HEADER    OXIDOREDUCTASE                          10-SEP-07   2VBD              
TITLE     ISOPENICILLIN N SYNTHASE WITH SUBSTRATE ANALOGUE L,L,L-ACOMP          
TITLE    2 (UNEXPOSED)                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ISOPENICILLIN N SYNTHETASE;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: IPNS, ISOPENICILLIN N SYNTHASE;                             
COMPND   5 EC: 1.21.3.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: EMERICELLA NIDULANS;                            
SOURCE   3 ORGANISM_COMMON: ASPERGILLUS NIDULANS;                               
SOURCE   4 ORGANISM_TAXID: 162425;                                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: NM554;                                     
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PJB703                                    
KEYWDS    ANTIBIOTIC BIOSYNTHESIS, PENICILLIN BIOSYNTHESIS, IRON, OXYGENASE,    
KEYWDS   2 VITAMIN C, METAL-BINDING, MONOCYCLIC INTERMEDIATE, OXIDOREDUCTASE,   
KEYWDS   3 B-LACTAM ANTIBIOTIC                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.GE,I.J.CLIFTON,R.M.ADLINGTON,J.E.BALDWIN,P.J.RUTLEDGE               
REVDAT   5   13-DEC-23 2VBD    1       REMARK LINK                              
REVDAT   4   30-JAN-13 2VBD    1       JRNL                                     
REVDAT   3   10-OCT-12 2VBD    1       JRNL   REMARK VERSN  FORMUL              
REVDAT   2   24-FEB-09 2VBD    1       VERSN                                    
REVDAT   1   23-SEP-08 2VBD    0                                                
JRNL        AUTH   W.GE,I.J.CLIFTON,J.E.STOK,R.M.ADLINGTON,J.E.BALDWIN,         
JRNL        AUTH 2 P.J.RUTLEDGE                                                 
JRNL        TITL   THE CRYSTAL STRUCTURE OF AN LLL-CONFIGURED DEPSIPEPTIDE      
JRNL        TITL 2 SUBSTRATE ANALOGUE BOUND TO ISOPENICILLIN N SYNTHASE.        
JRNL        REF    ORG.BIOMOL.CHEM.              V.   8   122 2010              
JRNL        REFN                   ISSN 1477-0520                               
JRNL        PMID   20024142                                                     
JRNL        DOI    10.1039/B910170E                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 58.22                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 22198                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 909                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1500                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 73                           
REMARK   3   BIN FREE R VALUE                    : 0.2710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2645                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 213                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.57                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.35000                                             
REMARK   3    B22 (A**2) : 0.63000                                              
REMARK   3    B33 (A**2) : -0.28000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.177         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.158         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.099         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.448         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2743 ; 0.024 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1831 ; 0.012 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3732 ; 1.798 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4460 ; 1.097 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   328 ; 6.752 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   141 ;34.496 ;24.681       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   428 ;13.755 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ; 8.975 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   390 ; 0.116 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3091 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   561 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   545 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1864 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1346 ; 0.184 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1332 ; 0.090 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   170 ; 0.150 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    11 ; 0.157 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    54 ; 0.253 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.112 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2107 ; 1.410 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2668 ; 1.728 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1304 ; 3.095 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1064 ; 4.281 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2VBD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-SEP-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290033733.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23160                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.990                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.170                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1BK0                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M LITHIUM SULPHATE, 76MM TRIS/HCL,    
REMARK 280  PH 8.5, 2.0MM FERROUS SULPHATE, 2.6MG/ML TRIPEPTIDE, 25MG/ML IPNS   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       23.26850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.32550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.65700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.32550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.26850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.65700            
REMARK 290   SMTRY3   4  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A   167     OD1  ASN A   169              1.92            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 167   CD    GLU A 167   OE2     0.066                       
REMARK 500    TYR A 224   CD1   TYR A 224   CE1     0.109                       
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    ARG A  27   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A  27   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP A 131   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A 173   CG  -  CD  -  NE  ANGL. DEV. = -13.5 DEGREES          
REMARK 500    ARG A 173   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  38     -115.76    -97.87                                   
REMARK 500    HIS A  82       56.81   -104.52                                   
REMARK 500    LYS A  97      -41.01   -135.76                                   
REMARK 500    THR A 123      -10.77     79.94                                   
REMARK 500    ASP A 179       -1.90   -140.01                                   
REMARK 500    ASN A 230      -31.29   -156.17                                   
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                             FE2 A1332  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 214   NE2                                                    
REMARK 620 2 ASP A 216   OD1  92.5                                              
REMARK 620 3 HIS A 270   NE2  83.4  85.9                                        
REMARK 620 4 V10 A1333   SAI  94.6  88.8 174.3                                  
REMARK 620 5 HOH A2149   O   171.6  86.1  88.2  93.7                            
REMARK 620 6 HOH A2212   O    92.2 175.2  93.8  91.6  89.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 1332                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE V10 A 1333                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HB1   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ANAEROBIC ACOV   
REMARK 900 FE COMPLEX)                                                          
REMARK 900 RELATED ID: 1IPS   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE        
REMARK 900 COMPLEX)                                                             
REMARK 900 RELATED ID: 1OC1   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL -AMINOBUTYRATE-FE    
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 1W04   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL -GLYCINE-FE-NO       
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 1W05   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL -ALANINE-FE COMPLEX  
REMARK 900 RELATED ID: 1W3V   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE D-(L-A-AMINOADIPOYL )-(3R)-METHYL-L-        
REMARK 900 CYSTEINE D-A- HYDROXYISOVALERYL ESTER COMPLEX (ANAEROBIC)            
REMARK 900 RELATED ID: 2BJS   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE C-TERMINAL TRUNCATION MUTANT                
REMARK 900 RELATED ID: 2JB4   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE WITH A 2- THIABICYCLOHEPTAN-6-ONE PRODUCT   
REMARK 900 ANALOGUE                                                             
REMARK 900 RELATED ID: 2VAU   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE WITH SUBSTRATE ANALOGUE ACOMP (UNEXPOSED)   
REMARK 900 RELATED ID: 1BK0   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ACV-FE COMPLEX)  
REMARK 900 RELATED ID: 1BLZ   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ACV-FE-NO        
REMARK 900 COMPLEX)                                                             
REMARK 900 RELATED ID: 1HB2   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (OXYGEN EXPOSED   
REMARK 900 PRODUCT FROM ANAEROBIC ACOV FE COMPLEX)                              
REMARK 900 RELATED ID: 1HB3   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (OXYGEN EXPOSED   
REMARK 900 PRODUCT FROM ANAEROBIC ACOV FE COMPLEX)                              
REMARK 900 RELATED ID: 1HB4   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (OXYGEN EXPOSED   
REMARK 900 PRODUCT FROM ANAEROBIC ACOV FE COMPLEX)                              
REMARK 900 RELATED ID: 1OBN   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL -AMINOBUTYRATE-FE-   
REMARK 900 NO COMPLEX                                                           
REMARK 900 RELATED ID: 1ODM   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ANAEROBIC AC-    
REMARK 900 VINYLGLYCINE FE COMPLEX)                                             
REMARK 900 RELATED ID: 1ODN   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (OXYGEN-EXPOSED   
REMARK 900 PRODUCT FROM ANAEROBIC AC-VINYLGLYCINE FE COMPLEX)                   
REMARK 900 RELATED ID: 1QIQ   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ACMC FE COMPLEX) 
REMARK 900 RELATED ID: 1QJE   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (IPN - FE         
REMARK 900 COMPLEX)                                                             
REMARK 900 RELATED ID: 1QJF   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MONOCYCLIC       
REMARK 900 SULFOXIDE - FE COMPLEX)                                              
REMARK 900 RELATED ID: 1UZW   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE WITH L-D-(A- AMINOADIPOYL)-L-CYSTEINYL-D-   
REMARK 900 ISODEHYDROVALINE                                                     
REMARK 900 RELATED ID: 1W03   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL -GLYCINE-FE COMPLEX  
REMARK 900 RELATED ID: 1W06   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL -ALANINE-FE NO       
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 1W3X   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE D-(L-A-AMINOADIPOYL )-(3R)-METHYL-L-        
REMARK 900 CYSTEINE D-A- HYDROXYISOVALERYL ESTER COMPLEX (OXYGEN EXPOSED 5      
REMARK 900 MINUTES 20 BAR)                                                      
REMARK 900 RELATED ID: 2BU9   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE COMPLEXED WITH L- AMINOADIPOYL-L-CYSTEINYL- 
REMARK 900 L-HEXAFLUOROVALINE                                                   
REMARK 900 RELATED ID: 2IVI   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ANAEROBIC AC-    
REMARK 900 METHYL-CYCLOPROPYLGLYCINE FE COMPLEX)                                
REMARK 900 RELATED ID: 2IVJ   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ANAEROBIC AC-    
REMARK 900 CYCLOPROPYLGLYCINE FE COMPLEX)                                       
REMARK 900 RELATED ID: 2VBB   RELATED DB: PDB                                   
REMARK 900 ISOPENICILLIN N SYNTHASE WITH SUBSTRATE ANALOGUE ACOMP (35MINUTES    
REMARK 900 OXYGEN EXPOSURE)                                                     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUES 1-2 NOT SEEN                                                
DBREF  2VBD A    1   331  UNP    P05326   IPNS_EMENI       1    331             
SEQRES   1 A  331  MET GLY SER VAL SER LYS ALA ASN VAL PRO LYS ILE ASP          
SEQRES   2 A  331  VAL SER PRO LEU PHE GLY ASP ASP GLN ALA ALA LYS MET          
SEQRES   3 A  331  ARG VAL ALA GLN GLN ILE ASP ALA ALA SER ARG ASP THR          
SEQRES   4 A  331  GLY PHE PHE TYR ALA VAL ASN HIS GLY ILE ASN VAL GLN          
SEQRES   5 A  331  ARG LEU SER GLN LYS THR LYS GLU PHE HIS MET SER ILE          
SEQRES   6 A  331  THR PRO GLU GLU LYS TRP ASP LEU ALA ILE ARG ALA TYR          
SEQRES   7 A  331  ASN LYS GLU HIS GLN ASP GLN VAL ARG ALA GLY TYR TYR          
SEQRES   8 A  331  LEU SER ILE PRO GLY LYS LYS ALA VAL GLU SER PHE CYS          
SEQRES   9 A  331  TYR LEU ASN PRO ASN PHE THR PRO ASP HIS PRO ARG ILE          
SEQRES  10 A  331  GLN ALA LYS THR PRO THR HIS GLU VAL ASN VAL TRP PRO          
SEQRES  11 A  331  ASP GLU THR LYS HIS PRO GLY PHE GLN ASP PHE ALA GLU          
SEQRES  12 A  331  GLN TYR TYR TRP ASP VAL PHE GLY LEU SER SER ALA LEU          
SEQRES  13 A  331  LEU LYS GLY TYR ALA LEU ALA LEU GLY LYS GLU GLU ASN          
SEQRES  14 A  331  PHE PHE ALA ARG HIS PHE LYS PRO ASP ASP THR LEU ALA          
SEQRES  15 A  331  SER VAL VAL LEU ILE ARG TYR PRO TYR LEU ASP PRO TYR          
SEQRES  16 A  331  PRO GLU ALA ALA ILE LYS THR ALA ALA ASP GLY THR LYS          
SEQRES  17 A  331  LEU SER PHE GLU TRP HIS GLU ASP VAL SER LEU ILE THR          
SEQRES  18 A  331  VAL LEU TYR GLN SER ASN VAL GLN ASN LEU GLN VAL GLU          
SEQRES  19 A  331  THR ALA ALA GLY TYR GLN ASP ILE GLU ALA ASP ASP THR          
SEQRES  20 A  331  GLY TYR LEU ILE ASN CYS GLY SER TYR MET ALA HIS LEU          
SEQRES  21 A  331  THR ASN ASN TYR TYR LYS ALA PRO ILE HIS ARG VAL LYS          
SEQRES  22 A  331  TRP VAL ASN ALA GLU ARG GLN SER LEU PRO PHE PHE VAL          
SEQRES  23 A  331  ASN LEU GLY TYR ASP SER VAL ILE ASP PRO PHE ASP PRO          
SEQRES  24 A  331  ARG GLU PRO ASN GLY LYS SER ASP ARG GLU PRO LEU SER          
SEQRES  25 A  331  TYR GLY ASP TYR LEU GLN ASN GLY LEU VAL SER LEU ILE          
SEQRES  26 A  331  ASN LYS ASN GLY GLN THR                                      
HET    FE2  A1332       1                                                       
HET    V10  A1333      24                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM     V10 N^6^-[(1R)-2-[(1R)-1-CARBOXY-2-(METHYLSULFANYL)ETHOXY]-          
HETNAM   2 V10  2-OXO-1-(SULFANYLMETHYL)ETHYL]-6-OXO-L-LYSINE                   
FORMUL   2  FE2    FE 2+                                                        
FORMUL   3  V10    C13 H22 N2 O7 S2                                             
FORMUL   4  HOH   *213(H2 O)                                                    
HELIX    1   1 SER A   15  GLY A   19  5                                   5    
HELIX    2   2 ASP A   21  ASP A   38  1                                  18    
HELIX    3   3 ASN A   50  ILE A   65  1                                  16    
HELIX    4   4 THR A   66  LEU A   73  1                                   8    
HELIX    5   5 HIS A  114  ALA A  119  1                                   6    
HELIX    6   6 GLY A  137  LEU A  164  1                                  28    
HELIX    7   7 PHE A  171  PHE A  175  5                                   5    
HELIX    8   8 PRO A  196  ILE A  200  5                                   5    
HELIX    9   9 GLY A  254  THR A  261  1                                   8    
HELIX   10  10 SER A  312  GLY A  329  1                                  18    
SHEET    1  AA 8 LYS A  11  ASP A  13  0                                        
SHEET    2  AA 8 PHE A  41  VAL A  45  1  O  TYR A  43   N  ILE A  12           
SHEET    3  AA 8 TYR A 249  CYS A 253 -1  O  TYR A 249   N  ALA A  44           
SHEET    4  AA 8 ILE A 220  GLN A 225 -1  O  THR A 221   N  ASN A 252           
SHEET    5  AA 8 ARG A 279  VAL A 286 -1  O  LEU A 282   N  TYR A 224           
SHEET    6  AA 8 SER A 183  TYR A 189 -1  O  SER A 183   N  PHE A 285           
SHEET    7  AA 8 GLU A 101  LEU A 106 -1  O  GLU A 101   N  ARG A 188           
SHEET    8  AA 8 GLY A  89  TYR A  91 -1  O  GLY A  89   N  CYS A 104           
SHEET    1  AB 5 LYS A 201  THR A 202  0                                        
SHEET    2  AB 5 LYS A 208  HIS A 214 -1  O  LEU A 209   N  LYS A 201           
SHEET    3  AB 5 HIS A 270  LYS A 273 -1  O  HIS A 270   N  HIS A 214           
SHEET    4  AB 5 LEU A 231  THR A 235 -1  O  GLN A 232   N  ARG A 271           
SHEET    5  AB 5 GLY A 238  ASP A 241 -1  O  GLY A 238   N  THR A 235           
LINK         NE2 HIS A 214                FE   FE2 A1332     1555   1555  2.19  
LINK         OD1 ASP A 216                FE   FE2 A1332     1555   1555  2.10  
LINK         NE2 HIS A 270                FE   FE2 A1332     1555   1555  2.33  
LINK        FE   FE2 A1332                 SAI V10 A1333     1555   1555  2.48  
LINK        FE   FE2 A1332                 O   HOH A2149     1555   1555  2.21  
LINK        FE   FE2 A1332                 O   HOH A2212     1555   1555  2.20  
CISPEP   1 ASP A  193    PRO A  194          0         4.04                     
SITE     1 AC1  6 HIS A 214  ASP A 216  HIS A 270  V10 A1333                    
SITE     2 AC1  6 HOH A2149  HOH A2212                                          
SITE     1 AC2 18 ARG A  87  TYR A  91  SER A 183  TYR A 189                    
SITE     2 AC2 18 PHE A 211  HIS A 214  ASP A 216  VAL A 272                    
SITE     3 AC2 18 LEU A 324  THR A 331  FE2 A1332  HOH A2206                    
SITE     4 AC2 18 HOH A2208  HOH A2209  HOH A2210  HOH A2211                    
SITE     5 AC2 18 HOH A2212  HOH A2213                                          
CRYST1   46.537   71.314  100.651  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021488  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014022  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009935        0.00000                         
ATOM      1  N   SER A   3     -14.766  45.687  -1.514  1.00 36.05           N  
ATOM      2  CA  SER A   3     -14.270  47.105  -1.475  1.00 35.56           C  
ATOM      3  C   SER A   3     -12.979  47.218  -2.297  1.00 34.80           C  
ATOM      4  O   SER A   3     -12.849  48.086  -3.167  1.00 34.34           O  
ATOM      5  CB  SER A   3     -14.006  47.533  -0.023  1.00 36.69           C  
ATOM      6  OG  SER A   3     -15.222  47.779   0.688  1.00 39.42           O  
ATOM      7  N   VAL A   4     -12.035  46.314  -2.003  1.00 33.74           N  
ATOM      8  CA  VAL A   4     -10.741  46.246  -2.688  1.00 31.52           C  
ATOM      9  C   VAL A   4     -10.858  45.312  -3.891  1.00 29.40           C  
ATOM     10  O   VAL A   4     -11.329  44.234  -3.768  1.00 27.85           O  
ATOM     11  CB  VAL A   4      -9.654  45.701  -1.704  1.00 32.47           C  
ATOM     12  CG1 VAL A   4      -8.289  45.531  -2.388  1.00 28.33           C  
ATOM     13  CG2 VAL A   4      -9.542  46.631  -0.462  1.00 32.86           C  
ATOM     14  N   SER A   5     -10.373  45.712  -5.047  1.00 28.48           N  
ATOM     15  CA  SER A   5     -10.442  44.843  -6.227  1.00 28.38           C  
ATOM     16  C   SER A   5      -9.255  43.881  -6.281  1.00 26.69           C  
ATOM     17  O   SER A   5      -8.248  44.082  -5.602  1.00 24.34           O  
ATOM     18  CB  SER A   5     -10.502  45.683  -7.490  1.00 29.03           C  
ATOM     19  OG  SER A   5      -9.344  46.482  -7.611  1.00 34.74           O  
ATOM     20  N   LYS A   6      -9.466  42.805  -7.032  1.00 25.72           N  
ATOM     21  CA  LYS A   6      -8.546  41.718  -7.248  1.00 25.44           C  
ATOM     22  C   LYS A   6      -7.376  42.117  -8.123  1.00 23.06           C  
ATOM     23  O   LYS A   6      -7.559  42.685  -9.195  1.00 23.49           O  
ATOM     24  CB  LYS A   6      -9.322  40.576  -7.911  1.00 26.37           C  
ATOM     25  CG  LYS A   6      -8.584  39.258  -7.973  1.00 28.58           C  
ATOM     26  CD  LYS A   6      -9.189  38.282  -9.001  1.00 31.70           C  
ATOM     27  CE  LYS A   6      -9.497  36.932  -8.366  1.00 36.59           C  
ATOM     28  NZ  LYS A   6      -8.236  36.094  -8.353  1.00 43.61           N  
ATOM     29  N   ALA A   7      -6.153  41.826  -7.679  1.00 20.58           N  
ATOM     30  CA  ALA A   7      -4.958  42.026  -8.496  1.00 20.11           C  
ATOM     31  C   ALA A   7      -4.924  40.964  -9.611  1.00 20.45           C  
ATOM     32  O   ALA A   7      -5.393  39.853  -9.427  1.00 19.61           O  
ATOM     33  CB  ALA A   7      -3.732  41.922  -7.656  1.00 17.98           C  
ATOM     34  N   ASN A   8      -4.415  41.367 -10.776  1.00 20.87           N  
ATOM     35  CA  ASN A   8      -4.077  40.477 -11.871  1.00 21.26           C  
ATOM     36  C   ASN A   8      -2.864  39.703 -11.531  1.00 19.06           C  
ATOM     37  O   ASN A   8      -1.761  40.269 -11.484  1.00 20.10           O  
ATOM     38  CB  ASN A   8      -3.680  41.278 -13.079  1.00 23.38           C  
ATOM     39  CG  ASN A   8      -4.346  40.810 -14.254  1.00 29.83           C  
ATOM     40  OD1 ASN A   8      -5.302  41.466 -14.735  1.00 36.88           O  
ATOM     41  ND2 ASN A   8      -3.923  39.642 -14.738  1.00 33.16           N  
ATOM     42  N   VAL A   9      -3.057  38.431 -11.212  1.00 16.71           N  
ATOM     43  CA  VAL A   9      -1.933  37.572 -10.921  1.00 14.30           C  
ATOM     44  C   VAL A   9      -2.138  36.365 -11.827  1.00 14.00           C  
ATOM     45  O   VAL A   9      -2.830  35.427 -11.501  1.00 12.23           O  
ATOM     46  CB  VAL A   9      -1.873  37.174  -9.443  1.00 14.51           C  
ATOM     47  CG1 VAL A   9      -0.594  36.340  -9.165  1.00 11.53           C  
ATOM     48  CG2 VAL A   9      -1.895  38.447  -8.585  1.00 12.13           C  
ATOM     49  N   PRO A  10      -1.520  36.392 -12.976  1.00 14.14           N  
ATOM     50  CA  PRO A  10      -1.672  35.192 -13.834  1.00 14.01           C  
ATOM     51  C   PRO A  10      -1.023  33.885 -13.301  1.00 13.96           C  
ATOM     52  O   PRO A  10      -0.028  33.924 -12.551  1.00 14.01           O  
ATOM     53  CB  PRO A  10      -1.019  35.629 -15.128  1.00 15.20           C  
ATOM     54  CG  PRO A  10      -0.194  36.824 -14.808  1.00 14.58           C  
ATOM     55  CD  PRO A  10      -0.713  37.467 -13.572  1.00 13.02           C  
ATOM     56  N   LYS A  11      -1.561  32.749 -13.723  1.00 13.64           N  
ATOM     57  CA  LYS A  11      -0.982  31.445 -13.460  1.00 14.95           C  
ATOM     58  C   LYS A  11      -0.167  31.081 -14.669  1.00 14.15           C  
ATOM     59  O   LYS A  11      -0.708  31.023 -15.755  1.00 14.13           O  
ATOM     60  CB  LYS A  11      -2.070  30.392 -13.228  1.00 16.94           C  
ATOM     61  CG  LYS A  11      -2.808  30.732 -11.872  1.00 19.94           C  
ATOM     62  CD  LYS A  11      -4.122  29.996 -11.692  1.00 22.64           C  
ATOM     63  CE  LYS A  11      -4.925  30.680 -10.560  1.00 25.10           C  
ATOM     64  NZ  LYS A  11      -4.135  30.779  -9.256  1.00 25.86           N  
ATOM     65  N   ILE A  12       1.118  30.850 -14.485  1.00 12.10           N  
ATOM     66  CA  ILE A  12       2.014  30.508 -15.583  1.00 10.90           C  
ATOM     67  C   ILE A  12       2.527  29.099 -15.418  1.00 11.32           C  
ATOM     68  O   ILE A  12       3.087  28.731 -14.353  1.00  8.72           O  
ATOM     69  CB  ILE A  12       3.216  31.538 -15.693  1.00 11.88           C  
ATOM     70  CG1 ILE A  12       2.708  33.013 -15.874  1.00 11.74           C  
ATOM     71  CG2 ILE A  12       4.213  31.079 -16.839  1.00  9.75           C  
ATOM     72  CD1 ILE A  12       3.807  34.187 -15.887  1.00  8.45           C  
ATOM     73  N   ASP A  13       2.346  28.264 -16.456  1.00 10.17           N  
ATOM     74  CA  ASP A  13       2.937  26.947 -16.476  1.00 10.26           C  
ATOM     75  C   ASP A  13       4.396  27.098 -16.813  1.00  9.50           C  
ATOM     76  O   ASP A  13       4.746  27.457 -17.930  1.00  9.80           O  
ATOM     77  CB  ASP A  13       2.236  26.051 -17.505  1.00 12.49           C  
ATOM     78  CG  ASP A  13       2.840  24.666 -17.606  1.00 12.37           C  
ATOM     79  OD1 ASP A  13       3.897  24.354 -17.048  1.00 13.05           O  
ATOM     80  OD2 ASP A  13       2.223  23.877 -18.331  1.00 16.78           O  
ATOM     81  N   VAL A  14       5.256  26.825 -15.814  1.00  8.89           N  
ATOM     82  CA  VAL A  14       6.693  27.088 -15.910  1.00  9.10           C  
ATOM     83  C   VAL A  14       7.420  25.807 -16.297  1.00  9.76           C  
ATOM     84  O   VAL A  14       8.651  25.779 -16.403  1.00 10.13           O  
ATOM     85  CB  VAL A  14       7.197  27.665 -14.621  1.00  8.84           C  
ATOM     86  CG1 VAL A  14       6.566  29.084 -14.367  1.00  6.82           C  
ATOM     87  CG2 VAL A  14       6.862  26.705 -13.426  1.00  8.66           C  
ATOM     88  N   SER A  15       6.665  24.738 -16.540  1.00  9.07           N  
ATOM     89  CA  SER A  15       7.291  23.451 -16.822  1.00  9.52           C  
ATOM     90  C   SER A  15       8.218  23.435 -18.079  1.00 10.85           C  
ATOM     91  O   SER A  15       9.227  22.716 -18.072  1.00  9.99           O  
ATOM     92  CB  SER A  15       6.302  22.296 -16.854  1.00  9.36           C  
ATOM     93  OG  SER A  15       5.355  22.384 -17.911  1.00 11.46           O  
ATOM     94  N   PRO A  16       7.953  24.254 -19.112  1.00 10.39           N  
ATOM     95  CA  PRO A  16       8.947  24.214 -20.204  1.00 11.10           C  
ATOM     96  C   PRO A  16      10.353  24.719 -19.823  1.00 11.91           C  
ATOM     97  O   PRO A  16      11.334  24.401 -20.497  1.00 10.93           O  
ATOM     98  CB  PRO A  16       8.330  25.086 -21.277  1.00 11.74           C  
ATOM     99  CG  PRO A  16       6.833  25.023 -21.006  1.00 11.76           C  
ATOM    100  CD  PRO A  16       6.811  25.085 -19.478  1.00 12.45           C  
ATOM    101  N   LEU A  17      10.451  25.412 -18.690  1.00 12.16           N  
ATOM    102  CA  LEU A  17      11.733  25.916 -18.211  1.00 12.16           C  
ATOM    103  C   LEU A  17      12.685  24.877 -17.669  1.00 13.17           C  
ATOM    104  O   LEU A  17      13.880  25.133 -17.474  1.00 12.61           O  
ATOM    105  CB  LEU A  17      11.554  27.074 -17.242  1.00 11.68           C  
ATOM    106  CG  LEU A  17      10.845  28.326 -17.774  1.00 12.95           C  
ATOM    107  CD1 LEU A  17      10.480  29.303 -16.625  1.00 13.51           C  
ATOM    108  CD2 LEU A  17      11.649  29.060 -18.846  1.00 12.32           C  
ATOM    109  N   PHE A  18      12.155  23.713 -17.364  1.00 14.49           N  
ATOM    110  CA  PHE A  18      12.962  22.600 -16.982  1.00 15.75           C  
ATOM    111  C   PHE A  18      13.507  21.830 -18.179  1.00 16.55           C  
ATOM    112  O   PHE A  18      14.347  20.976 -18.001  1.00 18.02           O  
ATOM    113  CB  PHE A  18      12.107  21.682 -16.102  1.00 16.05           C  
ATOM    114  CG  PHE A  18      11.754  22.289 -14.768  1.00 16.97           C  
ATOM    115  CD1 PHE A  18      10.496  22.825 -14.533  1.00 21.59           C  
ATOM    116  CD2 PHE A  18      12.689  22.306 -13.731  1.00 18.86           C  
ATOM    117  CE1 PHE A  18      10.160  23.395 -13.264  1.00 20.01           C  
ATOM    118  CE2 PHE A  18      12.370  22.805 -12.479  1.00 18.94           C  
ATOM    119  CZ  PHE A  18      11.100  23.403 -12.257  1.00 18.93           C  
ATOM    120  N   GLY A  19      13.004  22.079 -19.377  1.00 17.03           N  
ATOM    121  CA  GLY A  19      13.272  21.192 -20.527  1.00 19.35           C  
ATOM    122  C   GLY A  19      14.179  21.862 -21.557  1.00 20.01           C  
ATOM    123  O   GLY A  19      14.859  22.834 -21.273  1.00 20.25           O  
ATOM    124  N   ASP A  20      14.124  21.359 -22.775  1.00 21.10           N  
ATOM    125  CA  ASP A  20      15.048  21.781 -23.849  1.00 22.35           C  
ATOM    126  C   ASP A  20      14.250  22.238 -25.045  1.00 21.45           C  
ATOM    127  O   ASP A  20      14.788  22.284 -26.119  1.00 23.34           O  
ATOM    128  CB  ASP A  20      15.928  20.615 -24.332  1.00 24.01           C  
ATOM    129  CG  ASP A  20      16.844  20.107 -23.268  1.00 29.63           C  
ATOM    130  OD1 ASP A  20      16.796  18.889 -23.001  1.00 41.01           O  
ATOM    131  OD2 ASP A  20      17.606  20.905 -22.665  1.00 42.60           O  
ATOM    132  N   ASP A  21      12.972  22.542 -24.889  1.00 19.38           N  
ATOM    133  CA  ASP A  21      12.245  23.110 -25.980  1.00 19.04           C  
ATOM    134  C   ASP A  21      12.362  24.652 -25.965  1.00 17.87           C  
ATOM    135  O   ASP A  21      11.625  25.373 -25.246  1.00 16.25           O  
ATOM    136  CB  ASP A  21      10.826  22.594 -25.970  1.00 19.02           C  
ATOM    137  CG  ASP A  21       9.995  23.081 -27.172  1.00 21.55           C  
ATOM    138  OD1 ASP A  21      10.413  24.024 -27.878  1.00 20.32           O  
ATOM    139  OD2 ASP A  21       8.844  22.598 -27.331  1.00 25.50           O  
ATOM    140  N   GLN A  22      13.250  25.187 -26.807  1.00 17.31           N  
ATOM    141  CA  GLN A  22      13.618  26.623 -26.656  1.00 16.87           C  
ATOM    142  C   GLN A  22      12.485  27.570 -27.004  1.00 16.15           C  
ATOM    143  O   GLN A  22      12.313  28.628 -26.393  1.00 16.56           O  
ATOM    144  CB  GLN A  22      14.916  26.988 -27.388  1.00 17.97           C  
ATOM    145  CG  GLN A  22      16.064  25.988 -27.210  1.00 19.74           C  
ATOM    146  CD  GLN A  22      16.541  25.827 -25.774  1.00 25.40           C  
ATOM    147  OE1 GLN A  22      16.401  26.710 -24.931  1.00 25.60           O  
ATOM    148  NE2 GLN A  22      17.188  24.723 -25.518  1.00 28.23           N  
ATOM    149  N   ALA A  23      11.677  27.197 -27.968  1.00 16.14           N  
ATOM    150  CA  ALA A  23      10.558  28.040 -28.397  1.00 15.64           C  
ATOM    151  C   ALA A  23       9.497  28.115 -27.293  1.00 14.60           C  
ATOM    152  O   ALA A  23       8.905  29.156 -27.031  1.00 14.39           O  
ATOM    153  CB  ALA A  23       9.914  27.407 -29.678  1.00 16.98           C  
ATOM    154  N   ALA A  24       9.261  26.987 -26.641  1.00 15.08           N  
ATOM    155  CA  ALA A  24       8.269  26.902 -25.601  1.00 13.60           C  
ATOM    156  C   ALA A  24       8.770  27.716 -24.371  1.00 13.54           C  
ATOM    157  O   ALA A  24       7.987  28.363 -23.699  1.00 12.93           O  
ATOM    158  CB  ALA A  24       8.003  25.436 -25.256  1.00 13.43           C  
ATOM    159  N   LYS A  25      10.078  27.706 -24.093  1.00 13.22           N  
ATOM    160  CA  LYS A  25      10.654  28.563 -23.036  1.00 13.10           C  
ATOM    161  C   LYS A  25      10.453  30.044 -23.342  1.00 11.88           C  
