HEADER    TRANSFERASE                             12-JAN-06   2FO0              
TITLE     ORGANIZATION OF THE SH3-SH2 UNIT IN ACTIVE AND INACTIVE FORMS OF THE  
TITLE    2 C-ABL TYROSINE KINASE                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL1 (1B ISOFORM);  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ABL N-CAP (RESIDUES 1-531, RESIDUES 15-56 DELETED);        
COMPND   5 EC: 2.7.1.112;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: C-ABL;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1                                 
KEYWDS    N-TERMINAL CAP, AUTOINHIBITION, MYRISTOYLATION, SH3-SH2 CLAMP,        
KEYWDS   2 PHOSPHOSERINE, TRANSFERASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.NAGAR,O.HANTSCHEL,M.SEELIGER,J.M.DAVIES,W.I.WEIS,G.SUPERTI-FURGA,   
AUTHOR   2 J.KURIYAN                                                            
REVDAT   8   30-AUG-23 2FO0    1       REMARK                                   
REVDAT   7   20-OCT-21 2FO0    1       SEQADV                                   
REVDAT   6   30-JUN-21 2FO0    1       REMARK SEQADV LINK   ATOM                
REVDAT   5   02-AUG-17 2FO0    1       SOURCE                                   
REVDAT   4   13-JUL-11 2FO0    1       VERSN                                    
REVDAT   3   24-FEB-09 2FO0    1       VERSN                                    
REVDAT   2   04-APR-06 2FO0    1       AUTHOR                                   
REVDAT   1   21-MAR-06 2FO0    0                                                
JRNL        AUTH   B.NAGAR,O.HANTSCHEL,M.SEELIGER,J.M.DAVIES,W.I.WEIS,          
JRNL        AUTH 2 G.SUPERTI-FURGA,J.KURIYAN                                    
JRNL        TITL   ORGANIZATION OF THE SH3-SH2 UNIT IN ACTIVE AND INACTIVE      
JRNL        TITL 2 FORMS OF THE C-ABL TYROSINE KINASE.                          
JRNL        REF    MOL.CELL                      V.  21   787 2006              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   16543148                                                     
JRNL        DOI    10.1016/J.MOLCEL.2006.01.035                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.27 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 318702.330                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 24283                          
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 SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1656                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.27                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3000                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2700                       
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 235                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3748                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 145                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -9.32000                                             
REMARK   3    B22 (A**2) : -10.46000                                            
REMARK   3    B33 (A**2) : 19.77000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.27                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.35                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.33                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.33                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.850                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.580 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.680 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.230 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.400 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 33.70                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : LIGANDS.PAR                                    
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN_REP.TOP                                
REMARK   3  TOPOLOGY FILE  2   : LIGANDS.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2FO0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000036103.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-SEP-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL, SI(111)            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25639                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.270                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.140                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.28900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1OPK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 10000, 0.1M HEPES, PH 7.5,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       39.84400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.63300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.84400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.63300            
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 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 465     GLN A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     VAL A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     ASP A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     ARG A    14                                                      
REMARK 465     GLU A    57                                                      
REMARK 465     PRO A    58                                                      
REMARK 465     GLN A    59                                                      
REMARK 465     GLY A    60                                                      
REMARK 465     LEU A    61                                                      
REMARK 465     SER A    62                                                      
REMARK 465     GLU A    63                                                      
REMARK 465     ALA A    64                                                      
REMARK 465     LYS A   531                                                      
REMARK 465     GLU A   532                                                      
REMARK 465     ASN A   533                                                      
REMARK 465     LEU A   534                                                      
REMARK 465     TYR A   535                                                      
REMARK 465     GLY A   536                                                      
REMARK 465     GLN A   537                                                      
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    PRO A  77   C   -  N   -  CA  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    PRO A  82   C   -  N   -  CA  ANGL. DEV. =  11.9 DEGREES          
REMARK 500    PRO A  82   C   -  N   -  CD  ANGL. DEV. = -14.5 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    TRP A  67       76.61   -106.09                                   
REMARK 500    SEP A  69       25.96    -78.09                                   
REMARK 500    ASP A 226       60.49     38.86                                   
REMARK 500    ARG A 239      -70.08    -47.15                                   
REMARK 500    ASP A 252       68.89     35.79                                   
REMARK 500    LYS A 253       56.58   -114.03                                   
REMARK 500    LYS A 264     -145.76   -123.32                                   
REMARK 500    ASP A 295       -8.19    -59.68                                   
REMARK 500    MET A 297       77.59    -68.74                                   
REMARK 500    HIS A 380      -60.91   -101.49                                   
REMARK 500    ARG A 381       -3.96     80.44                                   
REMARK 500    ASP A 400       43.06    -95.45                                   
REMARK 500    ASP A 410      160.01    176.92                                   
REMARK 500    TRP A 495       30.57    -96.58                                   
