU A 101      19.137  11.123  45.789  1.00 10.40           C  
ATOM    673  C   GLU A 101      20.611  10.881  46.032  1.00 10.55           C  
ATOM    674  O   GLU A 101      21.052  10.828  47.187  1.00 11.21           O  
ATOM    675  CB  GLU A 101      18.415   9.783  45.535  1.00 11.19           C  
ATOM    676  CG  GLU A 101      16.887  10.014  45.643  1.00 12.39           C  
ATOM    677  CD  GLU A 101      16.353  10.535  46.983  1.00 13.49           C  
ATOM    678  OE1 GLU A 101      16.921  10.237  48.039  1.00 15.13           O  
ATOM    679  OE2 GLU A 101      15.353  11.247  46.970  1.00 15.47           O  
ATOM    680  N   ALA A 102      21.396  10.816  44.956  1.00 10.54           N  
ATOM    681  CA  ALA A 102      22.816  10.604  45.085  1.00  9.23           C  
ATOM    682  C   ALA A 102      23.416  11.818  45.765  1.00 11.45           C  
ATOM    683  O   ALA A 102      24.259  11.667  46.662  1.00 11.49           O  
ATOM    684  CB  ALA A 102      23.462  10.464  43.751  1.00  9.89           C  
ATOM    685  N   LEU A 103      22.946  13.024  45.422  1.00 12.12           N  
ATOM    686  CA  LEU A 103      23.463  14.249  46.047  1.00 11.50           C  
ATOM    687  C   LEU A 103      23.049  14.349  47.500  1.00 11.59           C  
ATOM    688  O   LEU A 103      23.846  14.763  48.355  1.00 10.85           O  
ATOM    689  CB  LEU A 103      22.965  15.495  45.318  1.00 12.65           C  
ATOM    690  CG  LEU A 103      23.615  15.732  43.972  1.00 14.26           C  
ATOM    691  CD1 LEU A 103      22.808  16.784  43.235  1.00 15.20           C  
ATOM    692  CD2 LEU A 103      25.082  16.122  44.155  1.00 14.22           C  
ATOM    693  N   ARG A 104      21.815  13.915  47.791  1.00 11.25           N  
ATOM    694  CA  ARG A 104      21.295  13.913  49.150  1.00 11.96           C  
ATOM    695  C   ARG A 104      22.214  13.078  50.036  1.00 11.60           C  
ATOM    696  O   ARG A 104      22.659  13.576  51.062  1.00 11.81           O  
ATOM    697  CB  ARG A 104      19.887  13.315  49.220  1.00 10.96           C  
ATOM    698  CG  ARG A 104      19.231  13.594  50.586  1.00  9.88           C  
ATOM    699  CD  ARG A 104      18.019  12.702  50.805  1.00  8.80           C  
ATOM    700  NE  ARG A 104      17.070  12.783  49.703  1.00 11.07           N  
ATOM    701  CZ  ARG A 104      16.276  13.841  49.480  1.00 10.23           C  
ATOM    702  NH1 ARG A 104      16.268  14.921  50.255  1.00 12.98           N  
ATOM    703  NH2 ARG A 104      15.522  13.846  48.392  1.00 12.52           N  
ATOM    704  N   ALA A 105      22.567  11.850  49.651  1.00 11.93           N  
ATOM    705  CA  ALA A 105      23.439  11.026  50.475  1.00 11.46           C  
ATOM    706  C   ALA A 105      24.800  11.671  50.711  1.00 11.93           C  
ATOM    707  O   ALA A 105      25.311  11.652  51.839  1.00 11.96           O  
ATOM    708  CB  ALA A 105      23.646   9.694  49.809  1.00 10.03           C  
ATOM    709  N   VAL A 106      25.385  12.320  49.690  1.00 11.79           N  
ATOM    710  CA  VAL A 106      26.699  12.954  49.867  1.00 12.35           C  
ATOM    711  C   VAL A 106      26.625  14.126  50.850  1.00 13.36           C  
ATOM    712  O   VAL A 106      27.472  14.246  51.747  1.00 13.91           O  
ATOM    713  CB  VAL A 106      27.219  13.435  48.505  1.00 11.33           C  
ATOM    714  CG1 VAL A 106      28.494  14.263  48.660  1.00 11.04           C  
ATOM    715  CG2 VAL A 106      27.558  12.195  47.659  1.00 10.65           C  
ATOM    716  N   GLY A 107      25.606  14.994  50.723  1.00 13.19           N  
ATOM    717  CA  GLY A 107      25.429  16.115  51.640  1.00 12.94           C  
ATOM    718  C   GLY A 107      25.239  15.655  53.088  1.00 14.36           C  
ATOM    719  O   GLY A 107      25.851  16.222  54.003  1.00 12.65           O  
ATOM    720  N   ILE A 108      24.403  14.646  53.328  1.00 15.18           N  
ATOM    721  CA  ILE A 108      24.186  14.105  54.662  1.00 16.21           C  
ATOM    722  C   ILE A 108      25.493  13.470  55.130  1.00 17.15           C  
ATOM    723  O   ILE A 108      25.900  13.741  56.257  1.00 18.80           O  
ATOM    724  CB  ILE A 108      23.030  13.081  54.580  1.00 17.32           C  
ATOM    725  CG1 ILE A 108      21.723  13.813  54.468  1.00 16.80           C  
ATOM    726  CG2 ILE A 108      23.018  12.183  55.796  1.00 20.00           C  
ATOM    727  CD1 ILE A 108      20.609  12.800  54.154  1.00 15.87           C  
ATOM    728  N   ASN A 109      26.241  12.705  54.336  1.00 17.11           N  
ATOM    729  CA  ASN A 109      27.488  12.114  54.808  1.00 18.16           C  
ATOM    730  C   ASN A 109      28.585  13.083  55.162  1.00 17.41           C  
ATOM    731  O   ASN A 109      29.304  12.849  56.123  1.00 19.42           O  
ATOM    732  CB  ASN A 109      28.035  11.159  53.786  1.00 19.67           C  
ATOM    733  CG  ASN A 109      27.188   9.895  53.712  1.00 24.10           C  
ATOM    734  OD1 ASN A 109      26.207   9.631  54.440  1.00 25.68           O  
ATOM    735  ND2 ASN A 109      27.565   9.071  52.757  1.00 25.60           N  
ATOM    736  N   HIS A 110      28.748  14.196  54.472  1.00 15.97           N  
ATOM    737  CA  HIS A 110      29.821  15.114  54.794  1.00 15.74           C  
ATOM    738  C   HIS A 110      29.401  16.280  55.657  1.00 15.71           C  
ATOM    739  O   HIS A 110      30.232  17.099  56.082  1.00 16.94           O  
ATOM    740  CB  HIS A 110      30.452  15.660  53.509  1.00 16.19           C  
ATOM    741  CG  HIS A 110      31.252  14.600  52.772  1.00 15.99           C  
ATOM    742  ND1 HIS A 110      30.781  13.786  51.736  1.00 17.88           N  
ATOM    743  CD2 HIS A 110      32.580  14.317  53.066  1.00 14.74           C  
ATOM    744  CE1 HIS A 110      31.844  13.019  51.423  1.00 13.97           C  
ATOM    745  NE2 HIS A 110      32.878  13.303  52.157  1.00 17.33           N  
ATOM    746  N   GLY A 111      28.116  16.401  55.918  1.00 14.08           N  
ATOM    747  CA  GLY A 111      27.619  17.459  56.753  1.00 14.41           C  
ATOM    748  C   GLY A 111      27.708  18.828  56.120  1.00 14.51           C  
ATOM    749  O   GLY A 111      27.984  19.781  56.848  1.00 16.95           O  
ATOM    750  N   VAL A 112      27.499  18.983  54.813  1.00 13.23           N  
ATOM    751  CA  VAL A 112      27.567  20.279  54.171  1.00 11.18           C  
ATOM    752  C   VAL A 112      26.150  20.689  53.790  1.00 13.16           C  
ATOM    753  O   VAL A 112      25.287  19.801  53.665  1.00 12.07           O  
ATOM    754  CB  VAL A 112      28.491  20.210  52.935  1.00 12.66           C  
ATOM    755  CG1 VAL A 112      29.905  19.918  53.438  1.00 12.05           C  
ATOM    756  CG2 VAL A 112      28.085  19.119  51.938  1.00 11.34           C  
ATOM    757  N   SER A 113      25.824  21.974  53.596  1.00 10.58           N  
ATOM    758  CA  SER A 113      24.461  22.342  53.277  1.00 10.78           C  
ATOM    759  C   SER A 113      24.125  21.929  51.853  1.00  9.16           C  
ATOM    760  O   SER A 113      24.994  21.864  50.982  1.00  9.35           O  
ATOM    761  CB  SER A 113      24.258  23.846  53.425  1.00  9.90           C  
ATOM    762  OG  SER A 113      24.917  24.639  52.457  1.00 12.35           O  
ATOM    763  N   PHE A 114      22.867  21.643  51.571  1.00  9.62           N  
ATOM    764  CA  PHE A 114      22.482  21.241  50.229  1.00  9.51           C  
ATOM    765  C   PHE A 114      22.738  22.287  49.167  1.00 10.59           C  
ATOM    766  O   PHE A 114      23.155  21.935  48.055  1.00 10.62           O  
ATOM    767  CB  PHE A 114      21.000  20.870  50.204  1.00 10.61           C  
ATOM    768  CG  PHE A 114      20.700  19.556  50.930  1.00 11.94           C  
ATOM    769  CD1 PHE A 114      21.655  18.548  51.009  1.00 12.07           C  
ATOM    770  CD2 PHE A 114      19.443  19.388  51.493  1.00 12.05           C  
ATOM    771  CE1 PHE A 114      21.342  17.370  51.659  1.00 13.14           C  
ATOM    772  CE2 PHE A 114      19.148  18.204  52.135  1.00 12.25           C  
ATOM    773  CZ  PHE A 114      20.090  17.200  52.221  1.00 12.52           C  
ATOM    774  N   GLY A 115      22.500  23.578  49.475  1.00  9.27           N  
ATOM    775  CA  GLY A 115      22.712  24.679  48.529  1.00  8.22           C  
ATOM    776  C   GLY A 115      24.170  24.784  48.134  1.00  7.88           C  
ATOM    777  O   GLY A 115      24.506  24.922  46.954  1.00  8.25           O  
ATOM    778  N   ASP A 116      25.061  24.645  49.108  1.00  9.16           N  
ATOM    779  CA  ASP A 116      26.489  24.669  48.842  1.00  9.46           C  
ATOM    780  C   ASP A 116      26.918  23.451  48.031  1.00 10.42           C  
ATOM    781  O   ASP A 116      27.687  23.552  47.058  1.00 11.69           O  
ATOM    782  CB  ASP A 116      27.306  24.663  50.143  1.00 10.78           C  
ATOM    783  CG  ASP A 116      27.408  25.959  50.953  1.00  9.44           C  
ATOM    784  OD1 ASP A 116      27.062  27.015  50.450  1.00 11.53           O  
ATOM    785  OD2 ASP A 116      27.867  25.909  52.090  1.00 12.81           O  
ATOM    786  N   LEU A 117      26.386  22.283  48.399  1.00  9.04           N  
ATOM    787  CA  LEU A 117      26.749  21.061  47.706  1.00  9.74           C  
ATOM    788  C   LEU A 117      26.430  21.138  46.220  1.00  7.87           C  
ATOM    789  O   LEU A 117      27.226  20.699  45.386  1.00  6.49           O  
ATOM    790  CB  LEU A 117      26.012  19.843  48.302  1.00 10.04           C  
ATOM    791  CG  LEU A 117      26.310  18.515  47.612  1.00 12.75           C  
ATOM    792  CD1 LEU A 117      27.768  18.112  47.786  1.00 12.18           C  
ATOM    793  CD2 LEU A 117      25.358  17.485  48.174  1.00 15.09           C  
ATOM    794  N   ILE A 118      25.263  21.681  45.863  1.00  7.13           N  
ATOM    795  CA  ILE A 118      24.895  21.760  44.457  1.00  7.42           C  
ATOM    796  C   ILE A 118      25.856  22.681  43.711  1.00  7.05           C  
ATOM    797  O   ILE A 118      26.301  22.343  42.610  1.00  6.88           O  
ATOM    798  CB  ILE A 118      23.421  22.236  44.341  1.00  7.70           C  
ATOM    799  CG1 ILE A 118      22.475  21.107  44.759  1.00  6.08           C  
ATOM    800  CG2 ILE A 118      23.101  22.615  42.895  1.00  9.53           C  
ATOM    801  CD1 ILE A 118      20.995  21.539  44.950  1.00  6.93           C  
ATOM    802  N   GLN A 119      26.235  23.805  44.326  1.00  6.27           N  
ATOM    803  CA  GLN A 119      27.161  24.734  43.682  1.00  7.56           C  
ATOM    804  C   GLN A 119      28.555  24.122  43.512  1.00  7.09           C  
ATOM    805  O   GLN A 119      29.237  24.301  42.496  1.00  8.43           O  
ATOM    806  CB  GLN A 119      27.252  26.017  44.508  1.00  7.42           C  
ATOM    807  CG  GLN A 119      25.970  26.855  44.521  1.00 10.19           C  
ATOM    808  CD  GLN A 119      25.440  27.239  43.141  1.00 10.47           C  
ATOM    809  OE1 GLN A 119      26.177  27.432  42.175  1.00 14.58           O  
ATOM    810  NE2 GLN A 119      24.154  27.327  42.921  1.00 14.12           N  
ATOM    811  N   PHE A 120      28.971  23.342  44.510  1.00  9.17           N  
ATOM    812  CA  PHE A 120      30.264  22.671  44.491  1.00  8.60           C  
ATOM    813  C   PHE A 120      30.251  21.569  43.446  1.00  8.42           C  
ATOM    814  O   PHE A 120      31.154  21.520  42.606  1.00  7.85           O  
ATOM    815  CB  PHE A 120      30.567  22.071  45.867  1.00  8.09           C  
ATOM    816  CG  PHE A 120      31.952  21.456  45.948  1.00  8.67           C  
ATOM    817  CD1 PHE A 120      33.060  22.268  45.925  1.00  8.90           C  
ATOM    818  CD2 PHE A 120      32.083  20.078  46.034  1.00  9.87           C  
ATOM    819  CE1 PHE A 120      34.324  21.714  45.987  1.00 10.81           C  
ATOM    820  CE2 PHE A 120      33.358  19.536  46.089  1.00 11.30           C  
ATOM    821  CZ  PHE A 120      34.471  20.347  46.067  1.00  8.87           C  
ATOM    822  N   ALA A 121      29.252  20.667  43.424  1.00  8.06           N  
ATOM    823  CA  ALA A 121      29.202  19.601  42.431  1.00  6.68           C  
ATOM    824  C   ALA A 121      29.135  20.200  41.041  1.00  7.18           C  
ATOM    825  O   ALA A 121      29.674  19.575  40.129  1.00  7.57           O  
ATOM    826  CB  ALA A 121      27.988  18.722  42.656  1.00  8.85           C  
ATOM    827  N   THR A 122      28.570  21.403  40.844  1.00  7.13           N  
ATOM    828  CA  THR A 122      28.580  22.018  39.519  1.00  8.27           C  
ATOM    829  C   THR A 122      30.002  22.428  39.123  1.00  8.31           C  
ATOM    830  O   THR A 122      30.466  22.067  38.039  1.00  8.34           O  
ATOM    831  CB  THR A 122      27.637  23.250  39.486  1.00  8.93           C  
ATOM    832  OG1 THR A 122      26.323  22.738  39.698  1.00  8.85           O  
ATOM    833  CG2 THR A 122      27.606  23.984  38.121  1.00  7.97           C  
ATOM    834  N   ALA A 123      30.735  23.108  40.002  1.00  8.63           N  
ATOM    835  CA  ALA A 123      32.097  23.505  39.665  1.00  8.70           C  
ATOM    836  C   ALA A 123      32.989  22.272  39.413  1.00  8.53           C  
ATOM    837  O   ALA A 123      33.744  22.217  38.425  1.00  8.47           O  
ATOM    838  CB  ALA A 123      32.623  24.356  40.820  1.00 10.36           C  
ATOM    839  N   VAL A 124      32.884  21.229  40.245  1.00  9.04           N  
ATOM    840  CA  VAL A 124      33.659  19.996  40.088  1.00  9.12           C  
ATOM    841  C   VAL A 124      33.288  19.231  38.816  1.00  8.96           C  
ATOM    842  O   VAL A 124      34.194  18.871  38.055  1.00  9.46           O  
ATOM    843  CB  VAL A 124      33.454  19.133  41.333  1.00 10.04           C  
ATOM    844  CG1 VAL A 124      34.179  17.786  41.194  1.00 10.18           C  
ATOM    845  CG2 VAL A 124      34.027  19.893  42.516  1.00  8.15           C  
ATOM    846  N   GLY A 125      31.998  19.002  38.544  1.00  9.64           N  
ATOM    847  CA  GLY A 125      31.541  18.338  37.339  1.00  9.73           C  
ATOM    848  C   GLY A 125      32.043  19.070  36.106  1.00 10.64           C  
ATOM    849  O   GLY A 125      32.554  18.429  35.172  1.00 11.03           O  
ATOM    850  N   MET A 126      31.970  20.415  36.085  1.00  8.84           N  
ATOM    851  CA  MET A 126      32.467  21.150  34.943  1.00 10.58           C  
ATOM    852  C   MET A 126      33.972  20.990  34.779  1.00 10.37           C  
ATOM    853  O   MET A 126      34.417  20.882  33.639  1.00 10.52           O  
ATOM    854  CB  MET A 126      32.135  22.616  35.050  1.00 10.73           C  
ATOM    855  CG  MET A 126      30.665  22.720  34.674  1.00 15.40           C  
ATOM    856  SD  MET A 126      30.290  24.339  33.972  1.00 17.06           S  
ATOM    857  CE  MET A 126      31.022  24.237  32.363  1.00 13.46           C  
ATOM    858  N   SER A 127      34.783  20.881  35.845  1.00  9.28           N  
ATOM    859  CA  SER A 127      36.212  20.692  35.697  1.00 10.83           C  
ATOM    860  C   SER A 127      36.560  19.374  35.005  1.00 11.42           C  
ATOM    861  O   SER A 127      37.716  19.198  34.598  1.00 14.79           O  
ATOM    862  CB  SER A 127      36.892  20.725  37.069  1.00  9.88           C  
ATOM    863  OG  SER A 127      36.844  19.544  37.864  1.00 12.53           O  
ATOM    864  N   ASN A 128      35.639  18.398  34.869  1.00 10.86           N  
ATOM    865  CA  ASN A 128      35.891  17.136  34.173  1.00 10.62           C  
ATOM    866  C   ASN A 128      35.662  17.250  32.670  1.00 11.66           C  
ATOM    867  O   ASN A 128      35.967  16.324  31.898  1.00 11.77           O  
ATOM    868  CB  ASN A 128      34.975  16.032  34.682  1.00 10.33           C  
ATOM    869  CG  ASN A 128      35.185  15.729  36.147  1.00 10.62           C  
ATOM    870  OD1 ASN A 128      34.288  15.267  36.854  1.00 10.89           O  
ATOM    871  ND2 ASN A 128      36.373  15.942  36.689  1.00 10.03           N  
ATOM    872  N   CYS A 129      35.102  18.376  32.223  1.00 10.22           N  
ATOM    873  CA  CYS A 129      34.778  18.544  30.830  1.00 10.70           C  
ATOM    874  C   CYS A 129      35.769  19.473  30.172  1.00 10.38           C  
ATOM    875  O   CYS A 129      35.883  20.631  30.595  1.00  9.98           O  
ATOM    876  CB  CYS A 129      33.387  19.128  30.697  1.00 10.21           C  
ATOM    877  SG  CYS A 129      32.188  18.107  31.562  1.00 12.23           S  
ATOM    878  N   PRO A 130      36.473  19.021  29.126  1.00  9.73           N  
ATOM    879  CA  PRO A 130      37.468  19.824  28.421  1.00  9.83           C  
ATOM    880  C   PRO A 130      36.935  21.167  27.951  1.00  9.55           C  
ATOM    881  O   PRO A 130      35.823  21.264  27.430  1.00  8.25           O  
ATOM    882  CB  PRO A 130      37.924  18.949  27.277  1.00 10.04           C  
ATOM    883  CG  PRO A 130      37.693  17.542  27.805  1.00 11.36           C  
ATOM    884  CD  PRO A 130      36.401  17.655  28.587  1.00 11.08           C  
ATOM    885  N   GLY A 131      37.734  22.197  28.177  1.00  9.24           N  
ATOM    886  CA  GLY A 131      37.383  23.524  27.737  1.00 11.02           C  
ATOM    887  C   GLY A 131      36.676  24.341  28.797  1.00 11.40           C  
ATOM    888  O   GLY A 131      36.523  25.548  28.586  1.00 11.66           O  
ATOM    889  N   SER A 132      36.250  23.756  29.916  1.00 11.51           N  
ATOM    890  CA  SER A 132      35.532  24.532  30.923  1.00 12.70           C  
ATOM    891  C   SER A 132      36.370  25.569  31.683  1.00 12.29           C  
ATOM    892  O   SER A 132      37.571  25.367  31.881  1.00 11.86           O  
ATOM    893  CB  SER A 132      34.899  23.599  31.944  1.00 10.34           C  
ATOM    894  OG  SER A 132      33.974  22.736  31.282  1.00 13.52           O  
ATOM    895  N   PRO A 133      35.796  26.708  32.098  1.00 13.24           N  
ATOM    896  CA  PRO A 133      36.471  27.670  32.955  1.00 12.95           C  
ATOM    897  C   PRO A 133      36.440  27.137  34.398  1.00 13.35           C  
ATOM    898  O   PRO A 133      35.734  26.164  34.719  1.00 13.62           O  
ATOM    899  CB  PRO A 133      35.685  28.957  32.729  1.00 12.75           C  
ATOM    900  CG  PRO A 133      34.274  28.474  32.504  1.00 14.28           C  
ATOM    901  CD  PRO A 133      34.486  27.216  31.665  1.00 13.36           C  
ATOM    902  N   ARG A 134      37.212  27.730  35.303  1.00 14.36           N  
ATOM    903  CA  ARG A 134      37.183  27.339  36.684  1.00 14.31           C  
ATOM    904  C   ARG A 134      36.080  28.195  37.296  1.00 12.85           C  
ATOM    905  O   ARG A 134      36.186  29.415  37.391  1.00 12.84           O  
ATOM    906  CB  ARG A 134      38.497  27.636  37.355  1.00 16.58           C  
ATOM    907  CG  ARG A 134      39.538  26.597  37.037  1.00 20.19           C  
ATOM    908  CD  ARG A 134      40.837  26.940  37.762  1.00 23.26           C  
ATOM    909  NE  ARG A 134      40.758  26.665  39.188  1.00 22.80           N  
ATOM    910  CZ  ARG A 134      41.071  27.567  40.121  1.00 24.91           C  
ATOM    911  NH1 ARG A 134      41.485  28.801  39.807  1.00 24.10           N  
ATOM    912  NH2 ARG A 134      40.936  27.220  41.404  1.00 23.23           N  
ATOM    913  N   LEU A 135      34.981  27.597  37.719  1.00 12.45           N  
ATOM    914  CA  LEU A 135      33.887  28.381  38.310  1.00 12.39           C  
ATOM    915  C   LEU A 135      34.205  28.798  39.739  1.00 10.74           C  
ATOM    916  O   LEU A 135      34.930  28.092  40.472  1.00 10.50           O  
ATOM    917  CB  LEU A 135      32.583  27.534  38.259  1.00 12.36           C  
ATOM    918  CG  LEU A 135      31.545  27.691  37.103  1.00 14.14           C  
ATOM    919  CD1 LEU A 135      32.192  27.964  35.793  1.00 13.99           C  
ATOM    920  CD2 LEU A 135      30.673  26.442  37.086  1.00 13.61           C  
ATOM    921  N   GLU A 136      33.688  29.956  40.141  1.00  9.47           N  
ATOM    922  CA  GLU A 136      33.874  30.437  41.502  1.00  8.96           C  
ATOM    923  C   GLU A 136      33.165  29.491  42.471  1.00  8.26           C  
ATOM    924  O   GLU A 136      32.168  28.873  42.069  1.00 10.12           O  
ATOM    925  CB  GLU A 136      33.280  31.826  41.598  1.00 10.23           C  
ATOM    926  CG  GLU A 136      33.301  32.449  42.978  1.00 11.97           C  
ATOM    927  CD  GLU A 136      32.630  33.806  42.989  1.00 13.46           C  
ATOM    928  OE1 GLU A 136      31.405  33.869  43.005  1.00 14.07           O  
ATOM    929  OE2 GLU A 136      33.341  34.804  42.965  1.00 16.83           O  
ATOM    930  N   PHE A 137      33.637  29.279  43.700  1.00  6.51           N  
ATOM    931  CA  PHE A 137      32.928  28.448  44.645  1.00  8.44           C  
ATOM    932  C   PHE A 137      32.970  29.141  45.986  1.00  9.40           C  
ATOM    933  O   PHE A 137      34.038  29.363  46.561  1.00 10.39           O  
ATOM    934  CB  PHE A 137      33.551  27.016  44.768  1.00  8.66           C  
ATOM    935  CG  PHE A 137      32.884  26.210  45.880  1.00 10.77           C  
ATOM    936  CD1 PHE A 137      31.498  26.040  45.890  1.00  9.34           C  
ATOM    937  CD2 PHE A 137      33.652  25.750  46.930  1.00  9.33           C  
ATOM    938  CE1 PHE A 137      30.882  25.426  46.965  1.00 11.75           C  
ATOM    939  CE2 PHE A 137      33.030  25.136  48.003  1.00 12.46           C  
ATOM    940  CZ  PHE A 137      31.648  24.977  48.025  1.00 11.60           C  
ATOM    941  N   LEU A 138      31.778  29.482  46.461  1.00  8.96           N  
ATOM    942  CA  LEU A 138      31.564  30.123  47.752  1.00 11.38           C  
ATOM    943  C   LEU A 138      30.881  29.155  48.717  1.00 10.87           C  
ATOM    944  O   LEU A 138      29.993  28.417  48.300  1.00 11.93           O  
ATOM    945  CB  LEU A 138      30.687  31.377  47.550  1.00 12.13           C  
ATOM    946  CG  LEU A 138      31.307  32.759  47.304  1.00 16.43           C  
ATOM    947  CD1 LEU A 138      32.656  32.692  46.632  1.00 15.64           C  
ATOM    948  CD2 LEU A 138      30.302  33.549  46.503  1.00 14.89           C  
ATOM    949  N   THR A 139      31.213  29.082  49.995  1.00 12.03           N  
ATOM    950  CA  THR A 139      30.573  28.171  50.916  1.00 11.10           C  
ATOM    951  C   THR A 139      29.945  29.012  52.026  1.00 12.17           C  
ATOM    952  O   THR A 139      30.390  30.138  52.276  1.00 11.85           O  
ATOM    953  CB  THR A 139      31.641  27.185  51.453  1.00 11.52           C  
ATOM    954  OG1 THR A 139      30.958  26.199  52.222  1.00 12.54           O  
ATOM    955  CG2 THR A 139      32.668  27.821  52.386  1.00 10.77           C  
ATOM    956  N   GLY A 140      28.932  28.491  52.729  1.00 11.23           N  