ATOM    162  O   LYS A  25      10.157  30.830 -22.453  1.00 11.18           O  
ATOM    163  CB  LYS A  25      12.154  28.235 -22.812  1.00 13.54           C  
ATOM    164  CG  LYS A  25      12.310  26.935 -22.167  1.00 16.29           C  
ATOM    165  CD  LYS A  25      13.551  26.210 -22.470  1.00 18.24           C  
ATOM    166  CE  LYS A  25      14.679  26.541 -21.690  1.00 22.14           C  
ATOM    167  NZ  LYS A  25      15.775  25.499 -21.948  1.00 22.87           N  
ATOM    168  N   MET A  26      10.559  30.438 -24.609  1.00 11.16           N  
ATOM    169  CA  MET A  26      10.304  31.841 -24.993  1.00 11.43           C  
ATOM    170  C   MET A  26       8.881  32.270 -24.791  1.00 10.38           C  
ATOM    171  O   MET A  26       8.632  33.359 -24.332  1.00 10.36           O  
ATOM    172  CB  MET A  26      10.713  32.129 -26.426  1.00 11.73           C  
ATOM    173  CG  MET A  26      12.237  32.091 -26.745  1.00 10.82           C  
ATOM    174  SD  MET A  26      13.208  33.356 -25.959  1.00 14.50           S  
ATOM    175  CE  MET A  26      12.931  34.856 -26.903  1.00 10.74           C  
ATOM    176  N   ARG A  27       7.923  31.392 -25.065  1.00 11.14           N  
ATOM    177  CA  ARG A  27       6.535  31.654 -24.717  1.00 10.90           C  
ATOM    178  C   ARG A  27       6.289  31.784 -23.202  1.00 11.16           C  
ATOM    179  O   ARG A  27       5.456  32.614 -22.770  1.00 12.27           O  
ATOM    180  CB  ARG A  27       5.614  30.615 -25.390  1.00 11.62           C  
ATOM    181  CG  ARG A  27       5.539  30.757 -26.943  1.00 11.54           C  
ATOM    182  CD  ARG A  27       4.418  29.877 -27.574  1.00 15.29           C  
ATOM    183  NE  ARG A  27       4.928  28.498 -27.582  1.00 17.89           N  
ATOM    184  CZ  ARG A  27       5.727  27.940 -28.509  1.00 24.08           C  
ATOM    185  NH1 ARG A  27       6.131  26.671 -28.278  1.00 23.15           N  
ATOM    186  NH2 ARG A  27       6.079  28.562 -29.684  1.00 22.23           N  
ATOM    187  N   VAL A  28       7.016  31.031 -22.384  1.00  9.90           N  
ATOM    188  CA  VAL A  28       6.963  31.276 -20.928  1.00  8.71           C  
ATOM    189  C   VAL A  28       7.581  32.597 -20.545  1.00  7.66           C  
ATOM    190  O   VAL A  28       6.991  33.348 -19.741  1.00  9.56           O  
ATOM    191  CB  VAL A  28       7.626  30.126 -20.116  1.00  9.03           C  
ATOM    192  CG1 VAL A  28       7.540  30.401 -18.608  1.00  8.78           C  
ATOM    193  CG2 VAL A  28       7.012  28.819 -20.437  1.00  8.09           C  
ATOM    194  N   ALA A  29       8.708  32.930 -21.175  1.00  6.98           N  
ATOM    195  CA  ALA A  29       9.424  34.179 -20.946  1.00  7.56           C  
ATOM    196  C   ALA A  29       8.512  35.366 -21.184  1.00  9.22           C  
ATOM    197  O   ALA A  29       8.466  36.309 -20.345  1.00  9.81           O  
ATOM    198  CB  ALA A  29      10.640  34.279 -21.821  1.00  8.58           C  
ATOM    199  N   GLN A  30       7.739  35.294 -22.282  1.00  8.68           N  
ATOM    200  CA  GLN A  30       6.840  36.358 -22.590  1.00  9.51           C  
ATOM    201  C   GLN A  30       5.814  36.538 -21.491  1.00  9.66           C  
ATOM    202  O   GLN A  30       5.456  37.665 -21.193  1.00  9.42           O  
ATOM    203  CB  GLN A  30       6.136  36.129 -23.928  1.00  9.03           C  
ATOM    204  CG  GLN A  30       5.167  37.270 -24.374  1.00 10.32           C  
ATOM    205  CD  GLN A  30       3.754  37.273 -23.651  1.00 10.12           C  
ATOM    206  OE1 GLN A  30       3.119  36.250 -23.431  1.00 11.46           O  
ATOM    207  NE2 GLN A  30       3.301  38.444 -23.325  1.00 14.21           N  
ATOM    208  N   GLN A  31       5.254  35.438 -20.962  1.00 10.43           N  
ATOM    209  CA  GLN A  31       4.291  35.574 -19.886  1.00 11.48           C  
ATOM    210  C   GLN A  31       4.895  36.246 -18.637  1.00 11.65           C  
ATOM    211  O   GLN A  31       4.240  37.062 -17.982  1.00 11.22           O  
ATOM    212  CB  GLN A  31       3.693  34.226 -19.541  1.00 11.68           C  
ATOM    213  CG  GLN A  31       2.935  33.601 -20.692  1.00 12.92           C  
ATOM    214  CD  GLN A  31       2.512  32.201 -20.350  1.00 15.32           C  
ATOM    215  OE1 GLN A  31       1.657  32.009 -19.497  1.00 20.26           O  
ATOM    216  NE2 GLN A  31       3.139  31.222 -20.970  1.00 15.88           N  
ATOM    217  N   ILE A  32       6.146  35.890 -18.334  1.00 11.42           N  
ATOM    218  CA  ILE A  32       6.872  36.435 -17.237  1.00 10.89           C  
ATOM    219  C   ILE A  32       7.077  37.939 -17.461  1.00 11.44           C  
ATOM    220  O   ILE A  32       6.922  38.733 -16.541  1.00 11.24           O  
ATOM    221  CB  ILE A  32       8.239  35.696 -17.017  1.00 11.46           C  
ATOM    222  CG1 ILE A  32       7.993  34.278 -16.527  1.00  8.18           C  
ATOM    223  CG2 ILE A  32       9.138  36.484 -16.020  1.00  9.45           C  
ATOM    224  CD1 ILE A  32       9.242  33.420 -16.294  1.00  9.90           C  
ATOM    225  N   ASP A  33       7.421  38.322 -18.683  1.00 12.45           N  
ATOM    226  CA  ASP A  33       7.648  39.734 -19.013  1.00 11.58           C  
ATOM    227  C   ASP A  33       6.348  40.534 -18.791  1.00 11.03           C  
ATOM    228  O   ASP A  33       6.346  41.583 -18.173  1.00 10.25           O  
ATOM    229  CB  ASP A  33       8.115  39.837 -20.451  1.00 11.92           C  
ATOM    230  CG  ASP A  33       8.252  41.249 -20.907  1.00 12.71           C  
ATOM    231  OD1 ASP A  33       9.266  41.846 -20.524  1.00 11.57           O  
ATOM    232  OD2 ASP A  33       7.376  41.739 -21.666  1.00 12.56           O  
ATOM    233  N   ALA A  34       5.235  39.959 -19.232  1.00 10.71           N  
ATOM    234  CA  ALA A  34       3.962  40.627 -19.138  1.00 11.30           C  
ATOM    235  C   ALA A  34       3.529  40.854 -17.663  1.00 11.31           C  
ATOM    236  O   ALA A  34       3.146  41.960 -17.249  1.00 10.65           O  
ATOM    237  CB  ALA A  34       2.891  39.820 -19.901  1.00 12.34           C  
ATOM    238  N   ALA A  35       3.659  39.789 -16.874  1.00 12.16           N  
ATOM    239  CA  ALA A  35       3.334  39.809 -15.452  1.00 11.52           C  
ATOM    240  C   ALA A  35       4.251  40.769 -14.704  1.00 11.65           C  
ATOM    241  O   ALA A  35       3.796  41.480 -13.791  1.00 13.06           O  
ATOM    242  CB  ALA A  35       3.464  38.444 -14.914  1.00  9.96           C  
ATOM    243  N   SER A  36       5.515  40.838 -15.121  1.00 11.98           N  
ATOM    244  CA  SER A  36       6.517  41.653 -14.453  1.00 12.14           C  
ATOM    245  C   SER A  36       6.310  43.136 -14.763  1.00 13.64           C  
ATOM    246  O   SER A  36       6.637  44.031 -13.936  1.00 12.68           O  
ATOM    247  CB  SER A  36       7.927  41.189 -14.797  1.00 13.13           C  
ATOM    248  OG  SER A  36       8.156  39.829 -14.398  1.00 10.07           O  
ATOM    249  N   ARG A  37       5.767  43.424 -15.950  1.00 12.38           N  
ATOM    250  CA  ARG A  37       5.458  44.820 -16.299  1.00 14.05           C  
ATOM    251  C   ARG A  37       4.100  45.296 -15.780  1.00 14.87           C  
ATOM    252  O   ARG A  37       3.824  46.489 -15.825  1.00 16.84           O  
ATOM    253  CB  ARG A  37       5.549  45.018 -17.844  1.00 12.66           C  
ATOM    254  CG  ARG A  37       6.894  44.732 -18.388  1.00 14.23           C  
ATOM    255  CD  ARG A  37       6.938  44.383 -19.882  1.00 15.38           C  
ATOM    256  NE  ARG A  37       6.368  45.465 -20.720  1.00 18.19           N  
ATOM    257  CZ  ARG A  37       6.177  45.378 -22.033  1.00 18.51           C  
ATOM    258  NH1 ARG A  37       6.468  44.252 -22.695  1.00 18.98           N  
ATOM    259  NH2 ARG A  37       5.639  46.406 -22.678  1.00 16.95           N  
ATOM    260  N   ASP A  38       3.234  44.379 -15.376  1.00 16.17           N  
ATOM    261  CA  ASP A  38       1.855  44.688 -14.931  1.00 16.93           C  
ATOM    262  C   ASP A  38       1.873  44.742 -13.357  1.00 16.83           C  
ATOM    263  O   ASP A  38       2.599  45.558 -12.817  1.00 16.51           O  
ATOM    264  CB  ASP A  38       0.842  43.681 -15.534  1.00 17.62           C  
ATOM    265  CG  ASP A  38      -0.663  43.968 -15.101  1.00 19.73           C  
ATOM    266  OD1 ASP A  38      -1.504  43.046 -15.111  1.00 26.22           O  
ATOM    267  OD2 ASP A  38      -0.988  45.108 -14.766  1.00 21.08           O  
ATOM    268  N   THR A  39       1.181  43.862 -12.626  1.00 17.03           N  
ATOM    269  CA  THR A  39       1.236  43.958 -11.158  1.00 16.85           C  
ATOM    270  C   THR A  39       2.546  43.525 -10.526  1.00 15.40           C  
ATOM    271  O   THR A  39       2.775  43.872  -9.373  1.00 15.17           O  
ATOM    272  CB  THR A  39       0.165  43.164 -10.437  1.00 17.81           C  
ATOM    273  OG1 THR A  39       0.491  41.752 -10.506  1.00 17.07           O  
ATOM    274  CG2 THR A  39      -1.218  43.479 -11.079  1.00 21.00           C  
ATOM    275  N   GLY A  40       3.390  42.786 -11.254  1.00 13.38           N  
ATOM    276  CA  GLY A  40       4.646  42.333 -10.695  1.00 14.08           C  
ATOM    277  C   GLY A  40       4.577  41.033  -9.928  1.00 14.54           C  
ATOM    278  O   GLY A  40       5.596  40.642  -9.291  1.00 18.60           O  
ATOM    279  N   PHE A  41       3.410  40.362  -9.966  1.00 12.61           N  
ATOM    280  CA  PHE A  41       3.202  39.080  -9.343  1.00 11.35           C  
ATOM    281  C   PHE A  41       2.661  38.109 -10.379  1.00 12.26           C  
ATOM    282  O   PHE A  41       1.860  38.502 -11.260  1.00 10.45           O  
ATOM    283  CB  PHE A  41       2.187  39.157  -8.197  1.00 10.29           C  
ATOM    284  CG  PHE A  41       2.768  39.730  -6.947  1.00  9.93           C  
ATOM    285  CD1 PHE A  41       2.757  41.107  -6.743  1.00  7.01           C  
ATOM    286  CD2 PHE A  41       3.353  38.901  -5.992  1.00  8.78           C  
ATOM    287  CE1 PHE A  41       3.327  41.638  -5.597  1.00 10.01           C  
ATOM    288  CE2 PHE A  41       3.928  39.405  -4.876  1.00 11.27           C  
ATOM    289  CZ  PHE A  41       3.944  40.803  -4.673  1.00  9.15           C  
ATOM    290  N   PHE A  42       3.095  36.841 -10.275  1.00 11.51           N  
ATOM    291  CA  PHE A  42       2.373  35.688 -10.898  1.00 10.37           C  
ATOM    292  C   PHE A  42       2.482  34.454 -10.062  1.00 10.54           C  
ATOM    293  O   PHE A  42       3.341  34.381  -9.154  1.00  8.36           O  
ATOM    294  CB  PHE A  42       2.864  35.359 -12.322  1.00 10.61           C  
ATOM    295  CG  PHE A  42       4.294  34.904 -12.422  1.00 11.94           C  
ATOM    296  CD1 PHE A  42       4.636  33.558 -12.525  1.00 11.33           C  
ATOM    297  CD2 PHE A  42       5.326  35.839 -12.443  1.00 14.01           C  
ATOM    298  CE1 PHE A  42       5.970  33.154 -12.670  1.00 10.44           C  
ATOM    299  CE2 PHE A  42       6.651  35.436 -12.612  1.00 11.62           C  
ATOM    300  CZ  PHE A  42       6.972  34.078 -12.706  1.00  9.80           C  
ATOM    301  N   TYR A  43       1.648  33.455 -10.384  1.00  9.49           N  
ATOM    302  CA  TYR A  43       1.789  32.118  -9.786  1.00 10.43           C  
ATOM    303  C   TYR A  43       2.436  31.243 -10.815  1.00 10.43           C  
ATOM    304  O   TYR A  43       1.981  31.210 -11.986  1.00 10.75           O  
ATOM    305  CB  TYR A  43       0.435  31.528  -9.370  1.00 10.50           C  
ATOM    306  CG  TYR A  43      -0.068  31.994  -8.030  1.00  9.31           C  
ATOM    307  CD1 TYR A  43      -1.146  32.882  -7.924  1.00  8.91           C  
ATOM    308  CD2 TYR A  43       0.534  31.529  -6.849  1.00 10.88           C  
ATOM    309  CE1 TYR A  43      -1.607  33.312  -6.675  1.00  9.55           C  
ATOM    310  CE2 TYR A  43       0.059  31.918  -5.588  1.00 11.94           C  
ATOM    311  CZ  TYR A  43      -0.977  32.847  -5.515  1.00 12.51           C  
ATOM    312  OH  TYR A  43      -1.410  33.266  -4.277  1.00 13.45           O  
ATOM    313  N   ALA A  44       3.511  30.581 -10.400  1.00  9.71           N  
ATOM    314  CA  ALA A  44       4.143  29.506 -11.145  1.00 10.24           C  
ATOM    315  C   ALA A  44       3.385  28.216 -10.889  1.00 10.39           C  
ATOM    316  O   ALA A  44       3.260  27.775  -9.729  1.00  9.70           O  
ATOM    317  CB  ALA A  44       5.644  29.325 -10.667  1.00  8.58           C  
ATOM    318  N   VAL A  45       2.872  27.611 -11.944  1.00  9.42           N  
ATOM    319  CA  VAL A  45       2.157  26.338 -11.840  1.00 12.14           C  
ATOM    320  C   VAL A  45       2.941  25.263 -12.594  1.00 12.07           C  
ATOM    321  O   VAL A  45       3.799  25.589 -13.391  1.00 12.86           O  
ATOM    322  CB  VAL A  45       0.655  26.424 -12.283  1.00 12.82           C  
ATOM    323  CG1 VAL A  45      -0.145  27.426 -11.366  1.00 12.85           C  
ATOM    324  CG2 VAL A  45       0.502  26.769 -13.776  1.00 11.05           C  
ATOM    325  N   ASN A  46       2.672  23.988 -12.305  1.00 11.60           N  
ATOM    326  CA  ASN A  46       3.451  22.860 -12.880  1.00 12.49           C  
ATOM    327  C   ASN A  46       4.951  22.965 -12.597  1.00 11.64           C  
ATOM    328  O   ASN A  46       5.803  22.746 -13.468  1.00 12.36           O  
ATOM    329  CB  ASN A  46       3.156  22.708 -14.362  1.00 12.90           C  
ATOM    330  CG  ASN A  46       1.707  22.448 -14.595  1.00 16.99           C  
ATOM    331  OD1 ASN A  46       1.203  21.457 -14.130  1.00 21.64           O  
ATOM    332  ND2 ASN A  46       1.007  23.398 -15.142  1.00 18.22           N  
ATOM    333  N   HIS A  47       5.228  23.242 -11.321  1.00 12.23           N  
ATOM    334  CA  HIS A  47       6.564  23.657 -10.802  1.00 11.51           C  
ATOM    335  C   HIS A  47       7.281  22.428 -10.286  1.00 11.28           C  
ATOM    336  O   HIS A  47       8.447  22.491  -9.993  1.00 11.08           O  
ATOM    337  CB  HIS A  47       6.426  24.709  -9.668  1.00 11.62           C  
ATOM    338  CG  HIS A  47       5.394  24.368  -8.622  1.00  8.76           C  
ATOM    339  ND1 HIS A  47       5.549  23.318  -7.735  1.00 14.16           N  
ATOM    340  CD2 HIS A  47       4.178  24.887  -8.366  1.00  8.11           C  
ATOM    341  CE1 HIS A  47       4.475  23.240  -6.961  1.00 11.76           C  
ATOM    342  NE2 HIS A  47       3.611  24.158  -7.364  1.00 13.27           N  
ATOM    343  N   GLY A  48       6.553  21.325 -10.158  1.00 11.01           N  
ATOM    344  CA  GLY A  48       7.155  20.051  -9.774  1.00 11.42           C  
ATOM    345  C   GLY A  48       7.461  19.809  -8.304  1.00 10.67           C  
ATOM    346  O   GLY A  48       7.994  18.757  -7.991  1.00 10.09           O  
ATOM    347  N   ILE A  49       7.152  20.748  -7.411  1.00  8.37           N  
ATOM    348  CA  ILE A  49       7.477  20.591  -6.001  1.00  9.56           C  
ATOM    349  C   ILE A  49       6.255  20.082  -5.204  1.00  9.26           C  
ATOM    350  O   ILE A  49       5.119  20.499  -5.438  1.00  9.15           O  
ATOM    351  CB  ILE A  49       8.006  21.919  -5.386  1.00  9.94           C  
ATOM    352  CG1 ILE A  49       9.362  22.326  -6.033  1.00 10.43           C  
ATOM    353  CG2 ILE A  49       8.248  21.804  -3.881  1.00  8.48           C  
ATOM    354  CD1 ILE A  49       9.908  23.735  -5.505  1.00  8.19           C  
ATOM    355  N   ASN A  50       6.501  19.174  -4.278  1.00  9.40           N  
ATOM    356  CA  ASN A  50       5.402  18.618  -3.473  1.00  8.51           C  
ATOM    357  C   ASN A  50       5.123  19.613  -2.342  1.00  8.20           C  
ATOM    358  O   ASN A  50       5.701  19.532  -1.248  1.00  7.50           O  
ATOM    359  CB  ASN A  50       5.774  17.236  -2.947  1.00  7.81           C  
ATOM    360  CG  ASN A  50       4.612  16.541  -2.221  1.00  9.39           C  
ATOM    361  OD1 ASN A  50       3.617  17.195  -1.805  1.00  9.11           O  
ATOM    362  ND2 ASN A  50       4.760  15.264  -1.994  1.00  6.34           N  
ATOM    363  N   VAL A  51       4.254  20.573  -2.614  1.00  7.16           N  
ATOM    364  CA  VAL A  51       4.002  21.582  -1.624  1.00  7.36           C  
ATOM    365  C   VAL A  51       3.116  21.083  -0.469  1.00  7.72           C  
ATOM    366  O   VAL A  51       3.155  21.644   0.572  1.00  8.48           O  
ATOM    367  CB  VAL A  51       3.459  22.920  -2.241  1.00  9.01           C  
ATOM    368  CG1 VAL A  51       4.574  23.622  -3.108  1.00 10.40           C  
ATOM    369  CG2 VAL A  51       2.234  22.694  -3.062  1.00  5.20           C  
ATOM    370  N   GLN A  52       2.261  20.081  -0.674  1.00  8.67           N  
ATOM    371  CA  GLN A  52       1.399  19.639   0.420  1.00  8.94           C  
ATOM    372  C   GLN A  52       2.263  18.954   1.491  1.00  7.99           C  
ATOM    373  O   GLN A  52       2.111  19.181   2.658  1.00  8.34           O  
ATOM    374  CB  GLN A  52       0.360  18.679  -0.112  1.00 10.26           C  
ATOM    375  CG  GLN A  52      -0.628  18.173   1.050  1.00  9.40           C  
ATOM    376  CD  GLN A  52      -0.110  17.043   1.904  1.00 11.58           C  
ATOM    377  OE1 GLN A  52       0.875  16.325   1.542  1.00 12.89           O  
ATOM    378  NE2 GLN A  52      -0.778  16.863   3.108  1.00 12.35           N  
ATOM    379  N   ARG A  53       3.281  18.225   1.055  1.00  8.85           N  
ATOM    380  CA  ARG A  53       4.278  17.655   1.957  1.00  8.99           C  
ATOM    381  C   ARG A  53       5.100  18.715   2.673  1.00  8.93           C  
ATOM    382  O   ARG A  53       5.282  18.636   3.874  1.00 10.63           O  
ATOM    383  CB  ARG A  53       5.198  16.698   1.200  1.00  9.19           C  
ATOM    384  CG  ARG A  53       6.050  15.844   2.123  1.00  9.31           C  
ATOM    385  CD  ARG A  53       6.685  14.730   1.362  1.00 12.31           C  
ATOM    386  NE  ARG A  53       7.500  13.883   2.234  1.00 10.08           N  
ATOM    387  CZ  ARG A  53       8.821  13.903   2.275  1.00 12.47           C  
ATOM    388  NH1 ARG A  53       9.509  14.723   1.509  1.00 11.52           N  
ATOM    389  NH2 ARG A  53       9.454  13.081   3.082  1.00 13.63           N  
ATOM    390  N   LEU A  54       5.615  19.707   1.941  1.00  9.69           N  
ATOM    391  CA  LEU A  54       6.259  20.861   2.556  1.00  9.08           C  
ATOM    392  C   LEU A  54       5.385  21.437   3.683  1.00 10.03           C  
ATOM    393  O   LEU A  54       5.856  21.696   4.774  1.00  9.15           O  
ATOM    394  CB  LEU A  54       6.536  21.935   1.478  1.00  9.92           C  
ATOM    395  CG  LEU A  54       6.962  23.310   1.930  1.00  9.11           C  
ATOM    396  CD1 LEU A  54       8.347  23.230   2.654  1.00  9.81           C  
ATOM    397  CD2 LEU A  54       6.869  24.354   0.781  1.00  5.55           C  
ATOM    398  N   SER A  55       4.119  21.672   3.402  1.00 10.14           N  
ATOM    399  CA  SER A  55       3.189  22.231   4.422  1.00 11.04           C  
ATOM    400  C   SER A  55       2.990  21.302   5.580  1.00 10.36           C  
ATOM    401  O   SER A  55       3.019  21.735   6.749  1.00  9.23           O  
ATOM    402  CB  SER A  55       1.849  22.575   3.769  1.00 12.35           C  
ATOM    403  OG  SER A  55       1.015  23.309   4.645  1.00 14.37           O  
ATOM    404  N   GLN A  56       2.956  19.998   5.306  1.00 11.06           N  
ATOM    405  CA  GLN A  56       2.783  19.032   6.410  1.00 11.63           C  
ATOM    406  C   GLN A  56       4.017  18.953   7.326  1.00 11.98           C  
ATOM    407  O   GLN A  56       3.909  19.003   8.561  1.00 11.13           O  
ATOM    408  CB  GLN A  56       2.442  17.629   5.845  1.00 10.81           C  
ATOM    409  CG  GLN A  56       2.299  16.530   6.920  1.00 14.37           C  
ATOM    410  CD  GLN A  56       1.171  16.774   7.915  1.00 19.06           C  
ATOM    411  OE1 GLN A  56       0.115  17.372   7.587  1.00 17.33           O  
ATOM    412  NE2 GLN A  56       1.372  16.258   9.133  1.00 22.45           N  
ATOM    413  N   LYS A  57       5.198  18.864   6.707  1.00 11.12           N  
ATOM    414  CA  LYS A  57       6.436  18.768   7.462  1.00 11.02           C  
ATOM    415  C   LYS A  57       6.653  20.047   8.270  1.00 11.27           C  
ATOM    416  O   LYS A  57       7.109  20.020   9.418  1.00  9.88           O  
ATOM    417  CB  LYS A  57       7.623  18.479   6.534  1.00 11.12           C  
ATOM    418  CG  LYS A  57       7.501  17.128   5.829  1.00  9.68           C  
ATOM    419  CD  LYS A  57       7.578  15.919   6.797  1.00 12.96           C  
ATOM    420  CE  LYS A  57       7.650  14.648   5.996  1.00 12.74           C  
ATOM    421  NZ  LYS A  57       7.763  13.325   6.746  1.00 11.31           N  
ATOM    422  N   THR A  58       6.298  21.172   7.665  1.00 11.64           N  
ATOM    423  CA  THR A  58       6.464  22.462   8.328  1.00 12.34           C  
ATOM    424  C   THR A  58       5.479  22.640   9.511  1.00 11.69           C  
ATOM    425  O   THR A  58       5.868  23.061  10.581  1.00 10.84           O  
ATOM    426  CB  THR A  58       6.349  23.619   7.320  1.00 11.46           C  
ATOM    427  OG1 THR A  58       7.452  23.523   6.396  1.00 13.46           O  
ATOM    428  CG2 THR A  58       6.394  24.982   8.081  1.00 12.92           C  
ATOM    429  N   LYS A  59       4.227  22.298   9.301  1.00 13.78           N  
ATOM    430  CA  LYS A  59       3.226  22.173  10.362  1.00 14.84           C  
ATOM    431  C   LYS A  59       3.735  21.330  11.556  1.00 14.83           C  
ATOM    432  O   LYS A  59       3.626  21.760  12.734  1.00 14.35           O  
ATOM    433  CB  LYS A  59       1.955  21.516   9.768  1.00 16.00           C  
ATOM    434  CG  LYS A  59       0.782  21.461  10.724  1.00 20.62           C  
ATOM    435  CD  LYS A  59      -0.425  20.690  10.062  1.00 20.19           C  
ATOM    436  CE  LYS A  59      -1.646  20.573  11.014  1.00 27.37           C  
ATOM    437  NZ  LYS A  59      -2.430  19.238  10.818  1.00 29.89           N  
ATOM    438  N   GLU A  60       4.282  20.138  11.259  1.00 13.52           N  
ATOM    439  CA  GLU A  60       4.741  19.230  12.318  1.00 15.08           C  
ATOM    440  C   GLU A  60       5.852  19.895  13.170  1.00 14.14           C  
ATOM    441  O   GLU A  60       5.815  19.794  14.355  1.00 14.41           O  
ATOM    442  CB  GLU A  60       5.276  17.927  11.744  1.00 15.17           C  
ATOM    443  CG  GLU A  60       4.171  17.030  11.200  1.00 19.33           C  
ATOM    444  CD  GLU A  60       4.715  15.846  10.405  1.00 19.12           C  
ATOM    445  OE1 GLU A  60       5.939  15.549  10.536  1.00 25.43           O  
ATOM    446  OE2 GLU A  60       3.926  15.206   9.680  1.00 23.86           O  
ATOM    447  N   PHE A  61       6.805  20.580  12.529  1.00 13.07           N  
ATOM    448  CA  PHE A  61       7.803  21.411  13.207  1.00 13.13           C  
ATOM    449  C   PHE A  61       7.209  22.531  14.027  1.00 11.78           C  
ATOM    450  O   PHE A  61       7.474  22.634  15.201  1.00 11.65           O  
ATOM    451  CB  PHE A  61       8.753  21.983  12.157  1.00 13.10           C  
ATOM    452  CG  PHE A  61       9.699  23.008  12.674  1.00 13.11           C  
ATOM    453  CD1 PHE A  61      10.759  22.646  13.494  1.00 14.00           C  
ATOM    454  CD2 PHE A  61       9.561  24.317  12.324  1.00 11.39           C  
ATOM    455  CE1 PHE A  61      11.661  23.601  13.994  1.00 14.34           C  
ATOM    456  CE2 PHE A  61      10.447  25.270  12.805  1.00 12.74           C  
ATOM    457  CZ  PHE A  61      11.515  24.905  13.609  1.00 11.74           C  
ATOM    458  N   HIS A  62       6.385  23.379  13.453  1.00 11.66           N  
ATOM    459  CA  HIS A  62       5.916  24.542  14.190  1.00 13.63           C  
ATOM    460  C   HIS A  62       5.099  24.133  15.434  1.00 16.35           C  
ATOM    461  O   HIS A  62       5.125  24.803  16.440  1.00 15.59           O  
ATOM    462  CB  HIS A  62       5.034  25.465  13.325  1.00 13.88           C  
ATOM    463  CG  HIS A  62       5.800  26.361  12.396  1.00 11.97           C  
ATOM    464  ND1 HIS A  62       5.390  26.620  11.101  1.00 13.54           N  
ATOM    465  CD2 HIS A  62       6.932  27.071  12.578  1.00 12.48           C  
ATOM    466  CE1 HIS A  62       6.233  27.455  10.538  1.00 14.14           C  
ATOM    467  NE2 HIS A  62       7.205  27.718  11.397  1.00 15.44           N  
ATOM    468  N   MET A  63       4.335  23.069  15.316  1.00 17.16           N  
ATOM    469  CA  MET A  63       3.482  22.690  16.352  1.00 19.50           C  
ATOM    470  C   MET A  63       4.195  21.886  17.427  1.00 20.09           C  
ATOM    471  O   MET A  63       3.713  21.872  18.556  1.00 22.50           O  
ATOM    472  CB  MET A  63       2.228  21.998  15.769  1.00 22.35           C  
ATOM    473  CG  MET A  63       1.278  23.011  14.880  1.00 22.92           C  
ATOM    474  SD  MET A  63       1.069  24.862  15.182  1.00 33.25           S  
ATOM    475  CE  MET A  63      -0.742  24.959  15.148  1.00 32.35           C  
ATOM    476  N   SER A  64       5.366  21.307  17.141  1.00 18.07           N  
ATOM    477  CA  SER A  64       6.049  20.531  18.135  1.00 16.95           C  
ATOM    478  C   SER A  64       7.317  21.194  18.791  1.00 16.86           C  
ATOM    479  O   SER A  64       7.817  20.743  19.835  1.00 16.85           O  
ATOM    480  CB  SER A  64       6.352  19.170  17.571  1.00 17.07           C  
ATOM    481  OG  SER A  64       7.349  19.206  16.629  1.00 18.03           O  
ATOM    482  N   ILE A  65       7.838  22.241  18.188  1.00 13.73           N  
ATOM    483  CA  ILE A  65       8.915  23.022  18.826  1.00 13.32           C  
ATOM    484  C   ILE A  65       8.422  23.655  20.161  1.00 12.35           C  
ATOM    485  O   ILE A  65       7.268  24.051  20.315  1.00 11.61           O  
ATOM    486  CB  ILE A  65       9.462  24.046  17.878  1.00 12.51           C  
ATOM    487  CG1 ILE A  65      10.757  24.702  18.453  1.00 13.54           C  
ATOM    488  CG2 ILE A  65       8.337  25.048  17.511  1.00 10.02           C  
ATOM    489  CD1 ILE A  65      11.827  24.955  17.432  1.00 11.14           C  
ATOM    490  N   THR A  66       9.275  23.606  21.164  1.00 12.77           N  
ATOM    491  CA  THR A  66       8.926  24.060  22.519  1.00 12.63           C  
ATOM    492  C   THR A  66       9.611  25.386  22.755  1.00 12.05           C  
ATOM    493  O   THR A  66      10.619  25.702  22.086  1.00 12.15           O  
ATOM    494  CB  THR A  66       9.383  23.003  23.582  1.00 11.84           C  
ATOM    495  OG1 THR A  66      10.817  22.857  23.476  1.00 11.76           O  
ATOM    496  CG2 THR A  66       8.727  21.660  23.268  1.00 13.23           C  
ATOM    497  N   PRO A  67       9.114  26.145  23.740  1.00 12.99           N  
ATOM    498  CA  PRO A  67       9.725  27.364  24.190  1.00 12.91           C  
ATOM    499  C   PRO A  67      11.207  27.227  24.497  1.00 13.32           C  
ATOM    500  O   PRO A  67      12.021  28.072  24.096  1.00 12.69           O  
ATOM    501  CB  PRO A  67       8.924  27.707  25.462  1.00 12.93           C  
ATOM    502  CG  PRO A  67       7.641  27.061  25.332  1.00 12.71           C  
ATOM    503  CD  PRO A  67       7.819  25.876  24.449  1.00 13.28           C  
ATOM    504  N   GLU A  68      11.578  26.138  25.168  1.00 14.45           N  
ATOM    505  CA  GLU A  68      12.964  25.883  25.471  1.00 14.37           C  
ATOM    506  C   GLU A  68      13.814  25.838  24.180  1.00 14.39           C  
ATOM    507  O   GLU A  68      14.896  26.412  24.064  1.00 13.76           O  
ATOM    508  CB  GLU A  68      13.070  24.563  26.222  1.00 14.63           C  
ATOM    509  CG  GLU A  68      14.514  24.099  26.486  1.00 16.49           C  
ATOM    510  CD  GLU A  68      14.615  22.697  27.070  1.00 15.00           C  
ATOM    511  OE1 GLU A  68      14.010  21.807  26.508  1.00 19.67           O  
ATOM    512  OE2 GLU A  68      15.243  22.520  28.129  1.00 24.77           O  
ATOM    513  N   GLU A  69      13.308  25.114  23.196  1.00 16.19           N  
ATOM    514  CA  GLU A  69      14.038  24.935  21.910  1.00 15.20           C  
ATOM    515  C   GLU A  69      14.194  26.255  21.180  1.00 13.40           C  
ATOM    516  O   GLU A  69      15.235  26.518  20.532  1.00 13.92           O  
ATOM    517  CB  GLU A  69      13.311  23.940  21.011  1.00 14.99           C  
ATOM    518  CG  GLU A  69      13.494  22.531  21.428  1.00 17.48           C  
ATOM    519  CD  GLU A  69      12.593  21.562  20.658  1.00 18.31           C  
ATOM    520  OE1 GLU A  69      13.150  20.637  20.079  1.00 22.40           O  
ATOM    521  OE2 GLU A  69      11.368  21.705  20.609  1.00 20.67           O  
ATOM    522  N   LYS A  70      13.186  27.103  21.308  1.00 11.81           N  
ATOM    523  CA  LYS A  70      13.196  28.382  20.582  1.00 11.95           C  
ATOM    524  C   LYS A  70      14.304  29.308  21.047  1.00 11.75           C  
ATOM    525  O   LYS A  70      14.964  29.936  20.240  1.00  9.76           O  
ATOM    526  CB  LYS A  70      11.825  29.098  20.748  1.00 11.24           C  
ATOM    527  CG  LYS A  70      10.666  28.316  20.063  1.00 11.47           C  
ATOM    528  CD  LYS A  70       9.311  29.025  20.221  1.00 11.15           C  
ATOM    529  CE  LYS A  70       8.167  28.109  19.732  1.00 14.37           C  
ATOM    530  NZ  LYS A  70       6.806  28.628  19.812  1.00 10.62           N  
ATOM    531  N   TRP A  71      14.480  29.419  22.377  1.00 11.00           N  
ATOM    532  CA  TRP A  71      15.630  30.188  22.950  1.00 11.62           C  
ATOM    533  C   TRP A  71      16.931  29.526  22.512  1.00 10.82           C  
ATOM    534  O   TRP A  71      17.860  30.223  22.105  1.00 10.58           O  
ATOM    535  CB  TRP A  71      15.625  30.218  24.498  1.00 10.47           C  
ATOM    536  CG  TRP A  71      14.533  30.961  25.129  1.00 10.66           C  
ATOM    537  CD1 TRP A  71      13.595  30.480  26.007  1.00 14.59           C  
ATOM    538  CD2 TRP A  71      14.255  32.329  24.956  1.00 10.69           C  
ATOM    539  NE1 TRP A  71      12.744  31.499  26.412  1.00 13.26           N  
ATOM    540  CE2 TRP A  71      13.136  32.647  25.766  1.00 11.59           C  
ATOM    541  CE3 TRP A  71      14.867  33.356  24.203  1.00 12.63           C  
ATOM    542  CZ2 TRP A  71      12.604  33.919  25.817  1.00 10.07           C  
ATOM    543  CZ3 TRP A  71      14.342  34.628  24.269  1.00 11.14           C  
ATOM    544  CH2 TRP A  71      13.228  34.904  25.074  1.00 12.55           C  
ATOM    545  N   ASP A  72      16.975  28.187  22.542  1.00 11.70           N  
ATOM    546  CA  ASP A  72      18.235  27.439  22.172  1.00 11.83           C  
ATOM    547  C   ASP A  72      18.695  27.662  20.713  1.00 11.86           C  
ATOM    548  O   ASP A  72      19.887  27.684  20.376  1.00 10.41           O  
ATOM    549  CB  ASP A  72      18.103  25.952  22.547  1.00 13.84           C  
ATOM    550  CG  ASP A  72      18.076  25.729  24.101  1.00 14.88           C  
ATOM    551  OD1 ASP A  72      18.153  26.729  24.905  1.00 14.70           O  
ATOM    552  OD2 ASP A  72      17.987  24.551  24.534  1.00 19.44           O  
ATOM    553  N   LEU A  73      17.708  27.963  19.867  1.00 12.03           N  
ATOM    554  CA  LEU A  73      17.889  28.201  18.456  1.00 11.82           C  
ATOM    555  C   LEU A  73      17.759  29.655  18.072  1.00 10.90           C  