REMARK 500    LEU A 529      -62.35    -91.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     MYR A  701                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P16 A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 704                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUES 15-56 OF THE ORIGINAL PROTEIN SEQUENCE WERE                 
REMARK 999 DELETED. MYRISTOYL GROUP (MYR) IS COVALENTLY ATTACHED TO THE         
REMARK 999 N-TERMINUS OF THE PROTEIN.                                           
DBREF  2FO0 A    1    14  UNP    P00519-2 ABL1_HUMAN       1     14             
DBREF  2FO0 A   57   531  UNP    P00519-2 ABL1_HUMAN      57    531             
SEQADV 2FO0 SEP A   69  UNP  P00519-2  SER    69 MODIFIED RESIDUE               
SEQADV 2FO0 ASN A  382  UNP  P00519-2  ASP   382 ENGINEERED MUTATION            
SEQADV 2FO0 GLU A  532  UNP  P00519-2            CLONING ARTIFACT               
SEQADV 2FO0 ASN A  533  UNP  P00519-2            CLONING ARTIFACT               
SEQADV 2FO0 LEU A  534  UNP  P00519-2            CLONING ARTIFACT               
SEQADV 2FO0 TYR A  535  UNP  P00519-2            CLONING ARTIFACT               
SEQADV 2FO0 GLY A  536  UNP  P00519-2            CLONING ARTIFACT               
SEQADV 2FO0 GLN A  537  UNP  P00519-2            CLONING ARTIFACT               
SEQRES   1 A  495  MET GLY GLN GLN PRO GLY LYS VAL LEU GLY ASP GLN ARG          
SEQRES   2 A  495  ARG GLU PRO GLN GLY LEU SER GLU ALA ALA ARG TRP ASN          
SEQRES   3 A  495  SEP LYS GLU ASN LEU LEU ALA GLY PRO SER GLU ASN ASP          
SEQRES   4 A  495  PRO ASN LEU PHE VAL ALA LEU TYR ASP PHE VAL ALA SER          
SEQRES   5 A  495  GLY ASP ASN THR LEU SER ILE THR LYS GLY GLU LYS LEU          
SEQRES   6 A  495  ARG VAL LEU GLY TYR ASN HIS ASN GLY GLU TRP CYS GLU          
SEQRES   7 A  495  ALA GLN THR LYS ASN GLY GLN GLY TRP VAL PRO SER ASN          
SEQRES   8 A  495  TYR ILE THR PRO VAL ASN SER LEU GLU LYS HIS SER TRP          
SEQRES   9 A  495  TYR HIS GLY PRO VAL SER ARG ASN ALA ALA GLU TYR LEU          
SEQRES  10 A  495  LEU SER SER GLY ILE ASN GLY SER PHE LEU VAL ARG GLU          
SEQRES  11 A  495  SER GLU SER SER PRO GLY GLN ARG SER ILE SER LEU ARG          
SEQRES  12 A  495  TYR GLU GLY ARG VAL TYR HIS TYR ARG ILE ASN THR ALA          
SEQRES  13 A  495  SER ASP GLY LYS LEU TYR VAL SER SER GLU SER ARG PHE          
SEQRES  14 A  495  ASN THR LEU ALA GLU LEU VAL HIS HIS HIS SER THR VAL          
SEQRES  15 A  495  ALA ASP GLY LEU ILE THR THR LEU HIS TYR PRO ALA PRO          
SEQRES  16 A  495  LYS ARG ASN LYS PRO THR VAL TYR GLY VAL SER PRO ASN          
SEQRES  17 A  495  TYR ASP LYS TRP GLU MET GLU ARG THR ASP ILE THR MET          
SEQRES  18 A  495  LYS HIS LYS LEU GLY GLY GLY GLN TYR GLY GLU VAL TYR          
SEQRES  19 A  495  GLU GLY VAL TRP LYS LYS TYR SER LEU THR VAL ALA VAL          
SEQRES  20 A  495  LYS THR LEU LYS GLU ASP THR MET GLU VAL GLU GLU PHE          
SEQRES  21 A  495  LEU LYS GLU ALA ALA VAL MET LYS GLU ILE LYS HIS PRO          
SEQRES  22 A  495  ASN LEU VAL GLN LEU LEU GLY VAL CYS THR ARG GLU PRO          
SEQRES  23 A  495  PRO PHE TYR ILE ILE THR GLU PHE MET THR TYR GLY ASN          
SEQRES  24 A  495  LEU LEU ASP TYR LEU ARG GLU CYS ASN ARG GLN GLU VAL          
SEQRES  25 A  495  ASN ALA VAL VAL LEU LEU TYR MET ALA THR GLN ILE SER          
SEQRES  26 A  495  SER ALA MET GLU TYR LEU GLU LYS LYS ASN PHE ILE HIS          
SEQRES  27 A  495  ARG ASN LEU ALA ALA ARG ASN CYS LEU VAL GLY GLU ASN          
SEQRES  28 A  495  HIS LEU VAL LYS VAL ALA ASP PHE GLY LEU SER ARG LEU          
SEQRES  29 A  495  MET THR GLY ASP THR TYR THR ALA HIS ALA GLY ALA LYS          
SEQRES  30 A  495  PHE PRO ILE LYS TRP THR ALA PRO GLU SER LEU ALA TYR          
SEQRES  31 A  495  ASN LYS PHE SER ILE LYS SER ASP VAL TRP ALA PHE GLY          
SEQRES  32 A  495  VAL LEU LEU TRP GLU ILE ALA THR TYR GLY MET SER PRO          
SEQRES  33 A  495  TYR PRO GLY ILE ASP LEU SER GLN VAL TYR GLU LEU LEU          
SEQRES  34 A  495  GLU LYS ASP TYR ARG MET GLU ARG PRO GLU GLY CYS PRO          
SEQRES  35 A  495  GLU LYS VAL TYR GLU LEU MET ARG ALA CYS TRP GLN TRP          
SEQRES  36 A  495  ASN PRO SER ASP ARG PRO SER PHE ALA GLU ILE HIS GLN          
SEQRES  37 A  495  ALA PHE GLU THR MET PHE GLN GLU SER SER ILE SER ASP          
SEQRES  38 A  495  GLU VAL GLU LYS GLU LEU GLY LYS GLU ASN LEU TYR GLY          
SEQRES  39 A  495  GLN                                                          
MODRES 2FO0 SEP A   69  SER  PHOSPHOSERINE                                      
HET    SEP  A  69      10                                                       
HET    MYR  A 701      15                                                       
HET    P16  A 702      29                                                       
HET    GOL  A 703       6                                                       
HET    GOL  A 704       6                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     MYR MYRISTIC ACID                                                    
HETNAM     P16 6-(2,6-DICHLOROPHENYL)-2-{[3-(HYDROXYMETHYL)                     
HETNAM   2 P16  PHENYL]AMINO}-8-METHYLPYRIDO[2,3-D]PYRIMIDIN-7(8H)-ONE          
HETNAM     GOL GLYCEROL                                                         
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     P16 PD166326                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   2  MYR    C14 H28 O2                                                   
FORMUL   3  P16    C21 H16 CL2 N4 O2                                            
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   6  HOH   *145(H2 O)                                                    
HELIX    1   1 TRP A   67  LEU A   73  5                                   7    
HELIX    2   2 GLY A   76  ASN A   80  5                                   5    
HELIX    3   3 SER A  140  HIS A  144  5                                   5    
HELIX    4   4 SER A  152  LEU A  160  1                                   9    
HELIX    5   5 THR A  213  VAL A  224  1                                  12    
HELIX    6   6 GLU A  257  THR A  259  5                                   3    
HELIX    7   7 GLY A  268  GLN A  271  5                                   4    
HELIX    8   8 LYS A  282  SER A  284  5                                   3    
HELIX    9   9 GLU A  298  ILE A  312  1                                  15    
HELIX   10  10 ASN A  341  CYS A  349  1                                   9    
HELIX   11  11 ASN A  355  LYS A  376  1                                  22    
HELIX   12  12 ALA A  384  ARG A  386  5                                   3    
HELIX   13  13 GLU A  392  HIS A  394  5                                   3    
HELIX   14  14 PRO A  421  THR A  425  5                                   5    
HELIX   15  15 ALA A  426  ASN A  433  1                                   8    
HELIX   16  16 SER A  436  THR A  453  1                                  18    
HELIX   17  17 ASP A  463  LYS A  473  1                                  11    
HELIX   18  18 PRO A  484  TRP A  495  1                                  12    
HELIX   19  19 ASN A  498  ARG A  502  5                                   5    
HELIX   20  20 SER A  504  THR A  514  1                                  11    
HELIX   21  21 SER A  520  GLY A  530  1                                  11    
SHEET    1   A 5 GLY A 126  PRO A 131  0                                        
SHEET    2   A 5 TRP A 118  THR A 123 -1  N  ALA A 121   O  GLY A 128           
SHEET    3   A 5 LYS A 106  TYR A 112 -1  N  GLY A 111   O  GLU A 120           
SHEET    4   A 5 PHE A  85  ALA A  87 -1  N  PHE A  85   O  LEU A 107           
SHEET    5   A 5 ILE A 135  PRO A 137 -1  O  THR A 136   N  VAL A  86           
SHEET    1   B 5 TYR A 147  PRO A 150  0                                        
SHEET    2   B 5 SER A 167  GLU A 172  1  O  VAL A 170   N  HIS A 148           