ATOM    957  CA  GLY A 140      28.273  29.203  53.814  1.00  9.13           C  
ATOM    958  C   GLY A 140      26.777  29.359  53.650  1.00  9.77           C  
ATOM    959  O   GLY A 140      26.130  29.879  54.544  1.00 11.32           O  
ATOM    960  N   ARG A 141      26.158  28.980  52.550  1.00  9.08           N  
ATOM    961  CA  ARG A 141      24.718  29.090  52.390  1.00 10.39           C  
ATOM    962  C   ARG A 141      23.980  28.258  53.446  1.00 11.60           C  
ATOM    963  O   ARG A 141      24.345  27.103  53.681  1.00 12.88           O  
ATOM    964  CB  ARG A 141      24.300  28.612  50.962  1.00 11.47           C  
ATOM    965  CG  ARG A 141      24.674  29.659  49.887  1.00 12.93           C  
ATOM    966  CD  ARG A 141      24.370  29.405  48.393  1.00 17.10           C  
ATOM    967  NE  ARG A 141      25.546  28.722  48.064  1.00 20.40           N  
ATOM    968  CZ  ARG A 141      26.546  29.023  47.261  1.00 17.46           C  
ATOM    969  NH1 ARG A 141      26.818  30.032  46.432  1.00 16.49           N  
ATOM    970  NH2 ARG A 141      27.549  28.296  47.663  1.00 19.91           N  
ATOM    971  N   SER A 142      23.013  28.839  54.158  1.00 11.04           N  
ATOM    972  CA  SER A 142      22.220  28.135  55.125  1.00 12.11           C  
ATOM    973  C   SER A 142      21.561  26.896  54.531  1.00 11.83           C  
ATOM    974  O   SER A 142      21.028  26.909  53.423  1.00 12.34           O  
ATOM    975  CB  SER A 142      21.100  29.017  55.661  1.00 14.02           C  
ATOM    976  OG  SER A 142      20.290  28.252  56.581  1.00 20.12           O  
ATOM    977  N   ASN A 143      21.534  25.825  55.315  1.00 11.83           N  
ATOM    978  CA  ASN A 143      20.891  24.586  54.930  1.00 11.33           C  
ATOM    979  C   ASN A 143      19.371  24.688  55.062  1.00 12.87           C  
ATOM    980  O   ASN A 143      18.664  23.811  54.552  1.00 13.02           O  
ATOM    981  CB  ASN A 143      21.393  23.486  55.815  1.00 11.07           C  
ATOM    982  CG  ASN A 143      21.007  22.106  55.328  1.00 10.93           C  
ATOM    983  OD1 ASN A 143      21.210  21.806  54.152  1.00 12.30           O  
ATOM    984  ND2 ASN A 143      20.506  21.259  56.229  1.00 11.92           N  
ATOM    985  N   SER A 144      18.792  25.685  55.733  1.00 12.82           N  
ATOM    986  CA  SER A 144      17.339  25.743  55.879  1.00 14.77           C  
ATOM    987  C   SER A 144      16.679  26.320  54.662  1.00 13.91           C  
ATOM    988  O   SER A 144      17.146  27.364  54.205  1.00 13.74           O  
ATOM    989  CB  SER A 144      16.956  26.603  57.063  1.00 16.49           C  
ATOM    990  OG  SER A 144      17.749  26.066  58.107  1.00 27.45           O  
ATOM    991  N   SER A 145      15.653  25.684  54.115  1.00 12.79           N  
ATOM    992  CA  SER A 145      14.961  26.226  52.966  1.00 13.31           C  
ATOM    993  C   SER A 145      13.470  25.936  53.046  1.00 14.06           C  
ATOM    994  O   SER A 145      12.990  25.145  53.867  1.00 16.08           O  
ATOM    995  CB  SER A 145      15.540  25.607  51.703  1.00 12.14           C  
ATOM    996  OG  SER A 145      15.422  24.204  51.782  1.00 12.71           O  
ATOM    997  N   GLN A 146      12.717  26.644  52.231  1.00 15.67           N  
ATOM    998  CA  GLN A 146      11.282  26.443  52.073  1.00 16.16           C  
ATOM    999  C   GLN A 146      11.158  26.004  50.619  1.00 15.15           C  
ATOM   1000  O   GLN A 146      12.066  26.299  49.819  1.00 13.14           O  
ATOM   1001  CB  GLN A 146      10.535  27.715  52.231  1.00 18.86           C  
ATOM   1002  CG  GLN A 146      10.217  27.990  53.673  1.00 25.34           C  
ATOM   1003  CD  GLN A 146      10.079  29.489  53.790  1.00 29.36           C  
ATOM   1004  OE1 GLN A 146      11.084  30.147  54.105  1.00 31.76           O  
ATOM   1005  NE2 GLN A 146       8.918  30.093  53.487  1.00 29.56           N  
ATOM   1006  N   PRO A 147      10.101  25.286  50.215  1.00 13.45           N  
ATOM   1007  CA  PRO A 147       9.877  24.849  48.853  1.00 12.66           C  
ATOM   1008  C   PRO A 147       9.798  26.005  47.866  1.00 12.52           C  
ATOM   1009  O   PRO A 147       9.211  27.046  48.164  1.00 13.25           O  
ATOM   1010  CB  PRO A 147       8.578  24.080  48.893  1.00 13.19           C  
ATOM   1011  CG  PRO A 147       8.392  23.737  50.332  1.00 13.68           C  
ATOM   1012  CD  PRO A 147       8.922  24.980  51.010  1.00 14.25           C  
ATOM   1013  N   SER A 148      10.370  25.842  46.680  1.00 11.72           N  
ATOM   1014  CA  SER A 148      10.269  26.842  45.645  1.00 11.69           C  
ATOM   1015  C   SER A 148       8.786  26.924  45.248  1.00 11.32           C  
ATOM   1016  O   SER A 148       8.059  25.908  45.259  1.00 12.10           O  
ATOM   1017  CB  SER A 148      11.097  26.431  44.426  1.00 10.07           C  
ATOM   1018  OG  SER A 148      10.881  27.300  43.333  1.00 10.27           O  
ATOM   1019  N   PRO A 149       8.263  28.129  44.979  1.00 12.05           N  
ATOM   1020  CA  PRO A 149       6.940  28.311  44.422  1.00 11.81           C  
ATOM   1021  C   PRO A 149       6.947  27.607  43.056  1.00 12.90           C  
ATOM   1022  O   PRO A 149       8.017  27.417  42.472  1.00 12.02           O  
ATOM   1023  CB  PRO A 149       6.790  29.804  44.325  1.00 11.76           C  
ATOM   1024  CG  PRO A 149       7.719  30.333  45.399  1.00 13.05           C  
ATOM   1025  CD  PRO A 149       8.911  29.411  45.234  1.00 11.86           C  
ATOM   1026  N   PRO A 150       5.829  27.154  42.498  1.00 13.32           N  
ATOM   1027  CA  PRO A 150       5.774  26.590  41.158  1.00 13.78           C  
ATOM   1028  C   PRO A 150       5.864  27.671  40.090  1.00 13.68           C  
ATOM   1029  O   PRO A 150       5.814  28.875  40.370  1.00 15.45           O  
ATOM   1030  CB  PRO A 150       4.462  25.849  41.117  1.00 13.95           C  
ATOM   1031  CG  PRO A 150       3.596  26.734  42.004  1.00 12.90           C  
ATOM   1032  CD  PRO A 150       4.538  27.021  43.175  1.00 14.12           C  
ATOM   1033  N   SER A 151       6.001  27.214  38.855  1.00 15.34           N  
ATOM   1034  CA  SER A 151       6.035  28.034  37.659  1.00 16.38           C  
ATOM   1035  C   SER A 151       7.149  29.055  37.532  1.00 16.06           C  
ATOM   1036  O   SER A 151       7.005  30.039  36.801  1.00 16.15           O  
ATOM   1037  CB  SER A 151       4.677  28.727  37.541  1.00 19.50           C  
ATOM   1038  OG  SER A 151       3.639  27.756  37.760  1.00 25.33           O  
ATOM   1039  N   LEU A 152       8.281  28.845  38.204  1.00 13.62           N  
ATOM   1040  CA  LEU A 152       9.386  29.771  38.098  1.00 12.73           C  
ATOM   1041  C   LEU A 152      10.478  29.255  37.162  1.00 11.93           C  
ATOM   1042  O   LEU A 152      11.454  29.951  36.893  1.00 12.07           O  
ATOM   1043  CB  LEU A 152       9.937  30.031  39.513  1.00 10.17           C  
ATOM   1044  CG  LEU A 152       9.006  30.764  40.471  1.00 11.04           C  
ATOM   1045  CD1 LEU A 152       9.742  31.015  41.743  1.00  8.33           C  
ATOM   1046  CD2 LEU A 152       8.544  32.083  39.886  1.00 10.69           C  
ATOM   1047  N   ILE A 153      10.364  28.051  36.603  1.00 11.40           N  
ATOM   1048  CA  ILE A 153      11.398  27.526  35.718  1.00 10.89           C  
ATOM   1049  C   ILE A 153      10.986  27.719  34.256  1.00 11.07           C  
ATOM   1050  O   ILE A 153       9.923  27.207  33.863  1.00 10.22           O  
ATOM   1051  CB  ILE A 153      11.622  26.016  36.019  1.00 10.91           C  
ATOM   1052  CG1 ILE A 153      11.983  25.815  37.478  1.00 10.24           C  
ATOM   1053  CG2 ILE A 153      12.752  25.467  35.122  1.00 10.61           C  
ATOM   1054  CD1 ILE A 153      11.953  24.347  37.899  1.00 10.84           C  
ATOM   1055  N   PRO A 154      11.746  28.435  33.393  1.00 11.14           N  
ATOM   1056  CA  PRO A 154      11.453  28.600  31.969  1.00 11.79           C  
ATOM   1057  C   PRO A 154      11.332  27.237  31.319  1.00 12.88           C  
ATOM   1058  O   PRO A 154      12.101  26.321  31.654  1.00 14.29           O  
ATOM   1059  CB  PRO A 154      12.612  29.373  31.387  1.00 13.04           C  
ATOM   1060  CG  PRO A 154      13.160  30.077  32.591  1.00 11.00           C  
ATOM   1061  CD  PRO A 154      12.993  29.118  33.747  1.00 10.97           C  
ATOM   1062  N   GLY A 155      10.385  27.079  30.405  1.00 12.47           N  
ATOM   1063  CA  GLY A 155      10.171  25.821  29.704  1.00 12.71           C  
ATOM   1064  C   GLY A 155      10.513  25.940  28.228  1.00 11.25           C  
ATOM   1065  O   GLY A 155      10.486  27.044  27.667  1.00 12.05           O  
ATOM   1066  N   PRO A 156      10.775  24.859  27.504  1.00 11.64           N  
ATOM   1067  CA  PRO A 156      11.189  24.900  26.109  1.00 12.39           C  
ATOM   1068  C   PRO A 156      10.114  25.347  25.129  1.00 13.27           C  
ATOM   1069  O   PRO A 156      10.413  25.688  23.979  1.00 14.38           O  
ATOM   1070  CB  PRO A 156      11.701  23.503  25.839  1.00 11.62           C  
ATOM   1071  CG  PRO A 156      10.785  22.654  26.673  1.00 11.53           C  
ATOM   1072  CD  PRO A 156      10.687  23.476  27.974  1.00 12.35           C  
ATOM   1073  N   GLY A 157       8.859  25.333  25.578  1.00 14.48           N  
ATOM   1074  CA  GLY A 157       7.773  25.781  24.734  1.00 15.83           C  
ATOM   1075  C   GLY A 157       7.456  27.242  25.019  1.00 16.29           C  
ATOM   1076  O   GLY A 157       6.562  27.776  24.374  1.00 18.29           O  
ATOM   1077  N   ASN A 158       8.109  27.940  25.963  1.00 15.23           N  
ATOM   1078  CA  ASN A 158       7.806  29.336  26.268  1.00 14.34           C  
ATOM   1079  C   ASN A 158       8.245  30.276  25.166  1.00 14.17           C  
ATOM   1080  O   ASN A 158       9.151  29.951  24.396  1.00 13.60           O  
ATOM   1081  CB  ASN A 158       8.504  29.783  27.533  1.00 15.44           C  
ATOM   1082  CG  ASN A 158       7.998  29.173  28.820  1.00 14.35           C  
ATOM   1083  OD1 ASN A 158       8.532  29.433  29.905  1.00 18.94           O  
ATOM   1084  ND2 ASN A 158       6.986  28.333  28.870  1.00 18.15           N  
ATOM   1085  N   THR A 159       7.632  31.440  25.030  1.00 13.47           N  
ATOM   1086  CA  THR A 159       8.079  32.376  24.018  1.00 13.23           C  
ATOM   1087  C   THR A 159       9.355  33.039  24.542  1.00 13.82           C  
ATOM   1088  O   THR A 159       9.653  32.958  25.758  1.00 12.64           O  
ATOM   1089  CB  THR A 159       7.022  33.475  23.768  1.00 13.88           C  
ATOM   1090  OG1 THR A 159       6.757  34.121  25.028  1.00 13.09           O  
ATOM   1091  CG2 THR A 159       5.753  32.892  23.129  1.00 14.27           C  
ATOM   1092  N   VAL A 160      10.050  33.764  23.655  1.00 12.55           N  
ATOM   1093  CA  VAL A 160      11.219  34.511  24.105  1.00 13.84           C  
ATOM   1094  C   VAL A 160      10.757  35.604  25.085  1.00 13.67           C  
ATOM   1095  O   VAL A 160      11.446  35.825  26.088  1.00 11.90           O  
ATOM   1096  CB  VAL A 160      11.952  35.118  22.884  1.00 14.52           C  
ATOM   1097  CG1 VAL A 160      13.123  36.030  23.300  1.00 13.22           C  
ATOM   1098  CG2 VAL A 160      12.474  33.955  22.044  1.00 13.62           C  
ATOM   1099  N   THR A 161       9.626  36.296  24.895  1.00 12.30           N  
ATOM   1100  CA  THR A 161       9.205  37.304  25.856  1.00 13.07           C  
ATOM   1101  C   THR A 161       9.010  36.670  27.231  1.00 11.95           C  
ATOM   1102  O   THR A 161       9.545  37.180  28.211  1.00 11.71           O  
ATOM   1103  CB  THR A 161       7.882  37.987  25.391  1.00 13.05           C  
ATOM   1104  OG1 THR A 161       8.151  38.603  24.132  1.00 14.21           O  
ATOM   1105  CG2 THR A 161       7.366  38.996  26.403  1.00 13.00           C  
ATOM   1106  N   ALA A 162       8.322  35.528  27.308  1.00 11.27           N  
ATOM   1107  CA  ALA A 162       8.118  34.819  28.562  1.00 11.69           C  
ATOM   1108  C   ALA A 162       9.441  34.437  29.262  1.00 10.21           C  
ATOM   1109  O   ALA A 162       9.613  34.620  30.475  1.00 11.08           O  
ATOM   1110  CB  ALA A 162       7.312  33.537  28.288  1.00  9.85           C  
ATOM   1111  N   ILE A 163      10.406  33.930  28.502  1.00  8.43           N  
ATOM   1112  CA  ILE A 163      11.703  33.549  29.063  1.00 10.13           C  
ATOM   1113  C   ILE A 163      12.416  34.803  29.571  1.00 10.20           C  
ATOM   1114  O   ILE A 163      12.862  34.841  30.727  1.00 10.30           O  
ATOM   1115  CB  ILE A 163      12.545  32.844  27.968  1.00  8.68           C  
ATOM   1116  CG1 ILE A 163      11.881  31.502  27.661  1.00 10.18           C  
ATOM   1117  CG2 ILE A 163      13.996  32.628  28.415  1.00  9.89           C  
ATOM   1118  CD1 ILE A 163      12.473  30.797  26.416  1.00  9.62           C  
ATOM   1119  N   LEU A 164      12.511  35.862  28.744  1.00 11.34           N  
ATOM   1120  CA  LEU A 164      13.181  37.079  29.187  1.00 12.31           C  
ATOM   1121  C   LEU A 164      12.526  37.709  30.410  1.00 12.10           C  
ATOM   1122  O   LEU A 164      13.238  38.156  31.305  1.00 12.63           O  
ATOM   1123  CB  LEU A 164      13.227  38.050  28.025  1.00 10.44           C  
ATOM   1124  CG  LEU A 164      14.127  37.560  26.917  1.00 10.64           C  
ATOM   1125  CD1 LEU A 164      14.197  38.642  25.862  1.00 10.29           C  
ATOM   1126  CD2 LEU A 164      15.495  37.189  27.470  1.00 11.09           C  
ATOM   1127  N   ASP A 165      11.203  37.703  30.522  1.00 12.48           N  
ATOM   1128  CA  ASP A 165      10.530  38.243  31.685  1.00 13.40           C  
ATOM   1129  C   ASP A 165      10.863  37.464  32.937  1.00 12.65           C  
ATOM   1130  O   ASP A 165      11.213  38.045  33.966  1.00 11.55           O  
ATOM   1131  CB  ASP A 165       9.033  38.196  31.529  1.00 18.26           C  
ATOM   1132  CG  ASP A 165       8.465  39.164  30.510  1.00 22.71           C  
ATOM   1133  OD1 ASP A 165       9.229  39.891  29.858  1.00 26.39           O  
ATOM   1134  OD2 ASP A 165       7.236  39.190  30.381  1.00 26.70           O  
ATOM   1135  N   ARG A 166      10.785  36.141  32.857  1.00 12.19           N  
ATOM   1136  CA  ARG A 166      11.076  35.288  34.004  1.00 12.37           C  
ATOM   1137  C   ARG A 166      12.529  35.448  34.460  1.00 11.40           C  
ATOM   1138  O   ARG A 166      12.827  35.709  35.631  1.00  9.90           O  
ATOM   1139  CB  ARG A 166      10.799  33.805  33.642  1.00 11.20           C  
ATOM   1140  CG  ARG A 166      11.089  32.753  34.714  1.00  8.82           C  
ATOM   1141  CD  ARG A 166      10.156  32.814  35.931  1.00  9.22           C  
ATOM   1142  NE  ARG A 166      10.500  33.823  36.918  1.00  8.66           N  
ATOM   1143  CZ  ARG A 166      11.451  33.638  37.845  1.00 11.34           C  
ATOM   1144  NH1 ARG A 166      12.164  32.500  37.957  1.00 10.22           N  
ATOM   1145  NH2 ARG A 166      11.711  34.646  38.659  1.00  9.51           N  
ATOM   1146  N   MET A 167      13.449  35.365  33.504  1.00 11.27           N  
ATOM   1147  CA  MET A 167      14.869  35.486  33.800  1.00 11.49           C  
ATOM   1148  C   MET A 167      15.206  36.882  34.301  1.00 11.78           C  
ATOM   1149  O   MET A 167      16.051  37.060  35.188  1.00 11.44           O  
ATOM   1150  CB  MET A 167      15.666  35.145  32.535  1.00 11.90           C  
ATOM   1151  CG  MET A 167      15.571  33.668  32.135  1.00 12.42           C  
ATOM   1152  SD  MET A 167      16.222  32.517  33.374  1.00 15.47           S  
ATOM   1153  CE  MET A 167      17.920  32.572  32.897  1.00 15.03           C  
ATOM   1154  N   GLY A 168      14.518  37.886  33.754  1.00 11.24           N  
ATOM   1155  CA  GLY A 168      14.704  39.271  34.149  1.00 11.44           C  
ATOM   1156  C   GLY A 168      14.254  39.524  35.575  1.00 12.91           C  
ATOM   1157  O   GLY A 168      14.974  40.200  36.317  1.00 13.31           O  
ATOM   1158  N   ASP A 169      13.113  38.930  35.956  1.00 11.82           N  
ATOM   1159  CA  ASP A 169      12.599  39.051  37.304  1.00 13.30           C  
ATOM   1160  C   ASP A 169      13.647  38.468  38.255  1.00 13.89           C  
ATOM   1161  O   ASP A 169      13.917  39.095  39.286  1.00 12.90           O  
ATOM   1162  CB  ASP A 169      11.275  38.294  37.430  1.00 11.69           C  
ATOM   1163  CG  ASP A 169      10.760  38.197  38.866  1.00 15.26           C  
ATOM   1164  OD1 ASP A 169      10.808  39.146  39.651  1.00 13.74           O  
ATOM   1165  OD2 ASP A 169      10.314  37.123  39.219  1.00 12.38           O  
ATOM   1166  N   ALA A 170      14.269  37.319  37.914  1.00 13.01           N  
ATOM   1167  CA  ALA A 170      15.310  36.724  38.742  1.00 14.47           C  
ATOM   1168  C   ALA A 170      16.532  37.635  38.844  1.00 15.04           C  
ATOM   1169  O   ALA A 170      17.271  37.592  39.834  1.00 17.12           O  
ATOM   1170  CB  ALA A 170      15.755  35.398  38.164  1.00 11.81           C  
ATOM   1171  N   GLY A 171      16.748  38.481  37.833  1.00 14.59           N  
ATOM   1172  CA  GLY A 171      17.814  39.455  37.851  1.00 13.93           C  
ATOM   1173  C   GLY A 171      18.714  39.399  36.630  1.00 13.48           C  
ATOM   1174  O   GLY A 171      19.739  40.088  36.610  1.00 15.94           O  
ATOM   1175  N   PHE A 172      18.417  38.639  35.588  1.00 12.51           N  
ATOM   1176  CA  PHE A 172      19.324  38.566  34.453  1.00 12.23           C  
ATOM   1177  C   PHE A 172      18.865  39.393  33.265  1.00 12.28           C  
ATOM   1178  O   PHE A 172      17.683  39.427  32.924  1.00 12.63           O  
ATOM   1179  CB  PHE A 172      19.525  37.096  33.981  1.00 12.58           C  
ATOM   1180  CG  PHE A 172      20.040  36.229  35.134  1.00 14.36           C  
ATOM   1181  CD1 PHE A 172      21.404  36.151  35.396  1.00 14.74           C  
ATOM   1182  CD2 PHE A 172      19.146  35.530  35.948  1.00 14.54           C  
ATOM   1183  CE1 PHE A 172      21.875  35.390  36.460  1.00 14.16           C  
ATOM   1184  CE2 PHE A 172      19.630  34.774  37.000  1.00 14.33           C  
ATOM   1185  CZ  PHE A 172      20.988  34.702  37.259  1.00 15.38           C  
ATOM   1186  N   SER A 173      19.809  40.087  32.641  1.00 12.12           N  
ATOM   1187  CA  SER A 173      19.545  40.857  31.454  1.00 10.97           C  
ATOM   1188  C   SER A 173      19.414  39.881  30.292  1.00 11.48           C  
ATOM   1189  O   SER A 173      19.857  38.728  30.461  1.00  9.40           O  
ATOM   1190  CB  SER A 173      20.708  41.790  31.217  1.00 13.08           C  
ATOM   1191  OG  SER A 173      21.960  41.129  31.024  1.00 13.03           O  
ATOM   1192  N   PRO A 174      18.869  40.227  29.101  1.00 11.40           N  
ATOM   1193  CA  PRO A 174      18.835  39.339  27.929  1.00 10.77           C  
ATOM   1194  C   PRO A 174      20.235  38.783  27.582  1.00  9.93           C  
ATOM   1195  O   PRO A 174      20.365  37.609  27.228  1.00 11.06           O  
ATOM   1196  CB  PRO A 174      18.229  40.213  26.829  1.00 10.55           C  
ATOM   1197  CG  PRO A 174      17.299  41.157  27.567  1.00  9.51           C  
ATOM   1198  CD  PRO A 174      18.103  41.458  28.835  1.00 10.32           C  
ATOM   1199  N   ASP A 175      21.307  39.595  27.633  1.00  8.27           N  
ATOM   1200  CA  ASP A 175      22.656  39.128  27.366  1.00  9.23           C  
ATOM   1201  C   ASP A 175      23.030  37.987  28.300  1.00 10.19           C  
ATOM   1202  O   ASP A 175      23.558  36.971  27.853  1.00 10.80           O  
ATOM   1203  CB  ASP A 175      23.722  40.211  27.581  1.00 11.18           C  
ATOM   1204  CG  ASP A 175      23.817  41.272  26.501  1.00 13.56           C  
ATOM   1205  OD1 ASP A 175      23.095  41.221  25.512  1.00 15.77           O  
ATOM   1206  OD2 ASP A 175      24.642  42.166  26.634  1.00 16.04           O  
ATOM   1207  N   GLU A 176      22.754  38.115  29.599  1.00 10.87           N  
ATOM   1208  CA  GLU A 176      23.107  37.092  30.562  1.00  9.22           C  
ATOM   1209  C   GLU A 176      22.349  35.797  30.358  1.00 10.80           C  
ATOM   1210  O   GLU A 176      22.898  34.729  30.656  1.00 10.62           O  
ATOM   1211  CB  GLU A 176      22.872  37.613  31.937  1.00 11.46           C  
ATOM   1212  CG  GLU A 176      23.916  38.663  32.266  1.00 14.18           C  
ATOM   1213  CD  GLU A 176      23.667  39.353  33.604  1.00 16.07           C  
ATOM   1214  OE1 GLU A 176      22.527  39.644  33.953  1.00 18.56           O  
ATOM   1215  OE2 GLU A 176      24.616  39.615  34.329  1.00 18.31           O  
ATOM   1216  N   VAL A 177      21.133  35.871  29.799  1.00 11.04           N  
ATOM   1217  CA  VAL A 177      20.342  34.685  29.471  1.00 10.78           C  
ATOM   1218  C   VAL A 177      21.117  33.948  28.383  1.00 10.87           C  
ATOM   1219  O   VAL A 177      21.361  32.745  28.528  1.00 13.27           O  
ATOM   1220  CB  VAL A 177      18.905  35.053  28.947  1.00 11.10           C  
ATOM   1221  CG1 VAL A 177      18.150  33.783  28.476  1.00 10.47           C  
ATOM   1222  CG2 VAL A 177      18.130  35.763  30.073  1.00  9.69           C  
ATOM   1223  N   VAL A 178      21.586  34.640  27.347  1.00  9.56           N  
ATOM   1224  CA  VAL A 178      22.355  34.002  26.312  1.00 10.15           C  
ATOM   1225  C   VAL A 178      23.621  33.425  26.943  1.00 10.31           C  
ATOM   1226  O   VAL A 178      23.993  32.290  26.658  1.00 10.37           O  
ATOM   1227  CB  VAL A 178      22.734  35.004  25.194  1.00  9.93           C  
ATOM   1228  CG1 VAL A 178      23.628  34.352  24.116  1.00  8.01           C  
ATOM   1229  CG2 VAL A 178      21.442  35.507  24.548  1.00 10.11           C  
ATOM   1230  N   ASP A 179      24.276  34.134  27.841  1.00  9.73           N  
ATOM   1231  CA  ASP A 179      25.501  33.622  28.426  1.00 10.03           C  
ATOM   1232  C   ASP A 179      25.347  32.355  29.252  1.00 10.86           C  
ATOM   1233  O   ASP A 179      26.187  31.440  29.218  1.00 10.81           O  
ATOM   1234  CB  ASP A 179      26.117  34.701  29.284  1.00 10.08           C  
ATOM   1235  CG  ASP A 179      26.498  35.985  28.567  1.00  9.43           C  
ATOM   1236  OD1 ASP A 179      26.596  36.016  27.351  1.00  9.33           O  
ATOM   1237  OD2 ASP A 179      26.703  36.970  29.265  1.00 10.37           O  
ATOM   1238  N   LEU A 180      24.246  32.303  29.992  1.00 10.19           N  
ATOM   1239  CA  LEU A 180      23.886  31.170  30.826  1.00 10.66           C  
ATOM   1240  C   LEU A 180      23.633  29.933  29.972  1.00  9.57           C  
ATOM   1241  O   LEU A 180      23.958  28.802  30.365  1.00 10.04           O  