ATOM    556  O   LEU A  73      17.859  29.964  16.905  1.00  9.15           O  
ATOM    557  CB  LEU A  73      16.821  27.393  17.670  1.00 12.23           C  
ATOM    558  CG  LEU A  73      17.033  25.881  17.696  1.00 13.78           C  
ATOM    559  CD1 LEU A  73      15.802  25.116  17.025  1.00 17.13           C  
ATOM    560  CD2 LEU A  73      18.346  25.567  17.040  1.00 13.85           C  
ATOM    561  N   ALA A  74      17.501  30.540  19.032  1.00  7.93           N  
ATOM    562  CA  ALA A  74      17.153  31.920  18.744  1.00 10.04           C  
ATOM    563  C   ALA A  74      18.297  32.746  18.073  1.00 10.76           C  
ATOM    564  O   ALA A  74      19.488  32.653  18.460  1.00 11.24           O  
ATOM    565  CB  ALA A  74      16.706  32.654  20.010  1.00  8.22           C  
ATOM    566  N   ILE A  75      17.903  33.576  17.110  1.00 10.11           N  
ATOM    567  CA  ILE A  75      18.830  34.576  16.576  1.00 11.12           C  
ATOM    568  C   ILE A  75      19.222  35.583  17.664  1.00 11.91           C  
ATOM    569  O   ILE A  75      18.575  35.725  18.753  1.00 10.91           O  
ATOM    570  CB  ILE A  75      18.283  35.339  15.302  1.00 10.67           C  
ATOM    571  CG1 ILE A  75      16.979  36.117  15.620  1.00 12.27           C  
ATOM    572  CG2 ILE A  75      18.071  34.369  14.141  1.00 10.75           C  
ATOM    573  CD1 ILE A  75      16.613  37.190  14.615  1.00 11.94           C  
ATOM    574  N   ARG A  76      20.263  36.311  17.325  1.00 13.07           N  
ATOM    575  CA  ARG A  76      20.914  37.261  18.232  1.00 15.06           C  
ATOM    576  C   ARG A  76      19.937  38.318  18.735  1.00 13.33           C  
ATOM    577  O   ARG A  76      20.026  38.778  19.844  1.00 14.34           O  
ATOM    578  CB  ARG A  76      22.051  37.918  17.464  1.00 15.56           C  
ATOM    579  CG  ARG A  76      22.814  38.965  18.225  1.00 18.57           C  
ATOM    580  CD  ARG A  76      24.174  39.150  17.585  1.00 23.96           C  
ATOM    581  NE  ARG A  76      24.208  40.067  16.465  1.00 28.91           N  
ATOM    582  CZ  ARG A  76      25.351  40.473  15.890  1.00 33.19           C  
ATOM    583  NH1 ARG A  76      26.538  40.024  16.327  1.00 34.28           N  
ATOM    584  NH2 ARG A  76      25.306  41.336  14.857  1.00 34.62           N  
ATOM    585  N   ALA A  77      19.033  38.759  17.882  1.00 13.04           N  
ATOM    586  CA  ALA A  77      18.062  39.784  18.268  1.00 12.01           C  
ATOM    587  C   ALA A  77      17.209  39.329  19.460  1.00 11.22           C  
ATOM    588  O   ALA A  77      16.639  40.165  20.183  1.00 11.98           O  
ATOM    589  CB  ALA A  77      17.107  40.102  17.065  1.00 11.84           C  
ATOM    590  N   TYR A  78      17.085  38.029  19.655  1.00 10.58           N  
ATOM    591  CA  TYR A  78      16.350  37.503  20.818  1.00 11.65           C  
ATOM    592  C   TYR A  78      17.231  36.892  21.879  1.00 13.16           C  
ATOM    593  O   TYR A  78      16.799  36.718  22.975  1.00 13.09           O  
ATOM    594  CB  TYR A  78      15.336  36.446  20.380  1.00 11.93           C  
ATOM    595  CG  TYR A  78      14.321  37.024  19.471  1.00  9.41           C  
ATOM    596  CD1 TYR A  78      14.462  36.935  18.087  1.00 11.34           C  
ATOM    597  CD2 TYR A  78      13.197  37.651  19.989  1.00 13.89           C  
ATOM    598  CE1 TYR A  78      13.481  37.493  17.231  1.00 13.43           C  
ATOM    599  CE2 TYR A  78      12.231  38.230  19.147  1.00 13.84           C  
ATOM    600  CZ  TYR A  78      12.380  38.164  17.767  1.00 13.80           C  
ATOM    601  OH  TYR A  78      11.386  38.739  16.915  1.00 14.24           O  
ATOM    602  N   ASN A  79      18.448  36.496  21.515  1.00 13.24           N  
ATOM    603  CA  ASN A  79      19.348  35.792  22.444  1.00 13.46           C  
ATOM    604  C   ASN A  79      20.731  36.314  22.225  1.00 14.32           C  
ATOM    605  O   ASN A  79      21.402  35.956  21.240  1.00 15.96           O  
ATOM    606  CB  ASN A  79      19.284  34.273  22.225  1.00 12.14           C  
ATOM    607  CG  ASN A  79      20.057  33.500  23.277  1.00 13.60           C  
ATOM    608  OD1 ASN A  79      20.970  34.034  23.915  1.00  9.84           O  
ATOM    609  ND2 ASN A  79      19.731  32.218  23.427  1.00 11.37           N  
ATOM    610  N   LYS A  80      21.140  37.212  23.095  1.00 16.06           N  
ATOM    611  CA  LYS A  80      22.446  37.785  22.925  1.00 17.86           C  
ATOM    612  C   LYS A  80      23.624  36.844  23.097  1.00 16.61           C  
ATOM    613  O   LYS A  80      24.717  37.255  22.796  1.00 16.11           O  
ATOM    614  CB  LYS A  80      22.653  39.042  23.743  1.00 19.70           C  
ATOM    615  CG  LYS A  80      22.459  38.975  25.126  1.00 25.33           C  
ATOM    616  CD  LYS A  80      23.075  37.809  25.840  1.00 29.99           C  
ATOM    617  CE  LYS A  80      22.995  38.051  27.359  1.00 30.93           C  
ATOM    618  NZ  LYS A  80      23.857  39.264  27.758  1.00 38.19           N  
ATOM    619  N   GLU A  81      23.397  35.617  23.549  1.00 15.62           N  
ATOM    620  CA  GLU A  81      24.452  34.595  23.547  1.00 16.82           C  
ATOM    621  C   GLU A  81      24.818  34.147  22.106  1.00 15.96           C  
ATOM    622  O   GLU A  81      25.878  33.592  21.859  1.00 15.21           O  
ATOM    623  CB  GLU A  81      24.041  33.347  24.393  1.00 16.06           C  
ATOM    624  CG  GLU A  81      23.716  33.619  25.874  1.00 18.70           C  
ATOM    625  CD  GLU A  81      23.336  32.356  26.663  1.00 19.55           C  
ATOM    626  OE1 GLU A  81      22.709  32.447  27.765  1.00 19.79           O  
ATOM    627  OE2 GLU A  81      23.655  31.237  26.174  1.00 23.50           O  
ATOM    628  N   HIS A  82      23.929  34.370  21.149  1.00 14.91           N  
ATOM    629  CA  HIS A  82      24.067  33.730  19.850  1.00 13.96           C  
ATOM    630  C   HIS A  82      24.571  34.786  18.872  1.00 14.40           C  
ATOM    631  O   HIS A  82      23.963  35.047  17.852  1.00 12.53           O  
ATOM    632  CB  HIS A  82      22.732  33.102  19.431  1.00 12.79           C  
ATOM    633  CG  HIS A  82      22.312  31.963  20.308  1.00 13.27           C  
ATOM    634  ND1 HIS A  82      21.061  31.394  20.259  1.00  9.55           N  
ATOM    635  CD2 HIS A  82      23.007  31.268  21.251  1.00 13.51           C  
ATOM    636  CE1 HIS A  82      20.999  30.411  21.141  1.00 14.18           C  
ATOM    637  NE2 HIS A  82      22.167  30.302  21.749  1.00 10.51           N  
ATOM    638  N   GLN A  83      25.715  35.397  19.192  1.00 13.99           N  
ATOM    639  CA  GLN A  83      26.242  36.496  18.392  1.00 15.33           C  
ATOM    640  C   GLN A  83      26.443  36.245  16.887  1.00 14.79           C  
ATOM    641  O   GLN A  83      26.304  37.166  16.078  1.00 14.36           O  
ATOM    642  CB  GLN A  83      27.535  36.977  19.021  1.00 17.44           C  
ATOM    643  CG  GLN A  83      27.280  37.636  20.390  1.00 19.42           C  
ATOM    644  CD  GLN A  83      26.505  38.927  20.248  1.00 24.88           C  
ATOM    645  OE1 GLN A  83      26.951  39.831  19.552  1.00 30.74           O  
ATOM    646  NE2 GLN A  83      25.309  38.997  20.847  1.00 22.92           N  
ATOM    647  N   ASP A  84      26.750  35.028  16.506  1.00 16.33           N  
ATOM    648  CA  ASP A  84      26.916  34.706  15.073  1.00 17.20           C  
ATOM    649  C   ASP A  84      25.594  34.498  14.341  1.00 17.50           C  
ATOM    650  O   ASP A  84      25.582  34.261  13.102  1.00 19.48           O  
ATOM    651  CB  ASP A  84      27.718  33.422  14.923  1.00 18.55           C  
ATOM    652  CG  ASP A  84      29.127  33.577  15.434  1.00 21.39           C  
ATOM    653  OD1 ASP A  84      29.701  34.678  15.287  1.00 24.71           O  
ATOM    654  OD2 ASP A  84      29.621  32.595  15.989  1.00 27.18           O  
ATOM    655  N   GLN A  85      24.490  34.457  15.082  1.00 14.63           N  
ATOM    656  CA  GLN A  85      23.195  34.181  14.463  1.00 14.69           C  
ATOM    657  C   GLN A  85      22.479  35.483  14.127  1.00 15.21           C  
ATOM    658  O   GLN A  85      21.582  35.964  14.882  1.00 15.00           O  
ATOM    659  CB  GLN A  85      22.306  33.269  15.312  1.00 13.79           C  
ATOM    660  CG  GLN A  85      22.803  31.863  15.590  1.00 13.38           C  
ATOM    661  CD  GLN A  85      21.796  30.975  16.339  1.00 13.92           C  
ATOM    662  OE1 GLN A  85      22.124  30.333  17.366  1.00 11.26           O  
ATOM    663  NE2 GLN A  85      20.573  30.867  15.784  1.00 11.15           N  
ATOM    664  N   VAL A  86      22.871  36.071  12.990  1.00 13.88           N  
ATOM    665  CA  VAL A  86      22.228  37.265  12.528  1.00 13.17           C  
ATOM    666  C   VAL A  86      20.995  36.896  11.711  1.00 13.97           C  
ATOM    667  O   VAL A  86      19.915  37.508  11.871  1.00 16.88           O  
ATOM    668  CB  VAL A  86      23.206  38.149  11.738  1.00 13.95           C  
ATOM    669  CG1 VAL A  86      22.481  39.359  11.080  1.00 15.01           C  
ATOM    670  CG2 VAL A  86      24.419  38.618  12.701  1.00 16.50           C  
ATOM    671  N   ARG A  87      21.145  35.912  10.836  1.00 10.78           N  
ATOM    672  CA  ARG A  87      20.079  35.539   9.841  1.00  9.96           C  
ATOM    673  C   ARG A  87      19.331  34.241  10.201  1.00  8.32           C  
ATOM    674  O   ARG A  87      18.102  34.201  10.179  1.00 10.89           O  
ATOM    675  CB  ARG A  87      20.690  35.362   8.445  1.00  8.84           C  
ATOM    676  CG  ARG A  87      21.199  36.654   7.805  1.00  9.53           C  
ATOM    677  CD  ARG A  87      21.870  36.387   6.468  1.00  8.76           C  
ATOM    678  NE  ARG A  87      20.832  36.103   5.476  1.00  6.59           N  
ATOM    679  CZ  ARG A  87      21.042  35.537   4.290  1.00  8.72           C  
ATOM    680  NH1 ARG A  87      22.241  35.204   3.869  1.00 10.19           N  
ATOM    681  NH2 ARG A  87      20.026  35.326   3.493  1.00  8.59           N  
ATOM    682  N   ALA A  88      20.078  33.193  10.525  1.00  7.53           N  
ATOM    683  CA  ALA A  88      19.567  31.828  10.609  1.00  7.97           C  
ATOM    684  C   ALA A  88      19.218  31.524  12.046  1.00  6.70           C  
ATOM    685  O   ALA A  88      20.015  31.807  12.944  1.00  9.12           O  
ATOM    686  CB  ALA A  88      20.635  30.786  10.141  1.00  7.87           C  
ATOM    687  N   GLY A  89      18.101  30.858  12.227  1.00  6.62           N  
ATOM    688  CA  GLY A  89      17.636  30.400  13.529  1.00  7.57           C  
ATOM    689  C   GLY A  89      16.191  30.813  13.766  1.00  7.22           C  
ATOM    690  O   GLY A  89      15.405  31.114  12.826  1.00  9.11           O  
ATOM    691  N   TYR A  90      15.839  30.813  15.030  1.00  6.58           N  
ATOM    692  CA  TYR A  90      14.461  31.046  15.425  1.00  8.38           C  
ATOM    693  C   TYR A  90      14.177  32.524  15.771  1.00  7.87           C  
ATOM    694  O   TYR A  90      14.959  33.226  16.432  1.00  6.87           O  
ATOM    695  CB  TYR A  90      14.043  30.104  16.554  1.00  8.80           C  
ATOM    696  CG  TYR A  90      12.602  29.779  16.480  1.00  7.50           C  
ATOM    697  CD1 TYR A  90      12.156  28.691  15.734  1.00  9.83           C  
ATOM    698  CD2 TYR A  90      11.653  30.576  17.120  1.00  7.66           C  
ATOM    699  CE1 TYR A  90      10.790  28.354  15.644  1.00 10.76           C  
ATOM    700  CE2 TYR A  90      10.280  30.259  17.011  1.00  7.94           C  
ATOM    701  CZ  TYR A  90       9.882  29.178  16.277  1.00 11.14           C  
ATOM    702  OH  TYR A  90       8.552  28.871  16.132  1.00 14.59           O  
ATOM    703  N   TYR A  91      13.083  33.018  15.213  1.00  8.49           N  
ATOM    704  CA  TYR A  91      12.601  34.361  15.416  1.00  9.23           C  
ATOM    705  C   TYR A  91      11.348  34.217  16.289  1.00  9.25           C  
ATOM    706  O   TYR A  91      10.306  33.803  15.767  1.00 10.02           O  
ATOM    707  CB  TYR A  91      12.222  34.997  14.076  1.00 10.45           C  
ATOM    708  CG  TYR A  91      13.384  35.274  13.076  1.00 11.13           C  
ATOM    709  CD1 TYR A  91      14.355  34.325  12.805  1.00 11.52           C  
ATOM    710  CD2 TYR A  91      13.467  36.488  12.420  1.00 10.43           C  
ATOM    711  CE1 TYR A  91      15.332  34.556  11.876  1.00  9.09           C  
ATOM    712  CE2 TYR A  91      14.502  36.764  11.556  1.00 10.63           C  
ATOM    713  CZ  TYR A  91      15.406  35.825  11.272  1.00  8.19           C  
ATOM    714  OH  TYR A  91      16.447  36.121  10.404  1.00  9.65           O  
ATOM    715  N   LEU A  92      11.441  34.560  17.573  1.00  8.13           N  
ATOM    716  CA  LEU A  92      10.378  34.291  18.538  1.00  9.56           C  
ATOM    717  C   LEU A  92       9.218  35.303  18.391  1.00  9.59           C  
ATOM    718  O   LEU A  92       9.437  36.428  17.920  1.00  7.93           O  
ATOM    719  CB  LEU A  92      10.891  34.388  19.958  1.00  9.39           C  
ATOM    720  CG  LEU A  92      11.770  33.258  20.488  1.00 11.20           C  
ATOM    721  CD1 LEU A  92      13.124  33.239  19.788  1.00 10.73           C  
ATOM    722  CD2 LEU A  92      11.852  33.286  22.078  1.00  9.18           C  
ATOM    723  N   SER A  93       7.997  34.870  18.736  1.00 11.27           N  
ATOM    724  CA  SER A  93       6.883  35.752  18.898  1.00 13.69           C  
ATOM    725  C   SER A  93       7.018  36.405  20.258  1.00 16.24           C  
ATOM    726  O   SER A  93       7.721  35.921  21.116  1.00 13.29           O  
ATOM    727  CB  SER A  93       5.551  35.002  18.858  1.00 14.81           C  
ATOM    728  OG  SER A  93       5.424  34.076  19.899  1.00 18.17           O  
ATOM    729  N   ILE A  94       6.224  37.438  20.475  1.00 18.35           N  
ATOM    730  CA  ILE A  94       5.990  37.963  21.842  1.00 20.39           C  
ATOM    731  C   ILE A  94       4.490  37.986  22.188  1.00 21.83           C  
ATOM    732  O   ILE A  94       3.766  38.905  21.741  1.00 20.95           O  
ATOM    733  CB  ILE A  94       6.529  39.380  21.928  1.00 20.70           C  
ATOM    734  CG1 ILE A  94       7.861  39.456  21.127  1.00 18.96           C  
ATOM    735  CG2 ILE A  94       6.653  39.745  23.367  1.00 19.71           C  
ATOM    736  CD1 ILE A  94       8.655  40.772  21.255  1.00 21.01           C  
ATOM    737  N   PRO A  95       4.000  36.950  22.902  1.00 22.82           N  
ATOM    738  CA  PRO A  95       2.574  36.968  23.235  1.00 23.26           C  
ATOM    739  C   PRO A  95       2.148  38.348  23.810  1.00 23.38           C  
ATOM    740  O   PRO A  95       2.917  38.989  24.569  1.00 23.34           O  
ATOM    741  CB  PRO A  95       2.431  35.834  24.246  1.00 23.68           C  
ATOM    742  CG  PRO A  95       3.614  34.923  23.977  1.00 23.81           C  
ATOM    743  CD  PRO A  95       4.696  35.764  23.421  1.00 23.78           C  
ATOM    744  N   GLY A  96       0.990  38.830  23.374  1.00 23.78           N  
ATOM    745  CA  GLY A  96       0.544  40.187  23.697  1.00 23.59           C  
ATOM    746  C   GLY A  96       1.029  41.286  22.769  1.00 23.62           C  
ATOM    747  O   GLY A  96       0.426  42.382  22.745  1.00 23.59           O  
ATOM    748  N   LYS A  97       2.094  41.035  21.984  1.00 23.09           N  
ATOM    749  CA  LYS A  97       2.741  42.117  21.171  1.00 22.75           C  
ATOM    750  C   LYS A  97       3.156  41.867  19.673  1.00 23.12           C  
ATOM    751  O   LYS A  97       3.098  42.766  18.835  1.00 24.48           O  
ATOM    752  CB  LYS A  97       4.004  42.550  21.879  1.00 23.51           C  
ATOM    753  CG  LYS A  97       3.889  42.697  23.329  1.00 22.81           C  
ATOM    754  CD  LYS A  97       3.139  43.952  23.585  1.00 26.72           C  
ATOM    755  CE  LYS A  97       3.344  44.472  24.999  1.00 29.14           C  
ATOM    756  NZ  LYS A  97       2.349  45.547  25.231  1.00 27.65           N  
ATOM    757  N   LYS A  98       3.706  40.695  19.386  1.00 22.92           N  
ATOM    758  CA  LYS A  98       4.176  40.362  18.032  1.00 20.84           C  
ATOM    759  C   LYS A  98       3.759  38.926  17.816  1.00 18.34           C  
ATOM    760  O   LYS A  98       4.287  38.045  18.474  1.00 16.91           O  
ATOM    761  CB  LYS A  98       5.665  40.459  17.937  1.00 22.39           C  
ATOM    762  CG  LYS A  98       6.220  39.836  16.665  1.00 22.55           C  
ATOM    763  CD  LYS A  98       7.707  39.999  16.690  1.00 22.99           C  
ATOM    764  CE  LYS A  98       8.429  39.285  15.563  1.00 21.65           C  
ATOM    765  NZ  LYS A  98       8.469  37.791  15.727  1.00 19.46           N  
ATOM    766  N   ALA A  99       2.790  38.702  16.943  1.00 14.27           N  
ATOM    767  CA  ALA A  99       2.174  37.400  16.848  1.00 15.96           C  
ATOM    768  C   ALA A  99       3.063  36.395  16.087  1.00 14.81           C  
ATOM    769  O   ALA A  99       3.130  35.240  16.453  1.00 14.40           O  
ATOM    770  CB  ALA A  99       0.844  37.517  16.173  1.00 17.22           C  
ATOM    771  N   VAL A 100       3.638  36.850  14.979  1.00 14.28           N  
ATOM    772  CA  VAL A 100       4.352  35.995  14.032  1.00 13.47           C  
ATOM    773  C   VAL A 100       5.655  35.461  14.633  1.00 11.77           C  
ATOM    774  O   VAL A 100       6.313  36.090  15.453  1.00 10.59           O  
ATOM    775  CB  VAL A 100       4.604  36.707  12.641  1.00 14.26           C  
ATOM    776  CG1 VAL A 100       5.651  37.791  12.774  1.00 15.72           C  
ATOM    777  CG2 VAL A 100       5.154  35.727  11.596  1.00 16.89           C  
ATOM    778  N   GLU A 101       5.983  34.252  14.234  1.00 10.17           N  
ATOM    779  CA  GLU A 101       7.229  33.621  14.536  1.00 11.15           C  
ATOM    780  C   GLU A 101       7.668  32.782  13.335  1.00 10.46           C  
ATOM    781  O   GLU A 101       6.870  32.474  12.425  1.00  8.58           O  
ATOM    782  CB  GLU A 101       7.156  32.728  15.765  1.00 10.82           C  
ATOM    783  CG  GLU A 101       6.116  31.650  15.728  1.00  9.64           C  
ATOM    784  CD  GLU A 101       5.922  30.975  17.106  1.00 14.94           C  
ATOM    785  OE1 GLU A 101       4.871  31.270  17.731  1.00 14.02           O  
ATOM    786  OE2 GLU A 101       6.772  30.140  17.544  1.00 19.43           O  
ATOM    787  N   SER A 102       8.946  32.462  13.332  1.00 10.97           N  
ATOM    788  CA  SER A 102       9.576  31.799  12.182  1.00 10.93           C  
ATOM    789  C   SER A 102      10.927  31.182  12.466  1.00 11.23           C  
ATOM    790  O   SER A 102      11.591  31.538  13.458  1.00  9.55           O  
ATOM    791  CB  SER A 102       9.761  32.795  11.050  1.00 11.50           C  
ATOM    792  OG  SER A 102      10.754  33.764  11.338  1.00 11.92           O  
ATOM    793  N   PHE A 103      11.342  30.315  11.524  1.00  8.76           N  
ATOM    794  CA  PHE A 103      12.621  29.710  11.492  1.00  8.35           C  
ATOM    795  C   PHE A 103      13.290  29.953  10.131  1.00  8.56           C  
ATOM    796  O   PHE A 103      12.718  29.630   9.084  1.00  7.66           O  
ATOM    797  CB  PHE A 103      12.464  28.220  11.692  1.00  8.95           C  
ATOM    798  CG  PHE A 103      13.769  27.428  11.660  1.00  8.95           C  
ATOM    799  CD1 PHE A 103      14.688  27.481  12.723  1.00  9.56           C  
ATOM    800  CD2 PHE A 103      14.092  26.649  10.558  1.00  9.76           C  
ATOM    801  CE1 PHE A 103      15.917  26.700  12.658  1.00  6.28           C  
ATOM    802  CE2 PHE A 103      15.280  25.851  10.530  1.00 10.67           C  
ATOM    803  CZ  PHE A 103      16.182  25.913  11.557  1.00  9.43           C  
ATOM    804  N   CYS A 104      14.497  30.482  10.145  1.00  8.15           N  
ATOM    805  CA  CYS A 104      15.197  30.773   8.895  1.00  7.35           C  
ATOM    806  C   CYS A 104      16.430  29.918   8.780  1.00  8.26           C  
ATOM    807  O   CYS A 104      17.209  29.775   9.766  1.00  7.58           O  
ATOM    808  CB  CYS A 104      15.568  32.279   8.827  1.00  6.83           C  
ATOM    809  SG  CYS A 104      16.708  32.788   7.480  1.00  7.56           S  
ATOM    810  N   TYR A 105      16.612  29.345   7.594  1.00  7.37           N  
ATOM    811  CA  TYR A 105      17.844  28.723   7.266  1.00  7.06           C  
ATOM    812  C   TYR A 105      18.404  29.092   5.883  1.00  7.15           C  
ATOM    813  O   TYR A 105      17.692  29.579   4.979  1.00  4.83           O  
ATOM    814  CB  TYR A 105      17.770  27.209   7.434  1.00  7.93           C  
ATOM    815  CG  TYR A 105      16.784  26.501   6.514  1.00  6.91           C  
ATOM    816  CD1 TYR A 105      17.218  25.774   5.426  1.00  5.55           C  
ATOM    817  CD2 TYR A 105      15.429  26.471   6.847  1.00  8.86           C  
ATOM    818  CE1 TYR A 105      16.297  25.083   4.623  1.00  8.13           C  
ATOM    819  CE2 TYR A 105      14.457  25.792   6.053  1.00  7.38           C  
ATOM    820  CZ  TYR A 105      14.905  25.108   4.963  1.00  7.52           C  
ATOM    821  OH  TYR A 105      14.023  24.413   4.235  1.00  7.23           O  
ATOM    822  N   LEU A 106      19.724  28.881   5.780  1.00  6.81           N  
ATOM    823  CA  LEU A 106      20.512  29.269   4.618  1.00  7.24           C  
ATOM    824  C   LEU A 106      21.049  28.036   3.869  1.00  8.45           C  
ATOM    825  O   LEU A 106      20.723  26.895   4.122  1.00  8.97           O  
ATOM    826  CB  LEU A 106      21.682  30.167   5.124  1.00  6.97           C  
ATOM    827  CG  LEU A 106      21.371  31.351   6.024  1.00  8.27           C  
ATOM    828  CD1 LEU A 106      22.708  32.095   6.448  1.00  7.22           C  
ATOM    829  CD2 LEU A 106      20.348  32.288   5.314  1.00  7.90           C  
ATOM    830  N   ASN A 107      21.852  28.309   2.885  1.00  9.14           N  
ATOM    831  CA  ASN A 107      22.583  27.310   2.138  1.00  8.76           C  
ATOM    832  C   ASN A 107      23.194  26.231   3.025  1.00  7.95           C  
ATOM    833  O   ASN A 107      24.059  26.488   3.893  1.00  7.92           O  
ATOM    834  CB  ASN A 107      23.648  28.051   1.318  1.00  8.40           C  
ATOM    835  CG  ASN A 107      24.252  27.194   0.234  1.00 12.14           C  
ATOM    836  OD1 ASN A 107      24.292  25.934   0.319  1.00 10.52           O  
ATOM    837  ND2 ASN A 107      24.801  27.876  -0.759  1.00  9.34           N  
ATOM    838  N   PRO A 108      22.711  25.010   2.871  1.00  8.06           N  
ATOM    839  CA  PRO A 108      23.329  23.911   3.648  1.00  8.79           C  
ATOM    840  C   PRO A 108      24.817  23.698   3.414  1.00  8.26           C  
ATOM    841  O   PRO A 108      25.470  23.083   4.239  1.00  8.53           O  
ATOM    842  CB  PRO A 108      22.485  22.684   3.254  1.00  9.13           C  
ATOM    843  CG  PRO A 108      21.176  23.307   2.669  1.00  8.42           C  
ATOM    844  CD  PRO A 108      21.522  24.581   2.106  1.00  7.66           C  
ATOM    845  N   ASN A 109      25.345  24.204   2.292  1.00  8.50           N  
ATOM    846  CA  ASN A 109      26.746  24.134   2.008  1.00  7.97           C  
ATOM    847  C   ASN A 109      27.577  25.104   2.828  1.00  8.21           C  
ATOM    848  O   ASN A 109      28.795  24.998   2.812  1.00 10.04           O  
ATOM    849  CB  ASN A 109      27.030  24.310   0.531  1.00  6.45           C  
ATOM    850  CG  ASN A 109      26.551  23.108  -0.301  1.00  8.61           C  
ATOM    851  OD1 ASN A 109      26.629  21.944   0.131  1.00  6.91           O  
ATOM    852  ND2 ASN A 109      26.010  23.399  -1.460  1.00  6.99           N  
ATOM    853  N   PHE A 110      26.942  25.987   3.584  1.00  8.44           N  
ATOM    854  CA  PHE A 110      27.663  26.880   4.502  1.00  8.91           C  
ATOM    855  C   PHE A 110      27.975  26.071   5.752  1.00  9.54           C  
ATOM    856  O   PHE A 110      27.250  26.071   6.761  1.00  8.97           O  
ATOM    857  CB  PHE A 110      26.900  28.156   4.867  1.00  9.29           C  
ATOM    858  CG  PHE A 110      26.671  29.132   3.707  1.00  5.92           C  
ATOM    859  CD1 PHE A 110      27.381  29.025   2.461  1.00  8.53           C  
ATOM    860  CD2 PHE A 110      25.710  30.168   3.876  1.00  6.34           C  
ATOM    861  CE1 PHE A 110      27.156  29.926   1.429  1.00  7.43           C  
ATOM    862  CE2 PHE A 110      25.485  31.065   2.869  1.00  7.12           C  
ATOM    863  CZ  PHE A 110      26.211  30.944   1.641  1.00  7.00           C  
ATOM    864  N   THR A 111      29.051  25.317   5.613  1.00  9.04           N  
ATOM    865  CA  THR A 111      29.544  24.408   6.649  1.00 10.13           C  
ATOM    866  C   THR A 111      30.741  25.062   7.371  1.00 11.04           C  
ATOM    867  O   THR A 111      31.241  26.089   6.954  1.00  9.52           O  
ATOM    868  CB  THR A 111      29.975  23.054   6.004  1.00 10.83           C  
ATOM    869  OG1 THR A 111      30.832  23.305   4.898  1.00 12.52           O  
ATOM    870  CG2 THR A 111      28.733  22.259   5.405  1.00  7.88           C  
ATOM    871  N   PRO A 112      31.146  24.525   8.519  1.00 12.64           N  
ATOM    872  CA  PRO A 112      32.280  25.134   9.190  1.00 13.39           C  
ATOM    873  C   PRO A 112      33.561  25.295   8.378  1.00 14.32           C  
ATOM    874  O   PRO A 112      34.288  26.265   8.595  1.00 13.79           O  
ATOM    875  CB  PRO A 112      32.506  24.158  10.347  1.00 15.83           C  
ATOM    876  CG  PRO A 112      31.064  23.698  10.690  1.00 14.89           C  
ATOM    877  CD  PRO A 112      30.502  23.461   9.347  1.00 12.46           C  
ATOM    878  N   ASP A 113      33.808  24.413   7.402  1.00 14.61           N  
ATOM    879  CA  ASP A 113      34.985  24.512   6.510  1.00 14.87           C  
ATOM    880  C   ASP A 113      34.781  25.400   5.275  1.00 13.26           C  
ATOM    881  O   ASP A 113      35.720  25.601   4.502  1.00 12.60           O  
ATOM    882  CB  ASP A 113      35.443  23.081   6.035  1.00 17.19           C  
ATOM    883  CG  ASP A 113      34.252  22.197   5.364  1.00 22.72           C  
ATOM    884  OD1 ASP A 113      33.166  22.732   5.082  1.00 28.10           O  
ATOM    885  OD2 ASP A 113      34.381  20.946   5.190  1.00 20.33           O  
ATOM    886  N   HIS A 114      33.569  25.908   5.041  1.00 11.54           N  
ATOM    887  CA  HIS A 114      33.323  26.748   3.869  1.00 11.20           C  
ATOM    888  C   HIS A 114      34.183  27.988   3.952  1.00 10.68           C  
ATOM    889  O   HIS A 114      34.292  28.572   5.035  1.00 10.96           O  
ATOM    890  CB  HIS A 114      31.836  27.111   3.795  1.00 10.92           C  
ATOM    891  CG  HIS A 114      31.443  27.779   2.528  1.00 10.00           C  
ATOM    892  ND1 HIS A 114      31.805  29.069   2.234  1.00  9.51           N  
ATOM    893  CD2 HIS A 114      30.699  27.346   1.484  1.00 11.43           C  
ATOM    894  CE1 HIS A 114      31.308  29.416   1.061  1.00 11.65           C  
ATOM    895  NE2 HIS A 114      30.613  28.395   0.590  1.00 12.12           N  
ATOM    896  N   PRO A 115      34.871  28.350   2.844  1.00 12.28           N  
ATOM    897  CA  PRO A 115      35.786  29.491   2.871  1.00 11.62           C  
ATOM    898  C   PRO A 115      35.154  30.803   3.362  1.00 11.21           C  
ATOM    899  O   PRO A 115      35.849  31.647   3.988  1.00  9.93           O  
ATOM    900  CB  PRO A 115      36.283  29.602   1.421  1.00 13.58           C  
ATOM    901  CG  PRO A 115      35.736  28.446   0.713  1.00 15.36           C  
ATOM    902  CD  PRO A 115      34.832  27.688   1.527  1.00 11.89           C  
ATOM    903  N   ARG A 116      33.876  31.026   3.075  1.00 10.36           N  
ATOM    904  CA  ARG A 116      33.237  32.243   3.531  1.00 10.08           C  
ATOM    905  C   ARG A 116      32.889  32.207   4.981  1.00 10.03           C  
ATOM    906  O   ARG A 116      32.798  33.254   5.597  1.00 11.09           O  
ATOM    907  CB  ARG A 116      31.959  32.556   2.733  1.00 10.64           C  
ATOM    908  CG  ARG A 116      32.193  32.850   1.298  1.00 12.70           C  
ATOM    909  CD  ARG A 116      32.883  34.214   1.196  1.00 17.78           C  
ATOM    910  NE  ARG A 116      32.897  34.633  -0.180  1.00 22.57           N  
ATOM    911  CZ  ARG A 116      33.332  35.791  -0.622  1.00 21.91           C  
ATOM    912  NH1 ARG A 116      33.817  36.704   0.201  1.00 25.69           N  
ATOM    913  NH2 ARG A 116      33.276  36.021  -1.923  1.00 27.16           N  
ATOM    914  N   ILE A 117      32.674  31.010   5.536  1.00  9.56           N  
ATOM    915  CA  ILE A 117      32.425  30.824   6.944  1.00 10.23           C  
ATOM    916  C   ILE A 117      33.760  30.979   7.717  1.00 11.30           C  
ATOM    917  O   ILE A 117      33.805  31.652   8.765  1.00 11.78           O  
ATOM    918  CB  ILE A 117      31.756  29.459   7.273  1.00  9.76           C  
ATOM    919  CG1 ILE A 117      30.332  29.379   6.666  1.00  8.83           C  
ATOM    920  CG2 ILE A 117      31.664  29.261   8.780  1.00 12.43           C  
ATOM    921  CD1 ILE A 117      29.304  30.461   7.208  1.00  9.99           C  
ATOM    922  N   GLN A 118      34.822  30.380   7.188  1.00 10.87           N  
ATOM    923  CA  GLN A 118      36.173  30.595   7.722  1.00 12.27           C  
ATOM    924  C   GLN A 118      36.564  32.077   7.778  1.00 12.26           C  
ATOM    925  O   GLN A 118      37.159  32.523   8.776  1.00 13.23           O  
ATOM    926  CB  GLN A 118      37.207  29.798   6.901  1.00 12.13           C  
ATOM    927  CG  GLN A 118      37.147  28.310   7.226  1.00 10.40           C  
ATOM    928  CD  GLN A 118      37.664  27.941   8.583  1.00 18.09           C  
ATOM    929  OE1 GLN A 118      38.754  28.360   8.975  1.00 21.50           O  
ATOM    930  NE2 GLN A 118      36.870  27.132   9.334  1.00 18.66           N  
ATOM    931  N   ALA A 119      36.276  32.817   6.705  1.00 12.91           N  
ATOM    932  CA  ALA A 119      36.572  34.246   6.659  1.00 13.54           C  
ATOM    933  C   ALA A 119      35.645  35.083   7.513  1.00 15.77           C  
ATOM    934  O   ALA A 119      35.877  36.287   7.656  1.00 16.58           O  
ATOM    935  CB  ALA A 119      36.542  34.762   5.273  1.00 12.56           C  
ATOM    936  N   LYS A 120      34.584  34.480   8.042  1.00 16.34           N  
ATOM    937  CA  LYS A 120      33.551  35.196   8.779  1.00 16.05           C  
ATOM    938  C   LYS A 120      32.936  36.325   7.958  1.00 15.69           C  
ATOM    939  O   LYS A 120      32.703  37.478   8.466  1.00 14.31           O  
ATOM    940  CB  LYS A 120      34.115  35.665  10.136  1.00 18.56           C  
ATOM    941  CG  LYS A 120      34.416  34.504  11.051  1.00 15.83           C  
ATOM    942  CD  LYS A 120      34.700  35.026  12.434  1.00 22.32           C  
ATOM    943  CE  LYS A 120      34.819  33.899  13.467  1.00 25.83           C  
ATOM    944  NZ  LYS A 120      33.494  33.230  13.552  1.00 32.76           N  
ATOM    945  N   THR A 121      32.680  36.023   6.689  1.00 13.98           N  
ATOM    946  CA  THR A 121      32.130  37.026   5.786  1.00 14.76           C  
ATOM    947  C   THR A 121      30.655  37.344   6.190  1.00 13.61           C  
ATOM    948  O   THR A 121      29.868  36.435   6.343  1.00 11.02           O  
ATOM    949  CB  THR A 121      32.141  36.582   4.335  1.00 15.38           C  