SHEET    3   B 5 ARG A 180  TYR A 186 -1  O  ARG A 185   N  SER A 167           
SHEET    4   B 5 ARG A 189  THR A 197 -1  O  TYR A 191   N  LEU A 184           
SHEET    5   B 5 LEU A 203  TYR A 204 -1  O  TYR A 204   N  ASN A 196           
SHEET    1   C 3 TYR A 147  PRO A 150  0                                        
SHEET    2   C 3 SER A 167  GLU A 172  1  O  VAL A 170   N  HIS A 148           
SHEET    3   C 3 TYR A 234  PRO A 235  1  O  TYR A 234   N  PHE A 168           
SHEET    1   D 5 ILE A 261  LYS A 266  0                                        
SHEET    2   D 5 VAL A 275  TRP A 280 -1  O  GLU A 277   N  HIS A 265           
SHEET    3   D 5 LEU A 285  THR A 291 -1  O  LEU A 285   N  TRP A 280           
SHEET    4   D 5 TYR A 331  GLU A 335 -1  O  ILE A 332   N  LYS A 290           
SHEET    5   D 5 LEU A 320  CYS A 324 -1  N  LEU A 321   O  ILE A 333           
SHEET    1   E 2 PHE A 378  ILE A 379  0                                        
SHEET    2   E 2 SER A 404  ARG A 405 -1  O  SER A 404   N  ILE A 379           
SHEET    1   F 2 CYS A 388  VAL A 390  0                                        
SHEET    2   F 2 VAL A 396  VAL A 398 -1  O  LYS A 397   N  LEU A 389           
SHEET    1   G 2 TYR A 412  THR A 413  0                                        
SHEET    2   G 2 LYS A 434  PHE A 435 -1  O  PHE A 435   N  TYR A 412           
LINK         C   ASN A  68                 N   SEP A  69     1555   1555  1.33  
LINK         C   SEP A  69                 N   LYS A  70     1555   1555  1.33  
CISPEP   1 PRO A  328    PRO A  329          0        -0.35                     
SITE     1 AC1  2 GLU A 481  ILE A 521                                          
SITE     1 AC2 14 TYR A 272  VAL A 275  ALA A 288  LYS A 290                    
SITE     2 AC2 14 GLU A 305  MET A 309  THR A 334  GLU A 335                    
SITE     3 AC2 14 PHE A 336  MET A 337  GLY A 340  LEU A 389                    
SITE     4 AC2 14 ALA A 399  ASP A 400                                          
SITE     1 AC3  5 TYR A 345  GLY A 391  GLU A 392  ASN A 393                    
SITE     2 AC3  5 HIS A 394                                                     
SITE     1 AC4  4 THR A 197  ALA A 198  THR A 296  MET A 297                    
CRYST1   79.688  117.266   60.416  90.00  90.00  90.00 P 21 21 2     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      0.012549  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008528  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016552        0.00000                         
ATOM      1  N   ALA A  65      14.854  31.217  -5.831  1.00 69.50           N  
ATOM      2  CA  ALA A  65      15.690  31.963  -4.844  1.00 69.01           C  
ATOM      3  C   ALA A  65      15.881  33.408  -5.292  1.00 68.54           C  
ATOM      4  O   ALA A  65      16.906  33.751  -5.884  1.00 69.07           O  
ATOM      5  CB  ALA A  65      17.048  31.281  -4.688  1.00 69.13           C  
ATOM      6  N   ARG A  66      14.896  34.255  -5.009  1.00 66.83           N  
ATOM      7  CA  ARG A  66      14.984  35.655  -5.402  1.00 64.57           C  
ATOM      8  C   ARG A  66      14.665  36.620  -4.271  1.00 60.62           C  
ATOM      9  O   ARG A  66      13.951  36.285  -3.329  1.00 61.11           O  
ATOM     10  CB  ARG A  66      14.050  35.936  -6.583  1.00 67.73           C  
ATOM     11  CG  ARG A  66      14.381  35.142  -7.837  1.00 71.87           C  
ATOM     12  CD  ARG A  66      13.569  35.622  -9.032  1.00 75.62           C  
ATOM     13  NE  ARG A  66      13.854  34.840 -10.233  1.00 78.64           N  
ATOM     14  CZ  ARG A  66      13.341  35.093 -11.435  1.00 79.79           C  
ATOM     15  NH1 ARG A  66      12.510  36.114 -11.606  1.00 79.94           N  
ATOM     16  NH2 ARG A  66      13.655  34.319 -12.467  1.00 80.31           N  
ATOM     17  N   TRP A  67      15.210  37.825  -4.375  1.00 55.95           N  
ATOM     18  CA  TRP A  67      14.982  38.866  -3.387  1.00 51.42           C  
ATOM     19  C   TRP A  67      14.027  39.875  -4.036  1.00 52.33           C  
ATOM     20  O   TRP A  67      14.432  40.949  -4.485  1.00 51.21           O  
ATOM     21  CB  TRP A  67      16.318  39.516  -3.014  1.00 44.60           C  
ATOM     22  CG  TRP A  67      16.250  40.536  -1.917  1.00 37.86           C  
ATOM     23  CD1 TRP A  67      15.126  41.045  -1.327  1.00 36.31           C  
ATOM     24  CD2 TRP A  67      17.361  41.206  -1.310  1.00 35.03           C  
ATOM     25  NE1 TRP A  67      15.472  41.993  -0.392  1.00 35.15           N  
ATOM     26  CE2 TRP A  67      16.837  42.110  -0.362  1.00 33.54           C  
ATOM     27  CE3 TRP A  67      18.754  41.127  -1.475  1.00 34.75           C  
ATOM     28  CZ2 TRP A  67      17.653  42.933   0.417  1.00 32.72           C  
ATOM     29  CZ3 TRP A  67      19.564  41.942  -0.704  1.00 31.09           C  
ATOM     30  CH2 TRP A  67      19.010  42.835   0.234  1.00 33.73           C  
ATOM     31  N   ASN A  68      12.754  39.491  -4.087  1.00 54.51           N  
ATOM     32  CA  ASN A  68      11.675  40.287  -4.675  1.00 56.20           C  
ATOM     33  C   ASN A  68      11.711  41.789  -4.429  1.00 56.01           C  
ATOM     34  O   ASN A  68      11.894  42.576  -5.355  1.00 56.89           O  
ATOM     35  CB  ASN A  68      10.318  39.770  -4.183  1.00 59.71           C  
ATOM     36  CG  ASN A  68      10.012  38.370  -4.665  1.00 63.23           C  
ATOM     37  OD1 ASN A  68      10.886  37.499  -4.684  1.00 65.98           O  
ATOM     38  ND2 ASN A  68       8.758  38.137  -5.043  1.00 63.86           N  
HETATM   39  N   SEP A  69      11.517  42.180  -3.175  1.00 55.48           N  
HETATM   40  CA  SEP A  69      11.467  43.589  -2.811  1.00 55.15           C  
HETATM   41  CB  SEP A  69      10.723  43.750  -1.483  1.00 56.01           C  
HETATM   42  OG  SEP A  69      11.595  43.428  -0.381  1.00 57.33           O  
HETATM   43  C   SEP A  69      12.811  44.290  -2.710  1.00 54.24           C  
HETATM   44  O   SEP A  69      12.935  45.284  -1.995  1.00 53.60           O  
HETATM   45  P   SEP A  69      11.460  42.015   0.423  1.00 57.93           P  
HETATM   46  O1P SEP A  69      10.071  42.021   1.048  1.00 58.16           O  
HETATM   47  O2P SEP A  69      12.561  42.053   1.470  1.00 56.40           O  
HETATM   48  O3P SEP A  69      11.641  40.911  -0.615  1.00 56.24           O  
ATOM     49  N   LYS A  70      13.813  43.799  -3.427  1.00 54.66           N  
ATOM     50  CA  LYS A  70      15.130  44.422  -3.353  1.00 56.02           C  
ATOM     51  C   LYS A  70      15.175  45.817  -3.983  1.00 57.48           C  
ATOM     52  O   LYS A  70      15.804  46.725  -3.439  1.00 56.00           O  
ATOM     53  CB  LYS A  70      16.185  43.527  -4.006  1.00 54.01           C  
ATOM     54  CG  LYS A  70      17.611  43.949  -3.694  1.00 52.74           C  
ATOM     55  CD  LYS A  70      18.616  42.992  -4.305  1.00 51.66           C  
ATOM     56  CE  LYS A  70      20.033  43.360  -3.910  1.00 50.86           C  
ATOM     57  NZ  LYS A  70      21.026  42.401  -4.470  1.00 50.60           N  
ATOM     58  N   GLU A  71      14.505  45.995  -5.117  1.00 59.52           N  
ATOM     59  CA  GLU A  71      14.514  47.294  -5.782  1.00 62.54           C  
ATOM     60  C   GLU A  71      13.649  48.339  -5.078  1.00 63.11           C  
ATOM     61  O   GLU A  71      13.329  49.378  -5.658  1.00 63.22           O  
ATOM     62  CB  GLU A  71      14.064  47.158  -7.240  1.00 64.29           C  
ATOM     63  CG  GLU A  71      12.597  46.808  -7.424  1.00 68.45           C  
ATOM     64  CD  GLU A  71      12.090  47.168  -8.813  1.00 70.63           C  
ATOM     65  OE1 GLU A  71      12.025  48.377  -9.127  1.00 71.50           O  
ATOM     66  OE2 GLU A  71      11.758  46.246  -9.591  1.00 71.52           O  
ATOM     67  N   ASN A  72      13.279  48.064  -3.830  1.00 63.01           N  
ATOM     68  CA  ASN A  72      12.450  48.979  -3.045  1.00 63.44           C  