ATOM   1242  CB  LEU A 180      22.654  31.580  31.587  1.00 11.21           C  
ATOM   1243  CG  LEU A 180      22.571  31.540  33.092  1.00 16.34           C  
ATOM   1244  CD1 LEU A 180      23.876  31.837  33.757  1.00 15.73           C  
ATOM   1245  CD2 LEU A 180      21.527  32.559  33.504  1.00 14.25           C  
ATOM   1246  N   LEU A 181      23.108  30.126  28.757  1.00  8.17           N  
ATOM   1247  CA  LEU A 181      22.808  29.032  27.860  1.00  7.49           C  
ATOM   1248  C   LEU A 181      24.052  28.342  27.301  1.00  9.72           C  
ATOM   1249  O   LEU A 181      23.940  27.360  26.553  1.00  8.89           O  
ATOM   1250  CB  LEU A 181      21.953  29.546  26.720  1.00 10.41           C  
ATOM   1251  CG  LEU A 181      20.526  29.061  26.452  1.00 13.52           C  
ATOM   1252  CD1 LEU A 181      20.138  27.834  27.245  1.00 13.15           C  
ATOM   1253  CD2 LEU A 181      19.630  30.206  26.768  1.00 13.82           C  
ATOM   1254  N   ALA A 182      25.271  28.789  27.638  1.00  8.72           N  
ATOM   1255  CA  ALA A 182      26.465  28.079  27.196  1.00  9.10           C  
ATOM   1256  C   ALA A 182      26.450  26.668  27.789  1.00  8.03           C  
ATOM   1257  O   ALA A 182      27.068  25.745  27.236  1.00  8.50           O  
ATOM   1258  CB  ALA A 182      27.742  28.780  27.653  1.00  7.90           C  
ATOM   1259  N   ALA A 183      25.707  26.435  28.883  1.00  6.16           N  
ATOM   1260  CA  ALA A 183      25.624  25.101  29.439  1.00  8.51           C  
ATOM   1261  C   ALA A 183      24.998  24.110  28.467  1.00  7.88           C  
ATOM   1262  O   ALA A 183      25.256  22.917  28.584  1.00  8.51           O  
ATOM   1263  CB  ALA A 183      24.792  25.089  30.691  1.00  8.89           C  
ATOM   1264  N   HIS A 184      24.224  24.518  27.447  1.00  7.53           N  
ATOM   1265  CA  HIS A 184      23.686  23.557  26.492  1.00  6.45           C  
ATOM   1266  C   HIS A 184      24.757  23.044  25.515  1.00  6.23           C  
ATOM   1267  O   HIS A 184      24.476  22.262  24.591  1.00  6.51           O  
ATOM   1268  CB  HIS A 184      22.511  24.184  25.725  1.00  7.13           C  
ATOM   1269  CG  HIS A 184      21.176  24.172  26.461  1.00  5.40           C  
ATOM   1270  ND1 HIS A 184      19.953  24.468  25.866  1.00  5.77           N  
ATOM   1271  CD2 HIS A 184      20.984  23.850  27.800  1.00  6.34           C  
ATOM   1272  CE1 HIS A 184      19.034  24.323  26.819  1.00  5.19           C  
ATOM   1273  NE2 HIS A 184      19.589  23.970  27.931  1.00  6.83           N  
ATOM   1274  N   SER A 185      26.005  23.493  25.690  1.00  6.79           N  
ATOM   1275  CA  SER A 185      27.121  22.967  24.920  1.00  6.12           C  
ATOM   1276  C   SER A 185      27.483  21.638  25.576  1.00  5.81           C  
ATOM   1277  O   SER A 185      28.288  20.915  25.007  1.00  6.97           O  
ATOM   1278  CB  SER A 185      28.329  23.898  24.987  1.00  6.25           C  
ATOM   1279  OG  SER A 185      29.427  23.453  24.184  1.00  5.63           O  
ATOM   1280  N   LEU A 186      26.943  21.231  26.719  1.00  7.42           N  
ATOM   1281  CA  LEU A 186      27.280  19.968  27.371  1.00  8.53           C  
ATOM   1282  C   LEU A 186      25.896  19.386  27.668  1.00  8.03           C  
ATOM   1283  O   LEU A 186      25.508  19.177  28.819  1.00  8.10           O  
ATOM   1284  CB  LEU A 186      28.068  20.361  28.611  1.00  9.45           C  
ATOM   1285  CG  LEU A 186      29.553  20.120  28.888  1.00 14.32           C  
ATOM   1286  CD1 LEU A 186      30.419  20.010  27.654  1.00 10.73           C  
ATOM   1287  CD2 LEU A 186      29.947  21.232  29.834  1.00 11.58           C  
ATOM   1288  N   ALA A 187      25.118  19.101  26.629  1.00  8.20           N  
ATOM   1289  CA  ALA A 187      23.733  18.725  26.854  1.00  8.35           C  
ATOM   1290  C   ALA A 187      23.110  17.742  25.909  1.00  8.79           C  
ATOM   1291  O   ALA A 187      23.538  17.579  24.763  1.00  9.12           O  
ATOM   1292  CB  ALA A 187      22.861  19.968  26.797  1.00  7.84           C  
ATOM   1293  N   SER A 188      22.072  17.104  26.408  1.00  8.34           N  
ATOM   1294  CA  SER A 188      21.293  16.206  25.601  1.00  9.02           C  
ATOM   1295  C   SER A 188      19.879  16.341  26.158  1.00  8.79           C  
ATOM   1296  O   SER A 188      19.621  17.127  27.074  1.00  8.96           O  
ATOM   1297  CB  SER A 188      21.819  14.758  25.751  1.00  8.38           C  
ATOM   1298  OG  SER A 188      21.473  14.108  26.969  1.00  9.73           O  
ATOM   1299  N   GLN A 189      18.919  15.630  25.576  1.00  9.54           N  
ATOM   1300  CA  GLN A 189      17.583  15.607  26.139  1.00  9.32           C  
ATOM   1301  C   GLN A 189      17.231  14.130  26.351  1.00 10.08           C  
ATOM   1302  O   GLN A 189      17.649  13.252  25.573  1.00  9.24           O  
ATOM   1303  CB  GLN A 189      16.594  16.283  25.158  1.00  8.49           C  
ATOM   1304  CG  GLN A 189      16.349  15.601  23.800  1.00  8.16           C  
ATOM   1305  CD  GLN A 189      15.410  14.398  23.827  1.00  8.29           C  
ATOM   1306  OE1 GLN A 189      14.510  14.284  24.684  1.00  9.05           O  
ATOM   1307  NE2 GLN A 189      15.563  13.488  22.883  1.00 10.10           N  
ATOM   1308  N   GLU A 190      16.400  13.827  27.318  1.00 10.58           N  
ATOM   1309  CA  GLU A 190      15.954  12.458  27.558  1.00 11.48           C  
ATOM   1310  C   GLU A 190      14.437  12.374  27.579  1.00 11.77           C  
ATOM   1311  O   GLU A 190      13.846  11.348  27.214  1.00 11.59           O  
ATOM   1312  CB  GLU A 190      16.452  11.949  28.892  1.00 10.77           C  
ATOM   1313  CG  GLU A 190      17.961  11.760  28.946  1.00 11.02           C  
ATOM   1314  CD  GLU A 190      18.524  11.239  30.272  1.00 12.16           C  
ATOM   1315  OE1 GLU A 190      17.779  11.016  31.226  1.00 11.18           O  
ATOM   1316  OE2 GLU A 190      19.732  11.069  30.358  1.00 10.28           O  
ATOM   1317  N   GLY A 191      13.791  13.468  27.982  1.00 13.08           N  
ATOM   1318  CA  GLY A 191      12.344  13.494  28.141  1.00 13.27           C  
ATOM   1319  C   GLY A 191      11.539  14.263  27.120  1.00 13.75           C  
ATOM   1320  O   GLY A 191      10.307  14.291  27.237  1.00 15.53           O  
ATOM   1321  N   LEU A 192      12.125  14.913  26.125  1.00 13.79           N  
ATOM   1322  CA  LEU A 192      11.331  15.645  25.155  1.00 15.43           C  
ATOM   1323  C   LEU A 192      10.970  14.696  24.019  1.00 15.91           C  
ATOM   1324  O   LEU A 192       9.838  14.717  23.525  1.00 17.57           O  
ATOM   1325  CB  LEU A 192      12.153  16.825  24.689  1.00 14.86           C  
ATOM   1326  CG  LEU A 192      11.939  18.254  25.210  1.00 17.07           C  
ATOM   1327  CD1 LEU A 192      11.233  18.329  26.532  1.00 14.64           C  
ATOM   1328  CD2 LEU A 192      13.295  18.884  25.212  1.00 14.34           C  
ATOM   1329  N   ASN A 193      11.886  13.821  23.602  1.00 14.30           N  
ATOM   1330  CA  ASN A 193      11.642  12.823  22.575  1.00 15.10           C  
ATOM   1331  C   ASN A 193      12.420  11.588  23.056  1.00 15.39           C  
ATOM   1332  O   ASN A 193      13.588  11.355  22.718  1.00 13.38           O  
ATOM   1333  CB  ASN A 193      12.162  13.297  21.204  1.00 13.61           C  
ATOM   1334  CG  ASN A 193      11.670  12.426  20.050  1.00 14.54           C  
ATOM   1335  OD1 ASN A 193      11.587  12.842  18.900  1.00 15.31           O  
ATOM   1336  ND2 ASN A 193      11.304  11.175  20.242  1.00 15.59           N  
ATOM   1337  N   SER A 194      11.763  10.715  23.832  1.00 17.78           N  
ATOM   1338  CA  SER A 194      12.441   9.556  24.418  1.00 19.45           C  
ATOM   1339  C   SER A 194      12.802   8.498  23.393  1.00 18.33           C  
ATOM   1340  O   SER A 194      13.626   7.631  23.677  1.00 19.05           O  
ATOM   1341  CB  SER A 194      11.569   8.963  25.547  1.00 20.59           C  
ATOM   1342  OG  SER A 194      10.199   8.885  25.170  1.00 24.86           O  
ATOM   1343  N   ALA A 195      12.234   8.601  22.196  1.00 16.47           N  
ATOM   1344  CA  ALA A 195      12.615   7.726  21.095  1.00 16.65           C  
ATOM   1345  C   ALA A 195      14.062   7.984  20.648  1.00 16.38           C  
ATOM   1346  O   ALA A 195      14.662   7.166  19.957  1.00 17.42           O  
ATOM   1347  CB  ALA A 195      11.707   7.952  19.883  1.00 15.81           C  
ATOM   1348  N   ILE A 196      14.675   9.133  20.942  1.00 14.70           N  
ATOM   1349  CA  ILE A 196      16.063   9.406  20.566  1.00 12.13           C  
ATOM   1350  C   ILE A 196      16.723   9.935  21.851  1.00 12.61           C  
ATOM   1351  O   ILE A 196      17.207  11.069  22.001  1.00 11.73           O  
ATOM   1352  CB  ILE A 196      16.155  10.454  19.415  1.00 11.91           C  
ATOM   1353  CG1 ILE A 196      15.170  11.608  19.585  1.00 10.63           C  
ATOM   1354  CG2 ILE A 196      15.956   9.692  18.117  1.00 11.46           C  
ATOM   1355  CD1 ILE A 196      15.361  12.740  18.557  1.00 14.58           C  
ATOM   1356  N   PHE A 197      16.677   9.036  22.824  1.00 11.75           N  
ATOM   1357  CA  PHE A 197      17.218   9.253  24.158  1.00 12.39           C  
ATOM   1358  C   PHE A 197      18.695   9.664  24.063  1.00 11.80           C  
ATOM   1359  O   PHE A 197      19.527   9.063  23.363  1.00 12.29           O  
ATOM   1360  CB  PHE A 197      17.038   7.951  24.943  1.00 10.93           C  
ATOM   1361  CG  PHE A 197      17.554   7.897  26.380  1.00  9.92           C  
ATOM   1362  CD1 PHE A 197      16.775   8.369  27.409  1.00 10.79           C  
ATOM   1363  CD2 PHE A 197      18.793   7.338  26.661  1.00 10.33           C  
ATOM   1364  CE1 PHE A 197      17.241   8.268  28.704  1.00 10.44           C  
ATOM   1365  CE2 PHE A 197      19.248   7.245  27.956  1.00  8.66           C  
ATOM   1366  CZ  PHE A 197      18.470   7.711  28.977  1.00 11.38           C  
ATOM   1367  N   ARG A 198      18.950  10.727  24.835  1.00 11.28           N  
ATOM   1368  CA  ARG A 198      20.256  11.387  24.949  1.00  9.64           C  
ATOM   1369  C   ARG A 198      20.805  11.935  23.624  1.00  9.70           C  
ATOM   1370  O   ARG A 198      22.025  12.008  23.400  1.00  9.42           O  
ATOM   1371  CB  ARG A 198      21.289  10.437  25.615  1.00  9.13           C  
ATOM   1372  CG  ARG A 198      21.104  10.390  27.105  1.00  7.61           C  
ATOM   1373  CD  ARG A 198      22.048   9.430  27.823  1.00  8.95           C  
ATOM   1374  NE  ARG A 198      21.595   9.290  29.210  1.00 11.28           N  
ATOM   1375  CZ  ARG A 198      22.156   8.482  30.115  1.00 10.09           C  
ATOM   1376  NH1 ARG A 198      23.201   7.713  29.805  1.00 12.43           N  
ATOM   1377  NH2 ARG A 198      21.643   8.443  31.347  1.00 12.85           N  
ATOM   1378  N   SER A 199      19.918  12.373  22.722  1.00  9.04           N  
ATOM   1379  CA  SER A 199      20.343  13.019  21.480  1.00  9.95           C  
ATOM   1380  C   SER A 199      21.052  14.312  21.903  1.00  9.70           C  
ATOM   1381  O   SER A 199      20.436  15.055  22.685  1.00  9.64           O  
ATOM   1382  CB  SER A 199      19.158  13.410  20.620  1.00  8.47           C  
ATOM   1383  OG  SER A 199      18.117  13.900  21.457  1.00 10.06           O  
ATOM   1384  N   PRO A 200      22.296  14.627  21.532  1.00 10.31           N  
ATOM   1385  CA  PRO A 200      22.970  15.854  21.952  1.00 10.27           C  
ATOM   1386  C   PRO A 200      22.364  17.133  21.377  1.00  9.23           C  
ATOM   1387  O   PRO A 200      21.742  17.112  20.311  1.00  9.56           O  
ATOM   1388  CB  PRO A 200      24.417  15.678  21.524  1.00  9.66           C  
ATOM   1389  CG  PRO A 200      24.570  14.221  21.178  1.00 11.35           C  
ATOM   1390  CD  PRO A 200      23.183  13.841  20.687  1.00 11.03           C  
ATOM   1391  N   LEU A 201      22.591  18.256  22.071  1.00  8.81           N  
ATOM   1392  CA  LEU A 201      22.150  19.559  21.620  1.00  8.95           C  
ATOM   1393  C   LEU A 201      23.268  20.180  20.792  1.00  9.78           C  
ATOM   1394  O   LEU A 201      23.021  21.194  20.129  1.00  9.26           O  
ATOM   1395  CB  LEU A 201      21.793  20.390  22.831  1.00 10.42           C  
ATOM   1396  CG  LEU A 201      20.295  20.466  23.224  1.00 15.38           C  
ATOM   1397  CD1 LEU A 201      19.599  19.119  23.106  1.00 12.18           C  
ATOM   1398  CD2 LEU A 201      20.208  21.071  24.624  1.00 11.66           C  
ATOM   1399  N   ASP A 202      24.528  19.735  20.861  1.00  8.47           N  
ATOM   1400  CA  ASP A 202      25.501  20.213  19.890  1.00  8.67           C  
ATOM   1401  C   ASP A 202      26.384  19.005  19.539  1.00  9.25           C  
ATOM   1402  O   ASP A 202      26.263  17.962  20.194  1.00  7.31           O  
ATOM   1403  CB  ASP A 202      26.345  21.415  20.432  1.00  7.76           C  
ATOM   1404  CG  ASP A 202      27.505  21.223  21.403  1.00  7.59           C  
ATOM   1405  OD1 ASP A 202      27.826  20.112  21.813  1.00  8.47           O  
ATOM   1406  OD2 ASP A 202      28.096  22.233  21.769  1.00  8.14           O  
ATOM   1407  N   SER A 203      27.335  19.096  18.599  1.00  8.68           N  
ATOM   1408  CA  SER A 203      28.120  17.941  18.214  1.00  8.85           C  
ATOM   1409  C   SER A 203      29.227  17.549  19.188  1.00 10.15           C  
ATOM   1410  O   SER A 203      29.948  16.589  18.899  1.00 10.71           O  
ATOM   1411  CB  SER A 203      28.711  18.193  16.831  1.00  9.54           C  
ATOM   1412  OG  SER A 203      29.545  19.349  16.834  1.00 12.02           O  
ATOM   1413  N   THR A 204      29.460  18.256  20.292  1.00  9.36           N  
ATOM   1414  CA  THR A 204      30.500  17.929  21.243  1.00  8.62           C  
ATOM   1415  C   THR A 204      29.877  17.977  22.639  1.00  9.85           C  
ATOM   1416  O   THR A 204      30.167  18.901  23.427  1.00  9.33           O  
ATOM   1417  CB  THR A 204      31.641  18.948  21.064  1.00  9.31           C  
ATOM   1418  OG1 THR A 204      31.046  20.243  21.128  1.00  9.45           O  
ATOM   1419  CG2 THR A 204      32.363  18.831  19.725  1.00 10.10           C  
ATOM   1420  N   PRO A 205      28.989  17.051  23.031  1.00  7.96           N  
ATOM   1421  CA  PRO A 205      28.347  17.090  24.321  1.00  8.47           C  
ATOM   1422  C   PRO A 205      29.308  16.914  25.477  1.00  9.41           C  
ATOM   1423  O   PRO A 205      28.922  17.050  26.638  1.00  8.49           O  
ATOM   1424  CB  PRO A 205      27.279  16.015  24.241  1.00  9.46           C  
ATOM   1425  CG  PRO A 205      27.865  15.024  23.255  1.00  7.45           C  
ATOM   1426  CD  PRO A 205      28.492  15.933  22.234  1.00 10.03           C  
ATOM   1427  N   GLN A 206      30.552  16.520  25.178  1.00 10.80           N  
ATOM   1428  CA  GLN A 206      31.565  16.380  26.212  1.00 11.10           C  
ATOM   1429  C   GLN A 206      32.622  17.476  26.105  1.00 10.26           C  
ATOM   1430  O   GLN A 206      33.696  17.318  26.699  1.00 11.37           O  
ATOM   1431  CB  GLN A 206      32.217  14.997  26.107  1.00 11.73           C  
ATOM   1432  CG  GLN A 206      31.284  13.866  26.523  1.00 14.14           C  
ATOM   1433  CD  GLN A 206      32.044  12.542  26.645  1.00 16.57           C  
ATOM   1434  OE1 GLN A 206      32.484  11.963  25.646  1.00 17.13           O  
ATOM   1435  NE2 GLN A 206      32.212  11.966  27.817  1.00 15.23           N  
ATOM   1436  N   VAL A 207      32.467  18.575  25.354  1.00  9.74           N  
ATOM   1437  CA  VAL A 207      33.480  19.645  25.275  1.00  8.58           C  
ATOM   1438  C   VAL A 207      32.748  20.979  25.484  1.00  8.41           C  
ATOM   1439  O   VAL A 207      31.751  21.238  24.792  1.00  8.44           O  
ATOM   1440  CB  VAL A 207      34.190  19.708  23.898  1.00  8.59           C  
ATOM   1441  CG1 VAL A 207      35.248  20.806  23.911  1.00  6.60           C  
ATOM   1442  CG2 VAL A 207      34.900  18.408  23.589  1.00  8.22           C  
ATOM   1443  N   PHE A 208      33.165  21.814  26.440  1.00  8.54           N  
ATOM   1444  CA  PHE A 208      32.539  23.097  26.691  1.00  8.08           C  
ATOM   1445  C   PHE A 208      33.147  24.042  25.679  1.00  8.78           C  
ATOM   1446  O   PHE A 208      34.283  24.527  25.829  1.00 10.24           O  
ATOM   1447  CB  PHE A 208      32.839  23.556  28.102  1.00  7.36           C  
ATOM   1448  CG  PHE A 208      32.141  24.853  28.476  1.00  8.19           C  
ATOM   1449  CD1 PHE A 208      30.767  24.857  28.676  1.00  9.39           C  
ATOM   1450  CD2 PHE A 208      32.882  26.019  28.597  1.00  9.74           C  
ATOM   1451  CE1 PHE A 208      30.128  26.037  29.000  1.00 10.26           C  
ATOM   1452  CE2 PHE A 208      32.240  27.178  28.918  1.00  9.09           C  
ATOM   1453  CZ  PHE A 208      30.882  27.184  29.115  1.00  8.62           C  
ATOM   1454  N   ASP A 209      32.401  24.235  24.590  1.00  8.12           N  
ATOM   1455  CA  ASP A 209      32.811  25.053  23.463  1.00  7.01           C  
ATOM   1456  C   ASP A 209      31.637  25.832  22.845  1.00  9.01           C  
ATOM   1457  O   ASP A 209      30.448  25.731  23.183  1.00 10.15           O  
ATOM   1458  CB  ASP A 209      33.465  24.140  22.398  1.00  7.32           C  
ATOM   1459  CG  ASP A 209      32.554  23.013  21.910  1.00  4.36           C  
ATOM   1460  OD1 ASP A 209      31.337  23.007  22.173  1.00  8.65           O  
ATOM   1461  OD2 ASP A 209      33.053  22.115  21.237  1.00  9.54           O  
ATOM   1462  N   THR A 210      31.981  26.578  21.846  1.00  8.30           N  
ATOM   1463  CA  THR A 210      31.085  27.409  21.079  1.00  8.99           C  
ATOM   1464  C   THR A 210      30.153  26.645  20.098  1.00  9.38           C  
ATOM   1465  O   THR A 210      29.253  27.261  19.510  1.00  9.87           O  
ATOM   1466  CB  THR A 210      32.218  28.282  20.559  1.00 11.13           C  
ATOM   1467  OG1 THR A 210      32.170  29.518  21.267  1.00 15.56           O  
ATOM   1468  CG2 THR A 210      32.282  28.132  19.118  1.00  5.20           C  
ATOM   1469  N   GLN A 211      30.315  25.325  19.846  1.00  7.45           N  
ATOM   1470  CA  GLN A 211      29.535  24.608  18.853  1.00  7.66           C  
ATOM   1471  C   GLN A 211      28.043  24.760  19.015  1.00  6.47           C  
ATOM   1472  O   GLN A 211      27.341  24.896  18.010  1.00  8.63           O  
ATOM   1473  CB  GLN A 211      29.881  23.106  18.843  1.00  5.63           C  
ATOM   1474  CG  GLN A 211      31.276  22.787  18.322  1.00  7.22           C  
ATOM   1475  CD  GLN A 211      31.665  23.448  16.997  1.00  8.67           C  
ATOM   1476  OE1 GLN A 211      32.703  24.124  16.890  1.00  9.63           O  
ATOM   1477  NE2 GLN A 211      30.894  23.255  15.932  1.00  8.61           N  
ATOM   1478  N   PHE A 212      27.522  24.819  20.229  1.00  7.97           N  
ATOM   1479  CA  PHE A 212      26.091  24.990  20.452  1.00  7.72           C  
ATOM   1480  C   PHE A 212      25.574  26.253  19.809  1.00  8.07           C  
ATOM   1481  O   PHE A 212      24.536  26.199  19.145  1.00  8.92           O  
ATOM   1482  CB  PHE A 212      25.803  25.015  21.945  1.00  7.06           C  
ATOM   1483  CG  PHE A 212      24.391  25.459  22.279  1.00  9.01           C  
ATOM   1484  CD1 PHE A 212      23.303  24.649  22.013  1.00  6.66           C  
ATOM   1485  CD2 PHE A 212      24.217  26.713  22.849  1.00  8.56           C  
ATOM   1486  CE1 PHE A 212      22.044  25.098  22.317  1.00  6.85           C  
ATOM   1487  CE2 PHE A 212      22.942  27.151  23.156  1.00  9.44           C  
ATOM   1488  CZ  PHE A 212      21.869  26.345  22.890  1.00  7.65           C  
ATOM   1489  N   TYR A 213      26.276  27.380  19.941  1.00  8.80           N  
ATOM   1490  CA  TYR A 213      25.794  28.623  19.353  1.00  7.62           C  
ATOM   1491  C   TYR A 213      25.844  28.551  17.841  1.00  9.34           C  
ATOM   1492  O   TYR A 213      24.921  29.009  17.165  1.00  9.95           O  
ATOM   1493  CB  TYR A 213      26.649  29.780  19.869  1.00  7.63           C  
ATOM   1494  CG  TYR A 213      26.464  30.000  21.375  1.00  7.39           C  
ATOM   1495  CD1 TYR A 213      25.333  30.635  21.861  1.00  8.56           C  
ATOM   1496  CD2 TYR A 213      27.433  29.594  22.269  1.00  8.63           C  
ATOM   1497  CE1 TYR A 213      25.156  30.881  23.220  1.00  9.69           C  
ATOM   1498  CE2 TYR A 213      27.262  29.839  23.627  1.00 10.26           C  
ATOM   1499  CZ  TYR A 213      26.129  30.484  24.102  1.00  8.22           C  
ATOM   1500  OH  TYR A 213      26.017  30.755  25.449  1.00  7.99           O  
ATOM   1501  N   ILE A 214      26.865  27.920  17.258  1.00  8.67           N  
ATOM   1502  CA  ILE A 214      26.986  27.800  15.804  1.00  9.76           C  
ATOM   1503  C   ILE A 214      25.868  26.936  15.226  1.00 10.32           C  
ATOM   1504  O   ILE A 214      25.129  27.300  14.306  1.00  9.83           O  
ATOM   1505  CB  ILE A 214      28.353  27.148  15.425  1.00 10.36           C  
ATOM   1506  CG1 ILE A 214      29.476  28.074  15.865  1.00 10.79           C  
ATOM   1507  CG2 ILE A 214      28.408  26.805  13.916  1.00 11.34           C  
ATOM   1508  CD1 ILE A 214      30.845  27.381  15.860  1.00  8.12           C  
ATOM   1509  N   GLU A 215      25.709  25.759  15.833  1.00 10.30           N  
ATOM   1510  CA  GLU A 215      24.793  24.766  15.305  1.00 10.02           C  
ATOM   1511  C   GLU A 215      23.318  25.066  15.475  1.00 10.38           C  
ATOM   1512  O   GLU A 215      22.554  24.614  14.627  1.00  8.91           O  
ATOM   1513  CB  GLU A 215      25.184  23.421  15.920  1.00 10.62           C  
ATOM   1514  CG  GLU A 215      26.566  22.982  15.399  1.00  9.39           C  
ATOM   1515  CD  GLU A 215      27.148  21.785  16.104  1.00 11.07           C  
ATOM   1516  OE1 GLU A 215      26.434  21.015  16.735  1.00 10.25           O  
ATOM   1517  OE2 GLU A 215      28.353  21.629  16.044  1.00 11.54           O  
ATOM   1518  N   THR A 216      22.894  25.835  16.496  1.00  9.79           N  
ATOM   1519  CA  THR A 216      21.505  26.222  16.599  1.00 10.01           C  
ATOM   1520  C   THR A 216      21.183  27.270  15.531  1.00 10.39           C  
ATOM   1521  O   THR A 216      20.012  27.506  15.230  1.00 10.84           O  
ATOM   1522  CB  THR A 216      21.226  26.773  17.995  1.00  9.08           C  
ATOM   1523  OG1 THR A 216      22.298  27.635  18.367  1.00 11.33           O  
ATOM   1524  CG2 THR A 216      21.101  25.642  18.978  1.00 10.72           C  
ATOM   1525  N   LEU A 217      22.196  27.935  14.951  1.00 11.10           N  
ATOM   1526  CA  LEU A 217      21.963  28.949  13.936  1.00 12.28           C  
ATOM   1527  C   LEU A 217      21.841  28.351  12.537  1.00 12.61           C  