ATOM    950  OG1 THR A 121      33.441  36.171   3.964  1.00 19.02           O  
ATOM    951  CG2 THR A 121      31.733  37.700   3.394  1.00 15.83           C  
ATOM    952  N   PRO A 122      30.273  38.629   6.271  1.00 14.96           N  
ATOM    953  CA  PRO A 122      28.884  38.973   6.632  1.00 15.01           C  
ATOM    954  C   PRO A 122      27.869  38.230   5.717  1.00 13.60           C  
ATOM    955  O   PRO A 122      28.161  38.014   4.528  1.00 12.33           O  
ATOM    956  CB  PRO A 122      28.790  40.489   6.361  1.00 16.01           C  
ATOM    957  CG  PRO A 122      30.254  41.001   6.457  1.00 16.45           C  
ATOM    958  CD  PRO A 122      31.095  39.834   5.959  1.00 16.98           C  
ATOM    959  N   THR A 123      26.735  37.866   6.314  1.00 12.38           N  
ATOM    960  CA  THR A 123      25.545  37.235   5.651  1.00 13.33           C  
ATOM    961  C   THR A 123      25.710  35.751   5.413  1.00 13.34           C  
ATOM    962  O   THR A 123      24.727  35.089   5.048  1.00 14.19           O  
ATOM    963  CB  THR A 123      25.038  37.938   4.296  1.00 13.84           C  
ATOM    964  OG1 THR A 123      25.916  37.655   3.216  1.00 12.22           O  
ATOM    965  CG2 THR A 123      24.954  39.482   4.448  1.00 12.84           C  
ATOM    966  N   HIS A 124      26.931  35.225   5.599  1.00 12.16           N  
ATOM    967  CA  HIS A 124      27.177  33.767   5.623  1.00 11.26           C  
ATOM    968  C   HIS A 124      27.152  33.214   7.079  1.00 10.71           C  
ATOM    969  O   HIS A 124      27.779  33.740   7.951  1.00  9.41           O  
ATOM    970  CB  HIS A 124      28.533  33.453   5.001  1.00 10.18           C  
ATOM    971  CG  HIS A 124      28.722  34.004   3.628  1.00  8.63           C  
ATOM    972  ND1 HIS A 124      29.015  35.327   3.400  1.00 11.76           N  
ATOM    973  CD2 HIS A 124      28.725  33.407   2.416  1.00 10.28           C  
ATOM    974  CE1 HIS A 124      29.158  35.532   2.096  1.00 11.01           C  
ATOM    975  NE2 HIS A 124      28.976  34.389   1.474  1.00  9.61           N  
ATOM    976  N   GLU A 125      26.368  32.182   7.341  1.00 11.04           N  
ATOM    977  CA  GLU A 125      26.328  31.528   8.667  1.00 11.45           C  
ATOM    978  C   GLU A 125      26.048  30.071   8.503  1.00 10.10           C  
ATOM    979  O   GLU A 125      25.435  29.639   7.517  1.00 10.36           O  
ATOM    980  CB  GLU A 125      25.225  32.098   9.542  1.00 11.46           C  
ATOM    981  CG  GLU A 125      25.261  33.611   9.751  1.00 14.92           C  
ATOM    982  CD  GLU A 125      23.951  34.071  10.342  1.00 14.57           C  
ATOM    983  OE1 GLU A 125      23.176  33.205  10.842  1.00 14.49           O  
ATOM    984  OE2 GLU A 125      23.696  35.275  10.313  1.00 14.22           O  
ATOM    985  N   VAL A 126      26.471  29.309   9.496  1.00 10.82           N  
ATOM    986  CA  VAL A 126      26.194  27.888   9.559  1.00 10.13           C  
ATOM    987  C   VAL A 126      24.778  27.699  10.168  1.00 10.60           C  
ATOM    988  O   VAL A 126      24.532  28.138  11.286  1.00  8.92           O  
ATOM    989  CB  VAL A 126      27.247  27.094  10.390  1.00 10.56           C  
ATOM    990  CG1 VAL A 126      26.951  25.637  10.350  1.00 12.49           C  
ATOM    991  CG2 VAL A 126      28.731  27.347   9.935  1.00  9.35           C  
ATOM    992  N   ASN A 127      23.906  26.943   9.497  1.00  9.32           N  
ATOM    993  CA  ASN A 127      22.575  26.732  10.022  1.00  9.59           C  
ATOM    994  C   ASN A 127      22.579  26.090  11.379  1.00  8.94           C  
ATOM    995  O   ASN A 127      23.417  25.294  11.661  1.00  8.25           O  
ATOM    996  CB  ASN A 127      21.760  25.889   9.059  1.00 10.18           C  
ATOM    997  CG  ASN A 127      21.456  26.619   7.768  1.00  9.88           C  
ATOM    998  OD1 ASN A 127      21.309  27.826   7.775  1.00  7.18           O  
ATOM    999  ND2 ASN A 127      21.366  25.868   6.647  1.00 10.52           N  
ATOM   1000  N   VAL A 128      21.588  26.446  12.200  1.00 10.10           N  
ATOM   1001  CA  VAL A 128      21.283  25.759  13.465  1.00  9.55           C  
ATOM   1002  C   VAL A 128      20.002  24.921  13.308  1.00 10.18           C  
ATOM   1003  O   VAL A 128      19.090  25.323  12.580  1.00 10.73           O  
ATOM   1004  CB  VAL A 128      21.149  26.759  14.606  1.00 10.15           C  
ATOM   1005  CG1 VAL A 128      22.507  27.508  14.845  1.00 11.16           C  
ATOM   1006  CG2 VAL A 128      19.980  27.770  14.340  1.00  9.10           C  
ATOM   1007  N   TRP A 129      19.975  23.733  13.908  1.00  9.81           N  
ATOM   1008  CA  TRP A 129      18.865  22.819  13.804  1.00 11.00           C  
ATOM   1009  C   TRP A 129      18.469  22.328  15.174  1.00 11.95           C  
ATOM   1010  O   TRP A 129      19.291  22.287  16.036  1.00 11.03           O  
ATOM   1011  CB  TRP A 129      19.202  21.647  12.900  1.00 10.31           C  
ATOM   1012  CG  TRP A 129      19.577  22.098  11.510  1.00  7.94           C  
ATOM   1013  CD1 TRP A 129      20.800  22.225  11.015  1.00  8.97           C  
ATOM   1014  CD2 TRP A 129      18.664  22.437  10.435  1.00  6.71           C  
ATOM   1015  NE1 TRP A 129      20.739  22.619   9.681  1.00  8.76           N  
ATOM   1016  CE2 TRP A 129      19.436  22.788   9.328  1.00 10.28           C  
ATOM   1017  CE3 TRP A 129      17.284  22.444  10.310  1.00  9.23           C  
ATOM   1018  CZ2 TRP A 129      18.881  23.133   8.117  1.00  7.82           C  
ATOM   1019  CZ3 TRP A 129      16.717  22.834   9.078  1.00 10.01           C  
ATOM   1020  CH2 TRP A 129      17.521  23.162   8.024  1.00  9.13           C  
ATOM   1021  N   PRO A 130      17.197  21.964  15.364  1.00 13.73           N  
ATOM   1022  CA  PRO A 130      16.768  21.363  16.620  1.00 12.99           C  
ATOM   1023  C   PRO A 130      17.335  19.957  16.697  1.00 15.05           C  
ATOM   1024  O   PRO A 130      17.996  19.483  15.735  1.00 13.09           O  
ATOM   1025  CB  PRO A 130      15.245  21.302  16.478  1.00 14.29           C  
ATOM   1026  CG  PRO A 130      14.942  21.324  15.086  1.00 14.54           C  
ATOM   1027  CD  PRO A 130      16.090  22.080  14.395  1.00 13.80           C  
ATOM   1028  N   ASP A 131      17.125  19.324  17.841  1.00 15.53           N  
ATOM   1029  CA  ASP A 131      17.597  18.009  18.107  1.00 15.67           C  
ATOM   1030  C   ASP A 131      16.834  17.009  17.218  1.00 14.61           C  
ATOM   1031  O   ASP A 131      15.604  17.054  17.150  1.00 13.12           O  
ATOM   1032  CB  ASP A 131      17.336  17.717  19.577  1.00 17.67           C  
ATOM   1033  CG  ASP A 131      17.568  16.236  19.949  1.00 22.76           C  
ATOM   1034  OD1 ASP A 131      18.568  15.533  19.525  1.00 38.41           O  
ATOM   1035  OD2 ASP A 131      16.695  15.746  20.705  1.00 37.97           O  
ATOM   1036  N   GLU A 132      17.583  16.134  16.578  1.00 13.29           N  
ATOM   1037  CA  GLU A 132      17.054  15.171  15.658  1.00 15.29           C  
ATOM   1038  C   GLU A 132      16.041  14.252  16.327  1.00 15.34           C  
ATOM   1039  O   GLU A 132      15.035  13.896  15.737  1.00 13.17           O  
ATOM   1040  CB  GLU A 132      18.198  14.366  15.073  1.00 15.20           C  
ATOM   1041  CG  GLU A 132      17.776  13.121  14.209  1.00 15.81           C  
ATOM   1042  CD  GLU A 132      17.072  13.481  12.905  1.00 17.10           C  
ATOM   1043  OE1 GLU A 132      17.394  14.515  12.291  1.00 18.44           O  
ATOM   1044  OE2 GLU A 132      16.222  12.681  12.465  1.00 14.99           O  
ATOM   1045  N   THR A 133      16.293  13.872  17.574  1.00 16.88           N  
ATOM   1046  CA  THR A 133      15.415  12.870  18.217  1.00 17.80           C  
ATOM   1047  C   THR A 133      14.111  13.600  18.539  1.00 17.39           C  
ATOM   1048  O   THR A 133      13.073  12.968  18.527  1.00 18.17           O  
ATOM   1049  CB  THR A 133      16.083  12.258  19.475  1.00 18.64           C  
ATOM   1050  OG1 THR A 133      16.415  13.331  20.348  1.00 25.09           O  
ATOM   1051  CG2 THR A 133      17.388  11.596  19.080  1.00 19.03           C  
ATOM   1052  N   LYS A 134      14.121  14.937  18.683  1.00 15.99           N  
ATOM   1053  CA  LYS A 134      12.860  15.655  18.957  1.00 16.01           C  
ATOM   1054  C   LYS A 134      12.080  16.028  17.715  1.00 15.42           C  
ATOM   1055  O   LYS A 134      10.878  16.274  17.798  1.00 13.12           O  
ATOM   1056  CB  LYS A 134      13.118  16.925  19.741  1.00 17.38           C  
ATOM   1057  CG  LYS A 134      13.932  16.698  21.043  1.00 21.91           C  
ATOM   1058  CD  LYS A 134      13.132  16.922  22.278  1.00 29.85           C  
ATOM   1059  CE  LYS A 134      13.867  17.882  23.311  1.00 30.62           C  
ATOM   1060  NZ  LYS A 134      13.594  19.359  23.047  1.00 32.20           N  
ATOM   1061  N   HIS A 135      12.788  16.100  16.584  1.00 14.69           N  
ATOM   1062  CA  HIS A 135      12.216  16.489  15.295  1.00 14.02           C  
ATOM   1063  C   HIS A 135      12.753  15.566  14.211  1.00 14.21           C  
ATOM   1064  O   HIS A 135      13.464  15.998  13.272  1.00 13.27           O  
ATOM   1065  CB  HIS A 135      12.655  17.936  15.021  1.00 14.33           C  
ATOM   1066  CG  HIS A 135      12.060  18.914  15.970  1.00 12.34           C  
ATOM   1067  ND1 HIS A 135      10.873  19.548  15.713  1.00 15.58           N  
ATOM   1068  CD2 HIS A 135      12.448  19.323  17.205  1.00 14.14           C  
ATOM   1069  CE1 HIS A 135      10.557  20.329  16.739  1.00 16.11           C  
ATOM   1070  NE2 HIS A 135      11.504  20.216  17.657  1.00 14.31           N  
ATOM   1071  N   PRO A 136      12.387  14.289  14.297  1.00 14.58           N  
ATOM   1072  CA  PRO A 136      13.045  13.335  13.422  1.00 14.26           C  
ATOM   1073  C   PRO A 136      12.753  13.660  11.955  1.00 12.50           C  
ATOM   1074  O   PRO A 136      11.628  13.940  11.601  1.00 12.86           O  
ATOM   1075  CB  PRO A 136      12.424  11.975  13.805  1.00 15.25           C  
ATOM   1076  CG  PRO A 136      11.365  12.221  14.801  1.00 16.84           C  
ATOM   1077  CD  PRO A 136      11.313  13.689  15.136  1.00 15.59           C  
ATOM   1078  N   GLY A 137      13.753  13.628  11.104  1.00 12.23           N  
ATOM   1079  CA  GLY A 137      13.504  13.860   9.705  1.00 11.81           C  
ATOM   1080  C   GLY A 137      13.489  15.331   9.291  1.00 11.11           C  
ATOM   1081  O   GLY A 137      13.623  15.617   8.096  1.00  9.09           O  
ATOM   1082  N   PHE A 138      13.351  16.258  10.251  1.00 10.28           N  
ATOM   1083  CA  PHE A 138      13.154  17.659   9.892  1.00 10.41           C  
ATOM   1084  C   PHE A 138      14.320  18.325   9.116  1.00  9.14           C  
ATOM   1085  O   PHE A 138      14.083  18.949   8.068  1.00  6.98           O  
ATOM   1086  CB  PHE A 138      12.775  18.513  11.116  1.00 10.46           C  
ATOM   1087  CG  PHE A 138      12.671  19.984  10.813  1.00 11.36           C  
ATOM   1088  CD1 PHE A 138      11.608  20.474  10.048  1.00 11.51           C  
ATOM   1089  CD2 PHE A 138      13.597  20.888  11.346  1.00 10.35           C  
ATOM   1090  CE1 PHE A 138      11.533  21.843   9.737  1.00  9.17           C  
ATOM   1091  CE2 PHE A 138      13.497  22.231  11.070  1.00 10.34           C  
ATOM   1092  CZ  PHE A 138      12.504  22.709  10.250  1.00  9.46           C  
ATOM   1093  N   GLN A 139      15.530  18.198   9.647  1.00  8.21           N  
ATOM   1094  CA  GLN A 139      16.695  18.796   9.055  1.00 10.11           C  
ATOM   1095  C   GLN A 139      16.908  18.231   7.643  1.00  9.98           C  
ATOM   1096  O   GLN A 139      17.163  18.976   6.716  1.00 10.56           O  
ATOM   1097  CB  GLN A 139      17.957  18.631   9.915  1.00  9.60           C  
ATOM   1098  CG  GLN A 139      19.229  18.992   9.128  1.00 10.01           C  
ATOM   1099  CD  GLN A 139      20.452  18.895   9.967  1.00 12.02           C  
ATOM   1100  OE1 GLN A 139      20.362  18.542  11.161  1.00 12.47           O  
ATOM   1101  NE2 GLN A 139      21.614  19.195   9.369  1.00 11.75           N  
ATOM   1102  N   ASP A 140      16.790  16.916   7.474  1.00 10.02           N  
ATOM   1103  CA  ASP A 140      16.984  16.330   6.156  1.00 10.59           C  
ATOM   1104  C   ASP A 140      15.892  16.735   5.174  1.00  9.88           C  
ATOM   1105  O   ASP A 140      16.168  16.953   4.003  1.00  8.37           O  
ATOM   1106  CB  ASP A 140      17.032  14.815   6.258  1.00 11.63           C  
ATOM   1107  CG  ASP A 140      18.162  14.353   7.150  1.00 15.04           C  
ATOM   1108  OD1 ASP A 140      19.286  14.908   7.072  1.00 19.73           O  
ATOM   1109  OD2 ASP A 140      17.873  13.470   7.955  1.00 19.66           O  
ATOM   1110  N   PHE A 141      14.653  16.800   5.644  1.00  9.40           N  
ATOM   1111  CA  PHE A 141      13.562  17.341   4.810  1.00  8.81           C  
ATOM   1112  C   PHE A 141      13.782  18.809   4.388  1.00  7.87           C  
ATOM   1113  O   PHE A 141      13.653  19.160   3.248  1.00  7.09           O  
ATOM   1114  CB  PHE A 141      12.228  17.289   5.494  1.00  9.89           C  
ATOM   1115  CG  PHE A 141      11.150  17.940   4.660  1.00 10.91           C  
ATOM   1116  CD1 PHE A 141      10.596  17.237   3.584  1.00 15.24           C  
ATOM   1117  CD2 PHE A 141      10.784  19.254   4.881  1.00 11.04           C  
ATOM   1118  CE1 PHE A 141       9.692  17.833   2.742  1.00 15.45           C  
ATOM   1119  CE2 PHE A 141       9.889  19.853   4.070  1.00 12.89           C  
ATOM   1120  CZ  PHE A 141       9.332  19.146   2.993  1.00 11.87           C  
ATOM   1121  N   ALA A 142      14.153  19.639   5.346  1.00  8.31           N  
ATOM   1122  CA  ALA A 142      14.357  21.035   5.159  1.00  7.70           C  
ATOM   1123  C   ALA A 142      15.536  21.292   4.206  1.00  7.53           C  
ATOM   1124  O   ALA A 142      15.472  22.161   3.341  1.00  6.31           O  
ATOM   1125  CB  ALA A 142      14.542  21.701   6.516  1.00  7.76           C  
ATOM   1126  N   GLU A 143      16.600  20.526   4.355  1.00  8.29           N  
ATOM   1127  CA  GLU A 143      17.767  20.695   3.462  1.00  9.01           C  
ATOM   1128  C   GLU A 143      17.384  20.254   2.058  1.00  8.36           C  
ATOM   1129  O   GLU A 143      17.725  20.932   1.097  1.00  8.67           O  
ATOM   1130  CB  GLU A 143      18.987  19.920   4.007  1.00  9.56           C  
ATOM   1131  CG  GLU A 143      19.547  20.600   5.287  1.00  7.85           C  
ATOM   1132  CD  GLU A 143      20.777  19.841   5.868  1.00 12.36           C  
ATOM   1133  OE1 GLU A 143      20.975  18.682   5.501  1.00 16.95           O  
ATOM   1134  OE2 GLU A 143      21.507  20.440   6.676  1.00 12.81           O  
ATOM   1135  N   GLN A 144      16.667  19.126   1.947  1.00  9.75           N  
ATOM   1136  CA  GLN A 144      16.151  18.694   0.681  1.00  9.02           C  
ATOM   1137  C   GLN A 144      15.238  19.747   0.028  1.00  8.60           C  
ATOM   1138  O   GLN A 144      15.292  19.979  -1.203  1.00  8.79           O  
ATOM   1139  CB  GLN A 144      15.483  17.260   0.774  1.00  9.80           C  
ATOM   1140  CG  GLN A 144      15.063  16.687  -0.637  1.00 10.13           C  
ATOM   1141  CD  GLN A 144      16.229  16.542  -1.595  1.00 13.61           C  
ATOM   1142  OE1 GLN A 144      17.110  15.711  -1.341  1.00 20.07           O  
ATOM   1143  NE2 GLN A 144      16.212  17.243  -2.729  1.00 12.78           N  
ATOM   1144  N   TYR A 145      14.379  20.370   0.844  1.00  8.10           N  
ATOM   1145  CA  TYR A 145      13.459  21.400   0.324  1.00  7.84           C  
ATOM   1146  C   TYR A 145      14.296  22.541  -0.301  1.00  7.81           C  
ATOM   1147  O   TYR A 145      14.008  23.024  -1.425  1.00  8.05           O  
ATOM   1148  CB  TYR A 145      12.509  21.960   1.415  1.00  6.86           C  
ATOM   1149  CG  TYR A 145      11.644  23.053   0.819  1.00  6.04           C  
ATOM   1150  CD1 TYR A 145      10.832  22.765  -0.222  1.00  7.03           C  
ATOM   1151  CD2 TYR A 145      11.745  24.374   1.218  1.00  7.06           C  
ATOM   1152  CE1 TYR A 145      10.069  23.752  -0.867  1.00  8.34           C  
ATOM   1153  CE2 TYR A 145      10.962  25.410   0.601  1.00  7.41           C  
ATOM   1154  CZ  TYR A 145      10.181  25.088  -0.443  1.00  5.52           C  
ATOM   1155  OH  TYR A 145       9.403  25.987  -1.057  1.00  5.23           O  
ATOM   1156  N   TYR A 146      15.292  22.995   0.423  1.00  6.98           N  
ATOM   1157  CA  TYR A 146      16.180  24.007  -0.106  1.00  6.84           C  
ATOM   1158  C   TYR A 146      16.622  23.664  -1.535  1.00  8.28           C  
ATOM   1159  O   TYR A 146      16.485  24.502  -2.442  1.00  7.59           O  
ATOM   1160  CB  TYR A 146      17.372  24.207   0.810  1.00  7.92           C  
ATOM   1161  CG  TYR A 146      18.223  25.458   0.566  1.00  6.31           C  
ATOM   1162  CD1 TYR A 146      18.095  26.612   1.395  1.00  3.27           C  
ATOM   1163  CD2 TYR A 146      19.159  25.488  -0.485  1.00  5.31           C  
ATOM   1164  CE1 TYR A 146      18.928  27.721   1.209  1.00  6.12           C  
ATOM   1165  CE2 TYR A 146      19.955  26.601  -0.708  1.00  5.81           C  
ATOM   1166  CZ  TYR A 146      19.825  27.716   0.118  1.00  6.96           C  
ATOM   1167  OH  TYR A 146      20.624  28.787  -0.174  1.00  9.57           O  
ATOM   1168  N   TRP A 147      17.067  22.425  -1.773  1.00  8.66           N  
ATOM   1169  CA  TRP A 147      17.534  22.060  -3.124  1.00  8.52           C  
ATOM   1170  C   TRP A 147      16.380  21.953  -4.156  1.00  7.41           C  
ATOM   1171  O   TRP A 147      16.571  22.283  -5.305  1.00  6.02           O  
ATOM   1172  CB  TRP A 147      18.493  20.827  -3.072  1.00  9.23           C  
ATOM   1173  CG  TRP A 147      19.703  21.154  -2.248  1.00  6.59           C  
ATOM   1174  CD1 TRP A 147      20.128  20.512  -1.097  1.00  8.40           C  
ATOM   1175  CD2 TRP A 147      20.632  22.248  -2.468  1.00  5.69           C  
ATOM   1176  NE1 TRP A 147      21.212  21.176  -0.581  1.00  8.80           N  
ATOM   1177  CE2 TRP A 147      21.551  22.240  -1.381  1.00  7.87           C  
ATOM   1178  CE3 TRP A 147      20.735  23.258  -3.420  1.00  9.08           C  
ATOM   1179  CZ2 TRP A 147      22.576  23.174  -1.260  1.00  7.29           C  
ATOM   1180  CZ3 TRP A 147      21.736  24.202  -3.293  1.00  8.36           C  
ATOM   1181  CH2 TRP A 147      22.667  24.145  -2.212  1.00  8.48           C  
ATOM   1182  N   ASP A 148      15.176  21.598  -3.722  1.00  7.62           N  
ATOM   1183  CA  ASP A 148      14.033  21.450  -4.625  1.00  7.78           C  
ATOM   1184  C   ASP A 148      13.627  22.868  -5.017  1.00  7.73           C  
ATOM   1185  O   ASP A 148      13.445  23.139  -6.201  1.00  7.41           O  
ATOM   1186  CB  ASP A 148      12.816  20.784  -4.011  1.00  7.13           C  
ATOM   1187  CG  ASP A 148      13.018  19.269  -3.721  1.00 11.14           C  
ATOM   1188  OD1 ASP A 148      13.972  18.688  -4.232  1.00 10.85           O  
ATOM   1189  OD2 ASP A 148      12.168  18.683  -2.981  1.00 13.57           O  
ATOM   1190  N   VAL A 149      13.508  23.788  -4.061  1.00  7.94           N  
ATOM   1191  CA  VAL A 149      13.167  25.160  -4.419  1.00  7.46           C  
ATOM   1192  C   VAL A 149      14.333  25.896  -5.170  1.00  7.65           C  
ATOM   1193  O   VAL A 149      14.113  26.753  -6.005  1.00  6.49           O  
ATOM   1194  CB  VAL A 149      12.593  25.968  -3.196  1.00  7.93           C  
ATOM   1195  CG1 VAL A 149      13.664  26.301  -2.092  1.00  4.62           C  
ATOM   1196  CG2 VAL A 149      11.740  27.243  -3.708  1.00  6.83           C  
ATOM   1197  N   PHE A 150      15.563  25.576  -4.838  1.00  7.18           N  
ATOM   1198  CA  PHE A 150      16.705  26.063  -5.585  1.00  7.95           C  
ATOM   1199  C   PHE A 150      16.527  25.704  -7.041  1.00  9.08           C  
ATOM   1200  O   PHE A 150      16.794  26.522  -7.934  1.00  9.07           O  
ATOM   1201  CB  PHE A 150      18.001  25.436  -5.068  1.00  8.06           C  
ATOM   1202  CG  PHE A 150      19.244  25.926  -5.795  1.00  6.96           C  
ATOM   1203  CD1 PHE A 150      20.010  26.938  -5.275  1.00  5.04           C  
ATOM   1204  CD2 PHE A 150      19.647  25.344  -7.000  1.00 12.04           C  
ATOM   1205  CE1 PHE A 150      21.161  27.437  -5.967  1.00  9.31           C  
ATOM   1206  CE2 PHE A 150      20.846  25.810  -7.691  1.00 11.31           C  
ATOM   1207  CZ  PHE A 150      21.549  26.847  -7.169  1.00  9.87           C  
ATOM   1208  N   GLY A 151      16.147  24.447  -7.266  1.00  9.51           N  
ATOM   1209  CA  GLY A 151      15.897  23.930  -8.664  1.00  9.98           C  
ATOM   1210  C   GLY A 151      14.824  24.721  -9.431  1.00  8.92           C  
ATOM   1211  O   GLY A 151      15.018  25.135 -10.631  1.00  7.79           O  
ATOM   1212  N   LEU A 152      13.666  24.889  -8.773  1.00  7.36           N  
ATOM   1213  CA  LEU A 152      12.612  25.738  -9.333  1.00  7.45           C  
ATOM   1214  C   LEU A 152      13.100  27.154  -9.626  1.00  7.72           C  
ATOM   1215  O   LEU A 152      12.825  27.708 -10.692  1.00  9.76           O  
ATOM   1216  CB  LEU A 152      11.397  25.853  -8.390  1.00  7.35           C  
ATOM   1217  CG  LEU A 152      10.195  26.715  -8.751  1.00  7.65           C  
ATOM   1218  CD1 LEU A 152       9.727  26.468 -10.249  1.00  6.37           C  
ATOM   1219  CD2 LEU A 152       9.106  26.466  -7.675  1.00  7.64           C  
ATOM   1220  N   SER A 153      13.858  27.737  -8.709  1.00  7.60           N  
ATOM   1221  CA  SER A 153      14.277  29.110  -8.882  1.00  7.71           C  
ATOM   1222  C   SER A 153      15.280  29.254 -10.064  1.00  7.94           C  
ATOM   1223  O   SER A 153      15.277  30.283 -10.795  1.00  7.03           O  
ATOM   1224  CB  SER A 153      14.870  29.654  -7.580  1.00  7.94           C  
ATOM   1225  OG  SER A 153      13.922  29.506  -6.510  1.00  6.23           O  
ATOM   1226  N   SER A 154      16.126  28.251 -10.255  1.00  8.06           N  
ATOM   1227  CA  SER A 154      17.045  28.292 -11.381  1.00  8.75           C  
ATOM   1228  C   SER A 154      16.213  28.329 -12.632  1.00  8.66           C  
ATOM   1229  O   SER A 154      16.494  29.107 -13.587  1.00  9.43           O  
ATOM   1230  CB  SER A 154      17.958  27.040 -11.398  1.00  9.37           C  
ATOM   1231  OG  SER A 154      18.697  26.982 -10.219  1.00 11.90           O  
ATOM   1232  N   ALA A 155      15.192  27.485 -12.668  1.00  9.23           N  
ATOM   1233  CA  ALA A 155      14.325  27.426 -13.886  1.00  8.90           C  
ATOM   1234  C   ALA A 155      13.715  28.794 -14.129  1.00  8.96           C  
ATOM   1235  O   ALA A 155      13.790  29.309 -15.258  1.00 10.55           O  
ATOM   1236  CB  ALA A 155      13.288  26.280 -13.836  1.00  8.49           C  
ATOM   1237  N   LEU A 156      13.129  29.389 -13.076  1.00  8.70           N  
ATOM   1238  CA  LEU A 156      12.520  30.688 -13.129  1.00  8.24           C  
ATOM   1239  C   LEU A 156      13.533  31.750 -13.590  1.00  8.70           C  
ATOM   1240  O   LEU A 156      13.223  32.601 -14.437  1.00  9.25           O  
ATOM   1241  CB  LEU A 156      11.930  31.062 -11.758  1.00  7.05           C  
ATOM   1242  CG  LEU A 156      10.773  30.236 -11.184  1.00 11.15           C  
ATOM   1243  CD1 LEU A 156      10.381  30.722  -9.761  1.00  5.82           C  
ATOM   1244  CD2 LEU A 156       9.556  30.263 -12.148  1.00  9.77           C  
ATOM   1245  N   LEU A 157      14.764  31.663 -13.106  1.00  8.00           N  
ATOM   1246  CA  LEU A 157      15.756  32.666 -13.494  1.00  9.28           C  
ATOM   1247  C   LEU A 157      16.131  32.519 -14.961  1.00  9.30           C  
ATOM   1248  O   LEU A 157      16.452  33.510 -15.633  1.00  9.70           O  
ATOM   1249  CB  LEU A 157      16.984  32.607 -12.573  1.00 10.36           C  
ATOM   1250  CG  LEU A 157      16.854  33.131 -11.182  1.00 10.52           C  
ATOM   1251  CD1 LEU A 157      18.203  32.860 -10.585  1.00  9.32           C  
ATOM   1252  CD2 LEU A 157      16.453  34.600 -11.036  1.00  9.44           C  
ATOM   1253  N   LYS A 158      15.997  31.320 -15.499  1.00  9.31           N  
ATOM   1254  CA  LYS A 158      16.167  31.132 -16.965  1.00 10.18           C  
ATOM   1255  C   LYS A 158      15.024  31.863 -17.747  1.00 10.62           C  
ATOM   1256  O   LYS A 158      15.251  32.565 -18.742  1.00 11.00           O  
ATOM   1257  CB  LYS A 158      16.195  29.638 -17.302  1.00 11.19           C  
ATOM   1258  CG  LYS A 158      17.484  28.961 -16.794  1.00 11.26           C  
ATOM   1259  CD  LYS A 158      17.464  27.536 -17.132  1.00 12.48           C  
ATOM   1260  CE  LYS A 158      18.602  26.838 -16.377  1.00 16.03           C  
ATOM   1261  NZ  LYS A 158      18.339  25.394 -16.526  1.00 17.40           N  
ATOM   1262  N   GLY A 159      13.802  31.762 -17.243  1.00  9.65           N  
ATOM   1263  CA  GLY A 159      12.686  32.494 -17.837  1.00  9.13           C  
ATOM   1264  C   GLY A 159      12.813  34.019 -17.766  1.00  8.42           C  
ATOM   1265  O   GLY A 159      12.585  34.699 -18.772  1.00  9.14           O  
ATOM   1266  N   TYR A 160      13.190  34.567 -16.606  1.00  8.89           N  
ATOM   1267  CA  TYR A 160      13.449  36.026 -16.469  1.00  9.24           C  
ATOM   1268  C   TYR A 160      14.578  36.502 -17.384  1.00  9.34           C  
ATOM   1269  O   TYR A 160      14.455  37.547 -17.979  1.00  8.68           O  
ATOM   1270  CB  TYR A 160      13.806  36.420 -15.041  1.00  9.64           C  
ATOM   1271  CG  TYR A 160      12.646  36.632 -14.117  1.00  9.42           C  
ATOM   1272  CD1 TYR A 160      12.239  35.616 -13.237  1.00 10.24           C  
ATOM   1273  CD2 TYR A 160      11.951  37.824 -14.096  1.00 10.36           C  
ATOM   1274  CE1 TYR A 160      11.169  35.784 -12.382  1.00  8.46           C  
ATOM   1275  CE2 TYR A 160      10.847  38.010 -13.220  1.00 11.93           C  
ATOM   1276  CZ  TYR A 160      10.508  36.982 -12.334  1.00 11.61           C  
ATOM   1277  OH  TYR A 160       9.469  37.085 -11.439  1.00 10.18           O  
ATOM   1278  N   ALA A 161      15.637  35.680 -17.546  1.00  8.54           N  
ATOM   1279  CA  ALA A 161      16.761  35.989 -18.458  1.00  9.46           C  
ATOM   1280  C   ALA A 161      16.254  36.148 -19.906  1.00  9.68           C  
ATOM   1281  O   ALA A 161      16.524  37.165 -20.586  1.00  9.27           O  
ATOM   1282  CB  ALA A 161      17.897  34.969 -18.379  1.00  8.47           C  
ATOM   1283  N   LEU A 162      15.508  35.148 -20.338  1.00  9.57           N  
ATOM   1284  CA  LEU A 162      14.963  35.128 -21.683  1.00  9.68           C  
ATOM   1285  C   LEU A 162      14.030  36.273 -21.839  1.00  9.48           C  
ATOM   1286  O   LEU A 162      14.029  36.870 -22.866  1.00 11.38           O  
ATOM   1287  CB  LEU A 162      14.228  33.818 -21.976  1.00  9.07           C  
ATOM   1288  CG  LEU A 162      15.157  32.609 -22.036  1.00  9.94           C  
ATOM   1289  CD1 LEU A 162      14.344  31.310 -22.300  1.00 10.39           C  
ATOM   1290  CD2 LEU A 162      16.286  32.752 -23.070  1.00  8.69           C  
ATOM   1291  N   ALA A 163      13.257  36.572 -20.809  1.00  9.73           N  
ATOM   1292  CA  ALA A 163      12.261  37.671 -20.808  1.00 10.75           C  
ATOM   1293  C   ALA A 163      12.920  39.032 -21.077  1.00 11.94           C  
ATOM   1294  O   ALA A 163      12.355  39.904 -21.780  1.00 11.34           O  
ATOM   1295  CB  ALA A 163      11.460  37.697 -19.478  1.00  9.25           C  
ATOM   1296  N   LEU A 164      14.148  39.181 -20.586  1.00 12.27           N  
ATOM   1297  CA  LEU A 164      14.853  40.441 -20.645  1.00 12.56           C  
ATOM   1298  C   LEU A 164      15.751  40.533 -21.875  1.00 12.99           C  
ATOM   1299  O   LEU A 164      16.511  41.499 -22.034  1.00 14.16           O  
ATOM   1300  CB  LEU A 164      15.630  40.631 -19.353  1.00 12.74           C  
ATOM   1301  CG  LEU A 164      14.784  40.993 -18.126  1.00 14.39           C  
ATOM   1302  CD1 LEU A 164      15.511  40.624 -16.825  1.00 15.17           C  
ATOM   1303  CD2 LEU A 164      14.418  42.460 -18.144  1.00 10.77           C  
ATOM   1304  N   GLY A 165      15.682  39.532 -22.737  1.00 13.17           N  
ATOM   1305  CA  GLY A 165      16.428  39.546 -24.015  1.00 13.25           C  
ATOM   1306  C   GLY A 165      17.828  39.020 -23.837  1.00 13.06           C  
ATOM   1307  O   GLY A 165      18.691  39.264 -24.656  1.00 13.57           O  
ATOM   1308  N   LYS A 166      18.048  38.262 -22.782  1.00 12.93           N  
ATOM   1309  CA  LYS A 166      19.396  37.738 -22.470  1.00 14.70           C  
ATOM   1310  C   LYS A 166      19.438  36.267 -22.733  1.00 14.07           C  
ATOM   1311  O   LYS A 166      18.408  35.681 -22.949  1.00 13.72           O  
ATOM   1312  CB  LYS A 166      19.784  37.987 -20.990  1.00 14.60           C  
ATOM   1313  CG  LYS A 166      19.667  39.384 -20.535  1.00 16.88           C  
ATOM   1314  CD  LYS A 166      20.573  40.330 -21.317  1.00 20.49           C  
ATOM   1315  CE  LYS A 166      20.440  41.738 -20.742  1.00 23.56           C  
ATOM   1316  NZ  LYS A 166      21.129  42.741 -21.588  1.00 24.93           N  
ATOM   1317  N   GLU A 167      20.638  35.668 -22.694  1.00 14.89           N  
ATOM   1318  CA  GLU A 167      20.772  34.196 -22.775  1.00 15.47           C  
ATOM   1319  C   GLU A 167      20.230  33.590 -21.472  1.00 14.76           C  
ATOM   1320  O   GLU A 167      20.131  34.270 -20.455  1.00 14.54           O  
ATOM   1321  CB  GLU A 167      22.214  33.726 -23.032  1.00 18.45           C  
ATOM   1322  CG  GLU A 167      23.375  34.576 -22.419  1.00 25.48           C  
ATOM   1323  CD  GLU A 167      23.516  34.564 -20.903  1.00 36.41           C  
ATOM   1324  OE1 GLU A 167      22.748  33.749 -20.324  1.00 43.32           O  
ATOM   1325  OE2 GLU A 167      24.428  35.292 -20.290  1.00 35.56           O  
ATOM   1326  N   GLU A 168      19.860  32.325 -21.508  1.00 14.89           N  
ATOM   1327  CA  GLU A 168      19.055  31.762 -20.425  1.00 16.10           C  
ATOM   1328  C   GLU A 168      19.905  31.666 -19.149  1.00 15.94           C  
ATOM   1329  O   GLU A 168      19.350  31.764 -18.070  1.00 15.08           O  
ATOM   1330  CB  GLU A 168      18.444  30.403 -20.773  1.00 17.14           C  
ATOM   1331  CG  GLU A 168      19.375  29.285 -20.576  1.00 18.21           C  
ATOM   1332  CD  GLU A 168      18.764  27.908 -20.796  1.00 20.33           C  
ATOM   1333  OE1 GLU A 168      19.526  26.959 -20.501  1.00 28.11           O  
ATOM   1334  OE2 GLU A 168      17.610  27.738 -21.258  1.00 21.16           O  
ATOM   1335  N   ASN A 169      21.228  31.535 -19.272  1.00 15.84           N  
ATOM   1336  CA  ASN A 169      22.132  31.528 -18.078  1.00 16.43           C  
ATOM   1337  C   ASN A 169      22.489  32.910 -17.475  1.00 15.01           C  
ATOM   1338  O   ASN A 169      23.298  33.007 -16.552  1.00 13.11           O  
ATOM   1339  CB  ASN A 169      23.414  30.723 -18.395  1.00 16.80           C  
ATOM   1340  CG  ASN A 169      24.505  31.572 -19.148  1.00 22.51           C  
ATOM   1341  OD1 ASN A 169      24.177  32.551 -19.850  1.00 26.49           O  
ATOM   1342  ND2 ASN A 169      25.806  31.193 -19.001  1.00 23.71           N  