ATOM     69  C   ASN A  72      13.141  49.287  -1.721  1.00 62.60           C  
ATOM     70  O   ASN A  72      12.640  50.053  -0.904  1.00 61.93           O  
ATOM     71  CB  ASN A  72      11.086  48.340  -2.750  1.00 65.61           C  
ATOM     72  CG  ASN A  72      10.299  48.009  -4.009  1.00 68.00           C  
ATOM     73  OD1 ASN A  72       9.395  47.172  -3.980  1.00 69.22           O  
ATOM     74  ND2 ASN A  72      10.629  48.672  -5.116  1.00 69.62           N  
ATOM     75  N   LEU A  73      14.301  48.675  -1.527  1.00 62.01           N  
ATOM     76  CA  LEU A  73      15.076  48.819  -0.308  1.00 61.99           C  
ATOM     77  C   LEU A  73      15.270  50.271   0.135  1.00 63.25           C  
ATOM     78  O   LEU A  73      15.155  50.593   1.328  1.00 62.86           O  
ATOM     79  CB  LEU A  73      16.427  48.124  -0.497  1.00 59.74           C  
ATOM     80  CG  LEU A  73      17.151  47.576   0.740  1.00 58.81           C  
ATOM     81  CD1 LEU A  73      16.189  46.804   1.638  1.00 55.51           C  
ATOM     82  CD2 LEU A  73      18.287  46.684   0.281  1.00 57.36           C  
ATOM     83  N   LEU A  74      15.556  51.143  -0.832  1.00 64.82           N  
ATOM     84  CA  LEU A  74      15.793  52.560  -0.548  1.00 66.51           C  
ATOM     85  C   LEU A  74      14.566  53.439  -0.664  1.00 68.45           C  
ATOM     86  O   LEU A  74      14.661  54.638  -0.953  1.00 67.96           O  
ATOM     87  CB  LEU A  74      16.864  53.130  -1.476  1.00 65.85           C  
ATOM     88  CG  LEU A  74      18.277  52.546  -1.419  1.00 65.52           C  
ATOM     89  CD1 LEU A  74      19.155  53.329  -2.370  1.00 65.32           C  
ATOM     90  CD2 LEU A  74      18.820  52.592  -0.008  1.00 63.70           C  
ATOM     91  N   ALA A  75      13.394  52.848  -0.502  1.00 71.15           N  
ATOM     92  CA  ALA A  75      12.177  53.644  -0.569  1.00 73.68           C  
ATOM     93  C   ALA A  75      11.740  54.295   0.751  1.00 76.04           C  
ATOM     94  O   ALA A  75      11.944  53.772   1.849  1.00 76.14           O  
ATOM     95  CB  ALA A  75      11.045  52.831  -1.148  1.00 73.34           C  
ATOM     96  N   GLY A  76      11.135  55.464   0.634  1.00 79.00           N  
ATOM     97  CA  GLY A  76      10.750  56.153   1.837  1.00 82.74           C  
ATOM     98  C   GLY A  76       9.488  55.713   2.555  1.00 85.41           C  
ATOM     99  O   GLY A  76       8.536  55.185   1.934  1.00 85.92           O  
ATOM    100  N   PRO A  77       9.481  55.933   3.894  1.00 87.39           N  
ATOM    101  CA  PRO A  77       8.447  55.662   4.900  1.00 88.73           C  
ATOM    102  C   PRO A  77       7.133  56.386   4.501  1.00 89.75           C  
ATOM    103  O   PRO A  77       6.016  55.892   4.718  1.00 89.90           O  
ATOM    104  CB  PRO A  77       9.046  56.252   6.178  1.00 88.71           C  
ATOM    105  CG  PRO A  77      10.480  55.877   6.027  1.00 88.56           C  
ATOM    106  CD  PRO A  77      10.800  56.084   4.554  1.00 87.98           C  
ATOM    107  N   SER A  78       7.296  57.576   3.923  1.00 91.20           N  
ATOM    108  CA  SER A  78       6.153  58.415   3.517  1.00 92.59           C  
ATOM    109  C   SER A  78       5.377  57.959   2.279  1.00 93.19           C  
ATOM    110  O   SER A  78       4.339  58.543   1.943  1.00 93.46           O  
ATOM    111  CB  SER A  78       6.584  59.877   3.293  1.00 92.83           C  
ATOM    112  OG  SER A  78       6.588  60.198   1.903  1.00 93.26           O  
ATOM    113  N   GLU A  79       5.864  56.921   1.607  1.00 93.70           N  
ATOM    114  CA  GLU A  79       5.184  56.451   0.415  1.00 94.28           C  
ATOM    115  C   GLU A  79       4.051  55.462   0.632  1.00 94.09           C  
ATOM    116  O   GLU A  79       3.413  55.042  -0.330  1.00 93.81           O  
ATOM    117  CB  GLU A  79       6.196  55.914  -0.594  1.00 95.21           C  
ATOM    118  CG  GLU A  79       7.087  57.019  -1.122  1.00 96.78           C  
ATOM    119  CD  GLU A  79       7.901  56.628  -2.332  1.00 97.94           C  
ATOM    120  OE1 GLU A  79       7.806  55.465  -2.783  1.00 97.93           O  
ATOM    121  OE2 GLU A  79       8.641  57.501  -2.835  1.00 98.37           O  
ATOM    122  N   ASN A  80       3.799  55.091   1.885  1.00 93.78           N  
ATOM    123  CA  ASN A  80       2.672  54.222   2.194  1.00 92.87           C  
ATOM    124  C   ASN A  80       1.910  54.807   3.389  1.00 91.64           C  
ATOM    125  O   ASN A  80       2.488  55.449   4.266  1.00 91.36           O  
ATOM    126  CB  ASN A  80       3.097  52.782   2.523  1.00 93.46           C  
ATOM    127  CG  ASN A  80       4.577  52.567   2.437  1.00 93.66           C  
ATOM    128  OD1 ASN A  80       5.330  53.106   3.239  1.00 94.00           O  
ATOM    129  ND2 ASN A  80       5.011  51.793   1.449  1.00 93.59           N  
ATOM    130  N   ASP A  81       0.610  54.614   3.379  1.00 90.17           N  
ATOM    131  CA  ASP A  81      -0.265  55.065   4.436  1.00 88.56           C  
ATOM    132  C   ASP A  81       0.068  54.229   5.687  1.00 86.11           C  
ATOM    133  O   ASP A  81      -0.169  53.019   5.721  1.00 86.04           O  
ATOM    134  CB  ASP A  81      -1.700  54.885   3.870  1.00 90.18           C  
ATOM    135  CG  ASP A  81      -2.750  54.528   4.893  1.00 90.97           C  
ATOM    136  OD1 ASP A  81      -2.454  54.398   6.085  1.00 91.55           O  
ATOM    137  OD2 ASP A  81      -3.921  54.368   4.460  1.00 91.52           O  
ATOM    138  N   PRO A  82       0.610  54.893   6.722  1.00 83.63           N  
ATOM    139  CA  PRO A  82       1.056  54.426   8.052  1.00 80.42           C  
ATOM    140  C   PRO A  82       0.227  53.314   8.689  1.00 76.26           C  
ATOM    141  O   PRO A  82       0.741  52.344   9.277  1.00 75.52           O  
ATOM    142  CB  PRO A  82       0.980  55.692   8.940  1.00 81.43           C  
ATOM    143  CG  PRO A  82       0.980  56.797   7.955  1.00 83.08           C  
ATOM    144  CD  PRO A  82       0.185  56.297   6.816  1.00 82.68           C  
ATOM    145  N   ASN A  83      -1.083  53.455   8.570  1.00 71.67           N  
ATOM    146  CA  ASN A  83      -2.018  52.573   9.245  1.00 66.50           C  
ATOM    147  C   ASN A  83      -2.408  51.206   8.641  1.00 61.90           C  
ATOM    148  O   ASN A  83      -3.160  50.408   9.228  1.00 60.33           O  
ATOM    149  CB  ASN A  83      -3.196  53.491   9.607  1.00 68.86           C  
ATOM    150  CG  ASN A  83      -2.675  54.884  10.048  1.00 70.29           C  
ATOM    151  OD1 ASN A  83      -1.755  54.998  10.883  1.00 69.42           O  
ATOM    152  ND2 ASN A  83      -3.193  55.936   9.415  1.00 70.55           N  
ATOM    153  N   LEU A  84      -1.816  50.943   7.485  1.00 56.05           N  
ATOM    154  CA  LEU A  84      -1.977  49.717   6.736  1.00 50.12           C  
ATOM    155  C   LEU A  84      -1.020  48.589   7.181  1.00 45.40           C  
ATOM    156  O   LEU A  84       0.038  48.840   7.765  1.00 43.75           O  
ATOM    157  CB  LEU A  84      -1.737  50.027   5.266  1.00 51.12           C  
ATOM    158  CG  LEU A  84      -2.478  49.216   4.205  1.00 54.01           C  
ATOM    159  CD1 LEU A  84      -3.964  49.536   4.239  1.00 53.65           C  
ATOM    160  CD2 LEU A  84      -1.896  49.528   2.836  1.00 55.63           C  
ATOM    161  N   PHE A  85      -1.400  47.347   6.889  1.00 39.32           N  
ATOM    162  CA  PHE A  85      -0.581  46.183   7.220  1.00 35.33           C  
ATOM    163  C   PHE A  85      -0.261  45.330   5.984  1.00 34.58           C  
ATOM    164  O   PHE A  85      -0.909  45.443   4.937  1.00 32.24           O  
ATOM    165  CB  PHE A  85      -1.282  45.277   8.241  1.00 32.23           C  
ATOM    166  CG  PHE A  85      -1.298  45.818   9.644  1.00 31.16           C  
ATOM    167  CD1 PHE A  85      -1.920  47.024   9.924  1.00 30.80           C  