ATOM   1528  O   LEU A 217      21.428  29.040  11.588  1.00 13.94           O  
ATOM   1529  CB  LEU A 217      23.116  29.933  14.075  1.00 11.11           C  
ATOM   1530  CG  LEU A 217      22.921  31.448  14.276  1.00 15.93           C  
ATOM   1531  CD1 LEU A 217      21.587  31.781  14.868  1.00 11.22           C  
ATOM   1532  CD2 LEU A 217      24.083  31.962  15.130  1.00 12.66           C  
ATOM   1533  N   LEU A 218      22.225  27.085  12.337  1.00 11.93           N  
ATOM   1534  CA  LEU A 218      22.115  26.479  11.010  1.00 13.37           C  
ATOM   1535  C   LEU A 218      20.641  26.202  10.681  1.00 13.53           C  
ATOM   1536  O   LEU A 218      19.797  26.011  11.576  1.00 13.65           O  
ATOM   1537  CB  LEU A 218      22.925  25.157  10.946  1.00 13.76           C  
ATOM   1538  CG  LEU A 218      24.453  25.243  11.051  1.00 14.89           C  
ATOM   1539  CD1 LEU A 218      25.010  23.896  11.494  1.00 16.33           C  
ATOM   1540  CD2 LEU A 218      25.064  25.584   9.700  1.00 16.52           C  
ATOM   1541  N   LYS A 219      20.311  26.205   9.385  1.00 14.89           N  
ATOM   1542  CA  LYS A 219      18.955  25.913   8.960  1.00 16.17           C  
ATOM   1543  C   LYS A 219      18.517  24.529   9.438  1.00 16.28           C  
ATOM   1544  O   LYS A 219      19.248  23.545   9.260  1.00 16.06           O  
ATOM   1545  CB  LYS A 219      18.797  25.854   7.448  1.00 21.15           C  
ATOM   1546  CG  LYS A 219      19.208  27.011   6.562  1.00 25.16           C  
ATOM   1547  CD  LYS A 219      20.139  26.579   5.380  1.00 29.63           C  
ATOM   1548  CE  LYS A 219      19.926  25.211   4.656  1.00 30.42           C  
ATOM   1549  NZ  LYS A 219      20.879  24.178   5.084  1.00 28.54           N  
ATOM   1550  N   GLY A 220      17.320  24.427  10.013  1.00 16.27           N  
ATOM   1551  CA  GLY A 220      16.733  23.173  10.461  1.00 16.90           C  
ATOM   1552  C   GLY A 220      16.352  22.422   9.198  1.00 17.56           C  
ATOM   1553  O   GLY A 220      15.529  22.887   8.412  1.00 18.39           O  
ATOM   1554  N   THR A 221      16.939  21.266   9.016  1.00 18.62           N  
ATOM   1555  CA  THR A 221      16.826  20.443   7.828  1.00 20.34           C  
ATOM   1556  C   THR A 221      16.377  18.986   8.041  1.00 21.01           C  
ATOM   1557  O   THR A 221      15.801  18.356   7.144  1.00 20.95           O  
ATOM   1558  CB  THR A 221      18.260  20.637   7.244  1.00 21.00           C  
ATOM   1559  OG1 THR A 221      18.157  21.431   6.069  1.00 22.75           O  
ATOM   1560  CG2 THR A 221      18.963  19.351   6.991  1.00 21.08           C  
ATOM   1561  N   THR A 222      16.663  18.454   9.233  1.00 20.82           N  
ATOM   1562  CA  THR A 222      16.506  17.044   9.537  1.00 20.09           C  
ATOM   1563  C   THR A 222      15.610  16.764  10.728  1.00 20.18           C  
ATOM   1564  O   THR A 222      15.672  17.467  11.739  1.00 19.84           O  
ATOM   1565  CB  THR A 222      17.925  16.472   9.805  1.00 19.94           C  
ATOM   1566  OG1 THR A 222      18.786  17.017   8.822  1.00 21.09           O  
ATOM   1567  CG2 THR A 222      17.983  14.972   9.751  1.00 21.31           C  
ATOM   1568  N   GLN A 223      14.776  15.729  10.660  1.00 19.19           N  
ATOM   1569  CA  GLN A 223      13.947  15.330  11.790  1.00 18.29           C  
ATOM   1570  C   GLN A 223      14.816  14.190  12.301  1.00 17.61           C  
ATOM   1571  O   GLN A 223      14.986  13.231  11.537  1.00 17.92           O  
ATOM   1572  CB  GLN A 223      12.595  14.811  11.303  1.00 18.52           C  
ATOM   1573  CG  GLN A 223      11.665  14.332  12.398  1.00 20.34           C  
ATOM   1574  CD  GLN A 223      10.332  13.839  11.841  1.00 22.70           C  
ATOM   1575  OE1 GLN A 223       9.570  14.540  11.153  1.00 21.76           O  
ATOM   1576  NE2 GLN A 223      10.040  12.582  12.127  1.00 22.67           N  
ATOM   1577  N   PRO A 224      15.435  14.226  13.488  1.00 16.26           N  
ATOM   1578  CA  PRO A 224      16.291  13.153  13.968  1.00 16.37           C  
ATOM   1579  C   PRO A 224      15.584  11.872  14.424  1.00 16.12           C  
ATOM   1580  O   PRO A 224      16.196  10.804  14.386  1.00 18.07           O  
ATOM   1581  CB  PRO A 224      17.111  13.809  15.068  1.00 14.37           C  
ATOM   1582  CG  PRO A 224      16.119  14.780  15.638  1.00 15.70           C  
ATOM   1583  CD  PRO A 224      15.472  15.366  14.395  1.00 15.97           C  
ATOM   1584  N   GLY A 225      14.328  11.898  14.848  1.00 16.29           N  
ATOM   1585  CA  GLY A 225      13.661  10.702  15.334  1.00 16.43           C  
ATOM   1586  C   GLY A 225      12.430  10.346  14.524  1.00 17.62           C  
ATOM   1587  O   GLY A 225      12.090  11.080  13.598  1.00 17.76           O  
ATOM   1588  N   PRO A 226      11.716   9.254  14.833  1.00 18.90           N  
ATOM   1589  CA  PRO A 226      10.521   8.817  14.123  1.00 20.29           C  
ATOM   1590  C   PRO A 226       9.370   9.812  14.133  1.00 20.93           C  
ATOM   1591  O   PRO A 226       8.542   9.787  13.218  1.00 22.97           O  
ATOM   1592  CB  PRO A 226      10.190   7.483  14.766  1.00 19.28           C  
ATOM   1593  CG  PRO A 226      10.779   7.578  16.149  1.00 20.15           C  
ATOM   1594  CD  PRO A 226      12.057   8.339  15.917  1.00 19.09           C  
ATOM   1595  N   SER A 227       9.257  10.666  15.141  1.00 20.48           N  
ATOM   1596  CA  SER A 227       8.250  11.702  15.175  1.00 20.64           C  
ATOM   1597  C   SER A 227       8.870  12.900  15.894  1.00 20.92           C  
ATOM   1598  O   SER A 227      10.062  12.860  16.235  1.00 19.86           O  
ATOM   1599  CB  SER A 227       7.025  11.204  15.906  1.00 19.68           C  
ATOM   1600  OG  SER A 227       7.397  10.680  17.165  1.00 23.47           O  
ATOM   1601  N   LEU A 228       8.140  13.998  16.082  1.00 21.95           N  
ATOM   1602  CA  LEU A 228       8.662  15.154  16.778  1.00 22.29           C  
ATOM   1603  C   LEU A 228       8.102  15.124  18.188  1.00 22.59           C  
ATOM   1604  O   LEU A 228       6.952  14.729  18.454  1.00 23.46           O  
ATOM   1605  CB  LEU A 228       8.259  16.407  15.996  1.00 23.69           C  
ATOM   1606  CG  LEU A 228       8.980  16.589  14.639  1.00 24.24           C  
ATOM   1607  CD1 LEU A 228       8.220  17.591  13.794  1.00 26.24           C  
ATOM   1608  CD2 LEU A 228      10.402  17.111  14.833  1.00 24.62           C  
ATOM   1609  N   GLY A 229       8.998  15.462  19.115  1.00 21.52           N  
ATOM   1610  CA  GLY A 229       8.714  15.466  20.539  1.00 19.25           C  
ATOM   1611  C   GLY A 229       8.161  16.801  21.028  1.00 19.16           C  
ATOM   1612  O   GLY A 229       7.836  17.687  20.228  1.00 18.62           O  
ATOM   1613  N   PHE A 230       8.032  16.971  22.340  1.00 18.06           N  
ATOM   1614  CA  PHE A 230       7.530  18.225  22.856  1.00 19.12           C  
ATOM   1615  C   PHE A 230       8.607  19.287  22.583  1.00 18.97           C  
ATOM   1616  O   PHE A 230       9.805  19.064  22.818  1.00 17.82           O  
ATOM   1617  CB  PHE A 230       7.275  18.127  24.350  1.00 19.62           C  
ATOM   1618  CG  PHE A 230       6.699  19.414  24.937  1.00 20.97           C  
ATOM   1619  CD1 PHE A 230       5.463  19.890  24.526  1.00 21.91           C  
ATOM   1620  CD2 PHE A 230       7.433  20.146  25.860  1.00 22.79           C  
ATOM   1621  CE1 PHE A 230       4.980  21.089  25.033  1.00 21.85           C  
ATOM   1622  CE2 PHE A 230       6.935  21.345  26.356  1.00 21.58           C  
ATOM   1623  CZ  PHE A 230       5.713  21.817  25.944  1.00 20.90           C  
ATOM   1624  N   ALA A 231       8.135  20.421  22.050  1.00 17.20           N  
ATOM   1625  CA  ALA A 231       8.962  21.565  21.732  1.00 16.68           C  
ATOM   1626  C   ALA A 231      10.179  21.260  20.864  1.00 16.15           C  
ATOM   1627  O   ALA A 231      11.209  21.946  20.956  1.00 17.80           O  
ATOM   1628  CB  ALA A 231       9.413  22.220  23.045  1.00 14.83           C  
ATOM   1629  N   GLU A 232      10.061  20.277  19.966  1.00 14.08           N  
ATOM   1630  CA  GLU A 232      11.155  19.882  19.106  1.00 14.20           C  
ATOM   1631  C   GLU A 232      11.062  20.584  17.774  1.00 14.75           C  
ATOM   1632  O   GLU A 232       9.953  20.740  17.244  1.00 16.72           O  
ATOM   1633  CB  GLU A 232      11.124  18.379  18.870  1.00 13.33           C  
ATOM   1634  CG  GLU A 232      12.334  17.893  18.079  1.00 11.43           C  
ATOM   1635  CD  GLU A 232      12.525  16.388  17.882  1.00 14.09           C  
ATOM   1636  OE1 GLU A 232      11.753  15.557  18.365  1.00 12.51           O  
ATOM   1637  OE2 GLU A 232      13.498  16.027  17.234  1.00 12.85           O  
ATOM   1638  N   GLU A 233      12.219  21.000  17.256  1.00 13.98           N  
ATOM   1639  CA  GLU A 233      12.336  21.645  15.969  1.00 14.28           C  
ATOM   1640  C   GLU A 233      13.211  20.796  15.062  1.00 14.77           C  
ATOM   1641  O   GLU A 233      13.919  19.887  15.531  1.00 15.89           O  
ATOM   1642  CB  GLU A 233      12.990  23.000  16.089  1.00 14.41           C  
ATOM   1643  CG  GLU A 233      12.142  24.084  16.728  1.00 19.44           C  
ATOM   1644  CD  GLU A 233      10.874  24.435  15.953  1.00 22.08           C  
ATOM   1645  OE1 GLU A 233      10.936  24.660  14.740  1.00 23.22           O  
ATOM   1646  OE2 GLU A 233       9.809  24.478  16.570  1.00 23.69           O  
ATOM   1647  N   LEU A 234      13.199  21.030  13.750  1.00 12.85           N  
ATOM   1648  CA  LEU A 234      14.085  20.324  12.837  1.00 14.11           C  
ATOM   1649  C   LEU A 234      15.529  20.743  13.188  1.00 14.62           C  
ATOM   1650  O   LEU A 234      15.781  21.911  13.518  1.00 14.52           O  
ATOM   1651  CB  LEU A 234      13.759  20.712  11.393  1.00 14.50           C  
ATOM   1652  CG  LEU A 234      12.935  19.814  10.469  1.00 17.07           C  
ATOM   1653  CD1 LEU A 234      11.857  19.035  11.199  1.00 16.33           C  
ATOM   1654  CD2 LEU A 234      12.352  20.709   9.422  1.00 16.40           C  
ATOM   1655  N   SER A 235      16.499  19.842  13.080  1.00 13.71           N  
ATOM   1656  CA  SER A 235      17.859  20.137  13.451  1.00 13.31           C  
ATOM   1657  C   SER A 235      18.726  20.141  12.202  1.00 13.37           C  
ATOM   1658  O   SER A 235      18.201  19.859  11.114  1.00 13.81           O  
ATOM   1659  CB  SER A 235      18.306  19.078  14.450  1.00 10.93           C  
ATOM   1660  OG  SER A 235      18.833  17.919  13.833  1.00 15.47           O  
ATOM   1661  N   PRO A 236      20.027  20.485  12.254  1.00 13.94           N  
ATOM   1662  CA  PRO A 236      20.881  20.528  11.084  1.00 14.47           C  
ATOM   1663  C   PRO A 236      21.475  19.203  10.607  1.00 14.50           C  
ATOM   1664  O   PRO A 236      22.072  19.163   9.533  1.00 14.09           O  
ATOM   1665  CB  PRO A 236      21.902  21.545  11.484  1.00 13.83           C  
ATOM   1666  CG  PRO A 236      22.137  21.272  12.946  1.00 12.62           C  
ATOM   1667  CD  PRO A 236      20.730  21.053  13.417  1.00 12.58           C  
ATOM   1668  N   PHE A 237      21.419  18.105  11.364  1.00 14.91           N  
ATOM   1669  CA  PHE A 237      21.968  16.823  10.924  1.00 15.15           C  
ATOM   1670  C   PHE A 237      21.527  15.692  11.870  1.00 14.56           C  
ATOM   1671  O   PHE A 237      21.073  15.937  13.003  1.00 12.08           O  
ATOM   1672  CB  PHE A 237      23.534  16.856  10.829  1.00 17.55           C  
ATOM   1673  CG  PHE A 237      24.298  17.757  11.780  1.00 17.41           C  
ATOM   1674  CD1 PHE A 237      24.345  17.466  13.114  1.00 18.31           C  
ATOM   1675  CD2 PHE A 237      24.911  18.883  11.261  1.00 19.60           C  
ATOM   1676  CE1 PHE A 237      25.015  18.337  13.941  1.00 19.39           C  
ATOM   1677  CE2 PHE A 237      25.577  19.747  12.093  1.00 18.67           C  
ATOM   1678  CZ  PHE A 237      25.624  19.465  13.435  1.00 19.25           C  
ATOM   1679  N   PRO A 238      21.538  14.441  11.363  1.00 14.00           N  
ATOM   1680  CA  PRO A 238      21.125  13.263  12.106  1.00 13.34           C  
ATOM   1681  C   PRO A 238      21.727  13.188  13.496  1.00 11.61           C  
ATOM   1682  O   PRO A 238      22.912  13.487  13.694  1.00 12.78           O  
ATOM   1683  CB  PRO A 238      21.551  12.124  11.219  1.00 13.74           C  
ATOM   1684  CG  PRO A 238      21.491  12.706   9.819  1.00 13.43           C  
ATOM   1685  CD  PRO A 238      22.063  14.064  10.039  1.00 13.44           C  
ATOM   1686  N   GLY A 239      20.893  12.782  14.446  1.00 11.59           N  
ATOM   1687  CA  GLY A 239      21.301  12.622  15.833  1.00  8.95           C  
ATOM   1688  C   GLY A 239      21.284  13.883  16.677  1.00  8.85           C  
ATOM   1689  O   GLY A 239      21.318  13.752  17.892  1.00  8.92           O  
ATOM   1690  N   GLU A 240      21.319  15.092  16.136  1.00  9.20           N  
ATOM   1691  CA  GLU A 240      21.277  16.299  16.950  1.00  9.30           C  
ATOM   1692  C   GLU A 240      19.819  16.675  17.193  1.00 10.19           C  
ATOM   1693  O   GLU A 240      19.006  16.586  16.274  1.00 10.80           O  
ATOM   1694  CB  GLU A 240      21.966  17.449  16.241  1.00  9.67           C  
ATOM   1695  CG  GLU A 240      22.009  18.685  17.135  1.00 10.72           C  
ATOM   1696  CD  GLU A 240      23.062  19.688  16.705  1.00 12.03           C  
ATOM   1697  OE1 GLU A 240      24.235  19.391  16.945  1.00 12.32           O  
ATOM   1698  OE2 GLU A 240      22.719  20.736  16.164  1.00 10.72           O  
ATOM   1699  N   PHE A 241      19.484  17.100  18.396  1.00  9.61           N  
ATOM   1700  CA  PHE A 241      18.142  17.514  18.768  1.00  9.89           C  
ATOM   1701  C   PHE A 241      18.133  19.041  18.814  1.00 10.15           C  
ATOM   1702  O   PHE A 241      19.120  19.620  19.288  1.00 10.83           O  
ATOM   1703  CB  PHE A 241      17.811  16.955  20.161  1.00 10.60           C  
ATOM   1704  CG  PHE A 241      16.416  17.292  20.672  1.00 11.24           C  
ATOM   1705  CD1 PHE A 241      16.191  18.462  21.379  1.00 11.25           C  
ATOM   1706  CD2 PHE A 241      15.376  16.420  20.423  1.00 11.78           C  
ATOM   1707  CE1 PHE A 241      14.921  18.751  21.834  1.00 10.22           C  
ATOM   1708  CE2 PHE A 241      14.113  16.716  20.883  1.00 11.17           C  
ATOM   1709  CZ  PHE A 241      13.882  17.879  21.587  1.00 11.18           C  
ATOM   1710  N   ARG A 242      17.072  19.733  18.410  1.00  8.32           N  
ATOM   1711  CA  ARG A 242      17.034  21.179  18.544  1.00  9.72           C  
ATOM   1712  C   ARG A 242      15.759  21.509  19.284  1.00  9.94           C  
ATOM   1713  O   ARG A 242      14.699  21.072  18.818  1.00 10.96           O  
ATOM   1714  CB  ARG A 242      17.010  21.856  17.188  1.00  8.55           C  
ATOM   1715  CG  ARG A 242      16.970  23.371  17.342  1.00  8.21           C  
ATOM   1716  CD  ARG A 242      17.001  24.008  15.956  1.00 11.06           C  
ATOM   1717  NE  ARG A 242      18.321  23.883  15.355  1.00 10.20           N  
ATOM   1718  CZ  ARG A 242      18.638  24.403  14.172  1.00 11.06           C  
ATOM   1719  NH1 ARG A 242      17.762  25.082  13.417  1.00 11.33           N  
ATOM   1720  NH2 ARG A 242      19.894  24.255  13.772  1.00 11.59           N  
ATOM   1721  N   MET A 243      15.775  22.209  20.432  1.00  9.55           N  
ATOM   1722  CA  MET A 243      14.522  22.573  21.089  1.00 12.09           C  
ATOM   1723  C   MET A 243      14.128  23.997  20.672  1.00 12.10           C  
ATOM   1724  O   MET A 243      14.958  24.850  20.320  1.00 10.15           O  
ATOM   1725  CB  MET A 243      14.621  22.471  22.635  1.00 12.17           C  
ATOM   1726  CG  MET A 243      15.454  23.455  23.405  1.00 15.44           C  
ATOM   1727  SD  MET A 243      15.583  23.060  25.166  1.00 16.20           S  
ATOM   1728  CE  MET A 243      16.137  24.643  25.607  1.00 24.83           C  
ATOM   1729  N   ARG A 244      12.813  24.238  20.666  1.00 13.08           N  
ATOM   1730  CA  ARG A 244      12.224  25.498  20.223  1.00 13.78           C  
ATOM   1731  C   ARG A 244      12.765  26.742  20.899  1.00 11.27           C  
ATOM   1732  O   ARG A 244      13.135  27.667  20.183  1.00 12.29           O  
ATOM   1733  CB  ARG A 244      10.724  25.420  20.423  1.00 14.86           C  
ATOM   1734  CG  ARG A 244       9.953  26.438  19.578  1.00 21.58           C  
ATOM   1735  CD  ARG A 244       8.459  26.092  19.582  1.00 24.45           C  
ATOM   1736  NE  ARG A 244       8.366  24.780  18.954  1.00 32.28           N  
ATOM   1737  CZ  ARG A 244       7.410  23.868  19.166  1.00 32.25           C  
ATOM   1738  NH1 ARG A 244       6.391  24.085  20.016  1.00 34.13           N  
ATOM   1739  NH2 ARG A 244       7.539  22.693  18.528  1.00 34.05           N  
ATOM   1740  N   SER A 245      12.925  26.784  22.215  1.00 10.13           N  
ATOM   1741  CA  SER A 245      13.402  27.985  22.884  1.00  9.40           C  
ATOM   1742  C   SER A 245      14.815  28.349  22.445  1.00 10.03           C  
ATOM   1743  O   SER A 245      15.087  29.534  22.254  1.00  9.59           O  
ATOM   1744  CB  SER A 245      13.344  27.751  24.373  1.00  9.22           C  
ATOM   1745  OG  SER A 245      14.045  26.573  24.739  1.00 10.13           O  
ATOM   1746  N   ASP A 246      15.697  27.343  22.218  1.00  9.13           N  
ATOM   1747  CA  ASP A 246      17.049  27.612  21.744  1.00  9.51           C  
ATOM   1748  C   ASP A 246      16.996  28.153  20.326  1.00  9.81           C  
ATOM   1749  O   ASP A 246      17.667  29.141  20.017  1.00 10.45           O  
ATOM   1750  CB  ASP A 246      17.930  26.357  21.724  1.00  8.32           C  
ATOM   1751  CG  ASP A 246      18.413  25.872  23.096  1.00  9.49           C  
ATOM   1752  OD1 ASP A 246      18.377  26.642  24.064  1.00  9.85           O  
ATOM   1753  OD2 ASP A 246      18.808  24.707  23.195  1.00  9.47           O  
ATOM   1754  N   ALA A 247      16.183  27.543  19.451  1.00  9.98           N  
ATOM   1755  CA  ALA A 247      16.042  28.014  18.084  1.00  9.77           C  
ATOM   1756  C   ALA A 247      15.534  29.458  18.051  1.00 10.04           C  
ATOM   1757  O   ALA A 247      16.040  30.346  17.350  1.00 11.57           O  
ATOM   1758  CB  ALA A 247      15.056  27.138  17.368  1.00  9.68           C  
ATOM   1759  N   LEU A 248      14.506  29.743  18.840  1.00 10.63           N  
ATOM   1760  CA  LEU A 248      13.934  31.082  18.897  1.00 12.68           C  
ATOM   1761  C   LEU A 248      14.903  32.107  19.505  1.00 12.83           C  
ATOM   1762  O   LEU A 248      15.079  33.169  18.897  1.00 11.61           O  
ATOM   1763  CB  LEU A 248      12.622  31.022  19.699  1.00 13.97           C  
ATOM   1764  CG  LEU A 248      11.285  31.100  18.992  1.00 17.38           C  
ATOM   1765  CD1 LEU A 248      11.312  30.377  17.676  1.00 17.50           C  
ATOM   1766  CD2 LEU A 248      10.240  30.630  19.993  1.00 16.23           C  
ATOM   1767  N   LEU A 249      15.592  31.831  20.617  1.00 11.19           N  
ATOM   1768  CA  LEU A 249      16.533  32.790  21.207  1.00 11.48           C  
ATOM   1769  C   LEU A 249      17.683  33.061  20.257  1.00 10.67           C  
ATOM   1770  O   LEU A 249      18.164  34.196  20.196  1.00 10.30           O  
ATOM   1771  CB  LEU A 249      17.107  32.277  22.545  1.00 10.57           C  
ATOM   1772  CG  LEU A 249      16.138  32.185  23.726  1.00  9.49           C  
ATOM   1773  CD1 LEU A 249      16.733  31.315  24.796  1.00  9.81           C  
ATOM   1774  CD2 LEU A 249      15.863  33.541  24.292  1.00 11.73           C  
ATOM   1775  N   ALA A 250      18.109  32.084  19.445  1.00  9.94           N  
ATOM   1776  CA  ALA A 250      19.179  32.307  18.506  1.00 11.02           C  
ATOM   1777  C   ALA A 250      18.802  33.340  17.447  1.00 10.91           C  
ATOM   1778  O   ALA A 250      19.625  34.108  16.957  1.00 11.74           O  
ATOM   1779  CB  ALA A 250      19.530  30.990  17.805  1.00 10.14           C  
ATOM   1780  N   ARG A 251      17.521  33.355  17.107  1.00 10.26           N  
ATOM   1781  CA  ARG A 251      17.007  34.198  16.059  1.00 11.50           C  
ATOM   1782  C   ARG A 251      16.265  35.461  16.466  1.00 11.83           C  
ATOM   1783  O   ARG A 251      15.971  36.276  15.591  1.00 14.79           O  
ATOM   1784  CB  ARG A 251      16.087  33.329  15.167  1.00 11.60           C  
ATOM   1785  CG  ARG A 251      16.897  32.326  14.384  1.00  9.50           C  
ATOM   1786  CD  ARG A 251      16.025  31.152  14.037  1.00 10.40           C  
ATOM   1787  NE  ARG A 251      16.790  30.191  13.265  1.00 10.71           N  
ATOM   1788  CZ  ARG A 251      17.576  29.256  13.837  1.00  9.21           C  
ATOM   1789  NH1 ARG A 251      17.709  29.139  15.138  1.00  9.51           N  
ATOM   1790  NH2 ARG A 251      18.280  28.439  13.077  1.00 12.47           N  
ATOM   1791  N   ASP A 252      15.901  35.650  17.724  1.00 11.30           N  
ATOM   1792  CA  ASP A 252      15.103  36.804  18.125  1.00 13.28           C  
ATOM   1793  C   ASP A 252      15.937  38.071  18.143  1.00 13.06           C  
ATOM   1794  O   ASP A 252      17.061  38.028  18.651  1.00 13.77           O  
ATOM   1795  CB  ASP A 252      14.529  36.499  19.489  1.00 13.43           C  
ATOM   1796  CG  ASP A 252      13.518  37.519  19.973  1.00 16.23           C  
ATOM   1797  OD1 ASP A 252      13.967  38.554  20.445  1.00 16.57           O  
ATOM   1798  OD2 ASP A 252      12.310  37.269  19.921  1.00 15.25           O  
ATOM   1799  N   SER A 253      15.398  39.227  17.729  1.00 13.60           N  
ATOM   1800  CA  SER A 253      16.199  40.449  17.681  1.00 13.52           C  
ATOM   1801  C   SER A 253      16.780  40.900  19.009  1.00 12.43           C  
ATOM   1802  O   SER A 253      17.816  41.565  19.042  1.00 14.05           O  
ATOM   1803  CB  SER A 253      15.370  41.595  17.114  1.00 15.46           C  
ATOM   1804  OG  SER A 253      14.236  41.877  17.934  1.00 20.25           O  
ATOM   1805  N   ARG A 254      16.123  40.542  20.112  1.00 11.68           N  
ATOM   1806  CA  ARG A 254      16.573  40.900  21.442  1.00 11.48           C  
ATOM   1807  C   ARG A 254      17.791  40.118  21.935  1.00 12.26           C  
ATOM   1808  O   ARG A 254      18.472  40.575  22.874  1.00 11.21           O  
ATOM   1809  CB  ARG A 254      15.433  40.702  22.425  1.00 12.73           C  
ATOM   1810  CG  ARG A 254      14.272  41.664  22.233  1.00 12.14           C  
ATOM   1811  CD  ARG A 254      13.018  41.242  22.998  1.00 13.27           C  
ATOM   1812  NE  ARG A 254      12.408  40.083  22.360  1.00 15.62           N  