ATOM   1343  N   PHE A 170      21.854  33.999 -17.941  1.00 13.95           N  
ATOM   1344  CA  PHE A 170      22.266  35.325 -17.487  1.00 13.30           C  
ATOM   1345  C   PHE A 170      22.286  35.531 -15.961  1.00 13.40           C  
ATOM   1346  O   PHE A 170      23.248  36.085 -15.406  1.00 12.04           O  
ATOM   1347  CB  PHE A 170      21.393  36.386 -18.150  1.00 13.75           C  
ATOM   1348  CG  PHE A 170      21.828  37.789 -17.885  1.00 13.93           C  
ATOM   1349  CD1 PHE A 170      22.914  38.377 -18.587  1.00 13.19           C  
ATOM   1350  CD2 PHE A 170      21.097  38.572 -17.005  1.00 10.79           C  
ATOM   1351  CE1 PHE A 170      23.274  39.698 -18.338  1.00 13.58           C  
ATOM   1352  CE2 PHE A 170      21.472  39.919 -16.735  1.00 15.52           C  
ATOM   1353  CZ  PHE A 170      22.547  40.482 -17.427  1.00 12.79           C  
ATOM   1354  N   PHE A 171      21.223  35.107 -15.290  1.00 12.71           N  
ATOM   1355  CA  PHE A 171      21.121  35.212 -13.813  1.00 13.02           C  
ATOM   1356  C   PHE A 171      21.675  33.930 -13.214  1.00 13.32           C  
ATOM   1357  O   PHE A 171      22.473  33.915 -12.219  1.00 14.24           O  
ATOM   1358  CB  PHE A 171      19.655  35.420 -13.376  1.00 11.16           C  
ATOM   1359  CG  PHE A 171      19.051  36.714 -13.822  1.00 11.92           C  
ATOM   1360  CD1 PHE A 171      17.945  36.731 -14.656  1.00  7.72           C  
ATOM   1361  CD2 PHE A 171      19.610  37.931 -13.450  1.00 11.94           C  
ATOM   1362  CE1 PHE A 171      17.379  37.957 -15.080  1.00 14.54           C  
ATOM   1363  CE2 PHE A 171      19.072  39.148 -13.883  1.00 12.92           C  
ATOM   1364  CZ  PHE A 171      17.912  39.161 -14.673  1.00 10.95           C  
ATOM   1365  N   ALA A 172      21.318  32.821 -13.836  1.00 13.40           N  
ATOM   1366  CA  ALA A 172      21.539  31.489 -13.198  1.00 14.11           C  
ATOM   1367  C   ALA A 172      23.020  31.148 -12.998  1.00 14.43           C  
ATOM   1368  O   ALA A 172      23.392  30.376 -12.129  1.00 12.70           O  
ATOM   1369  CB  ALA A 172      20.830  30.402 -14.034  1.00 14.43           C  
ATOM   1370  N   ARG A 173      23.886  31.757 -13.803  1.00 14.16           N  
ATOM   1371  CA  ARG A 173      25.311  31.510 -13.695  1.00 14.94           C  
ATOM   1372  C   ARG A 173      25.851  32.134 -12.391  1.00 14.61           C  
ATOM   1373  O   ARG A 173      26.901  31.734 -11.898  1.00 15.15           O  
ATOM   1374  CB  ARG A 173      26.011  32.024 -14.985  1.00 16.38           C  
ATOM   1375  CG  ARG A 173      26.191  33.505 -14.986  1.00 16.44           C  
ATOM   1376  CD  ARG A 173      26.584  34.232 -16.393  1.00 22.91           C  
ATOM   1377  NE  ARG A 173      26.066  35.600 -16.082  1.00 33.00           N  
ATOM   1378  CZ  ARG A 173      25.861  36.653 -16.875  1.00 31.11           C  
ATOM   1379  NH1 ARG A 173      26.115  36.596 -18.195  1.00 34.52           N  
ATOM   1380  NH2 ARG A 173      25.379  37.771 -16.293  1.00 25.75           N  
ATOM   1381  N   HIS A 174      25.091  33.063 -11.785  1.00 14.08           N  
ATOM   1382  CA  HIS A 174      25.441  33.731 -10.504  1.00 13.02           C  
ATOM   1383  C   HIS A 174      24.744  33.042  -9.287  1.00 11.91           C  
ATOM   1384  O   HIS A 174      24.891  33.453  -8.144  1.00 11.69           O  
ATOM   1385  CB  HIS A 174      25.040  35.215 -10.590  1.00 13.87           C  
ATOM   1386  CG  HIS A 174      25.824  35.976 -11.619  1.00 16.19           C  
ATOM   1387  ND1 HIS A 174      27.143  36.350 -11.422  1.00 17.43           N  
ATOM   1388  CD2 HIS A 174      25.499  36.359 -12.883  1.00 14.79           C  
ATOM   1389  CE1 HIS A 174      27.584  36.962 -12.526  1.00 17.18           C  
ATOM   1390  NE2 HIS A 174      26.599  36.992 -13.420  1.00 13.55           N  
ATOM   1391  N   PHE A 175      23.946  32.030  -9.571  1.00 10.20           N  
ATOM   1392  CA  PHE A 175      23.110  31.352  -8.578  1.00 10.31           C  
ATOM   1393  C   PHE A 175      23.568  29.888  -8.479  1.00 10.76           C  
ATOM   1394  O   PHE A 175      23.171  29.070  -9.273  1.00 10.86           O  
ATOM   1395  CB  PHE A 175      21.668  31.511  -9.055  1.00 10.67           C  
ATOM   1396  CG  PHE A 175      20.616  31.003  -8.068  1.00  9.44           C  
ATOM   1397  CD1 PHE A 175      19.752  29.968  -8.446  1.00  6.78           C  
ATOM   1398  CD2 PHE A 175      20.545  31.487  -6.772  1.00 10.32           C  
ATOM   1399  CE1 PHE A 175      18.825  29.494  -7.577  1.00 11.13           C  
ATOM   1400  CE2 PHE A 175      19.530  31.009  -5.853  1.00  8.61           C  
ATOM   1401  CZ  PHE A 175      18.684  30.009  -6.285  1.00  7.34           C  
ATOM   1402  N   LYS A 176      24.494  29.593  -7.567  1.00 11.35           N  
ATOM   1403  CA  LYS A 176      25.253  28.363  -7.560  1.00 11.52           C  
ATOM   1404  C   LYS A 176      25.141  27.705  -6.199  1.00 11.74           C  
ATOM   1405  O   LYS A 176      25.182  28.381  -5.195  1.00 10.74           O  
ATOM   1406  CB  LYS A 176      26.724  28.645  -7.803  1.00 13.29           C  
ATOM   1407  CG  LYS A 176      27.126  29.366  -9.146  1.00 18.22           C  
ATOM   1408  CD  LYS A 176      26.485  28.714 -10.350  1.00 28.03           C  
ATOM   1409  CE  LYS A 176      26.859  27.238 -10.542  1.00 34.63           C  
ATOM   1410  NZ  LYS A 176      28.341  26.926 -10.595  1.00 38.69           N  
ATOM   1411  N   PRO A 177      24.969  26.362  -6.161  1.00 11.23           N  
ATOM   1412  CA  PRO A 177      24.837  25.687  -4.893  1.00  9.81           C  
ATOM   1413  C   PRO A 177      25.957  26.025  -3.919  1.00  8.97           C  
ATOM   1414  O   PRO A 177      25.745  25.989  -2.728  1.00  8.46           O  
ATOM   1415  CB  PRO A 177      24.958  24.206  -5.276  1.00  9.35           C  
ATOM   1416  CG  PRO A 177      24.438  24.137  -6.699  1.00 10.70           C  
ATOM   1417  CD  PRO A 177      24.938  25.435  -7.309  1.00 12.13           C  
ATOM   1418  N   ASP A 178      27.174  26.222  -4.387  1.00  7.96           N  
ATOM   1419  CA  ASP A 178      28.285  26.316  -3.433  1.00  9.80           C  
ATOM   1420  C   ASP A 178      28.279  27.655  -2.737  1.00 11.01           C  
ATOM   1421  O   ASP A 178      28.949  27.807  -1.727  1.00 13.93           O  
ATOM   1422  CB  ASP A 178      29.645  26.088  -4.077  1.00  9.45           C  
ATOM   1423  CG  ASP A 178      29.933  24.643  -4.295  1.00 13.52           C  
ATOM   1424  OD1 ASP A 178      29.214  23.774  -3.703  1.00 10.51           O  
ATOM   1425  OD2 ASP A 178      30.923  24.384  -5.045  1.00  8.72           O  
ATOM   1426  N   ASP A 179      27.581  28.659  -3.280  1.00 12.23           N  
ATOM   1427  CA  ASP A 179      27.717  30.001  -2.665  1.00 10.91           C  
ATOM   1428  C   ASP A 179      26.515  30.904  -2.506  1.00  9.72           C  
ATOM   1429  O   ASP A 179      26.671  32.026  -1.960  1.00 10.86           O  
ATOM   1430  CB  ASP A 179      28.847  30.774  -3.309  1.00 13.85           C  
ATOM   1431  CG  ASP A 179      28.638  31.061  -4.739  1.00 18.62           C  
ATOM   1432  OD1 ASP A 179      29.674  31.247  -5.395  1.00 26.23           O  
ATOM   1433  OD2 ASP A 179      27.495  31.084  -5.226  1.00 26.87           O  
ATOM   1434  N   THR A 180      25.362  30.441  -2.980  1.00  7.77           N  
ATOM   1435  CA  THR A 180      24.131  31.258  -2.955  1.00  7.47           C  
ATOM   1436  C   THR A 180      23.795  31.703  -1.549  1.00  6.07           C  
ATOM   1437  O   THR A 180      23.920  30.952  -0.559  1.00  7.47           O  
ATOM   1438  CB  THR A 180      22.896  30.513  -3.604  1.00  7.08           C  
ATOM   1439  OG1 THR A 180      21.761  31.373  -3.457  1.00  9.06           O  
ATOM   1440  CG2 THR A 180      22.573  29.130  -2.967  1.00  5.12           C  
ATOM   1441  N   LEU A 181      23.400  32.946  -1.452  1.00  7.07           N  
ATOM   1442  CA  LEU A 181      22.964  33.553  -0.212  1.00  6.32           C  
ATOM   1443  C   LEU A 181      21.464  33.404   0.010  1.00  6.23           C  
ATOM   1444  O   LEU A 181      20.884  33.969   0.940  1.00  6.07           O  
ATOM   1445  CB  LEU A 181      23.424  35.003  -0.153  1.00  7.00           C  
ATOM   1446  CG  LEU A 181      24.958  35.178   0.083  1.00  6.60           C  
ATOM   1447  CD1 LEU A 181      25.482  36.630  -0.190  1.00  9.00           C  
ATOM   1448  CD2 LEU A 181      25.386  34.696   1.519  1.00  6.86           C  
ATOM   1449  N   ALA A 182      20.826  32.574  -0.807  1.00  7.15           N  
ATOM   1450  CA  ALA A 182      19.390  32.363  -0.690  1.00  6.92           C  
ATOM   1451  C   ALA A 182      19.014  31.799   0.708  1.00  7.49           C  
ATOM   1452  O   ALA A 182      19.789  31.062   1.339  1.00  7.52           O  
ATOM   1453  CB  ALA A 182      18.878  31.427  -1.821  1.00  3.91           C  
ATOM   1454  N   SER A 183      17.797  32.126   1.146  1.00  6.89           N  
ATOM   1455  CA  SER A 183      17.258  31.664   2.417  1.00  7.62           C  
ATOM   1456  C   SER A 183      15.829  31.162   2.290  1.00  7.52           C  
ATOM   1457  O   SER A 183      15.081  31.575   1.398  1.00  6.67           O  
ATOM   1458  CB  SER A 183      17.344  32.790   3.475  1.00  7.56           C  
ATOM   1459  OG  SER A 183      16.470  33.872   3.151  1.00  9.12           O  
ATOM   1460  N   VAL A 184      15.497  30.208   3.156  1.00  7.07           N  
ATOM   1461  CA  VAL A 184      14.156  29.758   3.402  1.00  7.39           C  
ATOM   1462  C   VAL A 184      13.748  30.294   4.746  1.00  7.66           C  
ATOM   1463  O   VAL A 184      14.527  30.223   5.712  1.00  8.00           O  
ATOM   1464  CB  VAL A 184      14.078  28.284   3.459  1.00  8.33           C  
ATOM   1465  CG1 VAL A 184      12.668  27.844   3.827  1.00  7.82           C  
ATOM   1466  CG2 VAL A 184      14.572  27.654   2.120  1.00  7.66           C  
ATOM   1467  N   VAL A 185      12.538  30.841   4.803  1.00  8.13           N  
ATOM   1468  CA  VAL A 185      11.890  31.202   6.074  1.00  7.23           C  
ATOM   1469  C   VAL A 185      10.570  30.448   6.244  1.00  6.16           C  
ATOM   1470  O   VAL A 185       9.672  30.467   5.358  1.00  6.84           O  
ATOM   1471  CB  VAL A 185      11.710  32.721   6.231  1.00  6.45           C  
ATOM   1472  CG1 VAL A 185      11.358  33.055   7.677  1.00  5.72           C  
ATOM   1473  CG2 VAL A 185      13.019  33.442   5.823  1.00  5.81           C  
ATOM   1474  N   LEU A 186      10.457  29.772   7.370  1.00  5.95           N  
ATOM   1475  CA  LEU A 186       9.267  29.001   7.680  1.00  6.80           C  
ATOM   1476  C   LEU A 186       8.483  29.857   8.670  1.00  8.07           C  
ATOM   1477  O   LEU A 186       8.789  29.805   9.860  1.00  7.80           O  
ATOM   1478  CB  LEU A 186       9.652  27.675   8.274  1.00  6.71           C  
ATOM   1479  CG  LEU A 186      10.541  26.790   7.400  1.00  7.25           C  
ATOM   1480  CD1 LEU A 186      10.650  25.558   8.216  1.00  7.73           C  
ATOM   1481  CD2 LEU A 186       9.929  26.529   6.003  1.00  4.15           C  
ATOM   1482  N   ILE A 187       7.553  30.679   8.143  1.00  7.81           N  
ATOM   1483  CA  ILE A 187       6.810  31.667   8.962  1.00  7.73           C  
ATOM   1484  C   ILE A 187       5.515  31.017   9.443  1.00  8.70           C  
ATOM   1485  O   ILE A 187       4.788  30.527   8.636  1.00  7.52           O  
ATOM   1486  CB  ILE A 187       6.471  32.963   8.231  1.00  8.02           C  
ATOM   1487  CG1 ILE A 187       7.694  33.624   7.608  1.00  6.35           C  
ATOM   1488  CG2 ILE A 187       5.811  34.035   9.170  1.00  7.70           C  
ATOM   1489  CD1 ILE A 187       7.379  34.656   6.516  1.00  9.11           C  
ATOM   1490  N   ARG A 188       5.249  31.107  10.754  1.00  8.76           N  
ATOM   1491  CA  ARG A 188       3.976  30.743  11.373  1.00  9.91           C  
ATOM   1492  C   ARG A 188       3.216  32.007  11.771  1.00 10.81           C  
ATOM   1493  O   ARG A 188       3.722  32.842  12.562  1.00 11.66           O  
ATOM   1494  CB  ARG A 188       4.163  29.907  12.606  1.00 11.02           C  
ATOM   1495  CG  ARG A 188       2.817  29.429  13.204  1.00 11.85           C  
ATOM   1496  CD  ARG A 188       2.867  29.201  14.652  1.00 13.45           C  
ATOM   1497  NE  ARG A 188       1.538  28.831  15.209  1.00 13.82           N  
ATOM   1498  CZ  ARG A 188       1.293  28.690  16.505  1.00 19.42           C  
ATOM   1499  NH1 ARG A 188       2.261  28.832  17.391  1.00 26.61           N  
ATOM   1500  NH2 ARG A 188       0.075  28.414  16.946  1.00 16.13           N  
ATOM   1501  N   TYR A 189       2.036  32.158  11.164  1.00 10.55           N  
ATOM   1502  CA  TYR A 189       1.024  33.137  11.587  1.00 11.50           C  
ATOM   1503  C   TYR A 189      -0.018  32.377  12.406  1.00 10.57           C  
ATOM   1504  O   TYR A 189      -0.629  31.470  11.871  1.00 10.58           O  
ATOM   1505  CB  TYR A 189       0.333  33.761  10.385  1.00 11.83           C  
ATOM   1506  CG  TYR A 189       1.133  34.843   9.736  1.00 14.12           C  
ATOM   1507  CD1 TYR A 189       2.000  34.570   8.653  1.00 14.49           C  
ATOM   1508  CD2 TYR A 189       1.089  36.151  10.231  1.00 12.20           C  
ATOM   1509  CE1 TYR A 189       2.771  35.620   8.069  1.00 15.94           C  
ATOM   1510  CE2 TYR A 189       1.850  37.170   9.657  1.00 12.76           C  
ATOM   1511  CZ  TYR A 189       2.674  36.901   8.597  1.00 16.11           C  
ATOM   1512  OH  TYR A 189       3.376  37.950   8.026  1.00 20.22           O  
ATOM   1513  N   PRO A 190      -0.200  32.725  13.698  1.00 10.69           N  
ATOM   1514  CA  PRO A 190      -1.138  32.048  14.527  1.00 11.05           C  
ATOM   1515  C   PRO A 190      -2.583  32.538  14.482  1.00 11.09           C  
ATOM   1516  O   PRO A 190      -2.822  33.703  14.258  1.00 10.13           O  
ATOM   1517  CB  PRO A 190      -0.580  32.336  15.935  1.00 11.46           C  
ATOM   1518  CG  PRO A 190      -0.178  33.758  15.825  1.00  9.52           C  
ATOM   1519  CD  PRO A 190       0.522  33.762  14.479  1.00 11.19           C  
ATOM   1520  N   TYR A 191      -3.506  31.641  14.796  1.00 11.47           N  
ATOM   1521  CA  TYR A 191      -4.843  32.010  15.280  1.00 12.76           C  
ATOM   1522  C   TYR A 191      -4.749  32.338  16.766  1.00 13.07           C  
ATOM   1523  O   TYR A 191      -4.151  31.592  17.548  1.00 11.41           O  
ATOM   1524  CB  TYR A 191      -5.835  30.866  15.090  1.00 13.83           C  
ATOM   1525  CG  TYR A 191      -7.180  31.133  15.689  1.00 13.97           C  
ATOM   1526  CD1 TYR A 191      -8.058  32.029  15.095  1.00 16.65           C  
ATOM   1527  CD2 TYR A 191      -7.547  30.551  16.889  1.00 16.23           C  
ATOM   1528  CE1 TYR A 191      -9.299  32.306  15.642  1.00 18.37           C  
ATOM   1529  CE2 TYR A 191      -8.788  30.811  17.449  1.00 18.99           C  
ATOM   1530  CZ  TYR A 191      -9.644  31.679  16.802  1.00 16.97           C  
ATOM   1531  OH  TYR A 191     -10.797  31.911  17.375  1.00 23.53           O  
ATOM   1532  N   LEU A 192      -5.306  33.462  17.151  1.00 12.43           N  
ATOM   1533  CA  LEU A 192      -5.276  33.903  18.537  1.00 14.91           C  
ATOM   1534  C   LEU A 192      -6.619  34.475  18.960  1.00 17.05           C  
ATOM   1535  O   LEU A 192      -7.180  35.269  18.253  1.00 16.76           O  
ATOM   1536  CB  LEU A 192      -4.235  35.009  18.673  1.00 13.56           C  
ATOM   1537  CG  LEU A 192      -2.760  34.619  18.524  1.00 13.48           C  
ATOM   1538  CD1 LEU A 192      -1.891  35.880  18.656  1.00 11.71           C  
ATOM   1539  CD2 LEU A 192      -2.293  33.477  19.487  1.00 14.20           C  
ATOM   1540  N   ASP A 193      -7.117  34.064  20.117  1.00 19.44           N  
ATOM   1541  CA  ASP A 193      -8.400  34.587  20.606  1.00 20.79           C  
ATOM   1542  C   ASP A 193      -8.208  34.857  22.095  1.00 20.82           C  
ATOM   1543  O   ASP A 193      -8.081  33.914  22.845  1.00 22.13           O  
ATOM   1544  CB  ASP A 193      -9.498  33.535  20.384  1.00 22.22           C  
ATOM   1545  CG  ASP A 193     -10.865  33.972  20.938  1.00 24.75           C  
ATOM   1546  OD1 ASP A 193     -11.591  33.070  21.439  1.00 30.16           O  
ATOM   1547  OD2 ASP A 193     -11.181  35.188  20.852  1.00 31.82           O  
ATOM   1548  N   PRO A 194      -8.113  36.124  22.504  1.00 20.55           N  
ATOM   1549  CA  PRO A 194      -8.258  37.327  21.662  1.00 20.38           C  
ATOM   1550  C   PRO A 194      -6.953  37.615  20.971  1.00 18.62           C  
ATOM   1551  O   PRO A 194      -5.876  37.192  21.441  1.00 19.36           O  
ATOM   1552  CB  PRO A 194      -8.611  38.447  22.658  1.00 21.07           C  
ATOM   1553  CG  PRO A 194      -7.814  37.993  23.991  1.00 21.92           C  
ATOM   1554  CD  PRO A 194      -7.731  36.442  23.905  1.00 21.35           C  
ATOM   1555  N   TYR A 195      -7.044  38.318  19.865  1.00 16.07           N  
ATOM   1556  CA  TYR A 195      -5.870  38.661  19.094  1.00 17.53           C  
ATOM   1557  C   TYR A 195      -5.415  40.000  19.619  1.00 17.97           C  
ATOM   1558  O   TYR A 195      -6.161  40.954  19.576  1.00 18.20           O  
ATOM   1559  CB  TYR A 195      -6.168  38.770  17.596  1.00 15.45           C  
ATOM   1560  CG  TYR A 195      -4.942  38.589  16.707  1.00 14.89           C  
ATOM   1561  CD1 TYR A 195      -4.798  37.448  15.951  1.00 14.23           C  
ATOM   1562  CD2 TYR A 195      -3.933  39.570  16.616  1.00 14.63           C  
ATOM   1563  CE1 TYR A 195      -3.696  37.239  15.130  1.00 11.69           C  
ATOM   1564  CE2 TYR A 195      -2.800  39.393  15.765  1.00 12.89           C  
ATOM   1565  CZ  TYR A 195      -2.708  38.173  15.031  1.00 14.03           C  
ATOM   1566  OH  TYR A 195      -1.664  37.873  14.186  1.00 13.65           O  
ATOM   1567  N   PRO A 196      -4.201  40.070  20.114  1.00 19.23           N  
ATOM   1568  CA  PRO A 196      -3.751  41.349  20.687  1.00 20.42           C  
ATOM   1569  C   PRO A 196      -3.620  42.506  19.653  1.00 19.98           C  
ATOM   1570  O   PRO A 196      -2.878  42.394  18.681  1.00 19.36           O  
ATOM   1571  CB  PRO A 196      -2.368  40.993  21.254  1.00 21.13           C  
ATOM   1572  CG  PRO A 196      -1.913  39.820  20.304  1.00 21.23           C  
ATOM   1573  CD  PRO A 196      -3.163  39.034  20.168  1.00 20.10           C  
ATOM   1574  N   GLU A 197      -4.275  43.623  19.934  1.00 20.34           N  
ATOM   1575  CA  GLU A 197      -4.213  44.825  19.066  1.00 20.83           C  
ATOM   1576  C   GLU A 197      -2.813  45.357  18.822  1.00 19.62           C  
ATOM   1577  O   GLU A 197      -2.463  45.867  17.754  1.00 15.81           O  
ATOM   1578  CB  GLU A 197      -5.051  45.898  19.685  1.00 22.59           C  
ATOM   1579  CG  GLU A 197      -6.537  45.684  19.409  1.00 29.28           C  
ATOM   1580  CD  GLU A 197      -6.908  45.816  17.921  1.00 36.27           C  
ATOM   1581  OE1 GLU A 197      -6.150  46.505  17.146  1.00 38.88           O  
ATOM   1582  OE2 GLU A 197      -7.971  45.233  17.531  1.00 39.65           O  
ATOM   1583  N   ALA A 198      -1.994  45.237  19.859  1.00 20.19           N  
ATOM   1584  CA  ALA A 198      -0.594  45.592  19.785  1.00 19.76           C  
ATOM   1585  C   ALA A 198       0.151  44.812  18.702  1.00 19.98           C  
ATOM   1586  O   ALA A 198       1.183  45.292  18.194  1.00 17.58           O  
ATOM   1587  CB  ALA A 198       0.066  45.412  21.145  1.00 20.38           C  
ATOM   1588  N   ALA A 199      -0.354  43.618  18.325  1.00 19.25           N  
ATOM   1589  CA  ALA A 199       0.245  42.863  17.215  1.00 19.19           C  
ATOM   1590  C   ALA A 199      -0.347  43.228  15.850  1.00 19.24           C  
ATOM   1591  O   ALA A 199       0.032  42.640  14.843  1.00 19.93           O  
ATOM   1592  CB  ALA A 199       0.066  41.301  17.463  1.00 20.77           C  
ATOM   1593  N   ILE A 200      -1.295  44.185  15.805  1.00 17.47           N  
ATOM   1594  CA  ILE A 200      -1.923  44.596  14.540  1.00 16.68           C  
ATOM   1595  C   ILE A 200      -1.487  46.041  14.206  1.00 17.39           C  
ATOM   1596  O   ILE A 200      -1.697  46.951  15.001  1.00 16.67           O  
ATOM   1597  CB  ILE A 200      -3.484  44.526  14.610  1.00 17.70           C  
ATOM   1598  CG1 ILE A 200      -3.974  43.143  15.099  1.00 14.90           C  
ATOM   1599  CG2 ILE A 200      -4.099  44.809  13.231  1.00 15.98           C  
ATOM   1600  CD1 ILE A 200      -5.446  43.027  15.397  1.00 15.30           C  
ATOM   1601  N   LYS A 201      -0.892  46.253  13.036  1.00 16.15           N  
ATOM   1602  CA  LYS A 201      -0.577  47.593  12.597  1.00 17.18           C  
ATOM   1603  C   LYS A 201      -1.742  48.098  11.768  1.00 16.71           C  
ATOM   1604  O   LYS A 201      -2.578  47.293  11.255  1.00 16.81           O  
ATOM   1605  CB  LYS A 201       0.752  47.601  11.823  1.00 17.11           C  
ATOM   1606  CG  LYS A 201       1.896  46.938  12.573  1.00 19.67           C  
ATOM   1607  CD  LYS A 201       2.744  46.036  11.664  1.00 22.45           C  
ATOM   1608  CE  LYS A 201       3.830  45.128  12.436  1.00 24.49           C  
ATOM   1609  NZ  LYS A 201       3.234  44.446  13.664  1.00 27.60           N  
ATOM   1610  N   THR A 202      -1.839  49.426  11.635  1.00 16.76           N  
ATOM   1611  CA  THR A 202      -2.911  50.037  10.800  1.00 15.54           C  
ATOM   1612  C   THR A 202      -2.310  50.880   9.713  1.00 15.58           C  
ATOM   1613  O   THR A 202      -1.471  51.791   9.995  1.00 13.76           O  
ATOM   1614  CB  THR A 202      -3.897  50.878  11.662  1.00 17.18           C  
ATOM   1615  OG1 THR A 202      -4.351  50.081  12.782  1.00 16.74           O  
ATOM   1616  CG2 THR A 202      -5.139  51.334  10.821  1.00 16.24           C  
ATOM   1617  N   ALA A 203      -2.700  50.578   8.470  1.00 14.08           N  
ATOM   1618  CA  ALA A 203      -2.240  51.329   7.292  1.00 15.17           C  
ATOM   1619  C   ALA A 203      -2.869  52.719   7.248  1.00 15.68           C  
ATOM   1620  O   ALA A 203      -3.908  52.968   7.883  1.00 14.90           O  
ATOM   1621  CB  ALA A 203      -2.584  50.547   5.969  1.00 14.74           C  
ATOM   1622  N   ALA A 204      -2.298  53.607   6.449  1.00 15.43           N  
ATOM   1623  CA  ALA A 204      -2.860  54.947   6.291  1.00 16.40           C  
ATOM   1624  C   ALA A 204      -4.323  54.881   5.827  1.00 18.01           C  
ATOM   1625  O   ALA A 204      -5.149  55.721   6.196  1.00 17.23           O  
ATOM   1626  CB  ALA A 204      -1.995  55.785   5.294  1.00 16.67           C  
ATOM   1627  N   ASP A 205      -4.660  53.864   5.048  1.00 17.49           N  
ATOM   1628  CA  ASP A 205      -6.018  53.728   4.563  1.00 18.01           C  
ATOM   1629  C   ASP A 205      -6.928  52.957   5.498  1.00 17.65           C  
ATOM   1630  O   ASP A 205      -8.067  52.644   5.139  1.00 18.08           O  
ATOM   1631  CB  ASP A 205      -6.027  53.114   3.150  1.00 18.65           C  
ATOM   1632  CG  ASP A 205      -5.658  51.624   3.117  1.00 18.33           C  
ATOM   1633  OD1 ASP A 205      -5.540  50.971   4.176  1.00 16.78           O  
ATOM   1634  OD2 ASP A 205      -5.553  51.093   1.985  1.00 16.70           O  
ATOM   1635  N   GLY A 206      -6.454  52.688   6.702  1.00 15.33           N  
ATOM   1636  CA  GLY A 206      -7.249  51.962   7.620  1.00 15.58           C  
ATOM   1637  C   GLY A 206      -7.178  50.460   7.578  1.00 16.02           C  
ATOM   1638  O   GLY A 206      -7.729  49.791   8.453  1.00 17.28           O  
ATOM   1639  N   THR A 207      -6.507  49.891   6.600  1.00 15.16           N  
ATOM   1640  CA  THR A 207      -6.383  48.428   6.558  1.00 14.06           C  
ATOM   1641  C   THR A 207      -5.552  47.911   7.749  1.00 13.31           C  
ATOM   1642  O   THR A 207      -4.516  48.471   8.127  1.00 14.11           O  
ATOM   1643  CB  THR A 207      -5.788  48.008   5.227  1.00 14.35           C  
ATOM   1644  OG1 THR A 207      -6.499  48.646   4.128  1.00 11.71           O  
ATOM   1645  CG2 THR A 207      -5.781  46.414   5.049  1.00 14.27           C  
ATOM   1646  N   LYS A 208      -6.058  46.879   8.415  1.00 13.41           N  
ATOM   1647  CA  LYS A 208      -5.305  46.186   9.453  1.00 14.55           C  
ATOM   1648  C   LYS A 208      -4.300  45.222   8.814  1.00 12.91           C  
ATOM   1649  O   LYS A 208      -4.655  44.382   7.944  1.00 11.10           O  
ATOM   1650  CB  LYS A 208      -6.236  45.450  10.397  1.00 15.29           C  
ATOM   1651  CG  LYS A 208      -7.226  46.354  11.171  1.00 18.43           C  
ATOM   1652  CD  LYS A 208      -8.149  45.445  12.054  1.00 18.28           C  
ATOM   1653  CE  LYS A 208      -9.023  46.226  13.024  1.00 23.24           C  
ATOM   1654  NZ  LYS A 208     -10.146  45.313  13.607  1.00 25.40           N  
ATOM   1655  N   LEU A 209      -3.061  45.350   9.289  1.00 12.90           N  
ATOM   1656  CA  LEU A 209      -1.892  44.691   8.727  1.00 13.17           C  
ATOM   1657  C   LEU A 209      -1.118  43.911   9.771  1.00 13.40           C  
ATOM   1658  O   LEU A 209      -1.078  44.300  10.914  1.00 15.18           O  
ATOM   1659  CB  LEU A 209      -0.918  45.704   8.128  1.00 11.00           C  
ATOM   1660  CG  LEU A 209      -1.425  46.698   7.097  1.00 10.56           C  
ATOM   1661  CD1 LEU A 209      -0.229  47.568   6.687  1.00 11.38           C  
ATOM   1662  CD2 LEU A 209      -2.054  46.019   5.921  1.00  9.21           C  
ATOM   1663  N   SER A 210      -0.517  42.820   9.331  1.00 11.92           N  
ATOM   1664  CA  SER A 210       0.516  42.127  10.074  1.00 12.69           C  
ATOM   1665  C   SER A 210       1.907  42.627   9.705  1.00 13.26           C  
ATOM   1666  O   SER A 210       2.777  42.567  10.533  1.00 12.09           O  
ATOM   1667  CB  SER A 210       0.457  40.635   9.826  1.00 12.76           C  
ATOM   1668  OG  SER A 210      -0.711  40.042  10.422  1.00 12.62           O  
ATOM   1669  N   PHE A 211       2.115  43.095   8.462  1.00 11.98           N  
ATOM   1670  CA  PHE A 211       3.410  43.630   8.018  1.00 11.93           C  
ATOM   1671  C   PHE A 211       3.168  44.711   7.025  1.00 11.68           C  
ATOM   1672  O   PHE A 211       2.347  44.524   6.115  1.00 11.09           O  
ATOM   1673  CB  PHE A 211       4.215  42.527   7.334  1.00 13.03           C  
ATOM   1674  CG  PHE A 211       5.687  42.818   7.195  1.00 12.99           C  
ATOM   1675  CD1 PHE A 211       6.496  42.786   8.288  1.00 14.48           C  
ATOM   1676  CD2 PHE A 211       6.275  43.048   5.934  1.00 16.25           C  
ATOM   1677  CE1 PHE A 211       7.904  43.025   8.172  1.00 16.77           C  
ATOM   1678  CE2 PHE A 211       7.646  43.246   5.838  1.00 16.66           C  
ATOM   1679  CZ  PHE A 211       8.451  43.270   6.959  1.00 12.26           C  
ATOM   1680  N   GLU A 212       3.849  45.852   7.205  1.00 12.16           N  
ATOM   1681  CA  GLU A 212       3.710  47.016   6.350  1.00 12.11           C  
ATOM   1682  C   GLU A 212       4.336  46.894   4.961  1.00 13.08           C  
ATOM   1683  O   GLU A 212       5.086  45.949   4.643  1.00 12.07           O  
ATOM   1684  CB  GLU A 212       4.286  48.253   7.033  1.00 12.46           C  
ATOM   1685  CG  GLU A 212       3.161  49.057   7.774  1.00 15.69           C  
ATOM   1686  CD  GLU A 212       2.290  49.970   6.880  1.00 19.91           C  
ATOM   1687  OE1 GLU A 212       1.857  51.008   7.474  1.00 21.61           O  
ATOM   1688  OE2 GLU A 212       2.054  49.700   5.624  1.00 22.47           O  
ATOM   1689  N   TRP A 213       4.043  47.917   4.184  1.00 13.26           N  
ATOM   1690  CA  TRP A 213       4.449  48.039   2.796  1.00 13.43           C  
ATOM   1691  C   TRP A 213       5.944  47.934   2.692  1.00 12.29           C  
ATOM   1692  O   TRP A 213       6.684  48.400   3.554  1.00 11.57           O  
ATOM   1693  CB  TRP A 213       3.887  49.310   2.157  1.00 14.55           C  
ATOM   1694  CG  TRP A 213       4.546  50.630   2.591  1.00 15.10           C  
ATOM   1695  CD1 TRP A 213       4.109  51.498   3.569  1.00 16.08           C  
ATOM   1696  CD2 TRP A 213       5.729  51.212   2.036  1.00 15.82           C  
ATOM   1697  NE1 TRP A 213       4.940  52.596   3.637  1.00 16.87           N  
ATOM   1698  CE2 TRP A 213       5.945  52.443   2.712  1.00 17.34           C  
ATOM   1699  CE3 TRP A 213       6.632  50.813   1.033  1.00 15.39           C  
ATOM   1700  CZ2 TRP A 213       7.024  53.267   2.423  1.00 19.63           C  
ATOM   1701  CZ3 TRP A 213       7.675  51.645   0.712  1.00 17.74           C  
ATOM   1702  CH2 TRP A 213       7.902  52.847   1.437  1.00 18.75           C  
ATOM   1703  N   HIS A 214       6.393  47.257   1.650  1.00 11.77           N  
ATOM   1704  CA  HIS A 214       7.812  47.149   1.413  1.00 11.95           C  
ATOM   1705  C   HIS A 214       8.052  46.627   0.027  1.00 11.89           C  
ATOM   1706  O   HIS A 214       7.128  46.057  -0.630  1.00 10.86           O  
ATOM   1707  CB  HIS A 214       8.433  46.125   2.432  1.00 13.07           C  
ATOM   1708  CG  HIS A 214       7.925  44.745   2.256  1.00 10.10           C  
ATOM   1709  ND1 HIS A 214       6.671  44.357   2.691  1.00  8.82           N  
ATOM   1710  CD2 HIS A 214       8.485  43.654   1.662  1.00 10.18           C  
ATOM   1711  CE1 HIS A 214       6.506  43.063   2.415  1.00 11.65           C  
ATOM   1712  NE2 HIS A 214       7.565  42.626   1.739  1.00  9.26           N  
ATOM   1713  N   GLU A 215       9.308  46.742  -0.414  1.00 11.60           N  
ATOM   1714  CA  GLU A 215       9.804  45.943  -1.516  1.00 12.66           C  
ATOM   1715  C   GLU A 215      10.651  44.795  -0.969  1.00 11.74           C  
ATOM   1716  O   GLU A 215      11.308  44.951   0.072  1.00  9.72           O  
ATOM   1717  CB  GLU A 215      10.696  46.828  -2.402  1.00 12.78           C  
ATOM   1718  CG  GLU A 215       9.973  47.915  -3.111  1.00 15.03           C  
ATOM   1719  CD  GLU A 215      10.925  49.005  -3.694  1.00 18.70           C  
ATOM   1720  OE1 GLU A 215      10.383  49.994  -4.221  1.00 25.65           O  
ATOM   1721  OE2 GLU A 215      12.168  48.855  -3.706  1.00 22.09           O  
ATOM   1722  N   ASP A 216      10.729  43.682  -1.700  1.00 11.86           N  
ATOM   1723  CA  ASP A 216      11.533  42.503  -1.211  1.00 10.26           C  
ATOM   1724  C   ASP A 216      13.023  42.728  -1.442  1.00 10.00           C  
ATOM   1725  O   ASP A 216      13.450  43.390  -2.428  1.00 10.46           O  
ATOM   1726  CB  ASP A 216      11.132  41.192  -1.897  1.00 10.28           C  
ATOM   1727  CG  ASP A 216       9.852  40.593  -1.340  1.00  9.68           C  
ATOM   1728  OD1 ASP A 216       9.262  41.196  -0.428  1.00  8.06           O  
ATOM   1729  OD2 ASP A 216       9.372  39.562  -1.848  1.00  8.17           O  
ATOM   1730  N   VAL A 217      13.794  42.269  -0.463  1.00 10.45           N  
ATOM   1731  CA  VAL A 217      15.265  42.220  -0.522  1.00 10.11           C  
ATOM   1732  C   VAL A 217      15.575  40.835  -1.122  1.00 10.12           C  
ATOM   1733  O   VAL A 217      15.639  39.794  -0.439  1.00 11.22           O  
ATOM   1734  CB  VAL A 217      15.937  42.473   0.848  1.00 10.29           C  
ATOM   1735  CG1 VAL A 217      17.497  42.419   0.709  1.00 12.46           C  
ATOM   1736  CG2 VAL A 217      15.495  43.772   1.420  1.00  9.94           C  