ATOM    168  CD2 PHE A  85      -0.723  45.102  10.693  1.00 29.72           C  
ATOM    169  CE1 PHE A  85      -1.976  47.515  11.221  1.00 31.20           C  
ATOM    170  CE2 PHE A  85      -0.775  45.588  11.999  1.00 29.82           C  
ATOM    171  CZ  PHE A  85      -1.404  46.795  12.261  1.00 29.67           C  
ATOM    172  N   VAL A  86       0.740  44.464   6.121  1.00 32.94           N  
ATOM    173  CA  VAL A  86       1.120  43.558   5.047  1.00 31.81           C  
ATOM    174  C   VAL A  86       1.303  42.159   5.635  1.00 32.41           C  
ATOM    175  O   VAL A  86       1.797  42.006   6.753  1.00 31.97           O  
ATOM    176  CB  VAL A  86       2.419  44.024   4.326  1.00 31.67           C  
ATOM    177  CG1 VAL A  86       3.555  44.183   5.320  1.00 30.52           C  
ATOM    178  CG2 VAL A  86       2.793  43.020   3.230  1.00 30.74           C  
ATOM    179  N   ALA A  87       0.885  41.147   4.879  1.00 32.07           N  
ATOM    180  CA  ALA A  87       0.958  39.750   5.301  1.00 32.12           C  
ATOM    181  C   ALA A  87       2.374  39.185   5.317  1.00 31.89           C  
ATOM    182  O   ALA A  87       3.099  39.297   4.342  1.00 33.25           O  
ATOM    183  CB  ALA A  87       0.079  38.899   4.390  1.00 29.27           C  
ATOM    184  N   LEU A  88       2.753  38.555   6.421  1.00 30.98           N  
ATOM    185  CA  LEU A  88       4.085  37.975   6.545  1.00 29.47           C  
ATOM    186  C   LEU A  88       4.133  36.508   6.124  1.00 28.85           C  
ATOM    187  O   LEU A  88       5.187  35.991   5.742  1.00 25.46           O  
ATOM    188  CB  LEU A  88       4.570  38.104   7.991  1.00 29.84           C  
ATOM    189  CG  LEU A  88       4.876  39.518   8.480  1.00 28.52           C  
ATOM    190  CD1 LEU A  88       5.163  39.497   9.965  1.00 29.13           C  
ATOM    191  CD2 LEU A  88       6.072  40.063   7.716  1.00 26.21           C  
ATOM    192  N   TYR A  89       2.991  35.834   6.205  1.00 27.89           N  
ATOM    193  CA  TYR A  89       2.924  34.420   5.841  1.00 29.86           C  
ATOM    194  C   TYR A  89       1.583  34.114   5.230  1.00 30.55           C  
ATOM    195  O   TYR A  89       0.623  34.853   5.426  1.00 32.14           O  
ATOM    196  CB  TYR A  89       3.090  33.520   7.072  1.00 28.30           C  
ATOM    197  CG  TYR A  89       4.306  33.811   7.923  1.00 30.41           C  
ATOM    198  CD1 TYR A  89       4.311  34.868   8.832  1.00 29.28           C  
ATOM    199  CD2 TYR A  89       5.456  33.021   7.820  1.00 29.66           C  
ATOM    200  CE1 TYR A  89       5.430  35.133   9.618  1.00 31.50           C  
ATOM    201  CE2 TYR A  89       6.577  33.275   8.601  1.00 30.61           C  
ATOM    202  CZ  TYR A  89       6.557  34.333   9.497  1.00 32.25           C  
ATOM    203  OH  TYR A  89       7.667  34.589  10.270  1.00 35.01           O  
ATOM    204  N   ASP A  90       1.507  33.019   4.488  1.00 33.27           N  
ATOM    205  CA  ASP A  90       0.229  32.634   3.912  1.00 33.95           C  
ATOM    206  C   ASP A  90      -0.598  32.060   5.053  1.00 33.93           C  
ATOM    207  O   ASP A  90      -0.063  31.415   5.959  1.00 34.72           O  
ATOM    208  CB  ASP A  90       0.391  31.546   2.848  1.00 35.00           C  
ATOM    209  CG  ASP A  90       1.140  32.021   1.631  1.00 37.87           C  
ATOM    210  OD1 ASP A  90       0.894  33.156   1.172  1.00 40.45           O  
ATOM    211  OD2 ASP A  90       1.969  31.245   1.119  1.00 41.30           O  
ATOM    212  N   PHE A  91      -1.899  32.306   5.021  1.00 32.66           N  
ATOM    213  CA  PHE A  91      -2.777  31.752   6.033  1.00 32.82           C  
ATOM    214  C   PHE A  91      -4.004  31.208   5.327  1.00 32.44           C  
ATOM    215  O   PHE A  91      -4.621  31.904   4.521  1.00 32.68           O  
ATOM    216  CB  PHE A  91      -3.210  32.808   7.054  1.00 30.98           C  
ATOM    217  CG  PHE A  91      -4.316  32.340   7.967  1.00 28.73           C  
ATOM    218  CD1 PHE A  91      -4.063  31.408   8.972  1.00 28.86           C  
ATOM    219  CD2 PHE A  91      -5.619  32.795   7.790  1.00 26.22           C  
ATOM    220  CE1 PHE A  91      -5.088  30.930   9.789  1.00 24.94           C  
ATOM    221  CE2 PHE A  91      -6.659  32.325   8.599  1.00 26.62           C  
ATOM    222  CZ  PHE A  91      -6.391  31.388   9.602  1.00 25.40           C  
ATOM    223  N   VAL A  92      -4.341  29.959   5.625  1.00 32.75           N  
ATOM    224  CA  VAL A  92      -5.513  29.320   5.037  1.00 33.36           C  
ATOM    225  C   VAL A  92      -6.623  29.314   6.091  1.00 33.74           C  
ATOM    226  O   VAL A  92      -6.407  28.885   7.225  1.00 34.21           O  
ATOM    227  CB  VAL A  92      -5.195  27.872   4.606  1.00 32.46           C  
ATOM    228  CG1 VAL A  92      -6.420  27.236   3.972  1.00 29.84           C  
ATOM    229  CG2 VAL A  92      -4.018  27.868   3.629  1.00 31.42           C  
ATOM    230  N   ALA A  93      -7.803  29.800   5.719  1.00 33.53           N  
ATOM    231  CA  ALA A  93      -8.932  29.856   6.646  1.00 35.29           C  
ATOM    232  C   ALA A  93      -9.062  28.594   7.510  1.00 35.02           C  
ATOM    233  O   ALA A  93      -9.000  27.473   7.008  1.00 35.04           O  
ATOM    234  CB  ALA A  93     -10.226  30.100   5.876  1.00 33.08           C  
ATOM    235  N   SER A  94      -9.235  28.798   8.812  1.00 35.90           N  
ATOM    236  CA  SER A  94      -9.380  27.699   9.764  1.00 37.91           C  
ATOM    237  C   SER A  94     -10.745  27.759  10.458  1.00 38.18           C  
ATOM    238  O   SER A  94     -11.070  26.917  11.297  1.00 38.65           O  
ATOM    239  CB  SER A  94      -8.254  27.753  10.810  1.00 37.62           C  
ATOM    240  OG  SER A  94      -8.215  29.007  11.476  1.00 38.56           O  
ATOM    241  N   GLY A  95     -11.537  28.761  10.091  1.00 38.63           N  
ATOM    242  CA  GLY A  95     -12.861  28.939  10.663  1.00 38.28           C  
ATOM    243  C   GLY A  95     -13.699  29.752   9.693  1.00 39.89           C  
ATOM    244  O   GLY A  95     -13.154  30.536   8.903  1.00 39.77           O  
ATOM    245  N   ASP A  96     -15.017  29.580   9.746  1.00 39.08           N  
ATOM    246  CA  ASP A  96     -15.917  30.289   8.840  1.00 38.30           C  
ATOM    247  C   ASP A  96     -15.760  31.804   8.818  1.00 36.70           C  
ATOM    248  O   ASP A  96     -15.920  32.433   7.775  1.00 36.59           O  
ATOM    249  CB  ASP A  96     -17.363  29.927   9.163  1.00 40.62           C  
ATOM    250  CG  ASP A  96     -17.711  28.528   8.725  1.00 42.51           C  
ATOM    251  OD1 ASP A  96     -16.777  27.738   8.478  1.00 43.27           O  
ATOM    252  OD2 ASP A  96     -18.914  28.214   8.632  1.00 45.38           O  
ATOM    253  N   ASN A  97     -15.448  32.394   9.962  1.00 33.93           N  
ATOM    254  CA  ASN A  97     -15.286  33.835  10.018  1.00 32.49           C  
ATOM    255  C   ASN A  97     -13.815  34.250   9.911  1.00 30.86           C  
ATOM    256  O   ASN A  97     -13.477  35.397  10.197  1.00 31.29           O  
ATOM    257  CB  ASN A  97     -15.895  34.365  11.314  1.00 32.11           C  
ATOM    258  CG  ASN A  97     -15.254  33.749  12.542  1.00 33.33           C  
ATOM    259  OD1 ASN A  97     -14.603  32.703  12.451  1.00 30.00           O  
ATOM    260  ND2 ASN A  97     -15.441  34.387  13.697  1.00 31.42           N  
ATOM    261  N   THR A  98     -12.949  33.317   9.512  1.00 30.31           N  
ATOM    262  CA  THR A  98     -11.522  33.609   9.351  1.00 31.80           C  
ATOM    263  C   THR A  98     -11.297  33.909   7.870  1.00 32.99           C  
ATOM    264  O   THR A  98     -12.064  33.446   7.020  1.00 34.48           O  
ATOM    265  CB  THR A  98     -10.619  32.423   9.788  1.00 30.74           C  
ATOM    266  OG1 THR A  98     -10.694  31.361   8.826  1.00 31.04           O  