ATOM   1813  CZ  ARG A 254      11.270  39.516  22.780  1.00 15.40           C  
ATOM   1814  NH1 ARG A 254      10.607  39.988  23.834  1.00 17.99           N  
ATOM   1815  NH2 ARG A 254      10.752  38.496  22.101  1.00 13.71           N  
ATOM   1816  N   THR A 255      18.047  38.933  21.353  1.00  9.21           N  
ATOM   1817  CA  THR A 255      19.133  38.079  21.818  1.00 10.20           C  
ATOM   1818  C   THR A 255      20.100  37.622  20.722  1.00  9.98           C  
ATOM   1819  O   THR A 255      21.195  37.092  21.015  1.00 11.20           O  
ATOM   1820  CB  THR A 255      18.514  36.831  22.529  1.00  9.15           C  
ATOM   1821  OG1 THR A 255      17.483  36.372  21.669  1.00 10.29           O  
ATOM   1822  CG2 THR A 255      17.893  37.110  23.895  1.00 10.50           C  
ATOM   1823  N   ALA A 256      19.723  37.847  19.467  1.00 10.58           N  
ATOM   1824  CA  ALA A 256      20.512  37.419  18.324  1.00 10.49           C  
ATOM   1825  C   ALA A 256      21.951  37.912  18.226  1.00 11.12           C  
ATOM   1826  O   ALA A 256      22.831  37.108  17.890  1.00  9.30           O  
ATOM   1827  CB  ALA A 256      19.806  37.816  17.032  1.00 10.42           C  
ATOM   1828  N   CYS A 257      22.252  39.188  18.521  1.00 10.79           N  
ATOM   1829  CA  CYS A 257      23.618  39.651  18.378  1.00 12.17           C  
ATOM   1830  C   CYS A 257      24.511  39.058  19.443  1.00 10.70           C  
ATOM   1831  O   CYS A 257      25.607  38.624  19.086  1.00 12.67           O  
ATOM   1832  CB  CYS A 257      23.616  41.194  18.380  1.00 12.09           C  
ATOM   1833  SG  CYS A 257      22.773  41.853  16.891  1.00 13.84           S  
ATOM   1834  N   ARG A 258      24.062  38.918  20.690  1.00 10.66           N  
ATOM   1835  CA  ARG A 258      24.852  38.292  21.739  1.00  9.46           C  
ATOM   1836  C   ARG A 258      25.058  36.821  21.372  1.00  9.93           C  
ATOM   1837  O   ARG A 258      26.174  36.325  21.516  1.00 10.59           O  
ATOM   1838  CB  ARG A 258      24.131  38.397  23.068  1.00  9.02           C  
ATOM   1839  CG  ARG A 258      24.895  37.893  24.277  1.00  9.72           C  
ATOM   1840  CD  ARG A 258      26.121  38.725  24.551  1.00  8.31           C  
ATOM   1841  NE  ARG A 258      26.555  38.528  25.924  1.00 10.37           N  
ATOM   1842  CZ  ARG A 258      27.452  39.328  26.496  1.00 10.23           C  
ATOM   1843  NH1 ARG A 258      27.990  40.350  25.843  1.00 11.87           N  
ATOM   1844  NH2 ARG A 258      27.871  39.095  27.721  1.00 10.70           N  
ATOM   1845  N   TRP A 259      24.050  36.097  20.891  1.00  9.54           N  
ATOM   1846  CA  TRP A 259      24.170  34.694  20.455  1.00  9.71           C  
ATOM   1847  C   TRP A 259      25.240  34.578  19.367  1.00 10.79           C  
ATOM   1848  O   TRP A 259      26.131  33.729  19.453  1.00 10.89           O  
ATOM   1849  CB  TRP A 259      22.852  34.207  19.882  1.00 12.03           C  
ATOM   1850  CG  TRP A 259      22.659  32.683  19.860  1.00 10.98           C  
ATOM   1851  CD1 TRP A 259      23.161  31.856  18.866  1.00 12.19           C  
ATOM   1852  CD2 TRP A 259      21.962  31.974  20.815  1.00 11.50           C  
ATOM   1853  NE1 TRP A 259      22.779  30.627  19.195  1.00 10.46           N  
ATOM   1854  CE2 TRP A 259      22.066  30.660  20.349  1.00 11.89           C  
ATOM   1855  CE3 TRP A 259      21.272  32.279  21.963  1.00 11.38           C  
ATOM   1856  CZ2 TRP A 259      21.463  29.632  21.058  1.00 10.24           C  
ATOM   1857  CZ3 TRP A 259      20.672  31.248  22.658  1.00 12.44           C  
ATOM   1858  CH2 TRP A 259      20.773  29.937  22.206  1.00 13.02           C  
ATOM   1859  N   GLN A 260      25.221  35.467  18.360  1.00 10.26           N  
ATOM   1860  CA  GLN A 260      26.216  35.464  17.291  1.00 10.11           C  
ATOM   1861  C   GLN A 260      27.609  35.750  17.832  1.00 10.23           C  
ATOM   1862  O   GLN A 260      28.577  35.129  17.383  1.00 10.35           O  
ATOM   1863  CB  GLN A 260      25.836  36.512  16.260  1.00  9.99           C  
ATOM   1864  CG  GLN A 260      26.740  36.524  15.048  1.00 12.68           C  
ATOM   1865  CD  GLN A 260      26.242  37.418  13.909  1.00 12.26           C  
ATOM   1866  OE1 GLN A 260      25.238  37.108  13.281  1.00 13.27           O  
ATOM   1867  NE2 GLN A 260      26.901  38.503  13.552  1.00 12.20           N  
ATOM   1868  N   SER A 261      27.776  36.655  18.798  1.00  9.97           N  
ATOM   1869  CA  SER A 261      29.096  36.954  19.341  1.00 11.45           C  
ATOM   1870  C   SER A 261      29.722  35.796  20.124  1.00 11.74           C  
ATOM   1871  O   SER A 261      30.919  35.778  20.410  1.00 13.09           O  
ATOM   1872  CB  SER A 261      28.990  38.189  20.243  1.00 12.11           C  
ATOM   1873  OG  SER A 261      28.351  37.962  21.498  1.00 10.11           O  
ATOM   1874  N   MET A 262      28.898  34.825  20.531  1.00 12.50           N  
ATOM   1875  CA  MET A 262      29.371  33.661  21.268  1.00 13.55           C  
ATOM   1876  C   MET A 262      29.851  32.589  20.324  1.00 13.94           C  
ATOM   1877  O   MET A 262      30.247  31.537  20.820  1.00 16.37           O  
ATOM   1878  CB  MET A 262      28.269  33.029  22.111  1.00 10.98           C  
ATOM   1879  CG  MET A 262      27.827  33.894  23.246  1.00 12.68           C  
ATOM   1880  SD  MET A 262      29.170  33.972  24.429  1.00 13.65           S  
ATOM   1881  CE  MET A 262      28.304  33.547  25.911  1.00 13.38           C  
ATOM   1882  N   THR A 263      29.787  32.744  19.003  1.00 13.18           N  
ATOM   1883  CA  THR A 263      30.198  31.655  18.123  1.00 13.10           C  
ATOM   1884  C   THR A 263      31.688  31.515  17.868  1.00 13.98           C  
ATOM   1885  O   THR A 263      32.135  30.412  17.581  1.00 13.93           O  
ATOM   1886  CB  THR A 263      29.552  31.758  16.709  1.00 13.05           C  
ATOM   1887  OG1 THR A 263      30.083  32.940  16.098  1.00 12.37           O  
ATOM   1888  CG2 THR A 263      28.046  31.824  16.747  1.00 12.31           C  
ATOM   1889  N   SER A 264      32.497  32.568  17.936  1.00 13.57           N  
ATOM   1890  CA  SER A 264      33.875  32.445  17.490  1.00 14.43           C  
ATOM   1891  C   SER A 264      34.992  32.303  18.480  1.00 11.71           C  
ATOM   1892  O   SER A 264      36.125  32.008  18.080  1.00 12.60           O  
ATOM   1893  CB  SER A 264      34.159  33.649  16.572  1.00 16.38           C  
ATOM   1894  OG  SER A 264      33.791  34.894  17.184  1.00 21.42           O  
ATOM   1895  N   SER A 265      34.694  32.515  19.750  1.00 10.75           N  
ATOM   1896  CA  SER A 265      35.719  32.450  20.760  1.00 10.91           C  
ATOM   1897  C   SER A 265      35.298  31.738  22.007  1.00 10.11           C  
ATOM   1898  O   SER A 265      34.455  32.183  22.803  1.00 10.06           O  
ATOM   1899  CB  SER A 265      36.184  33.858  21.128  1.00 10.84           C  
ATOM   1900  OG  SER A 265      37.113  33.815  22.211  1.00 10.92           O  
ATOM   1901  N   ASN A 266      36.016  30.640  22.187  1.00  9.87           N  
ATOM   1902  CA  ASN A 266      35.795  29.824  23.362  1.00  9.65           C  
ATOM   1903  C   ASN A 266      36.197  30.583  24.607  1.00  9.80           C  
ATOM   1904  O   ASN A 266      35.548  30.472  25.657  1.00  9.88           O  
ATOM   1905  CB  ASN A 266      36.597  28.544  23.287  1.00 10.53           C  
ATOM   1906  CG  ASN A 266      35.984  27.517  22.342  1.00 11.26           C  
ATOM   1907  OD1 ASN A 266      34.774  27.241  22.361  1.00 10.84           O  
ATOM   1908  ND2 ASN A 266      36.787  26.876  21.503  1.00 11.18           N  
ATOM   1909  N   GLU A 267      37.244  31.412  24.498  1.00  9.68           N  
ATOM   1910  CA  GLU A 267      37.702  32.190  25.632  1.00 11.83           C  
ATOM   1911  C   GLU A 267      36.672  33.228  26.125  1.00 11.68           C  
ATOM   1912  O   GLU A 267      36.441  33.401  27.320  1.00 12.44           O  
ATOM   1913  CB  GLU A 267      38.991  32.877  25.232  1.00 12.66           C  
ATOM   1914  CG  GLU A 267      39.674  33.503  26.440  1.00 13.37           C  
ATOM   1915  CD  GLU A 267      41.067  34.079  26.148  1.00 17.74           C  
ATOM   1916  OE1 GLU A 267      41.624  33.762  25.085  1.00 17.42           O  
ATOM   1917  OE2 GLU A 267      41.595  34.826  26.990  1.00 16.00           O  
ATOM   1918  N   VAL A 268      36.023  33.919  25.201  1.00 13.09           N  
ATOM   1919  CA  VAL A 268      35.006  34.927  25.517  1.00 13.75           C  
ATOM   1920  C   VAL A 268      33.776  34.234  26.099  1.00 12.97           C  
ATOM   1921  O   VAL A 268      33.245  34.673  27.123  1.00 10.68           O  
ATOM   1922  CB  VAL A 268      34.657  35.687  24.213  1.00 14.39           C  
ATOM   1923  CG1 VAL A 268      33.359  36.449  24.288  1.00 16.57           C  
ATOM   1924  CG2 VAL A 268      35.735  36.722  23.993  1.00 16.98           C  
ATOM   1925  N   MET A 269      33.330  33.135  25.460  1.00 12.26           N  
ATOM   1926  CA  MET A 269      32.166  32.408  25.943  1.00 10.34           C  
ATOM   1927  C   MET A 269      32.411  31.969  27.376  1.00  9.60           C  
ATOM   1928  O   MET A 269      31.565  32.215  28.234  1.00 10.42           O  
ATOM   1929  CB  MET A 269      31.885  31.164  25.108  1.00 11.36           C  
ATOM   1930  CG  MET A 269      30.801  30.245  25.699  1.00 13.68           C  
ATOM   1931  SD  MET A 269      30.687  28.706  24.743  1.00 14.60           S  
ATOM   1932  CE  MET A 269      32.087  27.940  25.493  1.00 15.48           C  
ATOM   1933  N   GLY A 270      33.557  31.363  27.677  1.00  8.53           N  
ATOM   1934  CA  GLY A 270      33.845  30.891  29.004  1.00  9.04           C  
ATOM   1935  C   GLY A 270      33.877  31.988  30.065  1.00  9.59           C  
ATOM   1936  O   GLY A 270      33.344  31.737  31.146  1.00  9.45           O  
ATOM   1937  N   GLN A 271      34.417  33.195  29.824  1.00  9.46           N  
ATOM   1938  CA  GLN A 271      34.431  34.236  30.848  1.00 12.06           C  
ATOM   1939  C   GLN A 271      33.032  34.736  31.110  1.00  9.40           C  
ATOM   1940  O   GLN A 271      32.674  34.985  32.262  1.00  8.42           O  
ATOM   1941  CB  GLN A 271      35.297  35.465  30.470  1.00 16.33           C  
ATOM   1942  CG  GLN A 271      34.803  36.805  29.788  1.00 27.60           C  
ATOM   1943  CD  GLN A 271      33.877  37.878  30.461  1.00 30.03           C  
ATOM   1944  OE1 GLN A 271      33.582  38.906  29.812  1.00 32.95           O  
ATOM   1945  NE2 GLN A 271      33.333  37.809  31.691  1.00 32.11           N  
ATOM   1946  N   ARG A 272      32.254  34.890  30.033  1.00  8.91           N  
ATOM   1947  CA  ARG A 272      30.866  35.343  30.111  1.00  9.08           C  
ATOM   1948  C   ARG A 272      30.039  34.351  30.923  1.00  8.85           C  
ATOM   1949  O   ARG A 272      29.322  34.753  31.851  1.00  8.72           O  
ATOM   1950  CB  ARG A 272      30.328  35.494  28.684  1.00 10.85           C  
ATOM   1951  CG  ARG A 272      30.630  36.936  28.369  1.00 14.19           C  
ATOM   1952  CD  ARG A 272      31.039  37.426  27.012  1.00 17.91           C  
ATOM   1953  NE  ARG A 272      30.217  37.042  25.919  1.00 18.21           N  
ATOM   1954  CZ  ARG A 272      30.131  37.750  24.777  1.00 16.95           C  
ATOM   1955  NH1 ARG A 272      30.753  38.889  24.508  1.00 17.63           N  
ATOM   1956  NH2 ARG A 272      29.435  37.214  23.800  1.00 16.29           N  
ATOM   1957  N   TYR A 273      30.180  33.050  30.631  1.00  7.04           N  
ATOM   1958  CA  TYR A 273      29.474  32.021  31.362  1.00  7.09           C  
ATOM   1959  C   TYR A 273      29.902  32.012  32.827  1.00  7.95           C  
ATOM   1960  O   TYR A 273      29.036  31.956  33.701  1.00  8.30           O  
ATOM   1961  CB  TYR A 273      29.763  30.678  30.693  1.00  6.77           C  
ATOM   1962  CG  TYR A 273      29.122  29.499  31.408  1.00  9.55           C  
ATOM   1963  CD1 TYR A 273      27.747  29.307  31.321  1.00  8.80           C  
ATOM   1964  CD2 TYR A 273      29.933  28.628  32.108  1.00  7.73           C  
ATOM   1965  CE1 TYR A 273      27.167  28.223  31.948  1.00  9.89           C  
ATOM   1966  CE2 TYR A 273      29.367  27.537  32.724  1.00  9.73           C  
ATOM   1967  CZ  TYR A 273      27.993  27.351  32.634  1.00 10.81           C  
ATOM   1968  OH  TYR A 273      27.437  26.227  33.212  1.00 12.08           O  
ATOM   1969  N   ARG A 274      31.195  32.104  33.162  1.00  8.36           N  
ATOM   1970  CA  ARG A 274      31.688  32.107  34.526  1.00  8.78           C  
ATOM   1971  C   ARG A 274      31.082  33.261  35.309  1.00  8.28           C  
ATOM   1972  O   ARG A 274      30.604  33.063  36.430  1.00  8.41           O  
ATOM   1973  CB  ARG A 274      33.205  32.207  34.499  1.00  9.11           C  
ATOM   1974  CG  ARG A 274      33.802  32.123  35.907  1.00 13.54           C  
ATOM   1975  CD  ARG A 274      35.312  32.412  35.994  1.00 15.96           C  
ATOM   1976  NE  ARG A 274      35.834  32.024  37.314  1.00 17.33           N  
ATOM   1977  CZ  ARG A 274      35.754  32.767  38.428  1.00 18.94           C  
ATOM   1978  NH1 ARG A 274      35.203  33.979  38.422  1.00 18.44           N  
ATOM   1979  NH2 ARG A 274      36.158  32.256  39.599  1.00 18.98           N  
ATOM   1980  N   ALA A 275      31.026  34.468  34.727  1.00  8.32           N  
ATOM   1981  CA  ALA A 275      30.431  35.617  35.395  1.00  7.63           C  
ATOM   1982  C   ALA A 275      28.941  35.411  35.669  1.00  8.43           C  
ATOM   1983  O   ALA A 275      28.460  35.659  36.790  1.00  8.92           O  
ATOM   1984  CB  ALA A 275      30.587  36.855  34.542  1.00  8.28           C  
ATOM   1985  N   ALA A 276      28.194  34.900  34.682  1.00  8.15           N  
ATOM   1986  CA  ALA A 276      26.748  34.705  34.835  1.00  8.76           C  
ATOM   1987  C   ALA A 276      26.442  33.629  35.856  1.00  7.78           C  
ATOM   1988  O   ALA A 276      25.539  33.803  36.685  1.00  7.69           O  
ATOM   1989  CB  ALA A 276      26.135  34.337  33.481  1.00  9.35           C  
ATOM   1990  N   MET A 277      27.242  32.560  35.886  1.00  6.87           N  
ATOM   1991  CA  MET A 277      27.070  31.496  36.867  1.00  7.98           C  
ATOM   1992  C   MET A 277      27.373  31.967  38.274  1.00 10.16           C  
ATOM   1993  O   MET A 277      26.653  31.581  39.205  1.00 10.60           O  
ATOM   1994  CB  MET A 277      27.977  30.320  36.565  1.00  9.55           C  
ATOM   1995  CG  MET A 277      27.498  29.542  35.358  1.00 11.15           C  
ATOM   1996  SD  MET A 277      25.902  28.709  35.610  1.00 13.80           S  
ATOM   1997  CE  MET A 277      26.502  27.264  36.452  1.00 13.69           C  
ATOM   1998  N   ALA A 278      28.408  32.813  38.501  1.00 10.65           N  
ATOM   1999  CA  ALA A 278      28.705  33.328  39.831  1.00 10.87           C  
ATOM   2000  C   ALA A 278      27.506  34.160  40.304  1.00 10.85           C  
ATOM   2001  O   ALA A 278      27.121  34.067  41.467  1.00 12.11           O  
ATOM   2002  CB  ALA A 278      29.953  34.204  39.814  1.00  9.73           C  
ATOM   2003  N   LYS A 279      26.814  34.885  39.428  1.00 10.70           N  
ATOM   2004  CA  LYS A 279      25.643  35.655  39.822  1.00 10.84           C  
ATOM   2005  C   LYS A 279      24.495  34.716  40.215  1.00 11.32           C  
ATOM   2006  O   LYS A 279      23.848  34.883  41.261  1.00 12.10           O  
ATOM   2007  CB  LYS A 279      25.267  36.549  38.648  1.00 11.17           C  
ATOM   2008  CG  LYS A 279      24.008  37.362  38.871  1.00 14.68           C  
ATOM   2009  CD  LYS A 279      23.876  38.239  37.643  1.00 15.16           C  
ATOM   2010  CE  LYS A 279      22.514  38.871  37.722  1.00 16.67           C  
ATOM   2011  NZ  LYS A 279      22.501  39.945  36.757  1.00 17.23           N  
ATOM   2012  N   MET A 280      24.290  33.670  39.427  1.00 10.04           N  
ATOM   2013  CA  MET A 280      23.242  32.709  39.680  1.00 11.25           C  
ATOM   2014  C   MET A 280      23.460  31.941  40.977  1.00 11.03           C  
ATOM   2015  O   MET A 280      22.489  31.656  41.677  1.00 10.19           O  
ATOM   2016  CB  MET A 280      23.144  31.709  38.503  1.00 10.09           C  
ATOM   2017  CG  MET A 280      21.890  30.872  38.663  1.00 13.67           C  
ATOM   2018  SD  MET A 280      21.416  29.915  37.234  1.00 16.36           S  
ATOM   2019  CE  MET A 280      22.700  28.719  37.295  1.00 16.26           C  
ATOM   2020  N   SER A 281      24.718  31.665  41.324  1.00  9.74           N  
ATOM   2021  CA  SER A 281      25.056  30.900  42.498  1.00  8.81           C  
ATOM   2022  C   SER A 281      24.709  31.605  43.798  1.00  9.87           C  
ATOM   2023  O   SER A 281      24.651  30.945  44.837  1.00 10.67           O  
ATOM   2024  CB  SER A 281      26.549  30.575  42.473  1.00  9.83           C  
ATOM   2025  OG  SER A 281      27.335  31.707  42.828  1.00 14.07           O  
ATOM   2026  N   VAL A 282      24.511  32.933  43.804  1.00  9.03           N  
ATOM   2027  CA  VAL A 282      24.181  33.603  45.044  1.00 10.42           C  
ATOM   2028  C   VAL A 282      22.789  34.213  45.033  1.00 10.97           C  
ATOM   2029  O   VAL A 282      22.478  35.084  45.853  1.00 11.67           O  
ATOM   2030  CB  VAL A 282      25.235  34.712  45.408  1.00 10.58           C  
ATOM   2031  CG1 VAL A 282      26.578  34.028  45.635  1.00 12.98           C  
ATOM   2032  CG2 VAL A 282      25.341  35.778  44.340  1.00 11.52           C  
ATOM   2033  N   LEU A 283      21.903  33.786  44.131  1.00 11.09           N  
ATOM   2034  CA  LEU A 283      20.531  34.273  44.120  1.00 12.20           C  
ATOM   2035  C   LEU A 283      19.903  33.846  45.446  1.00 12.07           C  
ATOM   2036  O   LEU A 283      19.918  32.669  45.812  1.00 12.72           O  
ATOM   2037  CB  LEU A 283      19.794  33.650  42.920  1.00 13.55           C  
ATOM   2038  CG  LEU A 283      19.374  34.449  41.663  1.00 16.61           C  
ATOM   2039  CD1 LEU A 283      20.384  35.485  41.222  1.00 15.24           C  
ATOM   2040  CD2 LEU A 283      19.089  33.410  40.598  1.00 14.60           C  
ATOM   2041  N   GLY A 284      19.385  34.813  46.203  1.00 12.17           N  
ATOM   2042  CA  GLY A 284      18.771  34.600  47.503  1.00 13.14           C  
ATOM   2043  C   GLY A 284      19.775  34.806  48.634  1.00 12.69           C  
ATOM   2044  O   GLY A 284      19.438  34.616  49.806  1.00 12.84           O  
ATOM   2045  N   PHE A 285      21.011  35.198  48.344  1.00 12.11           N  
ATOM   2046  CA  PHE A 285      22.074  35.340  49.338  1.00 12.16           C  
ATOM   2047  C   PHE A 285      22.891  36.600  49.099  1.00 13.69           C  
ATOM   2048  O   PHE A 285      22.836  37.227  48.034  1.00 14.88           O  
ATOM   2049  CB  PHE A 285      23.074  34.145  49.301  1.00 11.55           C  
ATOM   2050  CG  PHE A 285      22.399  32.838  49.674  1.00 10.59           C  
ATOM   2051  CD1 PHE A 285      21.715  32.135  48.690  1.00 11.51           C  
ATOM   2052  CD2 PHE A 285      22.396  32.407  50.984  1.00 11.32           C  
ATOM   2053  CE1 PHE A 285      21.010  30.990  49.031  1.00 12.72           C  
ATOM   2054  CE2 PHE A 285      21.692  31.268  51.315  1.00 11.21           C  
ATOM   2055  CZ  PHE A 285      20.996  30.560  50.341  1.00 14.24           C  
ATOM   2056  N   ASP A 286      23.651  36.932  50.131  1.00 14.30           N  
ATOM   2057  CA  ASP A 286      24.565  38.046  50.081  1.00 15.41           C  
ATOM   2058  C   ASP A 286      25.921  37.410  49.887  1.00 14.89           C  
ATOM   2059  O   ASP A 286      26.416  36.776  50.825  1.00 15.38           O  
ATOM   2060  CB  ASP A 286      24.537  38.794  51.386  1.00 18.50           C  
ATOM   2061  CG  ASP A 286      25.547  39.928  51.539  1.00 21.50           C  
ATOM   2062  OD1 ASP A 286      26.279  40.283  50.602  1.00 22.13           O  
ATOM   2063  OD2 ASP A 286      25.591  40.458  52.650  1.00 23.77           O  
ATOM   2064  N   ARG A 287      26.582  37.599  48.749  1.00 15.47           N  
ATOM   2065  CA  ARG A 287      27.881  36.972  48.566  1.00 16.96           C  
ATOM   2066  C   ARG A 287      28.919  37.429  49.562  1.00 17.06           C  
ATOM   2067  O   ARG A 287      29.861  36.696  49.841  1.00 17.43           O  
ATOM   2068  CB  ARG A 287      28.446  37.231  47.182  1.00 18.59           C  
ATOM   2069  CG  ARG A 287      28.679  38.675  46.791  1.00 20.47           C  
ATOM   2070  CD  ARG A 287      29.245  38.719  45.384  1.00 20.62           C  
ATOM   2071  NE  ARG A 287      30.605  38.230  45.379  1.00 22.98           N  
ATOM   2072  CZ  ARG A 287      30.989  37.175  44.650  1.00 23.21           C  
ATOM   2073  NH1 ARG A 287      30.162  36.481  43.855  1.00 23.54           N  
ATOM   2074  NH2 ARG A 287      32.242  36.774  44.783  1.00 24.11           N  
ATOM   2075  N   ASN A 288      28.761  38.614  50.156  1.00 17.71           N  
ATOM   2076  CA  ASN A 288      29.727  39.101  51.130  1.00 17.59           C  
ATOM   2077  C   ASN A 288      29.609  38.372  52.449  1.00 17.40           C  
ATOM   2078  O   ASN A 288      30.473  38.505  53.320  1.00 19.49           O  
ATOM   2079  CB  ASN A 288      29.561  40.595  51.386  1.00 19.56           C  
ATOM   2080  CG  ASN A 288      29.880  41.443  50.169  1.00 18.91           C  
ATOM   2081  OD1 ASN A 288      30.734  41.123  49.347  1.00 22.65           O  
ATOM   2082  ND2 ASN A 288      29.207  42.552  49.968  1.00 21.16           N  
ATOM   2083  N   ALA A 289      28.549  37.584  52.642  1.00 15.72           N  
ATOM   2084  CA  ALA A 289      28.423  36.810  53.862  1.00 14.21           C  
ATOM   2085  C   ALA A 289      28.969  35.398  53.625  1.00 14.35           C  
ATOM   2086  O   ALA A 289      28.965  34.551  54.526  1.00 15.16           O  
ATOM   2087  CB  ALA A 289      26.964  36.722  54.243  1.00 15.14           C  
ATOM   2088  N   LEU A 290      29.460  35.053  52.441  1.00 12.83           N  
ATOM   2089  CA  LEU A 290      29.916  33.688  52.171  1.00 12.59           C  
ATOM   2090  C   LEU A 290      31.427  33.606  52.149  1.00 13.68           C  
ATOM   2091  O   LEU A 290      32.056  34.670  52.033  1.00 16.56           O  
ATOM   2092  CB  LEU A 290      29.343  33.232  50.823  1.00 11.67           C  
ATOM   2093  CG  LEU A 290      27.803  33.237  50.717  1.00 12.02           C  
ATOM   2094  CD1 LEU A 290      27.322  32.905  49.320  1.00 13.24           C  
ATOM   2095  CD2 LEU A 290      27.266  32.228  51.728  1.00 13.68           C  
ATOM   2096  N   THR A 291      32.044  32.426  52.287  1.00 14.32           N  
ATOM   2097  CA  THR A 291      33.494  32.287  52.241  1.00 14.39           C  