ATOM   1737  N   SER A 218      15.706  40.842  -2.458  1.00 10.35           N  
ATOM   1738  CA  SER A 218      15.939  39.652  -3.235  1.00  9.32           C  
ATOM   1739  C   SER A 218      16.159  40.045  -4.695  1.00  9.70           C  
ATOM   1740  O   SER A 218      15.950  41.173  -5.096  1.00 11.63           O  
ATOM   1741  CB  SER A 218      14.724  38.691  -3.143  1.00 10.17           C  
ATOM   1742  OG  SER A 218      13.564  39.151  -3.874  1.00  7.49           O  
ATOM   1743  N   LEU A 219      16.565  39.076  -5.490  1.00  8.87           N  
ATOM   1744  CA  LEU A 219      16.483  39.180  -6.935  1.00  9.09           C  
ATOM   1745  C   LEU A 219      15.062  38.848  -7.362  1.00  9.09           C  
ATOM   1746  O   LEU A 219      14.402  39.695  -7.947  1.00  8.79           O  
ATOM   1747  CB  LEU A 219      17.473  38.239  -7.603  1.00  8.66           C  
ATOM   1748  CG  LEU A 219      17.486  38.200  -9.148  1.00  8.91           C  
ATOM   1749  CD1 LEU A 219      17.902  39.557  -9.718  1.00  8.76           C  
ATOM   1750  CD2 LEU A 219      18.405  37.020  -9.594  1.00  6.64           C  
ATOM   1751  N   ILE A 220      14.606  37.657  -6.976  1.00  8.97           N  
ATOM   1752  CA  ILE A 220      13.196  37.277  -6.952  1.00  8.40           C  
ATOM   1753  C   ILE A 220      12.869  36.520  -5.637  1.00  9.20           C  
ATOM   1754  O   ILE A 220      13.766  36.003  -4.949  1.00  7.50           O  
ATOM   1755  CB  ILE A 220      12.788  36.417  -8.205  1.00  8.72           C  
ATOM   1756  CG1 ILE A 220      13.272  34.982  -8.112  1.00 10.58           C  
ATOM   1757  CG2 ILE A 220      13.278  37.096  -9.502  1.00  7.05           C  
ATOM   1758  CD1 ILE A 220      12.689  34.040  -9.198  1.00 10.32           C  
ATOM   1759  N   THR A 221      11.578  36.484  -5.320  1.00  8.18           N  
ATOM   1760  CA  THR A 221      11.018  35.759  -4.169  1.00  7.97           C  
ATOM   1761  C   THR A 221      10.057  34.686  -4.752  1.00  8.19           C  
ATOM   1762  O   THR A 221       9.302  34.991  -5.666  1.00  7.08           O  
ATOM   1763  CB  THR A 221      10.291  36.735  -3.268  1.00  8.31           C  
ATOM   1764  OG1 THR A 221      11.217  37.797  -2.902  1.00  7.06           O  
ATOM   1765  CG2 THR A 221       9.700  36.086  -2.072  1.00  4.09           C  
ATOM   1766  N   VAL A 222      10.132  33.478  -4.191  1.00  7.23           N  
ATOM   1767  CA  VAL A 222       9.444  32.241  -4.610  1.00  7.18           C  
ATOM   1768  C   VAL A 222       8.706  31.736  -3.367  1.00  7.64           C  
ATOM   1769  O   VAL A 222       9.293  31.164  -2.412  1.00  8.48           O  
ATOM   1770  CB  VAL A 222      10.502  31.228  -5.154  1.00  6.88           C  
ATOM   1771  CG1 VAL A 222       9.908  29.881  -5.628  1.00  6.33           C  
ATOM   1772  CG2 VAL A 222      11.353  31.862  -6.278  1.00  5.26           C  
ATOM   1773  N   LEU A 223       7.410  31.975  -3.328  1.00  8.23           N  
ATOM   1774  CA  LEU A 223       6.701  31.907  -2.062  1.00  9.41           C  
ATOM   1775  C   LEU A 223       5.582  30.906  -2.115  1.00  9.40           C  
ATOM   1776  O   LEU A 223       4.795  30.924  -3.058  1.00  9.08           O  
ATOM   1777  CB  LEU A 223       6.092  33.299  -1.729  1.00  8.89           C  
ATOM   1778  CG  LEU A 223       5.152  33.380  -0.508  1.00  9.17           C  
ATOM   1779  CD1 LEU A 223       5.896  33.197   0.832  1.00  8.05           C  
ATOM   1780  CD2 LEU A 223       4.385  34.778  -0.493  1.00 11.13           C  
ATOM   1781  N   TYR A 224       5.559  29.989  -1.154  1.00 10.30           N  
ATOM   1782  CA  TYR A 224       4.410  29.152  -0.865  1.00 11.54           C  
ATOM   1783  C   TYR A 224       3.665  29.729   0.398  1.00 11.43           C  
ATOM   1784  O   TYR A 224       4.289  30.011   1.460  1.00  9.91           O  
ATOM   1785  CB  TYR A 224       4.786  27.688  -0.592  1.00 12.49           C  
ATOM   1786  CG  TYR A 224       3.584  26.871  -0.034  1.00 12.65           C  
ATOM   1787  CD1 TYR A 224       2.622  26.236  -0.886  1.00 15.26           C  
ATOM   1788  CD2 TYR A 224       3.354  26.847   1.324  1.00 16.62           C  
ATOM   1789  CE1 TYR A 224       1.439  25.532  -0.296  1.00 14.89           C  
ATOM   1790  CE2 TYR A 224       2.261  26.188   1.873  1.00 18.08           C  
ATOM   1791  CZ  TYR A 224       1.315  25.519   1.068  1.00 17.42           C  
ATOM   1792  OH  TYR A 224       0.258  24.895   1.788  1.00 18.16           O  
ATOM   1793  N   GLN A 225       2.359  29.842   0.282  1.00 11.06           N  
ATOM   1794  CA  GLN A 225       1.480  30.180   1.435  1.00 13.32           C  
ATOM   1795  C   GLN A 225       0.241  29.314   1.497  1.00 13.69           C  
ATOM   1796  O   GLN A 225      -0.198  28.792   0.473  1.00 14.36           O  
ATOM   1797  CB  GLN A 225       0.926  31.579   1.300  1.00 13.45           C  
ATOM   1798  CG  GLN A 225       1.932  32.658   1.182  1.00 17.48           C  
ATOM   1799  CD  GLN A 225       1.355  34.023   1.493  1.00 17.13           C  
ATOM   1800  OE1 GLN A 225       0.337  34.424   0.918  1.00 18.59           O  
ATOM   1801  NE2 GLN A 225       2.052  34.770   2.358  1.00 21.38           N  
ATOM   1802  N   SER A 226      -0.399  29.292   2.680  1.00 15.18           N  
ATOM   1803  CA  SER A 226      -1.653  28.628   2.831  1.00 15.35           C  
ATOM   1804  C   SER A 226      -2.703  29.301   1.990  1.00 15.94           C  
ATOM   1805  O   SER A 226      -2.552  30.422   1.516  1.00 16.64           O  
ATOM   1806  CB  SER A 226      -2.111  28.559   4.303  1.00 15.92           C  
ATOM   1807  OG  SER A 226      -1.014  28.358   5.181  1.00 11.18           O  
ATOM   1808  N   ASN A 227      -3.823  28.611   1.875  1.00 17.79           N  
ATOM   1809  CA  ASN A 227      -4.931  29.076   1.105  1.00 16.73           C  
ATOM   1810  C   ASN A 227      -5.804  30.033   1.922  1.00 17.00           C  
ATOM   1811  O   ASN A 227      -6.998  29.796   2.064  1.00 17.11           O  
ATOM   1812  CB  ASN A 227      -5.794  27.869   0.700  1.00 17.99           C  
ATOM   1813  CG  ASN A 227      -6.801  28.206  -0.397  1.00 21.71           C  
ATOM   1814  OD1 ASN A 227      -6.775  29.306  -1.008  1.00 28.37           O  
ATOM   1815  ND2 ASN A 227      -7.705  27.257  -0.664  1.00 31.06           N  
ATOM   1816  N   VAL A 228      -5.202  31.100   2.441  1.00 15.41           N  
ATOM   1817  CA  VAL A 228      -5.874  32.110   3.183  1.00 13.92           C  
ATOM   1818  C   VAL A 228      -5.412  33.424   2.582  1.00 13.72           C  
ATOM   1819  O   VAL A 228      -4.223  33.725   2.643  1.00 11.04           O  
ATOM   1820  CB  VAL A 228      -5.540  31.978   4.646  1.00 14.58           C  
ATOM   1821  CG1 VAL A 228      -6.186  33.084   5.427  1.00 17.52           C  
ATOM   1822  CG2 VAL A 228      -5.992  30.576   5.200  1.00 15.23           C  
ATOM   1823  N   GLN A 229      -6.345  34.189   1.981  1.00 13.44           N  
ATOM   1824  CA  GLN A 229      -6.037  35.461   1.329  1.00 12.64           C  
ATOM   1825  C   GLN A 229      -5.476  36.474   2.319  1.00 12.52           C  
ATOM   1826  O   GLN A 229      -6.014  36.640   3.418  1.00 10.67           O  
ATOM   1827  CB  GLN A 229      -7.272  36.019   0.620  1.00 12.96           C  
ATOM   1828  CG  GLN A 229      -6.984  37.100  -0.461  1.00 13.71           C  
ATOM   1829  CD  GLN A 229      -6.634  38.470   0.127  1.00 15.28           C  
ATOM   1830  OE1 GLN A 229      -7.291  38.953   1.070  1.00 14.54           O  
ATOM   1831  NE2 GLN A 229      -5.618  39.097  -0.429  1.00 16.23           N  
ATOM   1832  N   ASN A 230      -4.390  37.147   1.935  1.00 12.77           N  
ATOM   1833  CA  ASN A 230      -3.738  38.097   2.885  1.00 12.71           C  
ATOM   1834  C   ASN A 230      -2.922  39.182   2.252  1.00 13.26           C  
ATOM   1835  O   ASN A 230      -2.839  40.287   2.811  1.00 13.80           O  
ATOM   1836  CB  ASN A 230      -2.896  37.337   3.961  1.00 13.65           C  
ATOM   1837  CG  ASN A 230      -1.683  36.673   3.404  1.00 12.48           C  
ATOM   1838  OD1 ASN A 230      -0.590  37.241   3.422  1.00 13.11           O  
ATOM   1839  ND2 ASN A 230      -1.868  35.480   2.832  1.00  8.94           N  
ATOM   1840  N   LEU A 231      -2.321  38.889   1.095  1.00 12.27           N  
ATOM   1841  CA  LEU A 231      -1.395  39.824   0.418  1.00 11.75           C  
ATOM   1842  C   LEU A 231      -2.087  40.901  -0.409  1.00 10.57           C  
ATOM   1843  O   LEU A 231      -3.089  40.636  -1.047  1.00  9.18           O  
ATOM   1844  CB  LEU A 231      -0.475  39.025  -0.524  1.00 11.51           C  
ATOM   1845  CG  LEU A 231       0.596  38.210   0.246  1.00 14.17           C  
ATOM   1846  CD1 LEU A 231       1.498  37.384  -0.742  1.00 13.41           C  
ATOM   1847  CD2 LEU A 231       1.468  39.157   1.170  1.00 16.68           C  
ATOM   1848  N   GLN A 232      -1.571  42.141  -0.357  1.00 10.33           N  
ATOM   1849  CA  GLN A 232      -2.049  43.184  -1.278  1.00 10.56           C  
ATOM   1850  C   GLN A 232      -0.857  43.808  -1.967  1.00 10.82           C  
ATOM   1851  O   GLN A 232       0.213  43.941  -1.378  1.00 12.40           O  
ATOM   1852  CB  GLN A 232      -2.819  44.250  -0.552  1.00  8.98           C  
ATOM   1853  CG  GLN A 232      -3.956  43.737   0.265  1.00 12.91           C  
ATOM   1854  CD  GLN A 232      -4.751  44.902   0.810  1.00 13.45           C  
ATOM   1855  OE1 GLN A 232      -4.164  45.858   1.383  1.00 18.15           O  
ATOM   1856  NE2 GLN A 232      -6.061  44.868   0.625  1.00 14.79           N  
ATOM   1857  N   VAL A 233      -1.025  44.168  -3.218  1.00 11.01           N  
ATOM   1858  CA  VAL A 233      -0.002  44.826  -4.005  1.00 12.11           C  
ATOM   1859  C   VAL A 233      -0.477  46.225  -4.444  1.00 13.27           C  
ATOM   1860  O   VAL A 233      -1.620  46.417  -4.823  1.00 13.02           O  
ATOM   1861  CB  VAL A 233       0.386  43.949  -5.237  1.00 11.51           C  
ATOM   1862  CG1 VAL A 233      -0.895  43.589  -6.113  1.00 10.67           C  
ATOM   1863  CG2 VAL A 233       1.457  44.694  -6.120  1.00 11.87           C  
ATOM   1864  N   GLU A 234       0.395  47.222  -4.307  1.00 14.70           N  
ATOM   1865  CA  GLU A 234       0.045  48.540  -4.715  1.00 15.85           C  
ATOM   1866  C   GLU A 234       0.200  48.653  -6.248  1.00 17.43           C  
ATOM   1867  O   GLU A 234       1.210  48.232  -6.837  1.00 16.10           O  
ATOM   1868  CB  GLU A 234       0.924  49.556  -3.989  1.00 14.84           C  
ATOM   1869  CG  GLU A 234       0.561  50.992  -4.285  1.00 16.83           C  
ATOM   1870  CD  GLU A 234       1.395  51.953  -3.489  1.00 17.82           C  
ATOM   1871  OE1 GLU A 234       2.656  51.910  -3.580  1.00 16.74           O  
ATOM   1872  OE2 GLU A 234       0.772  52.721  -2.734  1.00 24.14           O  
ATOM   1873  N   THR A 235      -0.819  49.217  -6.886  1.00 19.79           N  
ATOM   1874  CA  THR A 235      -0.799  49.453  -8.328  1.00 20.85           C  
ATOM   1875  C   THR A 235      -1.204  50.902  -8.547  1.00 22.33           C  
ATOM   1876  O   THR A 235      -1.498  51.592  -7.574  1.00 22.12           O  
ATOM   1877  CB  THR A 235      -1.846  48.541  -9.043  1.00 21.95           C  
ATOM   1878  OG1 THR A 235      -3.169  48.936  -8.641  1.00 22.03           O  
ATOM   1879  CG2 THR A 235      -1.604  47.022  -8.713  1.00 21.73           C  
ATOM   1880  N   ALA A 236      -1.280  51.365  -9.802  1.00 23.54           N  
ATOM   1881  CA  ALA A 236      -1.746  52.767 -10.031  1.00 24.75           C  
ATOM   1882  C   ALA A 236      -3.219  52.917  -9.637  1.00 25.73           C  
ATOM   1883  O   ALA A 236      -3.667  54.024  -9.357  1.00 26.87           O  
ATOM   1884  CB  ALA A 236      -1.471  53.279 -11.509  1.00 25.99           C  
ATOM   1885  N   ALA A 237      -3.953  51.805  -9.536  1.00 25.21           N  
ATOM   1886  CA  ALA A 237      -5.344  51.840  -9.054  1.00 24.92           C  
ATOM   1887  C   ALA A 237      -5.489  51.576  -7.579  1.00 24.87           C  
ATOM   1888  O   ALA A 237      -6.604  51.287  -7.134  1.00 25.84           O  
ATOM   1889  CB  ALA A 237      -6.224  50.809  -9.849  1.00 26.00           C  
ATOM   1890  N   GLY A 238      -4.369  51.605  -6.832  1.00 23.99           N  
ATOM   1891  CA  GLY A 238      -4.369  51.472  -5.364  1.00 22.21           C  
ATOM   1892  C   GLY A 238      -3.968  50.053  -4.985  1.00 20.04           C  
ATOM   1893  O   GLY A 238      -3.468  49.335  -5.834  1.00 20.30           O  
ATOM   1894  N   TYR A 239      -4.150  49.686  -3.720  1.00 17.81           N  
ATOM   1895  CA  TYR A 239      -3.781  48.364  -3.251  1.00 17.76           C  
ATOM   1896  C   TYR A 239      -4.834  47.363  -3.746  1.00 18.34           C  
ATOM   1897  O   TYR A 239      -6.062  47.578  -3.567  1.00 17.53           O  
ATOM   1898  CB  TYR A 239      -3.649  48.266  -1.737  1.00 17.41           C  
ATOM   1899  CG  TYR A 239      -2.293  48.728  -1.226  1.00 17.17           C  
ATOM   1900  CD1 TYR A 239      -2.096  50.054  -0.824  1.00 17.23           C  
ATOM   1901  CD2 TYR A 239      -1.160  47.863  -1.261  1.00 17.71           C  
ATOM   1902  CE1 TYR A 239      -0.853  50.479  -0.364  1.00 18.41           C  
ATOM   1903  CE2 TYR A 239       0.061  48.295  -0.844  1.00 16.11           C  
ATOM   1904  CZ  TYR A 239       0.216  49.588  -0.400  1.00 15.59           C  
ATOM   1905  OH  TYR A 239       1.441  50.031   0.000  1.00 17.91           O  
ATOM   1906  N   GLN A 240      -4.370  46.277  -4.356  1.00 15.43           N  
ATOM   1907  CA  GLN A 240      -5.260  45.219  -4.790  1.00 16.97           C  
ATOM   1908  C   GLN A 240      -4.960  43.914  -4.085  1.00 15.52           C  
ATOM   1909  O   GLN A 240      -3.845  43.701  -3.661  1.00 15.65           O  
ATOM   1910  CB  GLN A 240      -5.137  45.027  -6.299  1.00 17.28           C  
ATOM   1911  CG  GLN A 240      -5.493  46.315  -6.996  1.00 19.75           C  
ATOM   1912  CD  GLN A 240      -5.472  46.183  -8.484  1.00 20.02           C  
ATOM   1913  OE1 GLN A 240      -4.577  45.545  -9.044  1.00 25.63           O  
ATOM   1914  NE2 GLN A 240      -6.460  46.817  -9.159  1.00 21.91           N  
ATOM   1915  N   ASP A 241      -5.971  43.084  -3.923  1.00 14.83           N  
ATOM   1916  CA  ASP A 241      -5.859  41.808  -3.205  1.00 14.60           C  
ATOM   1917  C   ASP A 241      -5.249  40.762  -4.150  1.00 13.76           C  
ATOM   1918  O   ASP A 241      -5.755  40.541  -5.287  1.00 13.03           O  
ATOM   1919  CB  ASP A 241      -7.233  41.332  -2.700  1.00 14.66           C  
ATOM   1920  CG  ASP A 241      -7.659  42.011  -1.354  1.00 17.87           C  
ATOM   1921  OD1 ASP A 241      -8.865  42.037  -1.095  1.00 18.19           O  
ATOM   1922  OD2 ASP A 241      -6.814  42.431  -0.520  1.00 15.75           O  
ATOM   1923  N   ILE A 242      -4.175  40.128  -3.684  1.00 12.12           N  
ATOM   1924  CA  ILE A 242      -3.662  38.952  -4.358  1.00 13.07           C  
ATOM   1925  C   ILE A 242      -4.399  37.745  -3.900  1.00 12.70           C  
ATOM   1926  O   ILE A 242      -4.450  37.462  -2.708  1.00 12.96           O  
ATOM   1927  CB  ILE A 242      -2.153  38.726  -4.114  1.00 13.11           C  
ATOM   1928  CG1 ILE A 242      -1.376  39.923  -4.713  1.00 15.31           C  
ATOM   1929  CG2 ILE A 242      -1.682  37.389  -4.758  1.00 12.97           C  
ATOM   1930  CD1 ILE A 242       0.068  40.034  -4.165  1.00 13.24           C  
ATOM   1931  N   GLU A 243      -5.011  37.027  -4.828  1.00 12.82           N  
ATOM   1932  CA  GLU A 243      -5.710  35.826  -4.418  1.00 15.36           C  
ATOM   1933  C   GLU A 243      -4.756  34.690  -3.969  1.00 14.86           C  
ATOM   1934  O   GLU A 243      -3.645  34.529  -4.490  1.00 11.52           O  
ATOM   1935  CB  GLU A 243      -6.669  35.330  -5.482  1.00 17.08           C  
ATOM   1936  CG  GLU A 243      -7.921  36.253  -5.614  1.00 24.66           C  
ATOM   1937  CD  GLU A 243      -8.439  36.999  -4.325  1.00 31.88           C  
ATOM   1938  OE1 GLU A 243      -8.238  38.253  -4.227  1.00 32.72           O  
ATOM   1939  OE2 GLU A 243      -9.080  36.344  -3.449  1.00 39.47           O  
ATOM   1940  N   ALA A 244      -5.220  33.915  -2.988  1.00 14.68           N  
ATOM   1941  CA  ALA A 244      -4.436  32.783  -2.478  1.00 15.79           C  
ATOM   1942  C   ALA A 244      -4.493  31.625  -3.510  1.00 16.73           C  
ATOM   1943  O   ALA A 244      -5.468  31.530  -4.296  1.00 17.20           O  
ATOM   1944  CB  ALA A 244      -4.982  32.298  -1.069  1.00 15.92           C  
ATOM   1945  N   ASP A 245      -3.431  30.819  -3.554  1.00 16.07           N  
ATOM   1946  CA  ASP A 245      -3.397  29.601  -4.319  1.00 16.17           C  
ATOM   1947  C   ASP A 245      -2.340  28.715  -3.718  1.00 16.81           C  
ATOM   1948  O   ASP A 245      -1.147  28.776  -4.105  1.00 18.34           O  
ATOM   1949  CB  ASP A 245      -3.009  29.833  -5.748  1.00 16.31           C  
ATOM   1950  CG  ASP A 245      -3.084  28.565  -6.588  1.00 17.96           C  
ATOM   1951  OD1 ASP A 245      -3.205  28.687  -7.809  1.00 19.73           O  
ATOM   1952  OD2 ASP A 245      -3.035  27.441  -6.057  1.00 21.71           O  
ATOM   1953  N   ASP A 246      -2.761  27.818  -2.850  1.00 15.14           N  
ATOM   1954  CA  ASP A 246      -1.770  26.986  -2.163  1.00 15.86           C  
ATOM   1955  C   ASP A 246      -1.412  25.729  -2.989  1.00 14.82           C  
ATOM   1956  O   ASP A 246      -0.901  24.790  -2.467  1.00 16.66           O  
ATOM   1957  CB  ASP A 246      -2.254  26.614  -0.766  1.00 14.85           C  
ATOM   1958  CG  ASP A 246      -3.433  25.637  -0.822  1.00 19.33           C  
ATOM   1959  OD1 ASP A 246      -3.823  25.055   0.222  1.00 18.53           O  
ATOM   1960  OD2 ASP A 246      -3.945  25.477  -1.938  1.00 20.35           O  
ATOM   1961  N   THR A 247      -1.584  25.751  -4.296  1.00 14.28           N  
ATOM   1962  CA  THR A 247      -0.988  24.746  -5.114  1.00 14.51           C  
ATOM   1963  C   THR A 247       0.208  25.278  -5.958  1.00 13.45           C  
ATOM   1964  O   THR A 247       1.034  24.501  -6.421  1.00 13.34           O  
ATOM   1965  CB  THR A 247      -2.030  24.135  -6.074  1.00 16.48           C  
ATOM   1966  OG1 THR A 247      -2.308  25.075  -7.124  1.00 17.36           O  
ATOM   1967  CG2 THR A 247      -3.286  23.800  -5.293  1.00 16.00           C  
ATOM   1968  N   GLY A 248       0.316  26.582  -6.107  1.00 12.15           N  
ATOM   1969  CA  GLY A 248       1.349  27.212  -6.909  1.00 11.61           C  
ATOM   1970  C   GLY A 248       2.333  27.978  -6.037  1.00 11.50           C  
ATOM   1971  O   GLY A 248       2.168  28.104  -4.775  1.00 11.58           O  
ATOM   1972  N   TYR A 249       3.392  28.451  -6.682  1.00  8.90           N  
ATOM   1973  CA  TYR A 249       4.272  29.398  -6.011  1.00  9.83           C  
ATOM   1974  C   TYR A 249       3.996  30.838  -6.493  1.00  9.30           C  
ATOM   1975  O   TYR A 249       3.998  31.099  -7.706  1.00  8.38           O  
ATOM   1976  CB  TYR A 249       5.753  29.049  -6.312  1.00  9.69           C  
ATOM   1977  CG  TYR A 249       6.298  27.973  -5.389  1.00  8.89           C  
ATOM   1978  CD1 TYR A 249       6.156  26.620  -5.673  1.00  8.96           C  
ATOM   1979  CD2 TYR A 249       6.906  28.332  -4.181  1.00  9.71           C  
ATOM   1980  CE1 TYR A 249       6.660  25.627  -4.765  1.00  9.66           C  
ATOM   1981  CE2 TYR A 249       7.431  27.361  -3.282  1.00  7.13           C  
ATOM   1982  CZ  TYR A 249       7.310  26.017  -3.589  1.00 10.15           C  
ATOM   1983  OH  TYR A 249       7.796  25.102  -2.664  1.00 11.20           O  
ATOM   1984  N   LEU A 250       3.833  31.762  -5.551  1.00  8.55           N  
ATOM   1985  CA  LEU A 250       3.707  33.181  -5.866  1.00  8.95           C  
ATOM   1986  C   LEU A 250       5.097  33.753  -6.092  1.00  9.32           C  
ATOM   1987  O   LEU A 250       6.026  33.615  -5.226  1.00  9.42           O  
ATOM   1988  CB  LEU A 250       3.007  33.946  -4.697  1.00 10.11           C  
ATOM   1989  CG  LEU A 250       2.653  35.430  -4.955  1.00  8.01           C  
ATOM   1990  CD1 LEU A 250       1.674  35.663  -6.132  1.00  8.57           C  
ATOM   1991  CD2 LEU A 250       2.113  36.128  -3.645  1.00  6.50           C  
ATOM   1992  N   ILE A 251       5.254  34.406  -7.235  1.00  8.15           N  
ATOM   1993  CA  ILE A 251       6.582  34.864  -7.660  1.00  8.83           C  
ATOM   1994  C   ILE A 251       6.500  36.348  -7.814  1.00  9.04           C  
ATOM   1995  O   ILE A 251       5.562  36.853  -8.472  1.00  7.44           O  
ATOM   1996  CB  ILE A 251       7.078  34.273  -8.986  1.00  7.61           C  
ATOM   1997  CG1 ILE A 251       6.824  32.785  -9.124  1.00 12.68           C  
ATOM   1998  CG2 ILE A 251       8.614  34.659  -9.241  1.00  6.37           C  
ATOM   1999  CD1 ILE A 251       7.518  31.853  -8.017  1.00  7.12           C  
ATOM   2000  N   ASN A 252       7.494  37.043  -7.247  1.00  9.77           N  
ATOM   2001  CA  ASN A 252       7.760  38.449  -7.603  1.00  9.18           C  
ATOM   2002  C   ASN A 252       9.242  38.827  -7.596  1.00  9.71           C  
ATOM   2003  O   ASN A 252      10.088  38.134  -7.067  1.00  9.16           O  
ATOM   2004  CB  ASN A 252       7.024  39.396  -6.634  1.00  9.55           C  
ATOM   2005  CG  ASN A 252       7.503  39.249  -5.178  1.00  8.80           C  
ATOM   2006  OD1 ASN A 252       7.067  38.368  -4.446  1.00 11.57           O  
ATOM   2007  ND2 ASN A 252       8.330  40.140  -4.763  1.00  8.34           N  
ATOM   2008  N   CYS A 253       9.506  39.972  -8.189  1.00  9.20           N  
ATOM   2009  CA  CYS A 253      10.834  40.558  -8.216  1.00 10.31           C  
ATOM   2010  C   CYS A 253      11.114  41.334  -6.946  1.00 10.56           C  
ATOM   2011  O   CYS A 253      10.165  41.961  -6.408  1.00 10.07           O  
ATOM   2012  CB  CYS A 253      10.950  41.491  -9.411  1.00 10.13           C  
ATOM   2013  SG  CYS A 253      11.046  40.612 -10.975  1.00 13.32           S  
ATOM   2014  N   GLY A 254      12.396  41.304  -6.506  1.00  9.48           N  
ATOM   2015  CA  GLY A 254      12.882  42.113  -5.420  1.00  9.19           C  
ATOM   2016  C   GLY A 254      13.651  43.299  -6.002  1.00  9.97           C  
ATOM   2017  O   GLY A 254      13.764  43.401  -7.218  1.00 10.07           O  
ATOM   2018  N   SER A 255      14.211  44.151  -5.133  1.00 10.00           N  
ATOM   2019  CA  SER A 255      14.797  45.408  -5.565  1.00 11.02           C  
ATOM   2020  C   SER A 255      16.133  45.207  -6.276  1.00 11.58           C  
ATOM   2021  O   SER A 255      16.576  46.120  -6.980  1.00 13.91           O  
ATOM   2022  CB  SER A 255      14.912  46.400  -4.399  1.00 10.95           C  
ATOM   2023  OG  SER A 255      15.648  45.856  -3.305  1.00 13.22           O  
ATOM   2024  N   TYR A 256      16.766  44.034  -6.154  1.00 11.49           N  
ATOM   2025  CA  TYR A 256      17.949  43.785  -6.988  1.00 12.13           C  
ATOM   2026  C   TYR A 256      17.627  43.678  -8.463  1.00 12.17           C  
ATOM   2027  O   TYR A 256      18.361  44.225  -9.331  1.00 12.39           O  
ATOM   2028  CB  TYR A 256      18.754  42.572  -6.584  1.00 12.83           C  
ATOM   2029  CG  TYR A 256      20.177  42.658  -7.111  1.00 11.71           C  
ATOM   2030  CD1 TYR A 256      21.098  43.550  -6.532  1.00 13.53           C  
ATOM   2031  CD2 TYR A 256      20.628  41.810  -8.121  1.00 12.55           C  
ATOM   2032  CE1 TYR A 256      22.466  43.592  -6.980  1.00 15.48           C  
ATOM   2033  CE2 TYR A 256      21.966  41.836  -8.593  1.00 12.88           C  
ATOM   2034  CZ  TYR A 256      22.886  42.762  -8.003  1.00 14.46           C  
ATOM   2035  OH  TYR A 256      24.182  42.798  -8.410  1.00 14.97           O  
ATOM   2036  N   MET A 257      16.538  42.990  -8.741  1.00 10.39           N  
ATOM   2037  CA  MET A 257      16.041  43.002 -10.119  1.00 11.78           C  
ATOM   2038  C   MET A 257      15.676  44.409 -10.660  1.00 11.17           C  
ATOM   2039  O   MET A 257      15.949  44.736 -11.788  1.00 10.19           O  
ATOM   2040  CB  MET A 257      14.858  42.059 -10.257  1.00 10.82           C  
ATOM   2041  CG  MET A 257      14.381  41.868 -11.710  1.00 10.96           C  
ATOM   2042  SD  MET A 257      15.462  40.933 -12.662  1.00 11.05           S  
ATOM   2043  CE  MET A 257      15.046  39.197 -12.227  1.00 11.34           C  
ATOM   2044  N   ALA A 258      14.998  45.201  -9.842  1.00 11.82           N  
ATOM   2045  CA  ALA A 258      14.683  46.586 -10.182  1.00 12.35           C  
ATOM   2046  C   ALA A 258      15.960  47.402 -10.465  1.00 12.73           C  
ATOM   2047  O   ALA A 258      16.030  48.183 -11.443  1.00 13.41           O  
ATOM   2048  CB  ALA A 258      13.785  47.259  -9.099  1.00 10.59           C  
ATOM   2049  N   HIS A 259      16.992  47.195  -9.691  1.00 12.42           N  
ATOM   2050  CA  HIS A 259      18.235  47.887  -9.967  1.00 13.14           C  
ATOM   2051  C   HIS A 259      18.847  47.501 -11.329  1.00 13.97           C  
ATOM   2052  O   HIS A 259      19.255  48.334 -12.091  1.00 14.26           O  
ATOM   2053  CB  HIS A 259      19.178  47.623  -8.788  1.00 13.37           C  
ATOM   2054  CG  HIS A 259      20.524  48.191  -8.975  1.00 17.27           C  
ATOM   2055  ND1 HIS A 259      20.739  49.546  -9.082  1.00 17.11           N  
ATOM   2056  CD2 HIS A 259      21.723  47.593  -9.167  1.00 17.44           C  
ATOM   2057  CE1 HIS A 259      22.018  49.761  -9.301  1.00 17.09           C  
ATOM   2058  NE2 HIS A 259      22.641  48.601  -9.327  1.00 18.49           N  
ATOM   2059  N   LEU A 260      18.947  46.203 -11.611  1.00 15.22           N  
ATOM   2060  CA  LEU A 260      19.591  45.660 -12.799  1.00 14.63           C  
ATOM   2061  C   LEU A 260      18.889  46.037 -14.093  1.00 14.38           C  
ATOM   2062  O   LEU A 260      19.515  46.132 -15.136  1.00 14.25           O  
ATOM   2063  CB  LEU A 260      19.538  44.115 -12.750  1.00 15.68           C  
ATOM   2064  CG  LEU A 260      20.481  43.427 -11.788  1.00 17.38           C  
ATOM   2065  CD1 LEU A 260      20.323  41.867 -11.815  1.00 15.03           C  
ATOM   2066  CD2 LEU A 260      21.933  43.907 -12.117  1.00 20.33           C  
ATOM   2067  N   THR A 261      17.589  46.154 -14.026  1.00 13.08           N  
ATOM   2068  CA  THR A 261      16.758  46.401 -15.196  1.00 13.72           C  
ATOM   2069  C   THR A 261      16.326  47.889 -15.287  1.00 14.77           C  
ATOM   2070  O   THR A 261      15.490  48.244 -16.125  1.00 12.34           O  
ATOM   2071  CB  THR A 261      15.459  45.524 -15.211  1.00 13.36           C  
ATOM   2072  OG1 THR A 261      14.572  45.910 -14.162  1.00  9.77           O  
ATOM   2073  CG2 THR A 261      15.747  44.036 -15.142  1.00 11.31           C  
ATOM   2074  N   ASN A 262      16.876  48.724 -14.414  1.00 16.42           N  
ATOM   2075  CA  ASN A 262      16.501  50.124 -14.351  1.00 17.62           C  
ATOM   2076  C   ASN A 262      14.988  50.291 -14.221  1.00 18.40           C  
ATOM   2077  O   ASN A 262      14.327  51.056 -14.937  1.00 17.62           O  
ATOM   2078  CB  ASN A 262      17.003  50.904 -15.559  1.00 18.74           C  
ATOM   2079  CG  ASN A 262      16.928  52.432 -15.315  1.00 20.56           C  
ATOM   2080  OD1 ASN A 262      17.216  52.916 -14.207  1.00 25.13           O  
ATOM   2081  ND2 ASN A 262      16.567  53.186 -16.357  1.00 24.33           N  
ATOM   2082  N   ASN A 263      14.408  49.510 -13.333  1.00 17.41           N  
ATOM   2083  CA  ASN A 263      12.990  49.634 -13.046  1.00 17.41           C  
ATOM   2084  C   ASN A 263      12.071  49.215 -14.193  1.00 16.92           C  
ATOM   2085  O   ASN A 263      10.864  49.313 -14.021  1.00 15.63           O  
ATOM   2086  CB  ASN A 263      12.665  51.059 -12.519  1.00 18.59           C  
ATOM   2087  CG  ASN A 263      11.990  51.060 -11.148  1.00 21.54           C  
ATOM   2088  OD1 ASN A 263      12.098  50.136 -10.352  1.00 21.83           O  
ATOM   2089  ND2 ASN A 263      11.276  52.116 -10.882  1.00 25.21           N  
ATOM   2090  N   TYR A 264      12.595  48.615 -15.270  1.00 15.01           N  
ATOM   2091  CA  TYR A 264      11.734  47.891 -16.208  1.00 15.40           C  
ATOM   2092  C   TYR A 264      10.872  46.761 -15.581  1.00 14.74           C  
ATOM   2093  O   TYR A 264       9.687  46.536 -15.969  1.00 14.01           O  
ATOM   2094  CB  TYR A 264      12.572  47.364 -17.427  1.00 16.03           C  
ATOM   2095  CG  TYR A 264      11.816  46.559 -18.483  1.00 17.09           C  
ATOM   2096  CD1 TYR A 264      10.881  47.173 -19.335  1.00 21.12           C  
ATOM   2097  CD2 TYR A 264      12.086  45.200 -18.693  1.00 18.83           C  
ATOM   2098  CE1 TYR A 264      10.177  46.419 -20.326  1.00 17.30           C  
ATOM   2099  CE2 TYR A 264      11.403  44.445 -19.689  1.00 19.54           C  
ATOM   2100  CZ  TYR A 264      10.458  45.069 -20.499  1.00 19.44           C  
ATOM   2101  OH  TYR A 264       9.769  44.337 -21.473  1.00 21.42           O  
ATOM   2102  N   TYR A 265      11.505  45.975 -14.706  1.00 14.07           N  
ATOM   2103  CA  TYR A 265      10.812  45.050 -13.804  1.00 13.29           C  
ATOM   2104  C   TYR A 265      10.924  45.659 -12.398  1.00 14.00           C  
ATOM   2105  O   TYR A 265      11.972  45.588 -11.731  1.00 12.98           O  
ATOM   2106  CB  TYR A 265      11.392  43.626 -13.861  1.00 13.20           C  
ATOM   2107  CG  TYR A 265      11.175  42.850 -15.162  1.00 12.05           C  
ATOM   2108  CD1 TYR A 265      11.775  41.580 -15.344  1.00 12.76           C  
ATOM   2109  CD2 TYR A 265      10.369  43.350 -16.207  1.00 10.74           C  
ATOM   2110  CE1 TYR A 265      11.603  40.857 -16.512  1.00 12.66           C  
ATOM   2111  CE2 TYR A 265      10.198  42.608 -17.415  1.00 10.67           C  
ATOM   2112  CZ  TYR A 265      10.843  41.393 -17.560  1.00 10.02           C  
ATOM   2113  OH  TYR A 265      10.679  40.655 -18.684  1.00 11.19           O  
ATOM   2114  N   LYS A 266       9.886  46.375 -12.000  1.00 12.99           N  
ATOM   2115  CA  LYS A 266       9.869  46.967 -10.690  1.00 14.35           C  
ATOM   2116  C   LYS A 266       9.759  45.857  -9.634  1.00 13.48           C  
ATOM   2117  O   LYS A 266       9.296  44.741  -9.876  1.00 12.74           O  
ATOM   2118  CB  LYS A 266       8.694  47.948 -10.538  1.00 14.93           C  
ATOM   2119  CG  LYS A 266       8.708  49.117 -11.600  1.00 18.54           C  
ATOM   2120  CD  LYS A 266       7.372  49.892 -11.656  1.00 20.37           C  
ATOM   2121  CE  LYS A 266       6.232  49.085 -12.357  1.00 25.76           C  
ATOM   2122  NZ  LYS A 266       6.415  48.770 -13.848  1.00 24.80           N  
ATOM   2123  N   ALA A 267      10.250  46.184  -8.451  1.00 13.26           N  
ATOM   2124  CA  ALA A 267       9.979  45.415  -7.288  1.00 11.63           C  
ATOM   2125  C   ALA A 267       8.609  45.908  -6.745  1.00 10.00           C  
ATOM   2126  O   ALA A 267       8.520  46.989  -6.211  1.00 10.78           O  
ATOM   2127  CB  ALA A 267      11.071  45.659  -6.275  1.00 10.74           C  
ATOM   2128  N   PRO A 268       7.575  45.095  -6.852  1.00  8.61           N  
ATOM   2129  CA  PRO A 268       6.272  45.521  -6.434  1.00 10.18           C  
ATOM   2130  C   PRO A 268       6.222  45.804  -4.965  1.00 10.17           C  