ATOM    267  CG2 THR A  98     -11.059  31.904  11.148  1.00 30.71           C  
ATOM    268  N   LEU A  99     -10.245  34.666   7.571  1.00 32.02           N  
ATOM    269  CA  LEU A  99      -9.940  35.094   6.203  1.00 32.99           C  
ATOM    270  C   LEU A  99      -8.589  34.636   5.642  1.00 32.38           C  
ATOM    271  O   LEU A  99      -7.538  34.886   6.232  1.00 31.26           O  
ATOM    272  CB  LEU A  99     -10.011  36.632   6.143  1.00 32.38           C  
ATOM    273  CG  LEU A  99      -9.605  37.351   4.850  1.00 32.29           C  
ATOM    274  CD1 LEU A  99     -10.628  37.062   3.760  1.00 31.50           C  
ATOM    275  CD2 LEU A  99      -9.513  38.846   5.098  1.00 27.62           C  
ATOM    276  N   SER A 100      -8.620  33.984   4.485  1.00 32.44           N  
ATOM    277  CA  SER A 100      -7.388  33.528   3.851  1.00 32.01           C  
ATOM    278  C   SER A 100      -6.595  34.704   3.258  1.00 31.93           C  
ATOM    279  O   SER A 100      -7.148  35.567   2.563  1.00 29.55           O  
ATOM    280  CB  SER A 100      -7.709  32.505   2.759  1.00 32.61           C  
ATOM    281  OG  SER A 100      -8.210  31.300   3.326  1.00 34.85           O  
ATOM    282  N   ILE A 101      -5.299  34.743   3.557  1.00 31.52           N  
ATOM    283  CA  ILE A 101      -4.430  35.800   3.056  1.00 30.59           C  
ATOM    284  C   ILE A 101      -3.144  35.214   2.482  1.00 32.17           C  
ATOM    285  O   ILE A 101      -2.771  34.081   2.792  1.00 32.21           O  
ATOM    286  CB  ILE A 101      -4.053  36.814   4.169  1.00 29.52           C  
ATOM    287  CG1 ILE A 101      -3.355  36.099   5.326  1.00 29.33           C  
ATOM    288  CG2 ILE A 101      -5.292  37.547   4.648  1.00 27.89           C  
ATOM    289  CD1 ILE A 101      -2.862  37.044   6.431  1.00 26.01           C  
ATOM    290  N   THR A 102      -2.467  35.994   1.646  1.00 33.35           N  
ATOM    291  CA  THR A 102      -1.223  35.554   1.027  1.00 33.18           C  
ATOM    292  C   THR A 102      -0.059  36.458   1.395  1.00 31.31           C  
ATOM    293  O   THR A 102      -0.213  37.665   1.501  1.00 32.09           O  
ATOM    294  CB  THR A 102      -1.348  35.537  -0.502  1.00 35.63           C  
ATOM    295  OG1 THR A 102      -2.378  34.618  -0.883  1.00 37.14           O  
ATOM    296  CG2 THR A 102      -0.031  35.114  -1.137  1.00 35.49           C  
ATOM    297  N   LYS A 103       1.107  35.864   1.591  1.00 31.81           N  
ATOM    298  CA  LYS A 103       2.303  36.621   1.929  1.00 33.62           C  
ATOM    299  C   LYS A 103       2.502  37.799   0.969  1.00 34.49           C  
ATOM    300  O   LYS A 103       2.433  37.632  -0.255  1.00 33.30           O  
ATOM    301  CB  LYS A 103       3.513  35.704   1.857  1.00 33.08           C  
ATOM    302  CG  LYS A 103       4.816  36.363   2.219  1.00 35.79           C  
ATOM    303  CD  LYS A 103       5.921  35.333   2.181  1.00 39.27           C  
ATOM    304  CE  LYS A 103       7.170  35.816   2.874  1.00 39.94           C  
ATOM    305  NZ  LYS A 103       8.130  34.684   3.004  1.00 45.11           N  
ATOM    306  N   GLY A 104       2.751  38.982   1.531  1.00 34.33           N  
ATOM    307  CA  GLY A 104       2.975  40.173   0.725  1.00 34.52           C  
ATOM    308  C   GLY A 104       1.721  40.989   0.468  1.00 35.19           C  
ATOM    309  O   GLY A 104       1.781  42.136   0.031  1.00 34.84           O  
ATOM    310  N   GLU A 105       0.574  40.389   0.749  1.00 36.20           N  
ATOM    311  CA  GLU A 105      -0.707  41.044   0.546  1.00 38.28           C  
ATOM    312  C   GLU A 105      -0.950  42.149   1.571  1.00 38.17           C  
ATOM    313  O   GLU A 105      -0.580  42.033   2.739  1.00 38.42           O  
ATOM    314  CB  GLU A 105      -1.811  39.984   0.609  1.00 41.25           C  
ATOM    315  CG  GLU A 105      -3.227  40.491   0.578  1.00 45.29           C  
ATOM    316  CD  GLU A 105      -4.212  39.379   0.253  1.00 50.25           C  
ATOM    317  OE1 GLU A 105      -4.057  38.264   0.803  1.00 50.69           O  
ATOM    318  OE2 GLU A 105      -5.143  39.619  -0.547  1.00 52.14           O  
ATOM    319  N   LYS A 106      -1.561  43.237   1.128  1.00 36.85           N  
ATOM    320  CA  LYS A 106      -1.847  44.333   2.034  1.00 36.73           C  
ATOM    321  C   LYS A 106      -3.238  44.187   2.654  1.00 35.10           C  
ATOM    322  O   LYS A 106      -4.145  43.621   2.043  1.00 34.38           O  
ATOM    323  CB  LYS A 106      -1.708  45.668   1.301  1.00 38.76           C  
ATOM    324  CG  LYS A 106      -0.253  46.031   1.013  1.00 41.01           C  
ATOM    325  CD  LYS A 106      -0.105  47.485   0.606  1.00 44.58           C  
ATOM    326  CE  LYS A 106       1.345  47.945   0.733  1.00 47.35           C  
ATOM    327  NZ  LYS A 106       2.292  47.098  -0.055  1.00 48.73           N  
ATOM    328  N   LEU A 107      -3.390  44.673   3.880  1.00 32.97           N  
ATOM    329  CA  LEU A 107      -4.661  44.582   4.575  1.00 33.81           C  
ATOM    330  C   LEU A 107      -4.861  45.793   5.466  1.00 33.59           C  
ATOM    331  O   LEU A 107      -3.906  46.507   5.785  1.00 33.91           O  
ATOM    332  CB  LEU A 107      -4.726  43.331   5.469  1.00 34.18           C  
ATOM    333  CG  LEU A 107      -3.868  42.077   5.247  1.00 38.85           C  
ATOM    334  CD1 LEU A 107      -2.433  42.319   5.721  1.00 33.31           C  
ATOM    335  CD2 LEU A 107      -4.481  40.912   6.035  1.00 36.98           C  
ATOM    336  N   ARG A 108      -6.116  46.010   5.858  1.00 33.22           N  
ATOM    337  CA  ARG A 108      -6.490  47.090   6.759  1.00 35.23           C  
ATOM    338  C   ARG A 108      -7.023  46.398   8.013  1.00 34.43           C  
ATOM    339  O   ARG A 108      -7.865  45.510   7.915  1.00 34.88           O  
ATOM    340  CB  ARG A 108      -7.590  47.961   6.146  1.00 37.34           C  
ATOM    341  CG  ARG A 108      -8.028  49.103   7.055  1.00 43.05           C  
ATOM    342  CD  ARG A 108      -9.205  49.878   6.474  1.00 50.00           C  
ATOM    343  NE  ARG A 108      -8.942  50.315   5.103  1.00 55.14           N  
ATOM    344  CZ  ARG A 108      -7.978  51.163   4.753  1.00 56.98           C  
ATOM    345  NH1 ARG A 108      -7.175  51.680   5.676  1.00 58.15           N  
ATOM    346  NH2 ARG A 108      -7.808  51.486   3.475  1.00 57.06           N  
ATOM    347  N   VAL A 109      -6.528  46.794   9.182  1.00 33.59           N  
ATOM    348  CA  VAL A 109      -6.959  46.187  10.434  1.00 32.07           C  
ATOM    349  C   VAL A 109      -8.091  46.962  11.109  1.00 32.74           C  
ATOM    350  O   VAL A 109      -7.982  48.161  11.359  1.00 32.69           O  
ATOM    351  CB  VAL A 109      -5.765  46.048  11.403  1.00 32.25           C  
ATOM    352  CG1 VAL A 109      -6.251  45.658  12.790  1.00 30.01           C  
ATOM    353  CG2 VAL A 109      -4.792  44.993  10.870  1.00 29.98           C  
ATOM    354  N   LEU A 110      -9.173  46.256  11.417  1.00 31.19           N  
ATOM    355  CA  LEU A 110     -10.338  46.863  12.040  1.00 31.37           C  
ATOM    356  C   LEU A 110     -10.365  46.725  13.560  1.00 32.95           C  
ATOM    357  O   LEU A 110     -10.880  47.604  14.255  1.00 31.86           O  
ATOM    358  CB  LEU A 110     -11.608  46.243  11.451  1.00 32.25           C  
ATOM    359  CG  LEU A 110     -11.678  46.194   9.920  1.00 33.83           C  
ATOM    360  CD1 LEU A 110     -12.941  45.468   9.487  1.00 33.09           C  
ATOM    361  CD2 LEU A 110     -11.634  47.617   9.354  1.00 30.99           C  
ATOM    362  N   GLY A 111      -9.819  45.621  14.073  1.00 32.87           N  
ATOM    363  CA  GLY A 111      -9.814  45.389  15.509  1.00 31.67           C  
ATOM    364  C   GLY A 111      -9.307  44.009  15.900  1.00 31.85           C  
ATOM    365  O   GLY A 111      -9.070  43.152  15.046  1.00 31.62           O  