ATOM   2098  C   THR A 291      33.936  31.737  50.896  1.00 14.47           C  
ATOM   2099  O   THR A 291      33.362  30.801  50.344  1.00 13.25           O  
ATOM   2100  CB  THR A 291      33.963  31.365  53.387  1.00 15.54           C  
ATOM   2101  OG1 THR A 291      33.628  32.070  54.578  1.00 16.26           O  
ATOM   2102  CG2 THR A 291      35.444  31.034  53.381  1.00 14.95           C  
ATOM   2103  N   ASP A 292      34.970  32.342  50.336  1.00 13.75           N  
ATOM   2104  CA  ASP A 292      35.501  31.926  49.070  1.00 14.31           C  
ATOM   2105  C   ASP A 292      36.439  30.733  49.187  1.00 14.05           C  
ATOM   2106  O   ASP A 292      37.545  30.842  49.738  1.00 14.46           O  
ATOM   2107  CB  ASP A 292      36.223  33.114  48.457  1.00 16.79           C  
ATOM   2108  CG  ASP A 292      36.530  32.979  46.968  1.00 19.68           C  
ATOM   2109  OD1 ASP A 292      36.454  31.880  46.431  1.00 20.59           O  
ATOM   2110  OD2 ASP A 292      36.831  33.995  46.335  1.00 21.75           O  
ATOM   2111  N   CYS A 293      36.040  29.622  48.585  1.00 11.57           N  
ATOM   2112  CA  CYS A 293      36.858  28.420  48.567  1.00 12.03           C  
ATOM   2113  C   CYS A 293      37.084  27.996  47.118  1.00 12.69           C  
ATOM   2114  O   CYS A 293      37.182  26.803  46.783  1.00 12.43           O  
ATOM   2115  CB  CYS A 293      36.154  27.319  49.314  1.00 10.86           C  
ATOM   2116  SG  CYS A 293      36.100  27.588  51.097  1.00 12.76           S  
ATOM   2117  N   SER A 294      37.268  28.984  46.229  1.00 12.21           N  
ATOM   2118  CA  SER A 294      37.472  28.713  44.810  1.00 12.23           C  
ATOM   2119  C   SER A 294      38.722  27.926  44.491  1.00 13.16           C  
ATOM   2120  O   SER A 294      38.735  27.155  43.534  1.00 13.04           O  
ATOM   2121  CB  SER A 294      37.537  29.994  44.019  1.00 13.55           C  
ATOM   2122  OG  SER A 294      36.276  30.642  44.079  1.00 10.56           O  
ATOM   2123  N   ASP A 295      39.756  28.071  45.327  1.00 14.73           N  
ATOM   2124  CA  ASP A 295      41.003  27.370  45.127  1.00 15.92           C  
ATOM   2125  C   ASP A 295      40.827  25.875  45.293  1.00 15.49           C  
ATOM   2126  O   ASP A 295      41.708  25.139  44.875  1.00 17.63           O  
ATOM   2127  CB  ASP A 295      42.068  27.908  46.106  1.00 21.72           C  
ATOM   2128  CG  ASP A 295      41.645  27.978  47.577  1.00 26.20           C  
ATOM   2129  OD1 ASP A 295      41.649  26.942  48.251  1.00 30.27           O  
ATOM   2130  OD2 ASP A 295      41.300  29.073  48.054  1.00 32.42           O  
ATOM   2131  N   VAL A 296      39.746  25.342  45.870  1.00 13.23           N  
ATOM   2132  CA  VAL A 296      39.560  23.892  45.984  1.00 12.99           C  
ATOM   2133  C   VAL A 296      39.214  23.320  44.592  1.00 13.95           C  
ATOM   2134  O   VAL A 296      39.438  22.135  44.335  1.00 13.10           O  
ATOM   2135  CB  VAL A 296      38.409  23.601  46.992  1.00 14.54           C  
ATOM   2136  CG1 VAL A 296      38.114  22.124  47.090  1.00 13.55           C  
ATOM   2137  CG2 VAL A 296      38.802  24.117  48.374  1.00 13.29           C  
ATOM   2138  N   ILE A 297      38.668  24.116  43.666  1.00 13.63           N  
ATOM   2139  CA  ILE A 297      38.236  23.621  42.363  1.00 15.24           C  
ATOM   2140  C   ILE A 297      39.428  23.387  41.423  1.00 16.06           C  
ATOM   2141  O   ILE A 297      40.190  24.328  41.182  1.00 15.48           O  
ATOM   2142  CB  ILE A 297      37.229  24.648  41.750  1.00 15.28           C  
ATOM   2143  CG1 ILE A 297      36.101  24.908  42.757  1.00 17.44           C  
ATOM   2144  CG2 ILE A 297      36.682  24.142  40.381  1.00 15.98           C  
ATOM   2145  CD1 ILE A 297      35.285  23.693  43.248  1.00 14.53           C  
ATOM   2146  N   PRO A 298      39.628  22.187  40.855  1.00 16.54           N  
ATOM   2147  CA  PRO A 298      40.734  21.893  39.945  1.00 17.78           C  
ATOM   2148  C   PRO A 298      40.514  22.434  38.539  1.00 17.95           C  
ATOM   2149  O   PRO A 298      39.407  22.795  38.118  1.00 17.06           O  
ATOM   2150  CB  PRO A 298      40.848  20.383  39.985  1.00 18.02           C  
ATOM   2151  CG  PRO A 298      39.380  19.978  40.088  1.00 18.28           C  
ATOM   2152  CD  PRO A 298      38.853  20.975  41.127  1.00 18.03           C  
ATOM   2153  N   SER A 299      41.635  22.502  37.833  1.00 18.32           N  
ATOM   2154  CA  SER A 299      41.658  22.898  36.450  1.00 18.99           C  
ATOM   2155  C   SER A 299      41.157  21.772  35.543  1.00 17.46           C  
ATOM   2156  O   SER A 299      41.397  20.591  35.789  1.00 17.28           O  
ATOM   2157  CB  SER A 299      43.071  23.238  36.021  1.00 19.30           C  
ATOM   2158  OG  SER A 299      43.472  24.432  36.648  1.00 25.84           O  
ATOM   2159  N   ALA A 300      40.428  22.170  34.507  1.00 16.52           N  
ATOM   2160  CA  ALA A 300      39.938  21.283  33.458  1.00 16.34           C  
ATOM   2161  C   ALA A 300      41.054  21.193  32.422  1.00 16.56           C  
ATOM   2162  O   ALA A 300      41.929  22.078  32.355  1.00 16.87           O  
ATOM   2163  CB  ALA A 300      38.725  21.862  32.714  1.00 15.33           C  
ATOM   2164  N   VAL A 301      41.100  20.153  31.617  1.00 14.86           N  
ATOM   2165  CA  VAL A 301      42.085  20.087  30.550  1.00 15.91           C  
ATOM   2166  C   VAL A 301      41.620  21.110  29.490  1.00 15.32           C  
ATOM   2167  O   VAL A 301      40.409  21.371  29.361  1.00 14.50           O  
ATOM   2168  CB  VAL A 301      42.155  18.586  30.038  1.00 16.67           C  
ATOM   2169  CG1 VAL A 301      40.804  17.940  29.849  1.00 18.29           C  
ATOM   2170  CG2 VAL A 301      42.744  18.558  28.637  1.00 18.26           C  
ATOM   2171  N   SER A 302      42.536  21.770  28.782  1.00 14.23           N  
ATOM   2172  CA  SER A 302      42.185  22.752  27.780  1.00 16.18           C  
ATOM   2173  C   SER A 302      41.622  22.154  26.516  1.00 16.18           C  
ATOM   2174  O   SER A 302      41.909  21.003  26.169  1.00 18.40           O  
ATOM   2175  CB  SER A 302      43.397  23.595  27.395  1.00 15.61           C  
ATOM   2176  OG  SER A 302      43.820  24.317  28.548  1.00 22.43           O  
ATOM   2177  N   ASN A 303      40.790  22.920  25.824  1.00 15.06           N  
ATOM   2178  CA  ASN A 303      40.256  22.463  24.562  1.00 15.94           C  
ATOM   2179  C   ASN A 303      41.101  23.126  23.464  1.00 15.73           C  
ATOM   2180  O   ASN A 303      41.207  24.351  23.336  1.00 15.83           O  
ATOM   2181  CB  ASN A 303      38.805  22.870  24.447  1.00 13.60           C  
ATOM   2182  CG  ASN A 303      38.295  22.782  23.031  1.00 15.71           C  
ATOM   2183  OD1 ASN A 303      38.754  21.937  22.266  1.00 14.28           O  
ATOM   2184  ND2 ASN A 303      37.360  23.625  22.619  1.00 14.51           N  
ATOM   2185  N   ASN A 304      41.739  22.309  22.638  1.00 15.68           N  
ATOM   2186  CA  ASN A 304      42.612  22.807  21.577  1.00 17.54           C  
ATOM   2187  C   ASN A 304      41.955  22.897  20.197  1.00 17.19           C  
ATOM   2188  O   ASN A 304      42.564  23.373  19.236  1.00 17.31           O  
ATOM   2189  CB  ASN A 304      43.878  21.915  21.521  1.00 18.54           C  
ATOM   2190  CG  ASN A 304      44.796  22.021  22.751  1.00 19.82           C  
ATOM   2191  OD1 ASN A 304      45.400  21.047  23.205  1.00 20.35           O  
ATOM   2192  ND2 ASN A 304      44.978  23.171  23.385  1.00 18.76           N  
ATOM   2193  N   ALA A 305      40.700  22.479  20.037  1.00 16.00           N  
ATOM   2194  CA  ALA A 305      40.014  22.572  18.761  1.00 15.46           C  
ATOM   2195  C   ALA A 305      39.470  23.972  18.525  1.00 15.62           C  
ATOM   2196  O   ALA A 305      39.043  24.670  19.446  1.00 16.71           O  
ATOM   2197  CB  ALA A 305      38.842  21.624  18.709  1.00 14.13           C  
ATOM   2198  N   ALA A 306      39.512  24.456  17.310  1.00 15.72           N  
ATOM   2199  CA  ALA A 306      38.943  25.740  16.980  1.00 16.39           C  
ATOM   2200  C   ALA A 306      37.467  25.534  16.613  1.00 16.00           C  
ATOM   2201  O   ALA A 306      37.043  24.416  16.285  1.00 15.08           O  
ATOM   2202  CB  ALA A 306      39.662  26.322  15.790  1.00 17.97           C  
ATOM   2203  N   PRO A 307      36.615  26.559  16.694  1.00 16.10           N  
ATOM   2204  CA  PRO A 307      35.218  26.492  16.276  1.00 16.02           C  
ATOM   2205  C   PRO A 307      35.111  26.111  14.804  1.00 15.95           C  
ATOM   2206  O   PRO A 307      35.976  26.499  14.009  1.00 15.75           O  
ATOM   2207  CB  PRO A 307      34.696  27.870  16.561  1.00 15.62           C  
ATOM   2208  CG  PRO A 307      35.574  28.395  17.672  1.00 17.89           C  
ATOM   2209  CD  PRO A 307      36.929  27.849  17.305  1.00 16.27           C  
ATOM   2210  N   VAL A 308      34.120  25.335  14.392  1.00 16.28           N  
ATOM   2211  CA  VAL A 308      33.935  24.968  12.988  1.00 15.70           C  
ATOM   2212  C   VAL A 308      32.457  24.846  12.656  1.00 15.77           C  
ATOM   2213  O   VAL A 308      31.611  24.593  13.533  1.00 15.20           O  
ATOM   2214  CB  VAL A 308      34.530  23.587  12.561  1.00 14.44           C  
ATOM   2215  CG1 VAL A 308      36.018  23.675  12.474  1.00 19.94           C  
ATOM   2216  CG2 VAL A 308      34.125  22.495  13.561  1.00 17.66           C  
ATOM   2217  N   ILE A 309      32.116  25.051  11.388  1.00 14.49           N  
ATOM   2218  CA  ILE A 309      30.771  24.810  10.900  1.00 16.57           C  
ATOM   2219  C   ILE A 309      30.965  23.350  10.470  1.00 17.07           C  
ATOM   2220  O   ILE A 309      31.830  23.056   9.629  1.00 16.71           O  
ATOM   2221  CB  ILE A 309      30.424  25.705   9.677  1.00 18.37           C  
ATOM   2222  CG1 ILE A 309      30.382  27.176  10.109  1.00 19.09           C  
ATOM   2223  CG2 ILE A 309      29.060  25.318   9.112  1.00 17.83           C  
ATOM   2224  CD1 ILE A 309      30.254  28.159   8.912  1.00 20.44           C  
ATOM   2225  N   PRO A 310      30.256  22.388  11.068  1.00 18.27           N  
ATOM   2226  CA  PRO A 310      30.416  20.962  10.796  1.00 19.95           C  
ATOM   2227  C   PRO A 310      29.935  20.506   9.429  1.00 20.39           C  
ATOM   2228  O   PRO A 310      29.092  21.154   8.804  1.00 21.00           O  
ATOM   2229  CB  PRO A 310      29.651  20.257  11.892  1.00 19.69           C  
ATOM   2230  CG  PRO A 310      29.362  21.340  12.901  1.00 20.01           C  
ATOM   2231  CD  PRO A 310      29.195  22.586  12.056  1.00 18.59           C  
ATOM   2232  N   GLY A 311      30.522  19.378   9.032  1.00 21.09           N  
ATOM   2233  CA  GLY A 311      30.201  18.585   7.854  1.00 21.23           C  
ATOM   2234  C   GLY A 311      29.970  19.171   6.480  1.00 21.38           C  
ATOM   2235  O   GLY A 311      29.021  18.754   5.824  1.00 22.59           O  
ATOM   2236  N   GLY A 312      30.771  20.085   5.970  1.00 22.44           N  
ATOM   2237  CA  GLY A 312      30.562  20.592   4.637  1.00 23.60           C  
ATOM   2238  C   GLY A 312      29.561  21.717   4.564  1.00 23.52           C  
ATOM   2239  O   GLY A 312      29.390  22.293   3.493  1.00 24.91           O  
ATOM   2240  N   LEU A 313      28.834  22.072   5.612  1.00 23.05           N  
ATOM   2241  CA  LEU A 313      27.914  23.206   5.558  1.00 22.27           C  
ATOM   2242  C   LEU A 313      28.763  24.477   5.533  1.00 21.54           C  
ATOM   2243  O   LEU A 313      29.930  24.446   5.943  1.00 22.42           O  
ATOM   2244  CB  LEU A 313      27.019  23.187   6.779  1.00 21.26           C  
ATOM   2245  CG  LEU A 313      26.126  21.982   6.933  1.00 20.40           C  
ATOM   2246  CD1 LEU A 313      25.332  22.094   8.217  1.00 21.83           C  
ATOM   2247  CD2 LEU A 313      25.208  21.895   5.722  1.00 23.40           C  
ATOM   2248  N   THR A 314      28.248  25.611   5.087  1.00 21.30           N  
ATOM   2249  CA  THR A 314      29.031  26.836   4.986  1.00 22.03           C  
ATOM   2250  C   THR A 314      28.302  27.955   5.697  1.00 21.59           C  
ATOM   2251  O   THR A 314      27.257  27.756   6.331  1.00 22.26           O  
ATOM   2252  CB  THR A 314      29.219  27.228   3.494  1.00 22.92           C  
ATOM   2253  OG1 THR A 314      27.911  27.532   2.971  1.00 20.80           O  
ATOM   2254  CG2 THR A 314      29.882  26.119   2.677  1.00 22.85           C  
ATOM   2255  N   VAL A 315      28.764  29.183   5.496  1.00 21.51           N  
ATOM   2256  CA  VAL A 315      28.110  30.311   6.108  1.00 22.12           C  
ATOM   2257  C   VAL A 315      26.767  30.507   5.426  1.00 21.35           C  
ATOM   2258  O   VAL A 315      25.877  31.137   5.992  1.00 20.69           O  
ATOM   2259  CB  VAL A 315      29.046  31.529   5.976  1.00 23.02           C  
ATOM   2260  CG1 VAL A 315      29.036  32.092   4.562  1.00 25.11           C  
ATOM   2261  CG2 VAL A 315      28.592  32.583   6.962  1.00 25.33           C  
ATOM   2262  N   ASP A 316      26.559  29.953   4.228  1.00 21.33           N  
ATOM   2263  CA  ASP A 316      25.277  30.093   3.565  1.00 21.98           C  
ATOM   2264  C   ASP A 316      24.207  29.269   4.254  1.00 22.09           C  
ATOM   2265  O   ASP A 316      23.018  29.458   3.983  1.00 22.84           O  
ATOM   2266  CB  ASP A 316      25.333  29.646   2.107  1.00 25.83           C  
ATOM   2267  CG  ASP A 316      26.266  30.463   1.218  1.00 28.61           C  
ATOM   2268  OD1 ASP A 316      26.194  31.699   1.254  1.00 29.91           O  
ATOM   2269  OD2 ASP A 316      27.060  29.850   0.493  1.00 31.48           O  
ATOM   2270  N   ASP A 317      24.568  28.336   5.150  1.00 20.40           N  
ATOM   2271  CA  ASP A 317      23.554  27.551   5.834  1.00 19.90           C  
ATOM   2272  C   ASP A 317      23.175  28.105   7.190  1.00 19.92           C  
ATOM   2273  O   ASP A 317      22.290  27.524   7.834  1.00 20.15           O  
ATOM   2274  CB  ASP A 317      24.040  26.131   5.995  1.00 20.32           C  
ATOM   2275  CG  ASP A 317      24.277  25.522   4.629  1.00 20.59           C  
ATOM   2276  OD1 ASP A 317      23.297  25.255   3.932  1.00 21.44           O  
ATOM   2277  OD2 ASP A 317      25.433  25.345   4.247  1.00 20.78           O  
ATOM   2278  N   ILE A 318      23.828  29.176   7.689  1.00 20.35           N  
ATOM   2279  CA  ILE A 318      23.413  29.705   8.974  1.00 19.84           C  
ATOM   2280  C   ILE A 318      22.501  30.877   8.654  1.00 18.65           C  
ATOM   2281  O   ILE A 318      22.676  31.640   7.698  1.00 18.79           O  
ATOM   2282  CB  ILE A 318      24.654  30.109   9.953  1.00 23.16           C  
ATOM   2283  CG1 ILE A 318      24.759  31.607  10.163  1.00 21.14           C  
ATOM   2284  CG2 ILE A 318      25.956  29.463   9.442  1.00 18.95           C  
ATOM   2285  CD1 ILE A 318      25.714  32.241   9.147  1.00 29.47           C  
ATOM   2286  N   GLU A 319      21.425  30.922   9.405  1.00 17.92           N  
ATOM   2287  CA  GLU A 319      20.400  31.936   9.266  1.00 18.45           C  
ATOM   2288  C   GLU A 319      20.870  33.140  10.066  1.00 18.43           C  
ATOM   2289  O   GLU A 319      20.565  33.254  11.259  1.00 19.17           O  
ATOM   2290  CB  GLU A 319      19.117  31.354   9.809  1.00 17.05           C  
ATOM   2291  CG  GLU A 319      18.742  30.110   9.042  1.00 20.59           C  
ATOM   2292  CD  GLU A 319      17.395  29.550   9.436  1.00 22.92           C  
ATOM   2293  OE1 GLU A 319      17.282  28.993  10.513  1.00 23.13           O  
ATOM   2294  OE2 GLU A 319      16.438  29.676   8.670  1.00 27.62           O  
ATOM   2295  N   VAL A 320      21.665  34.020   9.469  1.00 18.30           N  
ATOM   2296  CA  VAL A 320      22.213  35.173  10.187  1.00 18.25           C  
ATOM   2297  C   VAL A 320      21.022  36.001  10.632  1.00 18.32           C  
ATOM   2298  O   VAL A 320      20.140  36.329   9.832  1.00 18.70           O  
ATOM   2299  CB  VAL A 320      23.129  36.045   9.286  1.00 19.29           C  
ATOM   2300  CG1 VAL A 320      23.771  37.199  10.066  1.00 19.47           C  
ATOM   2301  CG2 VAL A 320      24.252  35.189   8.763  1.00 18.85           C  
ATOM   2302  N   SER A 321      21.030  36.315  11.920  1.00 16.92           N  
ATOM   2303  CA  SER A 321      19.958  37.031  12.568  1.00 16.57           C  
ATOM   2304  C   SER A 321      20.395  38.303  13.290  1.00 17.32           C  
ATOM   2305  O   SER A 321      19.535  39.000  13.849  1.00 17.06           O  
ATOM   2306  CB  SER A 321      19.301  36.058  13.529  1.00 16.52           C  
ATOM   2307  OG  SER A 321      18.755  34.928  12.865  1.00 18.57           O  
ATOM   2308  N   CYS A 322      21.690  38.607  13.391  1.00 16.65           N  
ATOM   2309  CA  CYS A 322      22.093  39.857  14.002  1.00 16.96           C  
ATOM   2310  C   CYS A 322      22.302  40.823  12.830  1.00 19.19           C  
ATOM   2311  O   CYS A 322      23.302  40.740  12.102  1.00 18.48           O  
ATOM   2312  CB  CYS A 322      23.386  39.700  14.776  1.00 16.22           C  
ATOM   2313  SG  CYS A 322      24.011  41.289  15.410  1.00 14.65           S  
ATOM   2314  N   PRO A 323      21.418  41.801  12.636  1.00 20.59           N  
ATOM   2315  CA  PRO A 323      21.448  42.706  11.496  1.00 23.00           C  
ATOM   2316  C   PRO A 323      22.597  43.683  11.461  1.00 24.73           C  
ATOM   2317  O   PRO A 323      22.934  44.228  10.416  1.00 27.40           O  
ATOM   2318  CB  PRO A 323      20.102  43.383  11.546  1.00 23.74           C  
ATOM   2319  CG  PRO A 323      19.838  43.466  13.026  1.00 23.00           C  
ATOM   2320  CD  PRO A 323      20.353  42.148  13.568  1.00 21.82           C  
ATOM   2321  N   SER A 324      23.248  43.925  12.575  1.00 25.15           N  
ATOM   2322  CA  SER A 324      24.316  44.888  12.585  1.00 26.56           C  
ATOM   2323  C   SER A 324      25.757  44.393  12.565  1.00 28.29           C  
ATOM   2324  O   SER A 324      26.647  45.207  12.308  1.00 30.49           O  
ATOM   2325  CB  SER A 324      24.047  45.734  13.789  1.00 25.69           C  
ATOM   2326  OG  SER A 324      23.887  44.885  14.930  1.00 25.51           O  
ATOM   2327  N   GLU A 325      26.036  43.113  12.856  1.00 28.03           N  
ATOM   2328  CA  GLU A 325      27.390  42.558  12.949  1.00 28.52           C  
ATOM   2329  C   GLU A 325      27.427  41.493  11.859  1.00 27.75           C  
ATOM   2330  O   GLU A 325      26.509  40.672  11.773  1.00 27.21           O  
ATOM   2331  CB  GLU A 325      27.593  41.920  14.352  1.00 30.18           C  
ATOM   2332  CG  GLU A 325      28.863  41.094  14.704  1.00 35.37           C  
ATOM   2333  CD  GLU A 325      28.727  39.879  15.693  1.00 37.79           C  
ATOM   2334  OE1 GLU A 325      27.915  39.885  16.648  1.00 38.36           O  
ATOM   2335  OE2 GLU A 325      29.452  38.888  15.503  1.00 35.54           O  
ATOM   2336  N   PRO A 326      28.396  41.472  10.946  1.00 28.12           N  
ATOM   2337  CA  PRO A 326      28.545  40.399   9.971  1.00 27.40           C  
ATOM   2338  C   PRO A 326      28.912  39.114  10.734  1.00 26.15           C  
ATOM   2339  O   PRO A 326      29.586  39.159  11.772  1.00 26.01           O  
ATOM   2340  CB  PRO A 326      29.616  40.941   9.049  1.00 28.60           C  
ATOM   2341  CG  PRO A 326      30.471  41.761   9.984  1.00 29.61           C  
ATOM   2342  CD  PRO A 326      29.391  42.521  10.740  1.00 28.28           C  
ATOM   2343  N   PHE A 327      28.438  37.959  10.265  1.00 25.12           N  
ATOM   2344  CA  PHE A 327      28.703  36.688  10.909  1.00 22.98           C  
ATOM   2345  C   PHE A 327      30.210  36.477  10.956  1.00 23.00           C  
ATOM   2346  O   PHE A 327      30.863  36.773   9.946  1.00 24.13           O  
ATOM   2347  CB  PHE A 327      28.019  35.574  10.112  1.00 21.62           C  
ATOM   2348  CG  PHE A 327      27.991  34.302  10.941  1.00 20.64           C  
ATOM   2349  CD1 PHE A 327      27.073  34.166  11.966  1.00 19.26           C  
ATOM   2350  CD2 PHE A 327      28.923  33.308  10.711  1.00 20.89           C  
ATOM   2351  CE1 PHE A 327      27.080  33.054  12.771  1.00 17.34           C  
ATOM   2352  CE2 PHE A 327      28.923  32.187  11.526  1.00 19.04           C  
ATOM   2353  CZ  PHE A 327      28.005  32.064  12.553  1.00 18.98           C  
ATOM   2354  N   PRO A 328      30.831  36.057  12.066  1.00 22.35           N  
ATOM   2355  CA  PRO A 328      32.279  35.838  12.141  1.00 22.49           C  
ATOM   2356  C   PRO A 328      32.807  34.754  11.195  1.00 22.98           C  
ATOM   2357  O   PRO A 328      32.108  33.806  10.828  1.00 21.98           O  
ATOM   2358  CB  PRO A 328      32.513  35.544  13.605  1.00 21.29           C  
ATOM   2359  CG  PRO A 328      31.198  34.967  14.032  1.00 21.82           C  
ATOM   2360  CD  PRO A 328      30.210  35.888  13.370  1.00 21.04           C  
ATOM   2361  N   GLU A 329      34.060  34.906  10.759  1.00 25.11           N  
ATOM   2362  CA  GLU A 329      34.664  33.960   9.833  1.00 28.29           C  
ATOM   2363  C   GLU A 329      35.032  32.742  10.668  1.00 26.93           C  
ATOM   2364  O   GLU A 329      35.839  32.843  11.588  1.00 27.87           O  
ATOM   2365  CB  GLU A 329      35.898  34.610   9.201  1.00 32.27           C  
ATOM   2366  CG  GLU A 329      36.114  34.308   7.717  1.00 39.86           C  
ATOM   2367  CD  GLU A 329      36.691  32.927   7.343  1.00 43.19           C  
ATOM   2368  OE1 GLU A 329      36.029  31.898   7.582  1.00 46.14           O  
ATOM   2369  OE2 GLU A 329      37.804  32.892   6.779  1.00 46.37           O  
ATOM   2370  N   ILE A 330      34.387  31.617  10.444  1.00 25.15           N  
ATOM   2371  CA  ILE A 330      34.652  30.422  11.214  1.00 22.97           C  
ATOM   2372  C   ILE A 330      35.087  29.423  10.171  1.00 22.93           C  
ATOM   2373  O   ILE A 330      34.708  29.555   9.008  1.00 22.53           O  
ATOM   2374  CB  ILE A 330      33.330  30.026  11.953  1.00 24.03           C  
ATOM   2375  CG1 ILE A 330      33.074  31.029  13.076  1.00 24.68           C  
ATOM   2376  CG2 ILE A 330      33.417  28.647  12.601  1.00 23.69           C  
ATOM   2377  CD1 ILE A 330      31.695  30.886  13.726  1.00 26.17           C  
ATOM   2378  N   ALA A 331      35.925  28.466  10.532  1.00 22.13           N  
ATOM   2379  CA  ALA A 331      36.344  27.431   9.611  1.00 22.05           C  
ATOM   2380  C   ALA A 331      35.221  26.459   9.269  1.00 22.64           C  
ATOM   2381  O   ALA A 331      34.253  26.272  10.012  1.00 21.20           O  
ATOM   2382  CB  ALA A 331      37.480  26.645  10.217  1.00 22.57           C  