ATOM   2131  O   PRO A 268       6.753  45.046  -4.221  1.00  9.92           O  
ATOM   2132  CB  PRO A 268       5.371  44.328  -6.758  1.00  8.29           C  
ATOM   2133  CG  PRO A 268       6.294  43.207  -7.021  1.00  8.19           C  
ATOM   2134  CD  PRO A 268       7.551  43.748  -7.445  1.00  9.56           C  
ATOM   2135  N   ILE A 269       5.567  46.913  -4.601  1.00 11.17           N  
ATOM   2136  CA  ILE A 269       5.289  47.240  -3.234  1.00 11.01           C  
ATOM   2137  C   ILE A 269       4.084  46.460  -2.793  1.00 10.79           C  
ATOM   2138  O   ILE A 269       3.079  46.372  -3.477  1.00 10.44           O  
ATOM   2139  CB  ILE A 269       5.094  48.721  -3.060  1.00 11.73           C  
ATOM   2140  CG1 ILE A 269       6.414  49.444  -3.367  1.00 15.05           C  
ATOM   2141  CG2 ILE A 269       4.608  49.041  -1.662  1.00 11.51           C  
ATOM   2142  CD1 ILE A 269       7.046  49.888  -2.166  1.00 22.09           C  
ATOM   2143  N   HIS A 270       4.247  45.777  -1.672  1.00 11.54           N  
ATOM   2144  CA  HIS A 270       3.202  44.941  -1.148  1.00 11.69           C  
ATOM   2145  C   HIS A 270       3.246  44.937   0.368  1.00 13.02           C  
ATOM   2146  O   HIS A 270       4.262  45.348   0.977  1.00 11.90           O  
ATOM   2147  CB  HIS A 270       3.313  43.512  -1.738  1.00 11.69           C  
ATOM   2148  CG  HIS A 270       4.616  42.854  -1.491  1.00 11.44           C  
ATOM   2149  ND1 HIS A 270       5.765  43.191  -2.179  1.00  8.91           N  
ATOM   2150  CD2 HIS A 270       4.960  41.868  -0.623  1.00 11.70           C  
ATOM   2151  CE1 HIS A 270       6.758  42.427  -1.747  1.00 14.54           C  
ATOM   2152  NE2 HIS A 270       6.294  41.622  -0.795  1.00 10.15           N  
ATOM   2153  N   ARG A 271       2.124  44.499   0.965  1.00 12.07           N  
ATOM   2154  CA  ARG A 271       1.947  44.436   2.406  1.00 11.97           C  
ATOM   2155  C   ARG A 271       1.090  43.211   2.713  1.00 12.15           C  
ATOM   2156  O   ARG A 271       0.451  42.628   1.791  1.00 12.14           O  
ATOM   2157  CB  ARG A 271       1.226  45.673   2.940  1.00 12.29           C  
ATOM   2158  CG  ARG A 271      -0.157  45.913   2.365  1.00 12.80           C  
ATOM   2159  CD  ARG A 271      -0.645  47.247   2.663  1.00 13.15           C  
ATOM   2160  NE  ARG A 271      -2.049  47.406   2.314  1.00 12.14           N  
ATOM   2161  CZ  ARG A 271      -2.700  48.566   2.457  1.00 16.76           C  
ATOM   2162  NH1 ARG A 271      -2.110  49.645   2.986  1.00 15.89           N  
ATOM   2163  NH2 ARG A 271      -3.963  48.641   2.106  1.00 16.71           N  
ATOM   2164  N   VAL A 272       1.083  42.850   3.982  1.00 11.91           N  
ATOM   2165  CA  VAL A 272       0.400  41.619   4.491  1.00 11.68           C  
ATOM   2166  C   VAL A 272      -0.728  42.068   5.432  1.00 12.60           C  
ATOM   2167  O   VAL A 272      -0.463  42.655   6.523  1.00 10.80           O  
ATOM   2168  CB  VAL A 272       1.325  40.735   5.284  1.00 11.96           C  
ATOM   2169  CG1 VAL A 272       0.508  39.523   5.870  1.00  8.07           C  
ATOM   2170  CG2 VAL A 272       2.546  40.318   4.444  1.00 12.95           C  
ATOM   2171  N   LYS A 273      -1.962  41.822   5.002  1.00 11.39           N  
ATOM   2172  CA  LYS A 273      -3.109  42.080   5.842  1.00 12.01           C  
ATOM   2173  C   LYS A 273      -3.156  41.181   7.049  1.00 11.81           C  
ATOM   2174  O   LYS A 273      -2.710  40.033   7.003  1.00 12.45           O  
ATOM   2175  CB  LYS A 273      -4.396  41.892   5.067  1.00 12.65           C  
ATOM   2176  CG  LYS A 273      -4.563  42.880   3.920  1.00 11.84           C  
ATOM   2177  CD  LYS A 273      -5.871  42.759   3.312  1.00 15.41           C  
ATOM   2178  CE  LYS A 273      -6.205  41.395   2.843  1.00 16.49           C  
ATOM   2179  NZ  LYS A 273      -7.572  41.425   2.220  1.00 20.11           N  
ATOM   2180  N   TRP A 274      -3.726  41.742   8.113  1.00 11.49           N  
ATOM   2181  CA  TRP A 274      -3.996  41.044   9.347  1.00 11.66           C  
ATOM   2182  C   TRP A 274      -5.171  40.117   9.086  1.00 11.65           C  
ATOM   2183  O   TRP A 274      -6.221  40.548   8.608  1.00 11.09           O  
ATOM   2184  CB  TRP A 274      -4.324  41.994  10.491  1.00 11.46           C  
ATOM   2185  CG  TRP A 274      -4.857  41.259  11.649  1.00 12.67           C  
ATOM   2186  CD1 TRP A 274      -4.150  40.406  12.474  1.00 13.87           C  
ATOM   2187  CD2 TRP A 274      -6.221  41.222  12.110  1.00 14.12           C  
ATOM   2188  NE1 TRP A 274      -5.000  39.821  13.386  1.00 13.50           N  
ATOM   2189  CE2 TRP A 274      -6.259  40.318  13.227  1.00 12.95           C  
ATOM   2190  CE3 TRP A 274      -7.404  41.851  11.701  1.00 14.12           C  
ATOM   2191  CZ2 TRP A 274      -7.437  40.033  13.938  1.00 13.46           C  
ATOM   2192  CZ3 TRP A 274      -8.580  41.611  12.421  1.00 13.13           C  
ATOM   2193  CH2 TRP A 274      -8.588  40.664  13.511  1.00 15.60           C  
ATOM   2194  N   VAL A 275      -4.958  38.841   9.365  1.00 11.69           N  
ATOM   2195  CA  VAL A 275      -6.019  37.807   9.318  1.00 11.92           C  
ATOM   2196  C   VAL A 275      -5.858  36.959  10.543  1.00 10.42           C  
ATOM   2197  O   VAL A 275      -4.760  36.537  10.826  1.00  9.55           O  
ATOM   2198  CB  VAL A 275      -5.868  36.880   8.042  1.00 12.34           C  
ATOM   2199  CG1 VAL A 275      -7.088  35.958   7.900  1.00 13.17           C  
ATOM   2200  CG2 VAL A 275      -5.716  37.721   6.817  1.00 16.07           C  
ATOM   2201  N   ASN A 276      -6.928  36.737  11.285  1.00 11.25           N  
ATOM   2202  CA  ASN A 276      -6.883  35.826  12.458  1.00 11.83           C  
ATOM   2203  C   ASN A 276      -7.095  34.368  12.027  1.00 10.63           C  
ATOM   2204  O   ASN A 276      -8.194  33.815  12.123  1.00 10.74           O  
ATOM   2205  CB  ASN A 276      -7.877  36.279  13.524  1.00 11.54           C  
ATOM   2206  CG  ASN A 276      -7.579  35.700  14.845  1.00 13.68           C  
ATOM   2207  OD1 ASN A 276      -6.596  34.937  15.005  1.00  9.29           O  
ATOM   2208  ND2 ASN A 276      -8.502  35.922  15.803  1.00 13.66           N  
ATOM   2209  N   ALA A 277      -6.013  33.788  11.516  1.00 10.82           N  
ATOM   2210  CA  ALA A 277      -5.992  32.420  10.932  1.00 11.10           C  
ATOM   2211  C   ALA A 277      -4.632  31.825  11.170  1.00 10.81           C  
ATOM   2212  O   ALA A 277      -3.612  32.567  11.072  1.00 10.71           O  
ATOM   2213  CB  ALA A 277      -6.235  32.474   9.441  1.00 10.41           C  
ATOM   2214  N   GLU A 278      -4.619  30.522  11.509  1.00  9.89           N  
ATOM   2215  CA  GLU A 278      -3.447  29.711  11.610  1.00 11.26           C  
ATOM   2216  C   GLU A 278      -2.979  29.347  10.203  1.00 11.52           C  
ATOM   2217  O   GLU A 278      -3.640  28.611   9.486  1.00 10.78           O  
ATOM   2218  CB  GLU A 278      -3.725  28.460  12.424  1.00 11.49           C  
ATOM   2219  CG  GLU A 278      -2.587  27.550  12.803  1.00 13.00           C  
ATOM   2220  CD  GLU A 278      -1.630  28.189  13.756  1.00 14.78           C  
ATOM   2221  OE1 GLU A 278      -0.463  28.278  13.371  1.00 16.61           O  
ATOM   2222  OE2 GLU A 278      -2.020  28.587  14.869  1.00 15.84           O  
ATOM   2223  N   ARG A 279      -1.868  29.939   9.815  1.00 11.04           N  
ATOM   2224  CA  ARG A 279      -1.396  29.818   8.453  1.00 11.22           C  
ATOM   2225  C   ARG A 279       0.118  29.848   8.334  1.00 10.98           C  
ATOM   2226  O   ARG A 279       0.835  30.080   9.302  1.00 13.37           O  
ATOM   2227  CB  ARG A 279      -2.051  30.894   7.638  1.00 10.49           C  
ATOM   2228  CG  ARG A 279      -1.617  32.215   7.891  1.00 12.11           C  
ATOM   2229  CD  ARG A 279      -2.391  33.194   6.958  1.00 14.96           C  
ATOM   2230  NE  ARG A 279      -1.857  34.550   7.126  1.00 14.10           N  
ATOM   2231  CZ  ARG A 279      -0.770  35.040   6.544  1.00 16.00           C  
ATOM   2232  NH1 ARG A 279      -0.106  34.380   5.605  1.00 20.73           N  
ATOM   2233  NH2 ARG A 279      -0.408  36.273   6.835  1.00 19.04           N  
ATOM   2234  N   GLN A 280       0.585  29.546   7.150  1.00 11.17           N  
ATOM   2235  CA  GLN A 280       1.990  29.500   6.818  1.00 12.20           C  
ATOM   2236  C   GLN A 280       2.309  30.409   5.683  1.00 10.79           C  
ATOM   2237  O   GLN A 280       1.569  30.539   4.728  1.00 11.82           O  
ATOM   2238  CB  GLN A 280       2.375  28.089   6.357  1.00 12.87           C  
ATOM   2239  CG  GLN A 280       2.026  27.024   7.366  1.00 12.21           C  
ATOM   2240  CD  GLN A 280       2.314  25.608   6.860  1.00 14.70           C  
ATOM   2241  OE1 GLN A 280       2.085  25.337   5.667  1.00 17.97           O  
ATOM   2242  NE2 GLN A 280       2.716  24.657   7.790  1.00 12.97           N  
ATOM   2243  N   SER A 281       3.464  31.009   5.782  1.00 11.10           N  
ATOM   2244  CA  SER A 281       4.079  31.734   4.673  1.00 10.06           C  
ATOM   2245  C   SER A 281       5.577  31.292   4.590  1.00  9.27           C  
ATOM   2246  O   SER A 281       6.343  31.397   5.579  1.00  8.18           O  
ATOM   2247  CB  SER A 281       3.887  33.192   4.863  1.00 11.35           C  
ATOM   2248  OG  SER A 281       4.403  33.914   3.796  1.00 13.07           O  
ATOM   2249  N   LEU A 282       5.926  30.652   3.483  1.00  6.51           N  
ATOM   2250  CA  LEU A 282       7.201  29.948   3.367  1.00  7.38           C  
ATOM   2251  C   LEU A 282       7.975  30.508   2.181  1.00  6.46           C  
ATOM   2252  O   LEU A 282       8.001  29.914   1.106  1.00  4.54           O  
ATOM   2253  CB  LEU A 282       6.984  28.431   3.183  1.00  6.73           C  
ATOM   2254  CG  LEU A 282       5.938  27.799   4.119  1.00  9.97           C  
ATOM   2255  CD1 LEU A 282       5.967  26.318   3.989  1.00  7.61           C  
ATOM   2256  CD2 LEU A 282       6.267  28.164   5.642  1.00 10.31           C  
ATOM   2257  N   PRO A 283       8.531  31.713   2.349  1.00  5.60           N  
ATOM   2258  CA  PRO A 283       9.353  32.244   1.298  1.00  7.17           C  
ATOM   2259  C   PRO A 283      10.740  31.653   1.124  1.00  6.91           C  
ATOM   2260  O   PRO A 283      11.396  31.287   2.083  1.00  7.16           O  
ATOM   2261  CB  PRO A 283       9.470  33.736   1.654  1.00  7.61           C  
ATOM   2262  CG  PRO A 283       9.516  33.692   3.108  1.00  6.99           C  
ATOM   2263  CD  PRO A 283       8.413  32.658   3.457  1.00  8.02           C  
ATOM   2264  N   PHE A 284      11.163  31.579  -0.139  1.00  7.97           N  
ATOM   2265  CA  PHE A 284      12.562  31.365  -0.551  1.00  6.89           C  
ATOM   2266  C   PHE A 284      13.005  32.638  -1.227  1.00  6.45           C  
ATOM   2267  O   PHE A 284      12.423  33.030  -2.228  1.00  5.09           O  
ATOM   2268  CB  PHE A 284      12.648  30.240  -1.566  1.00  7.18           C  
ATOM   2269  CG  PHE A 284      14.067  29.892  -1.986  1.00  7.07           C  
ATOM   2270  CD1 PHE A 284      15.006  29.362  -1.058  1.00  6.78           C  
ATOM   2271  CD2 PHE A 284      14.429  29.944  -3.316  1.00  5.90           C  
ATOM   2272  CE1 PHE A 284      16.243  28.948  -1.498  1.00  7.62           C  
ATOM   2273  CE2 PHE A 284      15.677  29.563  -3.733  1.00  5.31           C  
ATOM   2274  CZ  PHE A 284      16.596  29.097  -2.832  1.00  4.84           C  
ATOM   2275  N   PHE A 285      13.957  33.321  -0.630  1.00  7.19           N  
ATOM   2276  CA  PHE A 285      14.539  34.556  -1.188  1.00  7.33           C  
ATOM   2277  C   PHE A 285      15.725  34.148  -2.051  1.00  8.44           C  
ATOM   2278  O   PHE A 285      16.726  33.594  -1.544  1.00  6.18           O  
ATOM   2279  CB  PHE A 285      14.948  35.527  -0.091  1.00  7.28           C  
ATOM   2280  CG  PHE A 285      13.733  35.961   0.809  1.00  8.79           C  
ATOM   2281  CD1 PHE A 285      13.577  35.460   2.102  1.00  9.92           C  
ATOM   2282  CD2 PHE A 285      12.726  36.792   0.303  1.00  9.41           C  
ATOM   2283  CE1 PHE A 285      12.465  35.892   2.886  1.00  6.88           C  
ATOM   2284  CE2 PHE A 285      11.637  37.185   1.072  1.00  9.85           C  
ATOM   2285  CZ  PHE A 285      11.507  36.732   2.347  1.00  8.39           C  
ATOM   2286  N   VAL A 286      15.561  34.376  -3.365  1.00  8.06           N  
ATOM   2287  CA  VAL A 286      16.574  34.057  -4.357  1.00  7.99           C  
ATOM   2288  C   VAL A 286      17.635  35.134  -4.362  1.00  7.77           C  
ATOM   2289  O   VAL A 286      17.420  36.232  -4.861  1.00  9.29           O  
ATOM   2290  CB  VAL A 286      15.973  33.889  -5.721  1.00  7.47           C  
ATOM   2291  CG1 VAL A 286      17.043  33.751  -6.790  1.00  7.18           C  
ATOM   2292  CG2 VAL A 286      14.922  32.719  -5.705  1.00  7.23           C  
ATOM   2293  N   ASN A 287      18.728  34.835  -3.681  1.00  7.98           N  
ATOM   2294  CA  ASN A 287      19.910  35.734  -3.544  1.00  7.89           C  
ATOM   2295  C   ASN A 287      21.072  35.082  -4.320  1.00  8.50           C  
ATOM   2296  O   ASN A 287      21.172  33.857  -4.431  1.00  7.67           O  
ATOM   2297  CB  ASN A 287      20.301  35.913  -2.076  1.00  8.15           C  
ATOM   2298  CG  ASN A 287      19.235  36.628  -1.236  1.00 11.31           C  
ATOM   2299  OD1 ASN A 287      18.559  37.581  -1.709  1.00  8.09           O  
ATOM   2300  ND2 ASN A 287      19.026  36.128  -0.004  1.00 10.01           N  
ATOM   2301  N   LEU A 288      21.945  35.905  -4.877  1.00  8.84           N  
ATOM   2302  CA  LEU A 288      23.091  35.436  -5.590  1.00  9.01           C  
ATOM   2303  C   LEU A 288      24.228  35.239  -4.575  1.00  8.89           C  
ATOM   2304  O   LEU A 288      23.982  35.073  -3.364  1.00  8.91           O  
ATOM   2305  CB  LEU A 288      23.426  36.481  -6.698  1.00  8.66           C  
ATOM   2306  CG  LEU A 288      22.290  36.737  -7.731  1.00  8.90           C  
ATOM   2307  CD1 LEU A 288      22.748  37.800  -8.816  1.00  8.63           C  
ATOM   2308  CD2 LEU A 288      21.748  35.461  -8.362  1.00  6.04           C  
ATOM   2309  N   GLY A 289      25.447  35.193  -5.078  1.00 10.29           N  
ATOM   2310  CA  GLY A 289      26.683  35.039  -4.299  1.00 10.46           C  
ATOM   2311  C   GLY A 289      27.194  36.371  -3.787  1.00 11.13           C  
ATOM   2312  O   GLY A 289      26.855  37.461  -4.330  1.00 11.91           O  
ATOM   2313  N   TYR A 290      28.013  36.318  -2.742  1.00 12.33           N  
ATOM   2314  CA  TYR A 290      28.477  37.530  -2.069  1.00 12.71           C  
ATOM   2315  C   TYR A 290      29.138  38.547  -3.059  1.00 14.03           C  
ATOM   2316  O   TYR A 290      28.869  39.742  -3.006  1.00 13.63           O  
ATOM   2317  CB  TYR A 290      29.485  37.169  -1.004  1.00 14.27           C  
ATOM   2318  CG  TYR A 290      29.737  38.314  -0.057  1.00 13.36           C  
ATOM   2319  CD1 TYR A 290      28.805  38.653   0.867  1.00 11.69           C  
ATOM   2320  CD2 TYR A 290      30.913  39.054  -0.110  1.00 16.67           C  
ATOM   2321  CE1 TYR A 290      29.006  39.696   1.730  1.00 17.99           C  
ATOM   2322  CE2 TYR A 290      31.126  40.097   0.739  1.00 17.82           C  
ATOM   2323  CZ  TYR A 290      30.166  40.395   1.679  1.00 17.07           C  
ATOM   2324  OH  TYR A 290      30.317  41.457   2.566  1.00 19.56           O  
ATOM   2325  N   ASP A 291      29.930  38.022  -3.993  1.00 14.42           N  
ATOM   2326  CA  ASP A 291      30.700  38.834  -4.965  1.00 16.03           C  
ATOM   2327  C   ASP A 291      30.000  38.927  -6.317  1.00 15.89           C  
ATOM   2328  O   ASP A 291      30.576  39.491  -7.238  1.00 15.32           O  
ATOM   2329  CB  ASP A 291      32.055  38.193  -5.209  1.00 16.70           C  
ATOM   2330  CG  ASP A 291      33.005  38.436  -4.104  1.00 22.26           C  
ATOM   2331  OD1 ASP A 291      34.013  37.677  -4.061  1.00 33.10           O  
ATOM   2332  OD2 ASP A 291      32.744  39.344  -3.284  1.00 24.68           O  
ATOM   2333  N   SER A 292      28.786  38.381  -6.449  1.00 14.47           N  
ATOM   2334  CA  SER A 292      28.082  38.462  -7.715  1.00 14.22           C  
ATOM   2335  C   SER A 292      27.776  39.917  -8.076  1.00 13.29           C  
ATOM   2336  O   SER A 292      27.240  40.677  -7.305  1.00 12.78           O  
ATOM   2337  CB  SER A 292      26.806  37.598  -7.728  1.00 14.61           C  
ATOM   2338  OG  SER A 292      27.083  36.227  -7.425  1.00 12.93           O  
ATOM   2339  N   VAL A 293      28.231  40.343  -9.239  1.00 15.30           N  
ATOM   2340  CA  VAL A 293      27.916  41.672  -9.784  1.00 16.42           C  
ATOM   2341  C   VAL A 293      27.341  41.433 -11.196  1.00 17.31           C  
ATOM   2342  O   VAL A 293      27.922  40.763 -12.012  1.00 16.97           O  
ATOM   2343  CB  VAL A 293      29.168  42.616  -9.877  1.00 17.75           C  
ATOM   2344  CG1 VAL A 293      28.719  44.041 -10.251  1.00 20.04           C  
ATOM   2345  CG2 VAL A 293      29.902  42.668  -8.605  1.00 19.46           C  
ATOM   2346  N   ILE A 294      26.162  41.928 -11.463  1.00 18.13           N  
ATOM   2347  CA  ILE A 294      25.635  42.006 -12.821  1.00 17.42           C  
ATOM   2348  C   ILE A 294      25.639  43.470 -13.226  1.00 17.00           C  
ATOM   2349  O   ILE A 294      25.127  44.331 -12.497  1.00 14.76           O  
ATOM   2350  CB  ILE A 294      24.225  41.398 -12.848  1.00 18.40           C  
ATOM   2351  CG1 ILE A 294      24.305  39.913 -12.441  1.00 19.71           C  
ATOM   2352  CG2 ILE A 294      23.567  41.535 -14.227  1.00 19.21           C  
ATOM   2353  CD1 ILE A 294      22.992  39.206 -12.389  1.00 16.07           C  
ATOM   2354  N   ASP A 295      26.244  43.785 -14.377  1.00 17.87           N  
ATOM   2355  CA  ASP A 295      26.123  45.117 -14.932  1.00 18.26           C  
ATOM   2356  C   ASP A 295      24.661  45.521 -15.223  1.00 16.47           C  
ATOM   2357  O   ASP A 295      23.884  44.834 -15.906  1.00 15.35           O  
ATOM   2358  CB  ASP A 295      27.037  45.320 -16.135  1.00 21.31           C  
ATOM   2359  CG  ASP A 295      28.565  45.232 -15.739  1.00 27.72           C  
ATOM   2360  OD1 ASP A 295      28.938  45.452 -14.524  1.00 34.62           O  
ATOM   2361  OD2 ASP A 295      29.395  44.897 -16.651  1.00 37.16           O  
ATOM   2362  N   PRO A 296      24.265  46.637 -14.637  1.00 15.38           N  
ATOM   2363  CA  PRO A 296      22.914  47.096 -14.821  1.00 14.98           C  
ATOM   2364  C   PRO A 296      22.625  47.453 -16.273  1.00 15.03           C  
ATOM   2365  O   PRO A 296      23.541  47.821 -16.986  1.00 16.03           O  
ATOM   2366  CB  PRO A 296      22.862  48.348 -13.910  1.00 14.96           C  
ATOM   2367  CG  PRO A 296      23.863  48.133 -12.913  1.00 13.85           C  
ATOM   2368  CD  PRO A 296      24.998  47.496 -13.674  1.00 14.41           C  
ATOM   2369  N   PHE A 297      21.402  47.293 -16.730  1.00 14.09           N  
ATOM   2370  CA  PHE A 297      21.078  47.593 -18.117  1.00 15.14           C  
ATOM   2371  C   PHE A 297      19.665  48.111 -18.161  1.00 15.81           C  
ATOM   2372  O   PHE A 297      18.985  48.159 -17.146  1.00 15.02           O  
ATOM   2373  CB  PHE A 297      21.282  46.356 -18.996  1.00 15.51           C  
ATOM   2374  CG  PHE A 297      20.400  45.180 -18.632  1.00 15.61           C  
ATOM   2375  CD1 PHE A 297      19.203  44.966 -19.298  1.00 17.67           C  
ATOM   2376  CD2 PHE A 297      20.787  44.278 -17.639  1.00 12.28           C  
ATOM   2377  CE1 PHE A 297      18.403  43.891 -18.991  1.00 16.32           C  
ATOM   2378  CE2 PHE A 297      19.967  43.227 -17.275  1.00 16.02           C  
ATOM   2379  CZ  PHE A 297      18.773  43.029 -17.949  1.00 17.81           C  
ATOM   2380  N   ASP A 298      19.205  48.482 -19.350  1.00 18.77           N  
ATOM   2381  CA  ASP A 298      17.855  49.032 -19.552  1.00 19.17           C  
ATOM   2382  C   ASP A 298      17.301  48.532 -20.858  1.00 20.40           C  
ATOM   2383  O   ASP A 298      17.690  49.031 -21.942  1.00 21.06           O  
ATOM   2384  CB  ASP A 298      17.881  50.554 -19.577  1.00 20.77           C  
ATOM   2385  CG  ASP A 298      16.493  51.158 -19.463  1.00 19.25           C  
ATOM   2386  OD1 ASP A 298      15.528  50.439 -19.722  1.00 21.00           O  
ATOM   2387  OD2 ASP A 298      16.391  52.320 -19.004  1.00 19.16           O  
ATOM   2388  N   PRO A 299      16.376  47.587 -20.779  1.00 21.11           N  
ATOM   2389  CA  PRO A 299      15.685  47.011 -21.954  1.00 22.46           C  
ATOM   2390  C   PRO A 299      14.620  47.904 -22.647  1.00 23.03           C  
ATOM   2391  O   PRO A 299      13.913  47.451 -23.566  1.00 24.11           O  
ATOM   2392  CB  PRO A 299      15.040  45.742 -21.395  1.00 22.00           C  
ATOM   2393  CG  PRO A 299      15.400  45.658 -19.949  1.00 22.85           C  
ATOM   2394  CD  PRO A 299      15.926  46.957 -19.513  1.00 21.70           C  
ATOM   2395  N   ARG A 300      14.461  49.129 -22.155  1.00 24.08           N  
ATOM   2396  CA  ARG A 300      13.646  50.121 -22.793  1.00 24.21           C  
ATOM   2397  C   ARG A 300      14.503  51.118 -23.564  1.00 23.55           C  
ATOM   2398  O   ARG A 300      13.970  51.976 -24.248  1.00 25.38           O  
ATOM   2399  CB  ARG A 300      12.809  50.830 -21.770  1.00 24.53           C  
ATOM   2400  CG  ARG A 300      11.701  49.937 -21.291  1.00 26.50           C  
ATOM   2401  CD  ARG A 300      10.957  50.606 -20.195  1.00 28.60           C  
ATOM   2402  NE  ARG A 300      11.887  50.820 -19.090  1.00 35.25           N  
ATOM   2403  CZ  ARG A 300      11.562  51.397 -17.944  1.00 34.26           C  
ATOM   2404  NH1 ARG A 300      10.316  51.812 -17.727  1.00 35.63           N  
ATOM   2405  NH2 ARG A 300      12.508  51.565 -17.039  1.00 34.97           N  
ATOM   2406  N   GLU A 301      15.806  50.988 -23.483  1.00 21.94           N  
ATOM   2407  CA  GLU A 301      16.675  51.897 -24.185  1.00 23.58           C  
ATOM   2408  C   GLU A 301      17.376  51.170 -25.352  1.00 23.29           C  
ATOM   2409  O   GLU A 301      17.909  50.065 -25.153  1.00 21.34           O  
ATOM   2410  CB  GLU A 301      17.686  52.504 -23.215  1.00 23.58           C  
ATOM   2411  CG  GLU A 301      17.024  53.377 -22.164  1.00 27.90           C  
ATOM   2412  CD  GLU A 301      16.314  54.606 -22.754  1.00 33.36           C  
ATOM   2413  OE1 GLU A 301      15.128  54.871 -22.398  1.00 38.57           O  
ATOM   2414  OE2 GLU A 301      16.943  55.280 -23.599  1.00 38.72           O  
ATOM   2415  N   PRO A 302      17.385  51.784 -26.565  1.00 23.15           N  
ATOM   2416  CA  PRO A 302      18.015  51.177 -27.767  1.00 24.50           C  
ATOM   2417  C   PRO A 302      19.377  50.558 -27.558  1.00 24.91           C  
ATOM   2418  O   PRO A 302      19.605  49.463 -28.020  1.00 26.92           O  
ATOM   2419  CB  PRO A 302      18.112  52.349 -28.746  1.00 24.48           C  
ATOM   2420  CG  PRO A 302      16.994  53.167 -28.399  1.00 23.33           C  
ATOM   2421  CD  PRO A 302      16.765  53.064 -26.917  1.00 24.05           C  
ATOM   2422  N   ASN A 303      20.273  51.233 -26.848  1.00 26.30           N  
ATOM   2423  CA  ASN A 303      21.636  50.693 -26.643  1.00 25.85           C  
ATOM   2424  C   ASN A 303      21.726  49.838 -25.393  1.00 26.23           C  
ATOM   2425  O   ASN A 303      22.773  49.271 -25.116  1.00 26.46           O  
ATOM   2426  CB  ASN A 303      22.680  51.824 -26.607  1.00 27.24           C  
ATOM   2427  CG  ASN A 303      22.459  52.789 -25.451  1.00 28.95           C  
ATOM   2428  OD1 ASN A 303      21.726  52.472 -24.526  1.00 24.49           O  
ATOM   2429  ND2 ASN A 303      23.121  53.966 -25.489  1.00 27.70           N  
ATOM   2430  N   GLY A 304      20.623  49.734 -24.640  1.00 24.67           N  
ATOM   2431  CA  GLY A 304      20.576  48.905 -23.443  1.00 24.29           C  
ATOM   2432  C   GLY A 304      21.354  49.496 -22.270  1.00 23.55           C  
ATOM   2433  O   GLY A 304      21.501  48.844 -21.263  1.00 22.12           O  
ATOM   2434  N   LYS A 305      21.813  50.746 -22.371  1.00 23.06           N  
ATOM   2435  CA  LYS A 305      22.697  51.299 -21.305  1.00 23.80           C  
ATOM   2436  C   LYS A 305      21.894  51.908 -20.151  1.00 22.05           C  
ATOM   2437  O   LYS A 305      20.808  52.386 -20.336  1.00 20.84           O  
ATOM   2438  CB  LYS A 305      23.710  52.306 -21.860  1.00 24.93           C  
ATOM   2439  CG  LYS A 305      24.888  51.659 -22.579  1.00 26.17           C  
ATOM   2440  CD  LYS A 305      25.905  52.763 -23.058  1.00 28.06           C  
ATOM   2441  CE  LYS A 305      27.313  52.152 -23.238  1.00 32.47           C  
ATOM   2442  NZ  LYS A 305      27.878  52.384 -24.596  1.00 36.23           N  
ATOM   2443  N   SER A 306      22.461  51.881 -18.958  1.00 22.29           N  
ATOM   2444  CA  SER A 306      21.811  52.383 -17.755  1.00 22.39           C  
ATOM   2445  C   SER A 306      22.663  53.466 -17.040  1.00 21.75           C  
ATOM   2446  O   SER A 306      23.870  53.366 -17.026  1.00 19.69           O  
ATOM   2447  CB  SER A 306      21.661  51.193 -16.792  1.00 23.32           C  
ATOM   2448  OG  SER A 306      21.036  51.572 -15.602  1.00 21.23           O  
ATOM   2449  N   ASP A 307      22.037  54.465 -16.421  1.00 21.60           N  
ATOM   2450  CA  ASP A 307      22.799  55.387 -15.507  1.00 22.43           C  
ATOM   2451  C   ASP A 307      22.882  54.917 -14.035  1.00 21.55           C  
ATOM   2452  O   ASP A 307      23.139  55.739 -13.148  1.00 20.47           O  
ATOM   2453  CB  ASP A 307      22.237  56.818 -15.547  1.00 23.18           C  
ATOM   2454  CG  ASP A 307      22.428  57.491 -16.922  1.00 25.68           C  
ATOM   2455  OD1 ASP A 307      23.389  57.144 -17.629  1.00 26.03           O  
ATOM   2456  OD2 ASP A 307      21.597  58.334 -17.296  1.00 24.43           O  
ATOM   2457  N   ARG A 308      22.655  53.625 -13.791  1.00 20.89           N  
ATOM   2458  CA  ARG A 308      22.870  53.014 -12.457  1.00 20.69           C  
ATOM   2459  C   ARG A 308      24.268  52.411 -12.442  1.00 19.98           C  
ATOM   2460  O   ARG A 308      24.775  52.090 -13.506  1.00 21.07           O  
ATOM   2461  CB  ARG A 308      21.826  51.949 -12.162  1.00 20.23           C  
ATOM   2462  CG  ARG A 308      20.430  52.494 -11.936  1.00 19.64           C  
ATOM   2463  CD  ARG A 308      19.371  51.429 -11.879  1.00 20.19           C  
ATOM   2464  NE  ARG A 308      18.053  51.975 -11.560  1.00 21.34           N  
ATOM   2465  CZ  ARG A 308      17.507  51.972 -10.342  1.00 23.19           C  
ATOM   2466  NH1 ARG A 308      18.134  51.427  -9.285  1.00 18.16           N  
ATOM   2467  NH2 ARG A 308      16.289  52.480 -10.194  1.00 25.75           N  
ATOM   2468  N   GLU A 309      24.903  52.327 -11.269  1.00 19.82           N  
ATOM   2469  CA  GLU A 309      26.209  51.711 -11.092  1.00 20.39           C  
ATOM   2470  C   GLU A 309      26.154  50.232 -10.595  1.00 18.85           C  
ATOM   2471  O   GLU A 309      25.278  49.882  -9.862  1.00 18.48           O  
ATOM   2472  CB  GLU A 309      27.042  52.516 -10.085  1.00 21.87           C  
ATOM   2473  CG  GLU A 309      27.492  53.948 -10.567  1.00 25.41           C  
ATOM   2474  CD  GLU A 309      28.301  53.936 -11.885  1.00 30.62           C  
ATOM   2475  OE1 GLU A 309      29.227  53.102 -12.024  1.00 36.68           O  
ATOM   2476  OE2 GLU A 309      27.984  54.737 -12.798  1.00 31.20           O  
ATOM   2477  N   PRO A 310      27.150  49.413 -10.941  1.00 18.37           N  
ATOM   2478  CA  PRO A 310      27.122  48.027 -10.488  1.00 18.42           C  
ATOM   2479  C   PRO A 310      27.162  47.959  -9.005  1.00 17.91           C  
ATOM   2480  O   PRO A 310      27.770  48.804  -8.392  1.00 17.73           O  
ATOM   2481  CB  PRO A 310      28.388  47.388 -11.097  1.00 18.21           C  
ATOM   2482  CG  PRO A 310      28.740  48.302 -12.238  1.00 19.96           C  
ATOM   2483  CD  PRO A 310      28.337  49.685 -11.771  1.00 18.40           C  
ATOM   2484  N   LEU A 311      26.436  46.987  -8.443  1.00 17.54           N  
ATOM   2485  CA  LEU A 311      26.365  46.818  -7.004  1.00 16.68           C  
ATOM   2486  C   LEU A 311      26.495  45.335  -6.730  1.00 15.56           C  
ATOM   2487  O   LEU A 311      25.758  44.523  -7.336  1.00 15.84           O  
ATOM   2488  CB  LEU A 311      25.026  47.372  -6.578  1.00 17.06           C  
ATOM   2489  CG  LEU A 311      24.479  47.137  -5.185  1.00 17.92           C  
ATOM   2490  CD1 LEU A 311      25.410  47.787  -4.148  1.00 17.58           C  
ATOM   2491  CD2 LEU A 311      23.089  47.679  -5.115  1.00 16.33           C  
ATOM   2492  N   SER A 312      27.439  44.949  -5.875  1.00 14.19           N  
ATOM   2493  CA  SER A 312      27.700  43.556  -5.584  1.00 13.71           C  
ATOM   2494  C   SER A 312      26.520  43.009  -4.804  1.00 12.61           C  
ATOM   2495  O   SER A 312      25.929  43.715  -4.011  1.00 12.09           O  
ATOM   2496  CB  SER A 312      29.017  43.408  -4.763  1.00 14.90           C  
ATOM   2497  OG  SER A 312      28.758  43.668  -3.383  1.00 20.00           O  
ATOM   2498  N   TYR A 313      26.130  41.776  -5.055  1.00 13.18           N  
ATOM   2499  CA  TYR A 313      24.985  41.199  -4.298  1.00 12.69           C  
ATOM   2500  C   TYR A 313      25.200  41.242  -2.767  1.00 11.69           C  
ATOM   2501  O   TYR A 313      24.336  41.648  -2.020  1.00 12.27           O  
ATOM   2502  CB  TYR A 313      24.601  39.795  -4.793  1.00 12.86           C  
ATOM   2503  CG  TYR A 313      23.128  39.564  -4.516  1.00  9.89           C  
ATOM   2504  CD1 TYR A 313      22.179  39.940  -5.416  1.00 10.74           C  
ATOM   2505  CD2 TYR A 313      22.728  39.114  -3.316  1.00  6.79           C  
ATOM   2506  CE1 TYR A 313      20.833  39.783  -5.163  1.00 10.30           C  
ATOM   2507  CE2 TYR A 313      21.417  38.949  -3.019  1.00 10.57           C  
ATOM   2508  CZ  TYR A 313      20.453  39.307  -3.950  1.00 11.44           C  
ATOM   2509  OH  TYR A 313      19.130  39.192  -3.610  1.00 10.80           O  
ATOM   2510  N   GLY A 314      26.396  40.897  -2.308  1.00 12.77           N  
ATOM   2511  CA  GLY A 314      26.688  40.904  -0.896  1.00 13.82           C  
ATOM   2512  C   GLY A 314      26.453  42.243  -0.224  1.00 14.00           C  
ATOM   2513  O   GLY A 314      25.897  42.325   0.867  1.00 15.11           O  
ATOM   2514  N   ASP A 315      26.911  43.296  -0.871  1.00 15.40           N  
ATOM   2515  CA  ASP A 315      26.622  44.655  -0.436  1.00 15.29           C  
ATOM   2516  C   ASP A 315      25.119  44.958  -0.388  1.00 14.69           C  
ATOM   2517  O   ASP A 315      24.623  45.533   0.549  1.00 13.12           O  
ATOM   2518  CB  ASP A 315      27.272  45.673  -1.382  1.00 15.74           C  
ATOM   2519  CG  ASP A 315      28.788  45.908  -1.110  1.00 24.50           C  
ATOM   2520  OD1 ASP A 315      29.384  46.727  -1.901  1.00 33.10           O  
ATOM   2521  OD2 ASP A 315      29.365  45.323  -0.143  1.00 32.49           O  
ATOM   2522  N   TYR A 316      24.427  44.603  -1.463  1.00 13.57           N  
ATOM   2523  CA  TYR A 316      23.003  44.840  -1.573  1.00 13.02           C  