ATOM    366  N   TYR A 112      -9.158  43.781  17.201  1.00 31.57           N  
ATOM    367  CA  TYR A 112      -8.648  42.509  17.698  1.00 29.89           C  
ATOM    368  C   TYR A 112      -9.682  41.703  18.479  1.00 29.57           C  
ATOM    369  O   TYR A 112     -10.698  42.241  18.921  1.00 29.02           O  
ATOM    370  CB  TYR A 112      -7.421  42.777  18.571  1.00 31.49           C  
ATOM    371  CG  TYR A 112      -6.265  43.389  17.804  1.00 34.49           C  
ATOM    372  CD1 TYR A 112      -5.246  42.590  17.279  1.00 35.51           C  
ATOM    373  CD2 TYR A 112      -6.213  44.763  17.564  1.00 36.18           C  
ATOM    374  CE1 TYR A 112      -4.203  43.143  16.533  1.00 36.48           C  
ATOM    375  CE2 TYR A 112      -5.175  45.328  16.819  1.00 35.81           C  
ATOM    376  CZ  TYR A 112      -4.175  44.516  16.306  1.00 38.83           C  
ATOM    377  OH  TYR A 112      -3.149  45.080  15.568  1.00 40.76           O  
ATOM    378  N   ASN A 113      -9.424  40.407  18.641  1.00 28.34           N  
ATOM    379  CA  ASN A 113     -10.335  39.542  19.383  1.00 27.31           C  
ATOM    380  C   ASN A 113     -10.074  39.681  20.887  1.00 26.93           C  
ATOM    381  O   ASN A 113      -9.267  40.515  21.299  1.00 24.24           O  
ATOM    382  CB  ASN A 113     -10.175  38.093  18.922  1.00 24.87           C  
ATOM    383  CG  ASN A 113      -8.898  37.458  19.420  1.00 22.91           C  
ATOM    384  OD1 ASN A 113      -7.861  38.112  19.526  1.00 24.18           O  
ATOM    385  ND2 ASN A 113      -8.962  36.164  19.710  1.00 23.15           N  
ATOM    386  N   HIS A 114     -10.740  38.862  21.701  1.00 28.46           N  
ATOM    387  CA  HIS A 114     -10.610  38.954  23.161  1.00 28.42           C  
ATOM    388  C   HIS A 114      -9.219  38.830  23.764  1.00 28.92           C  
ATOM    389  O   HIS A 114      -8.937  39.457  24.784  1.00 29.84           O  
ATOM    390  CB  HIS A 114     -11.532  37.945  23.846  1.00 27.88           C  
ATOM    391  CG  HIS A 114     -11.229  36.521  23.504  1.00 27.42           C  
ATOM    392  ND1 HIS A 114     -11.430  36.000  22.243  1.00 28.48           N  
ATOM    393  CD2 HIS A 114     -10.719  35.515  24.251  1.00 27.37           C  
ATOM    394  CE1 HIS A 114     -11.055  34.733  22.229  1.00 29.15           C  
ATOM    395  NE2 HIS A 114     -10.620  34.414  23.436  1.00 28.15           N  
ATOM    396  N   ASN A 115      -8.345  38.026  23.171  1.00 29.29           N  
ATOM    397  CA  ASN A 115      -7.003  37.895  23.739  1.00 29.40           C  
ATOM    398  C   ASN A 115      -5.922  38.542  22.876  1.00 30.59           C  
ATOM    399  O   ASN A 115      -4.728  38.363  23.126  1.00 29.56           O  
ATOM    400  CB  ASN A 115      -6.661  36.422  23.978  1.00 28.31           C  
ATOM    401  CG  ASN A 115      -6.838  35.574  22.734  1.00 29.72           C  
ATOM    402  OD1 ASN A 115      -6.805  36.082  21.610  1.00 28.75           O  
ATOM    403  ND2 ASN A 115      -7.014  34.271  22.927  1.00 26.16           N  
ATOM    404  N   GLY A 116      -6.341  39.293  21.859  1.00 31.93           N  
ATOM    405  CA  GLY A 116      -5.384  39.952  20.989  1.00 32.03           C  
ATOM    406  C   GLY A 116      -4.619  39.028  20.054  1.00 32.02           C  
ATOM    407  O   GLY A 116      -3.767  39.480  19.296  1.00 32.68           O  
ATOM    408  N   GLU A 117      -4.929  37.737  20.078  1.00 31.84           N  
ATOM    409  CA  GLU A 117      -4.223  36.790  19.227  1.00 30.71           C  
ATOM    410  C   GLU A 117      -4.689  36.826  17.782  1.00 29.89           C  
ATOM    411  O   GLU A 117      -3.971  36.408  16.880  1.00 28.42           O  
ATOM    412  CB  GLU A 117      -4.362  35.382  19.795  1.00 31.50           C  
ATOM    413  CG  GLU A 117      -3.485  35.137  21.015  1.00 34.75           C  
ATOM    414  CD  GLU A 117      -3.778  33.805  21.679  1.00 36.23           C  
ATOM    415  OE1 GLU A 117      -4.227  32.880  20.975  1.00 39.41           O  
ATOM    416  OE2 GLU A 117      -3.551  33.675  22.901  1.00 39.21           O  
ATOM    417  N   TRP A 118      -5.898  37.321  17.561  1.00 29.37           N  
ATOM    418  CA  TRP A 118      -6.424  37.423  16.211  1.00 27.78           C  
ATOM    419  C   TRP A 118      -6.903  38.845  15.964  1.00 28.65           C  
ATOM    420  O   TRP A 118      -7.186  39.587  16.907  1.00 28.44           O  
ATOM    421  CB  TRP A 118      -7.614  36.490  16.018  1.00 26.41           C  
ATOM    422  CG  TRP A 118      -7.334  35.028  16.085  1.00 26.69           C  
ATOM    423  CD1 TRP A 118      -7.027  34.300  17.194  1.00 22.84           C  
ATOM    424  CD2 TRP A 118      -7.423  34.093  15.002  1.00 25.95           C  
ATOM    425  NE1 TRP A 118      -6.926  32.970  16.874  1.00 23.02           N  
ATOM    426  CE2 TRP A 118      -7.165  32.813  15.535  1.00 24.77           C  
ATOM    427  CE3 TRP A 118      -7.699  34.213  13.633  1.00 26.23           C  
ATOM    428  CZ2 TRP A 118      -7.173  31.657  14.746  1.00 24.77           C  
ATOM    429  CZ3 TRP A 118      -7.708  33.059  12.846  1.00 24.26           C  
ATOM    430  CH2 TRP A 118      -7.447  31.802  13.407  1.00 25.54           C  
ATOM    431  N   CYS A 119      -6.991  39.232  14.697  1.00 29.94           N  
ATOM    432  CA  CYS A 119      -7.500  40.555  14.363  1.00 31.20           C  
ATOM    433  C   CYS A 119      -8.361  40.457  13.112  1.00 29.79           C  
ATOM    434  O   CYS A 119      -8.133  39.609  12.249  1.00 29.78           O  
ATOM    435  CB  CYS A 119      -6.364  41.572  14.176  1.00 35.15           C  
ATOM    436  SG  CYS A 119      -5.404  41.416  12.684  1.00 41.25           S  
ATOM    437  N   GLU A 120      -9.384  41.297  13.042  1.00 29.64           N  
ATOM    438  CA  GLU A 120     -10.297  41.288  11.902  1.00 29.91           C  
ATOM    439  C   GLU A 120      -9.707  42.204  10.825  1.00 28.51           C  
ATOM    440  O   GLU A 120      -9.412  43.368  11.081  1.00 27.61           O  
ATOM    441  CB  GLU A 120     -11.679  41.771  12.357  1.00 29.51           C  
ATOM    442  CG  GLU A 120     -12.810  41.509  11.377  1.00 31.72           C  
ATOM    443  CD  GLU A 120     -14.165  41.956  11.919  1.00 33.58           C  
ATOM    444  OE1 GLU A 120     -15.180  41.778  11.209  1.00 32.44           O  
ATOM    445  OE2 GLU A 120     -14.213  42.483  13.054  1.00 34.37           O  
ATOM    446  N   ALA A 121      -9.532  41.674   9.622  1.00 29.31           N  
ATOM    447  CA  ALA A 121      -8.928  42.451   8.552  1.00 30.36           C  
ATOM    448  C   ALA A 121      -9.720  42.537   7.242  1.00 33.02           C  
ATOM    449  O   ALA A 121     -10.651  41.766   7.001  1.00 33.39           O  
ATOM    450  CB  ALA A 121      -7.534  41.897   8.274  1.00 28.74           C  
ATOM    451  N   GLN A 122      -9.332  43.495   6.403  1.00 34.85           N  
ATOM    452  CA  GLN A 122      -9.945  43.693   5.094  1.00 37.11           C  
ATOM    453  C   GLN A 122      -8.862  43.678   4.021  1.00 38.35           C  
ATOM    454  O   GLN A 122      -7.862  44.397   4.115  1.00 36.82           O  
ATOM    455  CB  GLN A 122     -10.653  45.041   4.998  1.00 38.04           C  
ATOM    456  CG  GLN A 122     -11.854  45.240   5.874  1.00 41.62           C  
ATOM    457  CD  GLN A 122     -12.636  46.472   5.451  1.00 46.25           C  
ATOM    458  OE1 GLN A 122     -12.050  47.487   5.065  1.00 47.83           O  
ATOM    459  NE2 GLN A 122     -13.959  46.393   5.524  1.00 47.19           N  
ATOM    460  N   THR A 123      -9.072  42.861   2.999  1.00 39.76           N  
ATOM    461  CA  THR A 123      -8.143  42.764   1.884  1.00 41.53           C  
ATOM    462  C   THR A 123      -9.011  42.892   0.648  1.00 43.58           C  
ATOM    463  O   THR A 123     -10.223  43.077   0.762  1.00 43.52           O  
ATOM    464  CB  THR A 123      -7.442  41.409   1.856  1.00 42.43           C  
ATOM    465  OG1 THR A 123      -8.392  40.389   1.535  1.00 44.51           O  