ATOM   2383  N   THR A 332      35.385  25.807   8.126  1.00 24.02           N  
ATOM   2384  CA  THR A 332      34.460  24.858   7.541  1.00 26.38           C  
ATOM   2385  C   THR A 332      35.162  23.497   7.625  1.00 28.07           C  
ATOM   2386  O   THR A 332      36.392  23.428   7.753  1.00 27.37           O  
ATOM   2387  CB  THR A 332      34.212  25.411   6.102  1.00 26.46           C  
ATOM   2388  OG1 THR A 332      33.204  26.414   6.287  1.00 28.85           O  
ATOM   2389  CG2 THR A 332      33.798  24.398   5.052  1.00 29.38           C  
ATOM   2390  N   ALA A 333      34.438  22.390   7.596  1.00 31.09           N  
ATOM   2391  CA  ALA A 333      35.027  21.072   7.680  1.00 33.20           C  
ATOM   2392  C   ALA A 333      34.717  20.395   6.355  1.00 35.04           C  
ATOM   2393  O   ALA A 333      33.649  20.581   5.762  1.00 34.89           O  
ATOM   2394  CB  ALA A 333      34.386  20.313   8.840  1.00 33.51           C  
ATOM   2395  N   SER A 334      35.633  19.610   5.817  1.00 38.11           N  
ATOM   2396  CA  SER A 334      35.408  18.953   4.538  1.00 40.11           C  
ATOM   2397  C   SER A 334      34.868  17.572   4.843  1.00 40.24           C  
ATOM   2398  O   SER A 334      35.614  16.737   5.368  1.00 41.58           O  
ATOM   2399  CB  SER A 334      36.741  18.858   3.761  1.00 41.42           C  
ATOM   2400  OG  SER A 334      37.473  20.096   3.705  1.00 44.15           O  
ATOM   2401  N   GLY A 335      33.587  17.293   4.648  1.00 40.20           N  
ATOM   2402  CA  GLY A 335      33.148  15.928   4.899  1.00 38.72           C  
ATOM   2403  C   GLY A 335      31.668  15.792   4.686  1.00 36.32           C  
ATOM   2404  O   GLY A 335      31.039  16.791   4.321  1.00 37.58           O  
ATOM   2405  N   PRO A 336      31.107  14.577   4.797  1.00 34.08           N  
ATOM   2406  CA  PRO A 336      29.659  14.357   4.771  1.00 31.88           C  
ATOM   2407  C   PRO A 336      29.055  14.955   6.049  1.00 29.39           C  
ATOM   2408  O   PRO A 336      29.753  15.186   7.044  1.00 29.81           O  
ATOM   2409  CB  PRO A 336      29.521  12.842   4.686  1.00 32.73           C  
ATOM   2410  CG  PRO A 336      30.752  12.328   5.440  1.00 31.06           C  
ATOM   2411  CD  PRO A 336      31.834  13.308   4.953  1.00 33.55           C  
ATOM   2412  N   LEU A 337      27.754  15.178   6.058  1.00 27.79           N  
ATOM   2413  CA  LEU A 337      27.043  15.674   7.227  1.00 26.65           C  
ATOM   2414  C   LEU A 337      27.245  14.683   8.385  1.00 25.92           C  
ATOM   2415  O   LEU A 337      27.157  13.465   8.158  1.00 26.47           O  
ATOM   2416  CB  LEU A 337      25.587  15.773   6.845  1.00 26.05           C  
ATOM   2417  CG  LEU A 337      24.737  16.942   7.266  1.00 26.87           C  
ATOM   2418  CD1 LEU A 337      25.371  18.262   6.864  1.00 26.36           C  
ATOM   2419  CD2 LEU A 337      23.379  16.778   6.614  1.00 26.69           C  
ATOM   2420  N   PRO A 338      27.566  15.076   9.619  1.00 25.33           N  
ATOM   2421  CA  PRO A 338      27.709  14.139  10.732  1.00 24.46           C  
ATOM   2422  C   PRO A 338      26.383  13.507  11.174  1.00 22.35           C  
ATOM   2423  O   PRO A 338      25.312  13.963  10.771  1.00 22.71           O  
ATOM   2424  CB  PRO A 338      28.397  14.986  11.813  1.00 24.80           C  
ATOM   2425  CG  PRO A 338      27.939  16.398  11.522  1.00 25.07           C  
ATOM   2426  CD  PRO A 338      27.946  16.434   9.989  1.00 25.48           C  
ATOM   2427  N   SER A 339      26.432  12.430  11.955  1.00 20.07           N  
ATOM   2428  CA  SER A 339      25.259  11.789  12.525  1.00 18.84           C  
ATOM   2429  C   SER A 339      25.776  11.645  13.947  1.00 17.94           C  
ATOM   2430  O   SER A 339      26.837  11.033  14.157  1.00 18.43           O  
ATOM   2431  CB  SER A 339      24.995  10.402  11.961  1.00 16.42           C  
ATOM   2432  OG  SER A 339      23.839   9.827  12.565  1.00 18.40           O  
ATOM   2433  N   LEU A 340      25.089  12.197  14.938  1.00 16.40           N  
ATOM   2434  CA  LEU A 340      25.611  12.152  16.285  1.00 13.61           C  
ATOM   2435  C   LEU A 340      25.206  10.952  17.095  1.00 13.25           C  
ATOM   2436  O   LEU A 340      24.041  10.554  17.098  1.00 13.00           O  
ATOM   2437  CB  LEU A 340      25.188  13.404  17.050  1.00 14.86           C  
ATOM   2438  CG  LEU A 340      25.459  14.768  16.414  1.00 13.91           C  
ATOM   2439  CD1 LEU A 340      25.070  15.796  17.449  1.00 14.15           C  
ATOM   2440  CD2 LEU A 340      26.915  14.930  15.979  1.00 14.41           C  
ATOM   2441  N   ALA A 341      26.190  10.390  17.773  1.00 11.86           N  
ATOM   2442  CA  ALA A 341      25.940   9.302  18.702  1.00 13.18           C  
ATOM   2443  C   ALA A 341      25.235   9.902  19.934  1.00 13.10           C  
ATOM   2444  O   ALA A 341      25.381  11.112  20.171  1.00 13.12           O  
ATOM   2445  CB  ALA A 341      27.255   8.665  19.165  1.00 11.50           C  
ATOM   2446  N   PRO A 342      24.446   9.169  20.742  1.00 14.01           N  
ATOM   2447  CA  PRO A 342      23.854   9.688  21.979  1.00 13.74           C  
ATOM   2448  C   PRO A 342      24.983  10.190  22.873  1.00 14.02           C  
ATOM   2449  O   PRO A 342      26.090   9.615  22.853  1.00 13.39           O  
ATOM   2450  CB  PRO A 342      23.127   8.536  22.643  1.00 13.36           C  
ATOM   2451  CG  PRO A 342      23.047   7.451  21.603  1.00 15.99           C  
ATOM   2452  CD  PRO A 342      24.127   7.748  20.569  1.00 15.11           C  
ATOM   2453  N   ALA A 343      24.696  11.201  23.692  1.00 11.50           N  
ATOM   2454  CA  ALA A 343      25.652  11.746  24.627  1.00 12.07           C  
ATOM   2455  C   ALA A 343      25.908  10.630  25.661  1.00 12.00           C  
ATOM   2456  O   ALA A 343      24.959   9.888  25.923  1.00 12.07           O  
ATOM   2457  CB  ALA A 343      25.015  12.972  25.260  1.00  9.41           C  
ATOM   2458  N   PRO A 344      27.106  10.396  26.216  1.00 12.65           N  
ATOM   2459  CA  PRO A 344      27.375   9.290  27.115  1.00 13.54           C  
ATOM   2460  C   PRO A 344      26.774   9.343  28.505  1.00 14.51           C  
ATOM   2461  O   PRO A 344      26.511  10.416  29.029  1.00 14.14           O  
ATOM   2462  CB  PRO A 344      28.878   9.208  27.125  1.00 14.06           C  
ATOM   2463  CG  PRO A 344      29.276  10.641  26.990  1.00 15.25           C  
ATOM   2464  CD  PRO A 344      28.309  11.168  25.947  1.00 12.48           C  
ATOM   2465  OXT PRO A 344      26.583   8.288  29.106  1.00 17.97           O  
TER    2466      PRO A 344                                                      
HETATM 2467  C1  NAG B   1      20.073  19.897  55.931  1.00 12.00           C  
HETATM 2468  C2  NAG B   1      20.766  18.895  56.855  1.00 13.60           C  
HETATM 2469  C3  NAG B   1      20.343  17.485  56.510  1.00 12.84           C  
HETATM 2470  C4  NAG B   1      18.830  17.393  56.500  1.00 13.91           C  
HETATM 2471  C5  NAG B   1      18.127  18.528  55.773  1.00 14.05           C  
HETATM 2472  C6  NAG B   1      16.664  18.552  56.135  1.00 14.11           C  
HETATM 2473  C7  NAG B   1      22.920  19.633  57.683  1.00 15.91           C  
HETATM 2474  C8  NAG B   1      24.426  19.614  57.548  1.00 15.66           C  
HETATM 2475  N2  NAG B   1      22.223  18.943  56.798  1.00 13.80           N  
HETATM 2476  O3  NAG B   1      20.880  16.629  57.490  1.00 12.56           O  
HETATM 2477  O4  NAG B   1      18.442  16.212  55.807  1.00 15.28           O  
HETATM 2478  O5  NAG B   1      18.663  19.797  56.154  1.00 13.38           O  
HETATM 2479  O6  NAG B   1      16.051  19.375  55.189  1.00 19.82           O  
HETATM 2480  O7  NAG B   1      22.359  20.330  58.534  1.00 17.35           O  
HETATM 2481  C1  NAG B   2      17.986  15.135  56.588  1.00 15.66           C  
HETATM 2482  C2  NAG B   2      17.331  14.170  55.653  1.00 16.50           C  
HETATM 2483  C3  NAG B   2      16.964  12.922  56.434  1.00 18.97           C  
HETATM 2484  C4  NAG B   2      18.202  12.327  57.122  1.00 19.67           C  
HETATM 2485  C5  NAG B   2      18.803  13.384  58.049  1.00 20.26           C  
HETATM 2486  C6  NAG B   2      20.082  12.906  58.734  1.00 18.84           C  
HETATM 2487  C7  NAG B   2      16.130  15.132  53.748  1.00 16.43           C  
HETATM 2488  C8  NAG B   2      14.832  15.694  53.220  1.00 16.66           C  
HETATM 2489  N2  NAG B   2      16.145  14.744  55.032  1.00 15.10           N  
HETATM 2490  O3  NAG B   2      16.417  11.973  55.538  1.00 20.40           O  
HETATM 2491  O4  NAG B   2      17.844  11.151  57.844  1.00 24.13           O  
HETATM 2492  O5  NAG B   2      19.096  14.536  57.257  1.00 17.28           O  
HETATM 2493  O6  NAG B   2      20.748  14.003  59.350  1.00 25.12           O  
HETATM 2494  O7  NAG B   2      17.117  15.030  53.015  1.00 16.47           O  
HETATM 2495  C   CYN A 800      17.772  23.183  31.501  1.00  7.37           C  
HETATM 2496  N   CYN A 800      16.917  23.148  32.262  1.00  9.43           N  
HETATM 2497 CA    CA A 346      15.888  26.592  45.329  1.00  8.80          CA  
HETATM 2498 CA    CA A 347      29.861  21.278  23.129  1.00  7.56          CA  
HETATM 2499  CHA HEM A 345      18.737  20.278  28.995  1.00  6.95           C  
HETATM 2500  CHB HEM A 345      15.408  23.730  28.783  1.00  7.54           C  
HETATM 2501  CHC HEM A 345      18.627  26.909  30.309  1.00  9.11           C  
HETATM 2502  CHD HEM A 345      21.590  23.302  31.404  1.00  6.41           C  
HETATM 2503  C1A HEM A 345      17.548  20.954  28.765  1.00  7.01           C  
HETATM 2504  C2A HEM A 345      16.315  20.316  28.416  1.00  7.86           C  
HETATM 2505  C3A HEM A 345      15.350  21.265  28.432  1.00  6.81           C  
HETATM 2506  C4A HEM A 345      16.012  22.487  28.802  1.00  7.64           C  
HETATM 2507  CMA HEM A 345      13.880  21.123  28.096  1.00  6.42           C  
HETATM 2508  CAA HEM A 345      16.161  18.835  28.137  1.00  7.79           C  
HETATM 2509  CBA HEM A 345      16.001  18.004  29.413  1.00  8.29           C  
HETATM 2510  CGA HEM A 345      15.603  16.579  29.112  1.00 10.31           C  
HETATM 2511  O1A HEM A 345      16.326  15.681  29.496  1.00  8.80           O  
HETATM 2512  O2A HEM A 345      14.571  16.327  28.477  1.00 11.86           O  
HETATM 2513  C1B HEM A 345      16.043  24.932  29.001  1.00  7.81           C  
HETATM 2514  C2B HEM A 345      15.421  26.236  28.829  1.00  8.83           C  
HETATM 2515  C3B HEM A 345      16.325  27.159  29.225  1.00 10.39           C  
HETATM 2516  C4B HEM A 345      17.533  26.393  29.606  1.00  9.45           C  
HETATM 2517  CMB HEM A 345      14.024  26.530  28.286  1.00  8.12           C  
HETATM 2518  CAB HEM A 345      16.010  28.518  29.403  1.00 11.13           C  
HETATM 2519  CBB HEM A 345      16.873  29.651  29.187  1.00 15.22           C  
HETATM 2520  C1C HEM A 345      19.646  26.185  30.877  1.00  8.10           C  
HETATM 2521  C2C HEM A 345      20.641  26.746  31.767  1.00  8.91           C  
HETATM 2522  C3C HEM A 345      21.428  25.707  32.174  1.00  7.71           C  
HETATM 2523  C4C HEM A 345      20.947  24.538  31.440  1.00  8.49           C  
HETATM 2524  CMC HEM A 345      20.725  28.216  32.160  1.00  7.93           C  
HETATM 2525  CAC HEM A 345      22.330  25.637  33.233  1.00 10.22           C  
HETATM 2526  CBC HEM A 345      23.431  26.540  33.517  1.00 13.87           C  
HETATM 2527  C1D HEM A 345      21.142  22.174  30.716  1.00  7.14           C  
HETATM 2528  C2D HEM A 345      21.874  20.942  30.577  1.00  6.63           C  
HETATM 2529  C3D HEM A 345      21.050  20.101  29.922  1.00  6.99           C  
HETATM 2530  C4D HEM A 345      19.851  20.818  29.613  1.00  6.80           C  
HETATM 2531  CMD HEM A 345      23.318  20.684  30.960  1.00  5.55           C  
HETATM 2532  CAD HEM A 345      21.320  18.661  29.537  1.00  5.87           C  
HETATM 2533  CBD HEM A 345      20.865  17.598  30.516  1.00  7.22           C  
HETATM 2534  CGD HEM A 345      21.157  16.197  30.052  1.00  8.66           C  
HETATM 2535  O1D HEM A 345      20.679  15.275  30.675  1.00  9.87           O  
HETATM 2536  O2D HEM A 345      21.878  16.002  29.079  1.00  8.51           O  
HETATM 2537  NA  HEM A 345      17.344  22.277  29.045  1.00  7.50           N  
HETATM 2538  NB  HEM A 345      17.345  25.034  29.425  1.00  8.04           N  
HETATM 2539  NC  HEM A 345      19.817  24.830  30.721  1.00  7.36           N  
HETATM 2540  ND  HEM A 345      19.925  22.101  30.082  1.00  7.14           N  
HETATM 2541 FE   HEM A 345      18.636  23.554  29.785  1.00  7.96          FE  
HETATM 2542  O   HOH A 350      42.650  17.903  53.436  1.00 32.13           O  
HETATM 2543  O   HOH A 351      30.869  26.946  54.993  1.00 23.76           O  
HETATM 2544  O   HOH A 352      36.181  22.718  56.690  1.00 27.52           O  
HETATM 2545  O   HOH A 353      28.839  10.036  50.532  1.00 30.06           O  
HETATM 2546  O   HOH A 354      29.775  10.807  45.270  1.00 17.67           O  
HETATM 2547  O   HOH A 355      38.797  10.129  40.175  1.00 35.07           O  
HETATM 2548  O   HOH A 356      26.498   8.325  31.710  1.00 21.19           O  
HETATM 2549  O   HOH A 357      22.577  10.265  35.016  1.00 16.41           O  
HETATM 2550  O   HOH A 358      34.546  11.832  30.317  1.00 20.01           O  
HETATM 2551  O   HOH A 359      38.714  15.620  31.547  1.00 34.49           O  
HETATM 2552  O   HOH A 360      21.834  12.809  30.444  1.00 11.29           O  
HETATM 2553  O   HOH A 361      15.025  14.127  31.776  1.00 12.21           O  
HETATM 2554  O   HOH A 362      22.429  25.827  44.905  1.00 15.70           O  
HETATM 2555  O   HOH A 363      13.033  28.049  47.998  1.00 11.35           O  
HETATM 2556  O   HOH A 365      12.879  35.468  48.588  1.00 33.81           O  
HETATM 2557  O   HOH A 366      21.340  25.078  51.564  1.00 17.03           O  
HETATM 2558  O   HOH A 367      12.976  23.494  41.113  1.00 12.35           O  
HETATM 2559  O   HOH A 368      13.320  12.243  45.449  1.00 36.27           O  
HETATM 2560  O   HOH A 369      12.674  13.761  38.507  1.00 11.47           O  
HETATM 2561  O   HOH A 370      18.451  11.497  37.250  1.00 12.37           O  
HETATM 2562  O   HOH A 371      23.026  11.270  37.456  1.00 16.83           O  
HETATM 2563  O   HOH A 373       7.085  23.926  30.589  1.00 55.20           O  
HETATM 2564  O   HOH A 375      12.656  19.622  31.111  1.00 13.43           O  
HETATM 2565  O   HOH A 376       8.970  20.659  30.052  1.00 36.55           O  
HETATM 2566  O   HOH A 378      23.459  18.103  54.246  1.00 16.12           O  
HETATM 2567  O   HOH A 379      27.884  23.910  53.883  1.00 15.71           O  
HETATM 2568  O   HOH A 380      25.080  28.794  39.909  1.00 25.15           O  
HETATM 2569  O   HOH A 381      34.742  24.671  37.298  1.00 13.79           O  
HETATM 2570  O   HOH A 382      39.137  24.972  34.241  1.00 20.48           O  
HETATM 2571  O   HOH A 383      31.611  31.223  38.509  1.00 11.63           O  
HETATM 2572  O   HOH A 384      29.944  30.204  40.420  1.00 15.91           O  
HETATM 2573  O   HOH A 385      29.459  29.257  44.599  1.00 12.21           O  
HETATM 2574  O   HOH A 386      23.055  25.708  57.820  1.00 19.15           O  
HETATM 2575  O   HOH A 387      18.070  23.214  51.776  1.00 15.60           O  
HETATM 2576  O   HOH A 388      13.437  28.710  55.244  1.00 41.08           O  
HETATM 2577  O   HOH A 389      11.954  26.210  40.951  1.00 16.05           O  
HETATM 2578  O   HOH A 390       9.271  26.656  40.028  1.00 11.37           O  
HETATM 2579  O   HOH A 391       9.545  31.568  31.178  1.00 29.28           O  
HETATM 2580  O   HOH A 392      16.025  39.194  30.765  1.00 17.17           O  
HETATM 2581  O   HOH A 393      21.759  40.546  21.589  1.00 13.66           O  
HETATM 2582  O   HOH A 394      18.116  15.397  31.498  1.00 12.72           O  
HETATM 2583  O   HOH A 395      19.121   6.513  22.197  1.00 27.61           O  
HETATM 2584  O   HOH A 396      20.428  22.120  19.433  1.00 10.53           O  
HETATM 2585  O   HOH A 397      18.475  22.954  21.209  1.00 10.22           O  
HETATM 2586  O   HOH A 398      20.675  22.672  16.706  1.00 13.77           O  
HETATM 2587  O   HOH A 399      28.658  14.989  28.625  1.00 11.54           O  
HETATM 2588  O   HOH A 400      21.751  23.231   7.803  1.00 16.26           O  
HETATM 2589  O   HOH A 401       7.884   8.856  10.513  1.00 42.68           O  
HETATM 2590  O   HOH A 402      15.429  18.025  16.818  1.00 11.65           O  
HETATM 2591  O   HOH A 403      14.655  24.542  13.196  1.00 28.20           O  
HETATM 2592  O   HOH A 404       9.747  28.034  22.476  1.00 21.21           O  
HETATM 2593  O   HOH A 405      16.385  27.479  25.762  1.00 12.01           O  
HETATM 2594  O   HOH A 406      22.312  34.975  16.353  1.00 11.01           O  
HETATM 2595  O   HOH A 407      23.035  35.576  13.662  1.00 14.76           O  
HETATM 2596  O   HOH A 408      23.061  37.324  42.482  1.00 20.18           O  
HETATM 2597  O   HOH A 409      41.639  20.569  44.043  1.00 18.32           O  
HETATM 2598  O   HOH A 410      42.096  24.738  31.393  1.00 22.96           O  
HETATM 2599  O   HOH A 411      40.316  25.350  27.077  1.00 23.55           O  
HETATM 2600  O   HOH A 413      41.585  19.471  22.536  1.00 20.83           O  
HETATM 2601  O   HOH A 414      24.299   7.304  26.596  1.00 23.29           O  
HETATM 2602  O   HOH A 416      12.187  17.392  29.582  1.00 19.72           O  
HETATM 2603  O   HOH A 417       9.413  17.899  29.846  1.00 38.44           O  
HETATM 2604  O   HOH A 418      12.276  15.415  31.528  1.00 20.47           O  
HETATM 2605  O   HOH A 419      10.262  13.512  31.832  1.00 41.58           O  
HETATM 2606  O   HOH A 420       8.370  16.396  32.063  1.00 39.57           O  
HETATM 2607  O   HOH A 421       8.153  15.960  28.243  1.00 37.56           O  
HETATM 2608  O   HOH A 422       7.428  15.030  25.866  1.00 30.34           O  
HETATM 2609  O   HOH A 423       7.413  24.732  27.959  1.00 18.26           O  
HETATM 2610  O   HOH A 424      14.030  28.166  45.437  1.00  9.04           O  
HETATM 2611  O   HOH A 425      14.466  25.315  43.660  1.00 11.30           O  
HETATM 2612  O   HOH A 426      44.058  24.585  47.266  1.00 25.90           O  
HETATM 2613  O   HOH A 427      30.615  31.548  55.545  1.00 36.15           O  
HETATM 2614  O   HOH A 428      32.556  24.811  54.743  1.00 39.93           O  
HETATM 2615  O   HOH A 429      30.110  23.049  55.226  1.00 34.81           O  
HETATM 2616  O   HOH A 430      34.198  14.470  55.491  1.00 37.56           O  
HETATM 2617  O   HOH A 431      32.374  13.658  58.577  1.00 42.78           O  
HETATM 2618  O   HOH A 433      36.253  11.530  50.559  1.00 31.66           O  
HETATM 2619  O   HOH A 434      38.930  12.042  51.399  1.00 39.66           O  
HETATM 2620  O   HOH A 435      25.469   9.135  46.761  1.00 26.00           O  
HETATM 2621  O   HOH A 436      28.008   6.727  43.647  1.00 41.93           O  
HETATM 2622  O   HOH A 437      39.089  17.959  37.066  1.00 32.23           O  
HETATM 2623  O   HOH A 438      42.963  16.347  37.912  1.00 40.30           O  
HETATM 2624  O   HOH A 439      39.110  15.701  35.755  1.00 34.67           O  
HETATM 2625  O   HOH A 440      40.315  14.151  38.917  1.00 31.22           O  
HETATM 2626  O   HOH A 441      26.523   8.812  39.288  1.00 31.46           O  
HETATM 2627  O   HOH A 442      25.090   7.202  37.570  1.00 33.42           O  
HETATM 2628  O   HOH A 443      23.845   7.819  34.868  1.00 20.92           O  
HETATM 2629  O   HOH A 444      29.845   9.673  34.941  1.00 25.06           O  
HETATM 2630  O   HOH A 445      29.966  12.415  34.915  1.00 23.39           O  
HETATM 2631  O   HOH A 446      35.607  13.889  28.626  1.00 37.12           O  
HETATM 2632  O   HOH A 447      33.507   9.528  28.383  1.00 34.21           O  
HETATM 2633  O   HOH A 448       5.173  42.188  41.859  1.00 36.29           O  
HETATM 2634  O   HOH A 449      12.687  37.546  46.304  1.00 32.76           O  
HETATM 2635  O   HOH A 450      10.248  36.023  49.370  1.00 26.70           O  
HETATM 2636  O   HOH A 451      10.843  42.364  45.733  1.00 30.66           O  
HETATM 2637  O   HOH A 452      -0.414  38.622  49.223  1.00 42.00           O  
HETATM 2638  O   HOH A 453       4.365  31.919  46.738  1.00 24.93           O  
HETATM 2639  O   HOH A 454      14.334  29.076  51.155  1.00 16.73           O  
HETATM 2640  O   HOH A 455      17.760  32.437  50.496  1.00 19.52           O  
HETATM 2641  O   HOH A 456      11.106  12.988  47.066  1.00 45.15           O  
HETATM 2642  O   HOH A 457       9.702  12.318  44.826  1.00 43.53           O  
HETATM 2643  O   HOH A 458       3.172  14.645  43.402  1.00 33.91           O  
HETATM 2644  O   HOH A 459      10.034  13.826  38.891  1.00 28.13           O  
HETATM 2645  O   HOH A 460       3.093  19.619  39.707  1.00 28.69           O  
HETATM 2646  O   HOH A 461       8.266  23.402  35.756  1.00 20.18           O  
HETATM 2647  O   HOH A 462       5.495  24.581  38.063  1.00 21.98           O  
HETATM 2648  O   HOH A 463      12.652  10.591  37.427  1.00 32.95           O  
HETATM 2649  O   HOH A 464      10.787  12.000  36.184  1.00 45.82           O  
HETATM 2650  O   HOH A 465      16.007  10.173  37.745  1.00 30.60           O  
HETATM 2651  O   HOH A 466      20.055   7.297  36.807  1.00 23.83           O  
HETATM 2652  O   HOH A 467      22.005   7.253  38.630  1.00 24.44           O  
HETATM 2653  O   HOH A 468      13.713   7.376  39.021  1.00 36.70           O  
HETATM 2654  O   HOH A 469      16.919   4.163  39.355  1.00 14.06           O  
HETATM 2655  O   HOH A 470      16.002   7.319  43.005  1.00 30.34           O  
HETATM 2656  O   HOH A 471      20.453   7.442  43.359  1.00 25.08           O  
HETATM 2657  O   HOH A 472      24.703   4.190  44.882  1.00 42.58           O  
HETATM 2658  O   HOH A 473      19.521   9.414  49.029  1.00 23.73           O  
HETATM 2659  O   HOH A 474      24.458  15.729  58.325  1.00 45.51           O  
HETATM 2660  O   HOH A 475      22.281  16.479  59.757  1.00 34.08           O  
HETATM 2661  O   HOH A 476      22.163  16.456  62.510  1.00 30.73           O  
HETATM 2662  O   HOH A 477      32.231  12.067  56.217  1.00 49.12           O  
HETATM 2663  O   HOH A 478      29.668  18.793  59.021  1.00 46.27           O  
HETATM 2664  O   HOH A 479      27.852  22.012  58.274  1.00 35.71           O  
HETATM 2665  O   HOH A 480      28.311  27.795  40.406  1.00 30.56           O  
HETATM 2666  O   HOH A 481      30.016  27.260  42.632  1.00 17.93           O  
HETATM 2667  O   HOH A 482      39.057  18.311  32.310  1.00 21.75           O  