ATOM   2524  C   TYR A 316      22.262  44.152  -0.442  1.00 12.85           C  
ATOM   2525  O   TYR A 316      21.421  44.773   0.246  1.00 10.91           O  
ATOM   2526  CB  TYR A 316      22.511  44.368  -2.915  1.00 11.99           C  
ATOM   2527  CG  TYR A 316      21.029  44.193  -3.025  1.00 10.62           C  
ATOM   2528  CD1 TYR A 316      20.184  45.290  -3.222  1.00 10.61           C  
ATOM   2529  CD2 TYR A 316      20.456  42.913  -2.834  1.00  8.85           C  
ATOM   2530  CE1 TYR A 316      18.791  45.118  -3.296  1.00 10.75           C  
ATOM   2531  CE2 TYR A 316      19.094  42.726  -2.883  1.00 12.59           C  
ATOM   2532  CZ  TYR A 316      18.251  43.812  -3.113  1.00 11.16           C  
ATOM   2533  OH  TYR A 316      16.918  43.584  -3.183  1.00 10.05           O  
ATOM   2534  N   LEU A 317      22.635  42.903  -0.213  1.00 13.81           N  
ATOM   2535  CA  LEU A 317      21.923  42.063   0.773  1.00 14.47           C  
ATOM   2536  C   LEU A 317      22.094  42.582   2.226  1.00 16.29           C  
ATOM   2537  O   LEU A 317      21.107  42.775   2.970  1.00 15.43           O  
ATOM   2538  CB  LEU A 317      22.358  40.597   0.632  1.00 13.80           C  
ATOM   2539  CG  LEU A 317      21.643  39.601   1.547  1.00 13.94           C  
ATOM   2540  CD1 LEU A 317      20.148  39.652   1.232  1.00 12.21           C  
ATOM   2541  CD2 LEU A 317      22.219  38.135   1.463  1.00 12.11           C  
ATOM   2542  N   GLN A 318      23.329  42.797   2.636  1.00 18.42           N  
ATOM   2543  CA  GLN A 318      23.561  43.209   4.008  1.00 20.23           C  
ATOM   2544  C   GLN A 318      22.934  44.568   4.320  1.00 21.00           C  
ATOM   2545  O   GLN A 318      22.250  44.715   5.357  1.00 20.97           O  
ATOM   2546  CB  GLN A 318      25.044  43.065   4.433  1.00 20.99           C  
ATOM   2547  CG  GLN A 318      26.029  43.813   3.610  1.00 26.51           C  
ATOM   2548  CD  GLN A 318      27.522  43.442   3.951  1.00 25.91           C  
ATOM   2549  OE1 GLN A 318      28.267  43.003   3.070  1.00 29.56           O  
ATOM   2550  NE2 GLN A 318      27.929  43.659   5.214  1.00 28.96           N  
ATOM   2551  N   ASN A 319      23.056  45.531   3.411  1.00 21.98           N  
ATOM   2552  CA  ASN A 319      22.323  46.813   3.597  1.00 21.48           C  
ATOM   2553  C   ASN A 319      20.803  46.652   3.575  1.00 20.15           C  
ATOM   2554  O   ASN A 319      20.090  47.273   4.344  1.00 18.93           O  
ATOM   2555  CB  ASN A 319      22.712  47.822   2.495  1.00 23.29           C  
ATOM   2556  CG  ASN A 319      21.653  48.966   2.318  1.00 27.87           C  
ATOM   2557  OD1 ASN A 319      20.715  48.865   1.472  1.00 37.30           O  
ATOM   2558  ND2 ASN A 319      21.828  50.083   3.084  1.00 34.08           N  
ATOM   2559  N   GLY A 320      20.303  45.872   2.619  1.00 18.58           N  
ATOM   2560  CA  GLY A 320      18.894  45.682   2.457  1.00 17.87           C  
ATOM   2561  C   GLY A 320      18.258  45.095   3.702  1.00 17.36           C  
ATOM   2562  O   GLY A 320      17.176  45.529   4.120  1.00 16.75           O  
ATOM   2563  N   LEU A 321      18.897  44.085   4.272  1.00 15.88           N  
ATOM   2564  CA  LEU A 321      18.278  43.426   5.375  1.00 17.31           C  
ATOM   2565  C   LEU A 321      18.270  44.256   6.620  1.00 17.78           C  
ATOM   2566  O   LEU A 321      17.290  44.199   7.398  1.00 18.80           O  
ATOM   2567  CB  LEU A 321      18.885  42.057   5.630  1.00 16.85           C  
ATOM   2568  CG  LEU A 321      18.733  41.013   4.493  1.00 14.74           C  
ATOM   2569  CD1 LEU A 321      19.379  39.743   4.984  1.00 13.62           C  
ATOM   2570  CD2 LEU A 321      17.246  40.708   4.004  1.00 12.22           C  
ATOM   2571  N   VAL A 322      19.322  45.048   6.803  1.00 18.14           N  
ATOM   2572  CA  VAL A 322      19.298  46.067   7.862  1.00 19.01           C  
ATOM   2573  C   VAL A 322      18.193  47.069   7.692  1.00 19.49           C  
ATOM   2574  O   VAL A 322      17.439  47.293   8.639  1.00 19.03           O  
ATOM   2575  CB  VAL A 322      20.621  46.824   7.960  1.00 19.39           C  
ATOM   2576  CG1 VAL A 322      20.467  47.928   9.042  1.00 21.79           C  
ATOM   2577  CG2 VAL A 322      21.747  45.823   8.285  1.00 19.80           C  
ATOM   2578  N   SER A 323      18.063  47.642   6.482  1.00 20.33           N  
ATOM   2579  CA  SER A 323      17.073  48.680   6.246  1.00 20.90           C  
ATOM   2580  C   SER A 323      15.654  48.189   6.422  1.00 21.60           C  
ATOM   2581  O   SER A 323      14.792  48.964   6.832  1.00 21.58           O  
ATOM   2582  CB  SER A 323      17.219  49.277   4.857  1.00 21.82           C  
ATOM   2583  OG  SER A 323      18.604  49.525   4.606  1.00 27.29           O  
ATOM   2584  N   LEU A 324      15.396  46.936   6.033  1.00 20.65           N  
ATOM   2585  CA  LEU A 324      14.085  46.363   6.178  1.00 21.05           C  
ATOM   2586  C   LEU A 324      13.682  46.265   7.672  1.00 21.03           C  
ATOM   2587  O   LEU A 324      12.552  46.580   8.043  1.00 19.78           O  
ATOM   2588  CB  LEU A 324      14.045  44.952   5.533  1.00 21.19           C  
ATOM   2589  CG  LEU A 324      12.822  44.484   4.697  1.00 21.99           C  
ATOM   2590  CD1 LEU A 324      12.578  42.943   4.773  1.00 20.16           C  
ATOM   2591  CD2 LEU A 324      11.482  45.330   4.865  1.00 18.92           C  
ATOM   2592  N   ILE A 325      14.609  45.789   8.503  1.00 21.73           N  
ATOM   2593  CA  ILE A 325      14.432  45.790   9.970  1.00 22.59           C  
ATOM   2594  C   ILE A 325      14.166  47.246  10.440  1.00 22.83           C  
ATOM   2595  O   ILE A 325      13.203  47.519  11.161  1.00 21.48           O  
ATOM   2596  CB  ILE A 325      15.666  45.162  10.712  1.00 22.63           C  
ATOM   2597  CG1 ILE A 325      15.798  43.658  10.376  1.00 25.44           C  
ATOM   2598  CG2 ILE A 325      15.606  45.300  12.276  1.00 22.28           C  
ATOM   2599  CD1 ILE A 325      17.246  43.090  10.503  1.00 22.41           C  
ATOM   2600  N   ASN A 326      14.969  48.187   9.980  1.00 23.35           N  
ATOM   2601  CA  ASN A 326      14.715  49.588  10.385  1.00 24.61           C  
ATOM   2602  C   ASN A 326      13.320  50.103   9.973  1.00 23.98           C  
ATOM   2603  O   ASN A 326      12.625  50.717  10.794  1.00 21.26           O  
ATOM   2604  CB  ASN A 326      15.825  50.519   9.853  1.00 25.30           C  
ATOM   2605  CG  ASN A 326      17.184  50.238  10.512  1.00 29.58           C  
ATOM   2606  OD1 ASN A 326      17.238  49.634  11.585  1.00 34.41           O  
ATOM   2607  ND2 ASN A 326      18.288  50.662   9.869  1.00 28.23           N  
ATOM   2608  N   LYS A 327      12.915  49.830   8.729  1.00 23.30           N  
ATOM   2609  CA  LYS A 327      11.653  50.365   8.184  1.00 23.87           C  
ATOM   2610  C   LYS A 327      10.461  49.718   8.873  1.00 22.65           C  
ATOM   2611  O   LYS A 327       9.536  50.388   9.322  1.00 21.09           O  
ATOM   2612  CB  LYS A 327      11.511  50.059   6.663  1.00 23.55           C  
ATOM   2613  CG  LYS A 327      10.386  50.858   5.944  1.00 25.16           C  
ATOM   2614  CD  LYS A 327       9.763  50.110   4.668  1.00 26.88           C  
ATOM   2615  CE  LYS A 327       8.331  50.621   4.257  1.00 27.54           C  
ATOM   2616  NZ  LYS A 327       7.058  50.366   5.231  1.00 21.05           N  
ATOM   2617  N   ASN A 328      10.486  48.383   8.910  1.00 21.83           N  
ATOM   2618  CA  ASN A 328       9.287  47.613   9.267  1.00 21.54           C  
ATOM   2619  C   ASN A 328       9.403  46.800  10.563  1.00 21.96           C  
ATOM   2620  O   ASN A 328       8.497  46.007  10.860  1.00 22.31           O  
ATOM   2621  CB  ASN A 328       8.913  46.694   8.091  1.00 21.81           C  
ATOM   2622  CG  ASN A 328       8.085  47.377   7.016  1.00 23.83           C  
ATOM   2623  OD1 ASN A 328       7.979  48.615   6.987  1.00 20.99           O  
ATOM   2624  ND2 ASN A 328       7.438  46.538   6.122  1.00 17.21           N  
ATOM   2625  N   GLY A 329      10.498  46.930  11.307  1.00 20.19           N  
ATOM   2626  CA  GLY A 329      10.650  46.201  12.564  1.00 19.99           C  
ATOM   2627  C   GLY A 329      11.348  44.835  12.510  1.00 19.20           C  
ATOM   2628  O   GLY A 329      11.315  44.149  11.496  1.00 19.63           O  
ATOM   2629  N   GLN A 330      11.967  44.424  13.614  1.00 18.46           N  
ATOM   2630  CA  GLN A 330      12.530  43.098  13.762  1.00 18.81           C  
ATOM   2631  C   GLN A 330      11.420  42.066  13.633  1.00 19.40           C  
ATOM   2632  O   GLN A 330      10.396  42.154  14.328  1.00 19.45           O  
ATOM   2633  CB  GLN A 330      13.224  42.925  15.136  1.00 19.80           C  
ATOM   2634  CG  GLN A 330      13.736  41.469  15.432  1.00 18.18           C  
ATOM   2635  CD  GLN A 330      14.724  41.007  14.414  1.00 18.46           C  
ATOM   2636  OE1 GLN A 330      15.790  41.625  14.256  1.00 16.16           O  
ATOM   2637  NE2 GLN A 330      14.412  39.901  13.710  1.00 15.35           N  
ATOM   2638  N   THR A 331      11.618  41.122  12.711  1.00 18.89           N  
ATOM   2639  CA  THR A 331      10.657  40.034  12.509  1.00 19.46           C  
ATOM   2640  C   THR A 331      10.910  38.893  13.496  1.00 18.77           C  
ATOM   2641  O   THR A 331      10.110  37.963  13.443  1.00 19.84           O  
ATOM   2642  CB  THR A 331      10.585  39.530  11.033  1.00 19.57           C  
ATOM   2643  OG1 THR A 331      11.796  38.869  10.623  1.00 22.57           O  
ATOM   2644  CG2 THR A 331      10.260  40.753  10.101  1.00 20.17           C  
ATOM   2645  OXT THR A 331      11.850  38.899  14.352  1.00 18.15           O  
TER    2646      THR A 331                                                      
HETATM 2647 FE   FE2 A1332       7.661  40.641   0.811  1.00 12.28          FE  
HETATM 2648  O   V10 A1333      18.270  36.354   6.365  1.00 10.98           O  
HETATM 2649  C   V10 A1333      17.282  36.244   5.577  1.00 11.26           C  
HETATM 2650  OXT V10 A1333      17.378  35.962   4.361  1.00 10.31           O  
HETATM 2651  CA  V10 A1333      15.872  36.419   6.070  1.00 12.06           C  
HETATM 2652  N   V10 A1333      15.733  36.479   7.528  1.00 11.31           N  
HETATM 2653  CB  V10 A1333      15.304  37.674   5.401  1.00 11.40           C  
HETATM 2654  CAJ V10 A1333      13.872  37.938   5.959  1.00 15.26           C  
HETATM 2655  CAL V10 A1333      13.372  39.231   5.331  1.00 15.47           C  
HETATM 2656  CAT V10 A1333      12.008  39.673   5.729  1.00 16.56           C  
HETATM 2657  OAE V10 A1333      11.747  40.020   6.880  1.00 16.21           O  
HETATM 2658  NAO V10 A1333      11.095  39.669   4.752  1.00 17.40           N  
HETATM 2659  CAW V10 A1333       9.744  40.129   5.143  1.00 18.26           C  
HETATM 2660  CAK V10 A1333       9.133  40.791   3.915  1.00 18.04           C  
HETATM 2661  SAI V10 A1333       9.302  39.738   2.441  1.00 14.48           S  
HETATM 2662  CAU V10 A1333       8.919  38.977   5.616  1.00 23.56           C  
HETATM 2663  OAF V10 A1333       9.366  37.858   5.831  1.00 23.18           O  
HETATM 2664  OAP V10 A1333       7.552  39.300   5.807  1.00 26.26           O  
HETATM 2665  CAX V10 A1333       6.686  38.386   6.418  1.00 27.71           C  
HETATM 2666  CAS V10 A1333       5.588  38.084   5.451  1.00 26.77           C  
HETATM 2667  OAD V10 A1333       4.601  37.404   5.857  1.00 30.07           O  
HETATM 2668  OAH V10 A1333       5.722  38.535   4.291  1.00 27.42           O  
HETATM 2669  CAN V10 A1333       6.098  39.122   7.602  1.00 27.03           C  
HETATM 2670  SAQ V10 A1333       7.202  39.232   8.938  1.00 29.17           S  
HETATM 2671  CAA V10 A1333       7.964  37.623   9.214  1.00 24.59           C  
HETATM 2672  O   HOH A2001      -5.331  37.856  -7.564  1.00 13.85           O  
HETATM 2673  O   HOH A2002       8.607  21.459 -22.780  1.00 32.70           O  
HETATM 2674  O   HOH A2003      -5.591  37.013 -11.681  1.00 24.83           O  
HETATM 2675  O   HOH A2004      -4.062  32.851 -15.238  1.00 18.73           O  
HETATM 2676  O   HOH A2005       3.458  27.788 -20.349  1.00 21.24           O  
HETATM 2677  O   HOH A2006       1.042  29.142 -18.920  1.00 16.65           O  
HETATM 2678  O   HOH A2007       3.020  42.799 -21.799  1.00 12.90           O  
HETATM 2679  O   HOH A2008       1.694  46.116 -18.798  1.00 27.90           O  
HETATM 2680  O   HOH A2009      11.097  22.918 -22.600  1.00 23.15           O  
HETATM 2681  O   HOH A2010       3.847  19.144 -12.133  1.00 31.31           O  
HETATM 2682  O   HOH A2011      14.257  23.721 -29.103  1.00 20.54           O  
HETATM 2683  O   HOH A2012      -0.716  20.726  -3.851  1.00 16.68           O  
HETATM 2684  O   HOH A2013      -1.597  14.160   7.052  1.00 33.32           O  
HETATM 2685  O   HOH A2014      13.187  14.020   2.572  1.00 13.81           O  
HETATM 2686  O   HOH A2015       5.324  27.769 -23.500  1.00 17.12           O  
HETATM 2687  O   HOH A2016       8.612  31.647  22.500  1.00 13.14           O  
HETATM 2688  O   HOH A2017       3.457  33.816 -24.533  1.00  8.57           O  
HETATM 2689  O   HOH A2018      24.275  42.757  19.959  1.00 34.79           O  
HETATM 2690  O   HOH A2019       1.571  37.076 -17.737  1.00 20.11           O  
HETATM 2691  O   HOH A2020       4.949  41.052 -22.684  1.00 14.23           O  
HETATM 2692  O   HOH A2021       2.241  43.595 -19.005  1.00 12.21           O  
HETATM 2693  O   HOH A2022       0.180  39.456 -17.591  1.00 24.63           O  
HETATM 2694  O   HOH A2023       6.830  48.065 -19.741  1.00 23.38           O  
HETATM 2695  O   HOH A2024      -0.717  40.291 -15.248  1.00 22.90           O  
HETATM 2696  O   HOH A2025       7.652  41.306 -10.111  1.00 12.57           O  
HETATM 2697  O   HOH A2026      26.816  22.146   8.839  1.00 19.69           O  
HETATM 2698  O   HOH A2027      34.855  24.259  -0.161  1.00 23.73           O  
HETATM 2699  O   HOH A2028       7.151  20.321 -13.719  1.00 23.80           O  
HETATM 2700  O   HOH A2029      10.588  21.102  -9.319  1.00 19.24           O  
HETATM 2701  O   HOH A2030       2.849  21.633  -9.773  1.00 22.33           O  
HETATM 2702  O   HOH A2031      11.003  18.889  -6.705  1.00 20.60           O  
HETATM 2703  O   HOH A2032       7.023  16.349  -6.505  1.00 19.16           O  
HETATM 2704  O   HOH A2033       3.413  20.142  -7.377  1.00 26.93           O  
HETATM 2705  O   HOH A2034       8.378  18.606  -0.406  1.00 12.49           O  
HETATM 2706  O   HOH A2035       7.579  14.420  -2.440  1.00 12.40           O  
HETATM 2707  O   HOH A2036       9.271  18.225  -4.163  1.00  9.04           O  
HETATM 2708  O   HOH A2037       6.896  15.937  19.153  1.00 25.54           O  
HETATM 2709  O   HOH A2038      -0.133  14.469   4.684  1.00 13.75           O  
HETATM 2710  O   HOH A2039       1.642  19.046  -3.354  1.00 11.46           O  
HETATM 2711  O   HOH A2040       2.135  14.606   3.323  1.00  7.69           O  
HETATM 2712  O   HOH A2041      16.730  13.303   3.411  1.00 22.23           O  
HETATM 2713  O   HOH A2042      19.748  17.425   0.922  1.00 17.59           O  
HETATM 2714  O   HOH A2043       8.845  16.114  -0.821  1.00 11.04           O  
HETATM 2715  O   HOH A2044      12.430  13.863  -0.904  1.00 21.65           O  
HETATM 2716  O   HOH A2045       8.829  18.187  10.550  1.00 22.04           O  
HETATM 2717  O   HOH A2046      10.326  13.789   7.258  1.00 20.22           O  
HETATM 2718  O   HOH A2047      18.824  45.503 -22.618  1.00 17.58           O  
HETATM 2719  O   HOH A2048       4.682  13.492   7.312  1.00 24.38           O  
HETATM 2720  O   HOH A2049       9.637  19.432  20.818  1.00 18.80           O  
HETATM 2721  O   HOH A2050      32.995  26.036  -1.689  1.00 21.60           O  
HETATM 2722  O   HOH A2051      12.078  21.044  24.850  1.00 17.91           O  
HETATM 2723  O   HOH A2052      10.771  30.610  23.977  1.00 14.88           O  
HETATM 2724  O   HOH A2053      15.588  20.660  19.759  1.00 21.59           O  
HETATM 2725  O   HOH A2054       4.682  26.757  19.566  1.00 26.96           O  
HETATM 2726  O   HOH A2055       6.938  29.447  22.616  1.00 13.53           O  
HETATM 2727  O   HOH A2056      19.101  29.419  25.162  1.00 14.29           O  
HETATM 2728  O   HOH A2057      21.713  40.914  20.803  1.00 27.71           O  
HETATM 2729  O   HOH A2058      14.239  40.756  21.062  1.00 27.32           O  
HETATM 2730  O   HOH A2059      24.631  36.004  28.661  1.00 43.61           O  
HETATM 2731  O   HOH A2060      22.320  34.963  28.468  1.00 19.18           O  
HETATM 2732  O   HOH A2061      21.726  30.028  24.426  1.00 16.84           O  
HETATM 2733  O   HOH A2062      26.511  32.329  17.971  1.00 21.25           O  
HETATM 2734  O   HOH A2063      24.831  30.149  17.879  1.00 13.22           O  
HETATM 2735  O   HOH A2064      21.347  28.099  18.229  1.00 10.66           O  
HETATM 2736  O   HOH A2065      19.667  38.825  14.605  1.00 12.59           O  
HETATM 2737  O   HOH A2066       7.784  32.203  19.898  1.00 11.30           O  
HETATM 2738  O   HOH A2067       7.554  33.985  23.150  1.00 13.96           O  
HETATM 2739  O   HOH A2068       3.797  40.627  26.329  1.00 15.37           O  
HETATM 2740  O   HOH A2069      -0.278  37.016  21.458  1.00 23.20           O  
HETATM 2741  O   HOH A2070     -11.228  38.406  12.403  1.00 21.43           O  
HETATM 2742  O   HOH A2071       2.732  39.689  14.295  1.00 23.24           O  
HETATM 2743  O   HOH A2072       5.606  27.756  16.408  1.00 23.62           O  
HETATM 2744  O   HOH A2073       2.843  32.530  16.950  1.00 21.47           O  
HETATM 2745  O   HOH A2074      13.048  33.894  10.111  1.00 22.22           O  
HETATM 2746  O   HOH A2075      26.815  41.139 -17.088  1.00 41.01           O  
HETATM 2747  O   HOH A2076      24.920  23.163   7.039  1.00 13.63           O  
HETATM 2748  O   HOH A2077      25.606  20.363   4.967  1.00 20.66           O  
HETATM 2749  O   HOH A2078      24.390  20.713   0.908  1.00 19.37           O  
HETATM 2750  O   HOH A2079      30.710  23.578   1.348  1.00 14.32           O  
HETATM 2751  O   HOH A2080      24.543  26.126   6.799  1.00 14.05           O  
HETATM 2752  O   HOH A2081      34.160  27.568  11.014  1.00 19.00           O  
HETATM 2753  O   HOH A2082      31.965  20.210   4.988  1.00 18.10           O  
HETATM 2754  O   HOH A2083      33.505  23.759   1.872  1.00 17.10           O  
HETATM 2755  O   HOH A2084      37.326  33.361   2.177  1.00 12.69           O  
HETATM 2756  O   HOH A2085      31.130  33.529  -2.118  1.00 13.52           O  
HETATM 2757  O   HOH A2086      23.336  31.105  12.300  1.00 23.27           O  
HETATM 2758  O   HOH A2087      27.894  30.681  11.599  1.00 13.30           O  
HETATM 2759  O   HOH A2088      24.166  22.918   9.898  1.00 21.58           O  
HETATM 2760  O   HOH A2089      19.057  27.684  10.941  1.00  7.98           O  
HETATM 2761  O   HOH A2090      22.463  22.758  14.942  1.00 22.91           O  
HETATM 2762  O   HOH A2091      18.196  18.224  13.428  1.00 21.86           O  
HETATM 2763  O   HOH A2092      20.887  15.972  16.679  1.00 25.04           O  
HETATM 2764  O   HOH A2093      15.874  10.283  13.319  1.00 17.95           O  
HETATM 2765  O   HOH A2094      19.705  15.766  12.051  1.00 18.22           O  
HETATM 2766  O   HOH A2095       9.286  16.911  19.783  1.00 17.26           O  
HETATM 2767  O   HOH A2096      15.815  16.970  12.349  1.00 11.04           O  
HETATM 2768  O   HOH A2097       9.369  18.402  13.387  1.00 19.04           O  
HETATM 2769  O   HOH A2098      10.400  15.621   9.583  1.00 20.12           O  
HETATM 2770  O   HOH A2099      13.116  13.761   6.237  1.00 10.83           O  
HETATM 2771  O   HOH A2100      18.268  15.845   3.072  1.00 13.82           O  
HETATM 2772  O   HOH A2101      16.692  14.938   9.692  1.00 11.70           O  
HETATM 2773  O   HOH A2102      12.364  17.800   1.136  1.00  9.11           O  
HETATM 2774  O   HOH A2103      23.978  20.151   7.029  1.00 31.19           O  
HETATM 2775  O   HOH A2104      20.338  16.251   4.800  1.00 15.63           O  
HETATM 2776  O   HOH A2105      22.193  22.904   7.062  1.00 13.03           O  
HETATM 2777  O   HOH A2106      16.667  14.143   0.744  1.00 19.52           O  
HETATM 2778  O   HOH A2107      18.741  21.764  -6.684  1.00 26.10           O  
HETATM 2779  O   HOH A2108      21.747  19.434   1.683  1.00 11.00           O  
HETATM 2780  O   HOH A2109      13.091  21.306  -8.010  1.00 25.21           O  
HETATM 2781  O   HOH A2110      10.731  19.325  -0.850  1.00 11.87           O  
HETATM 2782  O   HOH A2111      13.942  16.040  -5.091  1.00 17.66           O  
HETATM 2783  O   HOH A2112      11.512  16.146  -2.315  1.00 20.74           O  
HETATM 2784  O   HOH A2113      15.953  18.656  -6.290  1.00 28.14           O  
HETATM 2785  O   HOH A2114      16.121  23.748 -12.566  1.00 19.15           O  
HETATM 2786  O   HOH A2115      19.157  23.817 -10.365  1.00 24.91           O  
HETATM 2787  O   HOH A2116      16.071  24.627 -15.433  1.00 13.15           O  
HETATM 2788  O   HOH A2117       7.747  38.913 -11.972  1.00 11.86           O  
HETATM 2789  O   HOH A2118      16.135  36.309 -24.665  1.00 12.65           O  
HETATM 2790  O   HOH A2119      18.503  42.776 -23.317  1.00 22.52           O  
HETATM 2791  O   HOH A2120      18.247  39.065 -27.685  1.00 22.13           O  
HETATM 2792  O   HOH A2121      18.714  42.226 -25.851  1.00 18.82           O  
HETATM 2793  O   HOH A2122      23.077  37.427 -22.583  1.00 22.68           O  
HETATM 2794  O   HOH A2123      19.284  33.051 -15.916  1.00 14.73           O  
HETATM 2795  O   HOH A2124      21.409  27.832 -11.190  1.00 14.33           O  
HETATM 2796  O   HOH A2125      26.532  24.257 -10.604  1.00 29.76           O  
HETATM 2797  O   HOH A2126      28.223  25.260  -7.075  1.00 13.86           O  
HETATM 2798  O   HOH A2127      30.420  24.874  -0.946  1.00 14.92           O  
HETATM 2799  O   HOH A2128      27.676  21.696  -4.657  1.00 12.52           O  
HETATM 2800  O   HOH A2129      25.370  31.925  -6.010  1.00 11.45           O  
HETATM 2801  O   HOH A2130      28.449  33.855  -1.263  1.00  6.63           O  
HETATM 2802  O   HOH A2131      22.400  31.029   1.965  1.00  8.83           O  
HETATM 2803  O   HOH A2132       1.551  28.498  20.638  1.00 30.15           O  
HETATM 2804  O   HOH A2133      -4.445  35.880  22.915  1.00 23.18           O  
HETATM 2805  O   HOH A2134      -1.748  35.634  12.723  1.00 14.90           O  
HETATM 2806  O   HOH A2135      -0.278  40.064  13.187  1.00 17.27           O  
HETATM 2807  O   HOH A2136      -4.146  47.642  16.390  1.00 17.91           O  
HETATM 2808  O   HOH A2137      -2.819  44.510  22.922  1.00 29.38           O  
HETATM 2809  O   HOH A2138      -0.255  53.857   9.268  1.00 17.61           O  
HETATM 2810  O   HOH A2139      -4.138  52.006  14.705  1.00 28.77           O  
HETATM 2811  O   HOH A2140      -7.225  47.349   2.029  1.00 17.26           O  
HETATM 2812  O   HOH A2141      -6.973  43.015   7.388  1.00 19.22           O  
HETATM 2813  O   HOH A2142      -8.784  45.801   7.747  1.00 18.07           O  
HETATM 2814  O   HOH A2143       1.330  50.769  10.079  1.00 24.43           O  
HETATM 2815  O   HOH A2144       0.572  50.319   3.502  1.00 17.98           O  
HETATM 2816  O   HOH A2145       5.758  46.166   9.385  1.00 15.50           O  
HETATM 2817  O   HOH A2146       9.197  49.508  -6.253  1.00 29.65           O  
HETATM 2818  O   HOH A2147      11.113  48.467   1.353  1.00 11.54           O  
HETATM 2819  O   HOH A2148      13.327  49.203  -6.270  1.00 14.62           O  
HETATM 2820  O   HOH A2149       7.592  38.775  -0.370  1.00  7.50           O  
HETATM 2821  O   HOH A2150      12.429  40.752   1.610  1.00 15.91           O  
HETATM 2822  O   HOH A2151      14.559  38.867   1.866  1.00 10.05           O  
HETATM 2823  O   HOH A2152      -2.125  32.318   3.343  1.00 23.44           O  
HETATM 2824  O   HOH A2153      -9.690  38.083   2.043  1.00 26.56           O  
HETATM 2825  O   HOH A2154      -7.921  38.285   4.139  1.00 23.03           O  
HETATM 2826  O   HOH A2155       2.505  46.668  -8.797  1.00 23.28           O  
HETATM 2827  O   HOH A2156       3.992  48.275  -6.482  1.00 20.60           O  
HETATM 2828  O   HOH A2157      -1.457  53.576  -6.157  1.00 33.28           O  
HETATM 2829  O   HOH A2158       1.952  52.732   0.471  1.00 31.10           O  
HETATM 2830  O   HOH A2159      -4.310  44.221 -11.469  1.00 21.01           O  
HETATM 2831  O   HOH A2160      -3.107  36.487  -0.573  1.00  8.53           O  
HETATM 2832  O   HOH A2161      -7.988  34.078  -2.200  1.00 17.13           O  
HETATM 2833  O   HOH A2162      -1.507  31.234  -1.376  1.00 17.61           O  
HETATM 2834  O   HOH A2163      -5.886  26.764  -5.519  1.00 25.08           O  
HETATM 2835  O   HOH A2164      -3.538  25.777   2.778  1.00 20.30           O  
HETATM 2836  O   HOH A2165      -1.221  22.213  -1.812  1.00 21.00           O  
HETATM 2837  O   HOH A2166      -4.079  22.503  -1.928  1.00 18.99           O  
HETATM 2838  O   HOH A2167       0.609  21.906  -6.279  1.00 20.51           O  
HETATM 2839  O   HOH A2168       1.376  29.727  -2.628  1.00 12.86           O  
HETATM 2840  O   HOH A2169       5.439  38.043  -2.184  1.00 21.65           O  
HETATM 2841  O   HOH A2170       6.039  36.005  -3.735  1.00 11.27           O  
HETATM 2842  O   HOH A2171      11.160  49.021  -8.042  1.00 11.62           O  
HETATM 2843  O   HOH A2172       8.191  48.320 -17.314  1.00 16.81           O  
HETATM 2844  O   HOH A2173       7.972  43.461 -11.563  1.00 22.87           O  
HETATM 2845  O   HOH A2174       7.540  46.693 -13.769  1.00 12.52           O  
HETATM 2846  O   HOH A2175       9.107  43.521  -4.078  1.00  7.32           O  
HETATM 2847  O   HOH A2176      -2.594  52.692   2.984  1.00 14.86           O  
HETATM 2848  O   HOH A2177      -2.034  37.999   8.826  1.00 16.32           O  
HETATM 2849  O   HOH A2178      -2.828  35.015  10.066  1.00 19.47           O  
HETATM 2850  O   HOH A2179      -9.452  37.907  10.369  1.00 13.97           O  
HETATM 2851  O   HOH A2180      -9.492  31.595  11.359  1.00 20.11           O  
HETATM 2852  O   HOH A2181     -10.526  37.714  15.219  1.00 17.06           O  
HETATM 2853  O   HOH A2182      -3.699  27.255  15.912  1.00 23.02           O  
HETATM 2854  O   HOH A2183      -7.218  29.397  11.753  1.00 19.16           O  
HETATM 2855  O   HOH A2184       0.542  27.764  11.079  1.00 14.07           O  
HETATM 2856  O   HOH A2185       2.670  25.723  10.400  1.00 16.52           O  
HETATM 2857  O   HOH A2186       9.681  28.686  -0.669  1.00 11.41           O  
HETATM 2858  O   HOH A2187      28.848  35.324  -9.424  1.00 16.97           O  
HETATM 2859  O   HOH A2188      30.187  38.714 -10.796  1.00 17.24           O  
HETATM 2860  O   HOH A2189      24.508  45.501 -10.158  1.00 10.23           O  
HETATM 2861  O   HOH A2190      24.392  43.325 -17.920  1.00 25.46           O  
HETATM 2862  O   HOH A2191      18.490  53.717 -19.343  1.00 27.95           O  
HETATM 2863  O   HOH A2192      14.578  54.120 -19.738  1.00 28.25           O  
HETATM 2864  O   HOH A2193      12.933  52.952 -27.119  1.00 16.06           O  
HETATM 2865  O   HOH A2194      17.966  47.338 -24.768  1.00 26.40           O  
HETATM 2866  O   HOH A2195      19.936  49.409 -14.818  1.00 21.55           O  
HETATM 2867  O   HOH A2196      15.012  51.338  -7.596  1.00 33.78           O  
HETATM 2868  O   HOH A2197      30.217  42.048  -2.038  1.00 25.60           O  
HETATM 2869  O   HOH A2198      29.025  46.994  -4.642  1.00 20.88           O  
HETATM 2870  O   HOH A2199      20.307  47.183  -0.397  1.00 17.50           O  
HETATM 2871  O   HOH A2200      15.424  46.987   2.725  1.00 18.72           O  
HETATM 2872  O   HOH A2201      15.614  41.787   7.229  1.00 15.79           O  
HETATM 2873  O   HOH A2202       7.722  53.146   6.100  1.00 30.96           O  
HETATM 2874  O   HOH A2203      11.333  44.013   8.869  1.00 14.99           O  
HETATM 2875  O   HOH A2204      16.498  39.510  11.233  1.00 26.46           O  
HETATM 2876  O   HOH A2205      18.347  40.495  13.098  1.00 23.23           O  
HETATM 2877  O   HOH A2206      11.042  37.306   8.369  1.00 20.52           O  
HETATM 2878  O   HOH A2207      13.752  40.727  10.679  1.00 16.14           O  
HETATM 2879  O   HOH A2208      13.039  42.010   8.309  1.00 20.90           O  
HETATM 2880  O   HOH A2209      13.364  35.883   8.377  1.00 13.89           O  
HETATM 2881  O   HOH A2210      16.569  39.340   8.325  1.00 19.31           O  
HETATM 2882  O   HOH A2211      17.156  37.538   1.974  1.00 13.76           O  
HETATM 2883  O   HOH A2212       5.971  39.905   2.009  1.00  8.41           O  
HETATM 2884  O   HOH A2213       2.081  36.456   4.874  1.00 13.63           O  
CONECT 1712 2647                                                                
CONECT 1728 2647                                                                
CONECT 2152 2647                                                                
CONECT 2647 1712 1728 2152 2661                                                 
CONECT 2647 2820 2883                                                           
CONECT 2648 2649                                                                
CONECT 2649 2648 2650 2651                                                      
CONECT 2650 2649                                                                
CONECT 2651 2649 2652 2653                                                      
CONECT 2652 2651                                                                
CONECT 2653 2651 2654                                                           
CONECT 2654 2653 2655                                                           
CONECT 2655 2654 2656                                                           
CONECT 2656 2655 2657 2658                                                      
CONECT 2657 2656                                                                
CONECT 2658 2656 2659                                                           
CONECT 2659 2658 2660 2662                                                      
CONECT 2660 2659 2661                                                           
CONECT 2661 2647 2660                                                           
CONECT 2662 2659 2663 2664                                                      
CONECT 2663 2662                                                                
CONECT 2664 2662 2665                                                           
CONECT 2665 2664 2666 2669                                                      
CONECT 2666 2665 2667 2668                                                      
CONECT 2667 2666                                                                
CONECT 2668 2666                                                                
CONECT 2669 2665 2670                                                           
CONECT 2670 2669 2671                                                           
CONECT 2671 2670                                                                
CONECT 2820 2647                                                                
CONECT 2883 2647                                                                
MASTER      429    0    2   10   13    0    7    6 2883    1   31   26          
END                                                                             