HETATM 2668  O   HOH A 483      39.658  24.789  30.127  1.00 20.16           O  
HETATM 2669  O   HOH A 484      37.435  31.477  29.155  1.00 32.32           O  
HETATM 2670  O   HOH A 485      37.463  23.955  36.142  1.00 17.44           O  
HETATM 2671  O   HOH A 486      39.677  27.924  31.452  1.00 45.65           O  
HETATM 2672  O   HOH A 487      38.180  30.394  34.487  1.00 35.42           O  
HETATM 2673  O   HOH A 488      40.286  28.774  34.019  1.00 50.18           O  
HETATM 2674  O   HOH A 489      41.742  30.515  36.819  1.00 42.94           O  
HETATM 2675  O   HOH A 490      37.668  28.167  41.048  1.00 18.04           O  
HETATM 2676  O   HOH A 491      38.254  30.440  39.798  1.00 29.66           O  
HETATM 2677  O   HOH A 492      29.901  31.488  43.026  1.00 21.35           O  
HETATM 2678  O   HOH A 493      26.212  25.934  55.392  1.00 36.22           O  
HETATM 2679  O   HOH A 494      23.027  31.721  54.552  1.00 19.07           O  
HETATM 2680  O   HOH A 495      24.011  34.955  52.566  1.00 38.09           O  
HETATM 2681  O   HOH A 496      18.976  28.554  52.489  1.00 16.72           O  
HETATM 2682  O   HOH A 497      13.769  21.932  55.307  1.00 36.64           O  
HETATM 2683  O   HOH A 498       6.766  28.757  52.050  1.00 55.10           O  
HETATM 2684  O   HOH A 499       5.450  25.231  46.160  1.00 29.28           O  
HETATM 2685  O   HOH A 500       3.666  23.603  44.634  1.00 36.64           O  
HETATM 2686  O   HOH A 501       5.153  31.373  26.626  1.00 19.47           O  
HETATM 2687  O   HOH A 502       9.231  33.937  20.893  1.00 16.46           O  
HETATM 2688  O   HOH A 503       8.382  36.336  22.065  1.00 21.22           O  
HETATM 2689  O   HOH A 504       7.531  34.618  32.394  1.00 33.47           O  
HETATM 2690  O   HOH A 505       5.385  37.169  28.603  1.00 40.61           O  
HETATM 2691  O   HOH A 506      11.052  44.308  24.704  1.00 41.57           O  
HETATM 2692  O   HOH A 507       8.427  35.954  36.996  1.00 14.71           O  
HETATM 2693  O   HOH A 508      14.569  41.421  29.843  1.00 25.28           O  
HETATM 2694  O   HOH A 509      10.960  41.837  39.519  1.00 19.63           O  
HETATM 2695  O   HOH A 510       9.776  43.005  41.597  1.00 17.03           O  
HETATM 2696  O   HOH A 511      21.057  42.618  27.821  1.00 20.82           O  
HETATM 2697  O   HOH A 512      20.987  39.839  24.144  1.00 18.02           O  
HETATM 2698  O   HOH A 513      27.170  38.698  34.246  1.00 25.80           O  
HETATM 2699  O   HOH A 514      27.854  37.317  31.760  1.00 11.48           O  
HETATM 2700  O   HOH A 515      25.685  19.588  23.759  1.00 10.49           O  
HETATM 2701  O   HOH A 516      15.256  10.134  32.040  1.00 25.56           O  
HETATM 2702  O   HOH A 517      13.314  11.972  31.219  1.00 25.96           O  
HETATM 2703  O   HOH A 518       8.249  11.185  28.607  1.00 47.02           O  
HETATM 2704  O   HOH A 519      10.362   5.220  23.693  1.00 44.67           O  
HETATM 2705  O   HOH A 520      16.440   5.628  22.160  1.00 36.42           O  
HETATM 2706  O   HOH A 521      23.469   5.111  31.353  1.00 25.60           O  
HETATM 2707  O   HOH A 522      21.957   6.212  33.321  1.00 18.73           O  
HETATM 2708  O   HOH A 523      19.981   9.732  35.491  1.00 21.07           O  
HETATM 2709  O   HOH A 524      19.704   5.602  34.510  1.00 19.88           O  
HETATM 2710  O   HOH A 525      18.008   6.680  32.647  1.00 24.50           O  
HETATM 2711  O   HOH A 526      31.956  15.482  22.744  1.00 12.28           O  
HETATM 2712  O   HOH A 527      36.521  25.408  24.799  1.00 16.41           O  
HETATM 2713  O   HOH A 528      35.486  21.813  19.969  1.00 14.39           O  
HETATM 2714  O   HOH A 529      36.118  24.574  19.802  1.00 17.76           O  
HETATM 2715  O   HOH A 530      33.642  25.486  19.120  1.00 12.09           O  
HETATM 2716  O   HOH A 531      35.197  22.187  17.273  1.00 25.21           O  
HETATM 2717  O   HOH A 532      15.712  26.639  10.617  1.00 31.41           O  
HETATM 2718  O   HOH A 533       7.949   7.639  18.222  1.00 36.43           O  
HETATM 2719  O   HOH A 534       9.693   9.870  18.433  1.00 30.90           O  
HETATM 2720  O   HOH A 535      12.558  13.927  15.522  1.00 13.88           O  
HETATM 2721  O   HOH A 536       5.748  14.391  14.454  1.00 29.63           O  
HETATM 2722  O   HOH A 537      11.494  23.075  12.695  1.00 30.64           O  
HETATM 2723  O   HOH A 538      21.646  20.508   7.342  1.00 16.47           O  
HETATM 2724  O   HOH A 540       7.928  25.589  14.090  1.00 37.23           O  
HETATM 2725  O   HOH A 541      13.055  34.097  17.180  1.00 16.76           O  
HETATM 2726  O   HOH A 542      10.999  35.000  18.917  1.00 19.94           O  
HETATM 2727  O   HOH A 544      12.839  36.381  15.535  1.00 39.46           O  
HETATM 2728  O   HOH A 546      32.564  33.661  21.208  1.00 38.52           O  
HETATM 2729  O   HOH A 547      38.154  30.042  20.232  1.00 25.95           O  
HETATM 2730  O   HOH A 549      34.410  36.254  33.939  1.00 35.75           O  
HETATM 2731  O   HOH A 550      29.429  37.843  38.265  1.00 20.66           O  
HETATM 2732  O   HOH A 551      33.573  35.602  36.480  1.00 33.49           O  
HETATM 2733  O   HOH A 552      35.461  43.050  36.978  1.00 38.58           O  
HETATM 2734  O   HOH A 553      34.924  40.987  38.715  1.00 49.21           O  
HETATM 2735  O   HOH A 554      28.112  36.999  42.266  1.00 31.41           O  
HETATM 2736  O   HOH A 555      25.873  38.840  42.768  1.00 34.98           O  
HETATM 2737  O   HOH A 556      22.506  37.804  45.193  1.00 29.54           O  
HETATM 2738  O   HOH A 557      19.609  37.730  45.345  1.00 29.52           O  
HETATM 2739  O   HOH A 558      25.143  38.893  46.432  1.00 23.04           O  
HETATM 2740  O   HOH A 559      32.826  36.616  49.858  1.00 37.27           O  
HETATM 2741  O   HOH A 560      29.187  42.262  54.412  1.00 35.96           O  
HETATM 2742  O   HOH A 561      40.529  30.187  58.760  1.00 33.56           O  
HETATM 2743  O   HOH A 562      32.317  36.969  55.017  1.00 48.20           O  
HETATM 2744  O   HOH A 563      39.310  33.369  54.007  1.00 44.33           O  
HETATM 2745  O   HOH A 564      36.536  34.438  51.584  1.00 43.98           O  
HETATM 2746  O   HOH A 565      38.878  32.601  51.425  1.00 32.06           O  
HETATM 2747  O   HOH A 566      38.550  19.406  21.351  1.00 29.86           O  
HETATM 2748  O   HOH A 567      43.218  28.593  27.460  1.00 47.45           O  
HETATM 2749  O   HOH A 568      48.032  27.899  27.322  1.00 49.93           O  
HETATM 2750  O   HOH A 569      37.674  22.331  14.860  1.00 34.60           O  
HETATM 2751  O   HOH A 570      41.509  17.392  14.907  1.00 37.97           O  
HETATM 2752  O   HOH A 571      37.260  28.812  13.372  1.00 26.08           O  
HETATM 2753  O   HOH A 572      31.692  22.592   7.021  1.00 21.69           O  
HETATM 2754  O   HOH A 573      19.376  27.732  -0.304  1.00 44.21           O  
HETATM 2755  O   HOH A 574      21.979  19.691   4.684  1.00 39.60           O  
HETATM 2756  O   HOH A 575      20.783  39.442   9.476  1.00 30.79           O  
HETATM 2757  O   HOH A 576      16.371  34.971  11.426  1.00 38.11           O  
HETATM 2758  O   HOH A 577      31.730  39.488  13.561  1.00 38.53           O  
HETATM 2759  O   HOH A 578      23.686  32.969   5.252  1.00 40.97           O  
HETATM 2760  O   HOH A 580      32.994  30.620   6.891  1.00 37.36           O  
HETATM 2761  O   HOH A 583      21.725  11.008  18.892  1.00 21.34           O  
HETATM 2762  O   HOH A 584      28.864  11.460  17.412  1.00 20.33           O  
HETATM 2763  O   HOH A 585      27.628  12.498  20.769  1.00 23.94           O  
HETATM 2764  O   HOH A 586      29.084   8.694  15.684  1.00 45.65           O  
HETATM 2765  O   HOH A 589      32.640  16.097  57.309  1.00 37.64           O  
HETATM 2766  O   HOH A 590      27.483   9.202  44.948  1.00 34.50           O  
HETATM 2767  O   HOH A 591       7.223  13.182  41.423  1.00 51.27           O  
HETATM 2768  O   HOH A 594      16.583  42.255  34.909  1.00 28.88           O  
HETATM 2769  O   HOH A 595      19.133   9.146  32.759  1.00 22.95           O  
HETATM 2770  O   HOH A 596      39.634  26.722  21.196  1.00 45.71           O  
HETATM 2771  O   HOH A 597      45.390  26.953  27.170  1.00 37.79           O  
HETATM 2772  O   HOH A 598      24.558  12.315   8.294  1.00 51.44           O  
HETATM 2773  O   HOH A 599      37.540  10.978  31.971  1.00 38.62           O  
HETATM 2774  O   HOH A 600      31.562  29.158   4.886  1.00 36.48           O  
HETATM 2775  O   HOH A 601      21.488  34.357   6.311  1.00 36.56           O  
HETATM 2776  O   HOH A 602      18.637  31.181  52.839  1.00 31.82           O  
HETATM 2777  O   HOH A 603      20.432  32.375  54.426  1.00 44.92           O  
HETATM 2778  O   HOH A 604      23.984   7.076  45.682  1.00 49.25           O  
HETATM 2779  O   HOH A 605      18.704   5.735  42.087  1.00 33.40           O  
HETATM 2780  O   HOH A 606      16.539  38.909  14.443  1.00 35.35           O  
HETATM 2781  O   HOH A 607      16.053  35.032  50.051  1.00 46.12           O  
HETATM 2782  O   HOH A 608      23.859  35.589  55.910  1.00 42.30           O  
HETATM 2783  O   HOH A 609       6.814  27.639  49.513  1.00 29.90           O  
HETATM 2784  O   HOH A 610      21.541  39.256  41.219  1.00 36.87           O  
HETATM 2785  O   HOH A 611      12.148   4.055  22.020  1.00 32.79           O  
HETATM 2786  O   HOH A 612      11.934  40.311  19.077  1.00 39.76           O  
HETATM 2787  O   HOH A 613      32.406  36.716  41.024  1.00 28.11           O  
HETATM 2788  O   HOH A 614      30.112  38.897  31.376  1.00 33.88           O  
HETATM 2789  O   HOH A 615      31.453  40.953  46.658  1.00 38.18           O  
HETATM 2790  O   HOH A 616      28.476  41.944  45.892  1.00 41.23           O  
HETATM 2791  O   HOH A 617      23.448  41.916  38.893  1.00 36.48           O  
HETATM 2792  O   HOH A 618      18.577  38.924  41.645  1.00 32.48           O  
HETATM 2793  O   HOH A 619      25.653  41.365  40.433  1.00 45.53           O  
HETATM 2794  O   HOH A 620      38.378  26.959  26.273  1.00 33.76           O  
HETATM 2795  O   HOH A 621      35.364  28.419  27.651  1.00 25.66           O  
HETATM 2796  O   HOH A 622      37.520  28.716  29.292  1.00 38.42           O  
HETATM 2797  O   HOH A 623      39.369  30.953  22.475  1.00 28.86           O  
HETATM 2798  O   HOH A 624      34.580  14.837  22.657  1.00 44.79           O  
HETATM 2799  O   HOH A 625      34.547  19.440  16.983  1.00 39.83           O  
HETATM 2800  O   HOH A 626      32.190  18.620  15.796  1.00 34.55           O  
HETATM 2801  O   HOH A 627      32.007  16.010  16.908  1.00 41.30           O  
HETATM 2802  O   HOH A 628      32.945  19.073  12.980  1.00 43.05           O  
HETATM 2803  O   HOH A 629      31.004  17.263  13.554  1.00 40.03           O  
HETATM 2804  O   HOH A 630      41.059  19.993  13.567  1.00 42.70           O  
HETATM 2805  O   HOH A 631      23.466  30.160  -0.492  1.00 49.30           O  
HETATM 2806  O   HOH A 633      21.831  28.849   1.258  1.00 47.19           O  
HETATM 2807  O   HOH A 634      17.637  16.428   5.744  1.00 46.72           O  
HETATM 2808  O   HOH A 635      20.097  17.645   4.523  1.00 41.57           O  
HETATM 2809  O   HOH A 636      29.403  12.246  14.551  1.00 47.92           O  
HETATM 2810  O   HOH A 637      18.956  10.869  13.799  1.00 25.58           O  
HETATM 2811  O   HOH A 638      26.468   6.993  15.008  1.00 32.15           O  
HETATM 2812  O   HOH A 639      40.270  18.049  54.621  1.00 33.42           O  
HETATM 2813  O   HOH A 640      14.922  20.964  32.190  1.00 11.65           O  
HETATM 2814  O   HOH A 641      11.180  17.788  32.892  1.00 14.41           O  
HETATM 2815  O   HOH A 642       7.015  35.504  39.368  1.00 27.43           O  
HETATM 2816  O   HOH A 643       8.345  25.257  37.717  1.00 29.02           O  
HETATM 2817  O   HOH A 644      27.260   8.685  48.804  1.00 29.78           O  
HETATM 2818  O   HOH A 645      27.346  40.358  55.127  1.00 38.28           O  
HETATM 2819  O   HOH A 646      27.421   7.186  23.312  1.00 32.24           O  
HETATM 2820  O   HOH A 647       7.193  32.565  19.503  1.00 29.62           O  
HETATM 2821  O   HOH A 648      23.687  43.013  32.387  1.00 36.03           O  
HETATM 2822  O   HOH A 649      32.211  36.952  38.384  1.00 34.07           O  
HETATM 2823  O   HOH A 650      24.389  17.948   3.331  1.00 36.67           O  
HETATM 2824  O   HOH A 651      19.836  15.469   6.998  1.00 34.44           O  
HETATM 2825  O   HOH A 652      14.026  23.198   5.952  1.00 36.63           O  
HETATM 2826  O   HOH A 653      13.702  41.938  39.780  1.00 29.41           O  
HETATM 2827  O   HOH A 654       7.169  43.901  41.200  1.00 29.45           O  
HETATM 2828  O   HOH A 655      10.895  42.511  36.928  1.00 34.44           O  
HETATM 2829  O   HOH A 656      35.661  15.058  26.000  1.00 30.52           O  
HETATM 2830  O   HOH A 657      36.372  19.022  19.824  1.00 33.61           O  
HETATM 2831  O   HOH A 658      31.079  12.891  23.088  1.00 35.10           O  
HETATM 2832  O   HOH A 659      32.868   9.315  25.316  1.00 38.43           O  
HETATM 2833  O   HOH A 660      17.745  18.686   3.398  1.00 35.53           O  
HETATM 2834  O   HOH A 661      13.988  24.986   9.119  1.00 39.10           O  
HETATM 2835  O   HOH A 662      32.536  40.293  53.228  1.00 29.96           O  
HETATM 2836  O   HOH A 663      33.704  39.103  51.076  1.00 40.65           O  
HETATM 2837  O   HOH A 664      39.914  16.391  40.372  1.00 32.08           O  
HETATM 2838  O   HOH A 665      38.957  13.935  33.797  1.00 31.86           O  
HETATM 2839  O   HOH A 666      41.148  12.364  34.300  1.00 34.10           O  
HETATM 2840  O   HOH A 667       4.900  33.505  39.518  1.00 31.22           O  
HETATM 2841  O   HOH A 668       8.359  24.784  33.372  1.00 33.00           O  
HETATM 2842  O   HOH A 669      24.119  10.135  39.540  1.00 34.43           O  
HETATM 2843  O   HOH A 670      20.331   9.523  51.844  1.00 33.87           O  
HETATM 2844  O   HOH A 671      23.612   9.111  53.564  1.00 36.70           O  
HETATM 2845  O   HOH A 672       9.400  22.844  31.565  1.00 29.98           O  
HETATM 2846  O   HOH A 673      13.062   9.662  29.450  1.00 34.60           O  
HETATM 2847  O   HOH A 674      39.599  34.994  21.994  1.00 38.14           O  
CONECT   26  104                                                                
CONECT   98 2116                                                                
CONECT  104   26                                                                
CONECT  264  877                                                                
CONECT  380 2497                                                                
CONECT  383 2497                                                                
CONECT  495 2497                                                                
CONECT  507 2497                                                                
CONECT  518 2497                                                                
CONECT  877  264                                                                
CONECT  984 2467                                                                
CONECT 1273 2541                                                                
CONECT 1277 2498                                                                
CONECT 1279 2498                                                                
CONECT 1405 2498                                                                
CONECT 1406 2498                                                                
CONECT 1416 2498                                                                
CONECT 1418 2498                                                                
CONECT 1439 2498                                                                
CONECT 1460 2498                                                                
CONECT 1833 2313                                                                
CONECT 2116   98                                                                
CONECT 2313 1833                                                                
CONECT 2467  984 2468 2478                                                      
CONECT 2468 2467 2469 2475                                                      
CONECT 2469 2468 2470 2476                                                      
CONECT 2470 2469 2471 2477                                                      
CONECT 2471 2470 2472 2478                                                      
CONECT 2472 2471 2479                                                           
CONECT 2473 2474 2475 2480                                                      
CONECT 2474 2473                                                                
CONECT 2475 2468 2473                                                           
CONECT 2476 2469                                                                
CONECT 2477 2470 2481                                                           
CONECT 2478 2467 2471                                                           
CONECT 2479 2472                                                                
CONECT 2480 2473                                                                
CONECT 2481 2477 2482 2492                                                      
CONECT 2482 2481 2483 2489                                                      
CONECT 2483 2482 2484 2490                                                      
CONECT 2484 2483 2485 2491                                                      
CONECT 2485 2484 2486 2492                                                      
CONECT 2486 2485 2493                                                           
CONECT 2487 2488 2489 2494                                                      
CONECT 2488 2487                                                                
CONECT 2489 2482 2487                                                           
CONECT 2490 2483                                                                
CONECT 2491 2484                                                                
CONECT 2492 2481 2485                                                           
CONECT 2493 2486                                                                
CONECT 2494 2487                                                                
CONECT 2495 2496 2541                                                           
CONECT 2496 2495 2541                                                           
CONECT 2497  380  383  495  507                                                 
CONECT 2497  518 2610 2611                                                      
CONECT 2498 1277 1279 1405 1406                                                 
CONECT 2498 1416 1418 1439 1460                                                 
CONECT 2499 2503 2530                                                           
CONECT 2500 2506 2513                                                           
CONECT 2501 2516 2520                                                           
CONECT 2502 2523 2527                                                           
CONECT 2503 2499 2504 2537                                                      
CONECT 2504 2503 2505 2508                                                      
CONECT 2505 2504 2506 2507                                                      
CONECT 2506 2500 2505 2537                                                      
CONECT 2507 2505                                                                
CONECT 2508 2504 2509                                                           
CONECT 2509 2508 2510                                                           
CONECT 2510 2509 2511 2512                                                      
CONECT 2511 2510                                                                
CONECT 2512 2510                                                                
CONECT 2513 2500 2514 2538                                                      
CONECT 2514 2513 2515 2517                                                      
CONECT 2515 2514 2516 2518                                                      
CONECT 2516 2501 2515 2538                                                      
CONECT 2517 2514                                                                
CONECT 2518 2515 2519                                                           
CONECT 2519 2518                                                                
CONECT 2520 2501 2521 2539                                                      
CONECT 2521 2520 2522 2524                                                      
CONECT 2522 2521 2523 2525                                                      
CONECT 2523 2502 2522 2539                                                      
CONECT 2524 2521                                                                
CONECT 2525 2522 2526                                                           
CONECT 2526 2525                                                                
CONECT 2527 2502 2528 2540                                                      
CONECT 2528 2527 2529 2531                                                      
CONECT 2529 2528 2530 2532                                                      
CONECT 2530 2499 2529 2540                                                      
CONECT 2531 2528                                                                
CONECT 2532 2529 2533                                                           
CONECT 2533 2532 2534                                                           
CONECT 2534 2533 2535 2536                                                      
CONECT 2535 2534                                                                
CONECT 2536 2534                                                                
CONECT 2537 2503 2506 2541                                                      
CONECT 2538 2513 2516 2541                                                      
CONECT 2539 2520 2523 2541                                                      
CONECT 2540 2527 2530 2541                                                      
CONECT 2541 1273 2495 2496 2537                                                 
CONECT 2541 2538 2539 2540                                                      
CONECT 2610 2497                                                                
CONECT 2611 2497                                                                
MASTER      378    0    6   12    8    0    5    6 2846    1  103   27          
END                                                                             