ATOM    466  CG2 THR A 123      -6.833  41.107   3.210  1.00 43.97           C  
ATOM    467  N   LYS A 124      -8.418  42.798  -0.534  1.00 46.32           N  
ATOM    468  CA  LYS A 124      -9.226  42.917  -1.738  1.00 49.27           C  
ATOM    469  C   LYS A 124     -10.155  41.731  -1.904  1.00 49.61           C  
ATOM    470  O   LYS A 124     -11.147  41.811  -2.628  1.00 50.64           O  
ATOM    471  CB  LYS A 124      -8.346  43.068  -2.979  1.00 51.68           C  
ATOM    472  CG  LYS A 124      -8.284  44.503  -3.480  1.00 56.64           C  
ATOM    473  CD  LYS A 124      -9.695  45.060  -3.713  1.00 59.22           C  
ATOM    474  CE  LYS A 124      -9.667  46.537  -4.091  1.00 61.82           C  
ATOM    475  NZ  LYS A 124     -11.039  47.085  -4.322  1.00 63.20           N  
ATOM    476  N   ASN A 125      -9.841  40.637  -1.219  1.00 49.02           N  
ATOM    477  CA  ASN A 125     -10.653  39.430  -1.306  1.00 48.97           C  
ATOM    478  C   ASN A 125     -11.803  39.380  -0.314  1.00 47.21           C  
ATOM    479  O   ASN A 125     -12.702  38.557  -0.455  1.00 48.21           O  
ATOM    480  CB  ASN A 125      -9.771  38.193  -1.133  1.00 50.59           C  
ATOM    481  CG  ASN A 125      -8.768  38.046  -2.250  1.00 51.64           C  
ATOM    482  OD1 ASN A 125      -9.135  38.023  -3.423  1.00 53.21           O  
ATOM    483  ND2 ASN A 125      -7.495  37.951  -1.896  1.00 54.24           N  
ATOM    484  N   GLY A 126     -11.779  40.249   0.691  1.00 45.55           N  
ATOM    485  CA  GLY A 126     -12.857  40.249   1.663  1.00 43.09           C  
ATOM    486  C   GLY A 126     -12.487  40.693   3.065  1.00 41.31           C  
ATOM    487  O   GLY A 126     -11.439  41.304   3.295  1.00 40.81           O  
ATOM    488  N   GLN A 127     -13.363  40.373   4.011  1.00 37.93           N  
ATOM    489  CA  GLN A 127     -13.161  40.739   5.404  1.00 34.66           C  
ATOM    490  C   GLN A 127     -13.250  39.495   6.284  1.00 32.45           C  
ATOM    491  O   GLN A 127     -14.106  38.641   6.081  1.00 30.20           O  
ATOM    492  CB  GLN A 127     -14.221  41.757   5.818  1.00 34.99           C  
ATOM    493  CG  GLN A 127     -14.039  42.334   7.197  1.00 38.09           C  
ATOM    494  CD  GLN A 127     -15.047  43.425   7.487  1.00 41.40           C  
ATOM    495  OE1 GLN A 127     -15.188  44.371   6.707  1.00 42.02           O  
ATOM    496  NE2 GLN A 127     -15.752  43.307   8.614  1.00 40.25           N  
ATOM    497  N   GLY A 128     -12.354  39.398   7.258  1.00 31.23           N  
ATOM    498  CA  GLY A 128     -12.353  38.251   8.145  1.00 28.54           C  
ATOM    499  C   GLY A 128     -11.236  38.286   9.170  1.00 27.53           C  
ATOM    500  O   GLY A 128     -10.448  39.239   9.232  1.00 25.14           O  
ATOM    501  N   TRP A 129     -11.163  37.226   9.967  1.00 25.32           N  
ATOM    502  CA  TRP A 129     -10.156  37.121  11.012  1.00 23.44           C  
ATOM    503  C   TRP A 129      -8.898  36.414  10.553  1.00 22.60           C  
ATOM    504  O   TRP A 129      -8.960  35.445   9.805  1.00 22.56           O  
ATOM    505  CB  TRP A 129     -10.727  36.388  12.231  1.00 20.29           C  
ATOM    506  CG  TRP A 129     -11.798  37.145  12.923  1.00 20.16           C  
ATOM    507  CD1 TRP A 129     -13.140  37.082  12.681  1.00 19.26           C  
ATOM    508  CD2 TRP A 129     -11.619  38.114  13.965  1.00 19.01           C  
ATOM    509  NE1 TRP A 129     -13.812  37.953  13.515  1.00 21.46           N  
ATOM    510  CE2 TRP A 129     -12.901  38.596  14.313  1.00 20.50           C  
ATOM    511  CE3 TRP A 129     -10.497  38.618  14.642  1.00 18.71           C  
ATOM    512  CZ2 TRP A 129     -13.095  39.565  15.306  1.00 19.86           C  
ATOM    513  CZ3 TRP A 129     -10.691  39.583  15.636  1.00 18.95           C  
ATOM    514  CH2 TRP A 129     -11.981  40.042  15.956  1.00 19.79           C  
ATOM    515  N   VAL A 130      -7.753  36.911  11.013  1.00 22.58           N  
ATOM    516  CA  VAL A 130      -6.465  36.317  10.670  1.00 22.97           C  
ATOM    517  C   VAL A 130      -5.577  36.396  11.895  1.00 21.78           C  
ATOM    518  O   VAL A 130      -5.803  37.229  12.772  1.00 22.35           O  
ATOM    519  CB  VAL A 130      -5.774  37.070   9.494  1.00 23.88           C  
ATOM    520  CG1 VAL A 130      -6.739  37.156   8.302  1.00 21.36           C  
ATOM    521  CG2 VAL A 130      -5.301  38.464   9.943  1.00 17.00           C  
ATOM    522  N   PRO A 131      -4.568  35.518  11.988  1.00 22.70           N  
ATOM    523  CA  PRO A 131      -3.676  35.554  13.153  1.00 23.03           C  
ATOM    524  C   PRO A 131      -2.932  36.888  13.210  1.00 23.52           C  
ATOM    525  O   PRO A 131      -2.348  37.324  12.214  1.00 22.86           O  
ATOM    526  CB  PRO A 131      -2.742  34.369  12.909  1.00 21.27           C  
ATOM    527  CG  PRO A 131      -3.591  33.423  12.120  1.00 21.68           C  
ATOM    528  CD  PRO A 131      -4.275  34.348  11.142  1.00 22.71           C  
ATOM    529  N   SER A 132      -2.953  37.524  14.378  1.00 23.73           N  
ATOM    530  CA  SER A 132      -2.307  38.819  14.577  1.00 26.42           C  
ATOM    531  C   SER A 132      -0.808  38.844  14.295  1.00 26.22           C  
ATOM    532  O   SER A 132      -0.285  39.837  13.804  1.00 27.77           O  
ATOM    533  CB  SER A 132      -2.552  39.314  16.009  1.00 26.17           C  
ATOM    534  OG  SER A 132      -3.944  39.414  16.268  1.00 29.66           O  
ATOM    535  N   ASN A 133      -0.105  37.768  14.608  1.00 26.61           N  
ATOM    536  CA  ASN A 133       1.325  37.772  14.368  1.00 28.35           C  
ATOM    537  C   ASN A 133       1.667  37.219  12.991  1.00 28.57           C  
ATOM    538  O   ASN A 133       2.791  36.805  12.746  1.00 31.92           O  
ATOM    539  CB  ASN A 133       2.059  36.999  15.468  1.00 26.54           C  
ATOM    540  CG  ASN A 133       1.639  35.554  15.546  1.00 27.05           C  
ATOM    541  OD1 ASN A 133       0.896  35.059  14.699  1.00 30.12           O  
ATOM    542  ND2 ASN A 133       2.120  34.862  16.565  1.00 28.97           N  
ATOM    543  N   TYR A 134       0.688  37.212  12.094  1.00 27.75           N  
ATOM    544  CA  TYR A 134       0.916  36.754  10.728  1.00 27.71           C  
ATOM    545  C   TYR A 134       1.000  37.981   9.826  1.00 28.00           C  
ATOM    546  O   TYR A 134       1.324  37.874   8.645  1.00 28.99           O  
ATOM    547  CB  TYR A 134      -0.225  35.848  10.251  1.00 26.27           C  
ATOM    548  CG  TYR A 134       0.024  34.369  10.451  1.00 25.29           C  
ATOM    549  CD1 TYR A 134       0.425  33.870  11.686  1.00 27.66           C  
ATOM    550  CD2 TYR A 134      -0.170  33.464   9.409  1.00 26.80           C  
ATOM    551  CE1 TYR A 134       0.627  32.505  11.879  1.00 28.95           C  
ATOM    552  CE2 TYR A 134       0.026  32.102   9.589  1.00 27.84           C  
ATOM    553  CZ  TYR A 134       0.423  31.628  10.826  1.00 29.40           C  
ATOM    554  OH  TYR A 134       0.606  30.275  11.022  1.00 30.87           O  
ATOM    555  N   ILE A 135       0.703  39.148  10.392  1.00 25.25           N  
ATOM    556  CA  ILE A 135       0.750  40.394   9.639  1.00 25.89           C  
ATOM    557  C   ILE A 135       1.573  41.411  10.411  1.00 27.22           C  
ATOM    558  O   ILE A 135       1.837  41.227  11.601  1.00 27.75           O  
ATOM    559  CB  ILE A 135      -0.664  40.978   9.410  1.00 25.04           C  
ATOM    560  CG1 ILE A 135      -1.295  41.365  10.748  1.00 24.63           C  
ATOM    561  CG2 ILE A 135      -1.535  39.968   8.692  1.00 20.84           C  
ATOM    562  CD1 ILE A 135      -2.649  42.042  10.619  1.00 25.19           C  
ATOM    563  N   THR A 136       1.972  42.484   9.736  1.00 28.70           N  
ATOM    564  CA  THR A 136       2.776  43.526  10.364  1.00 29.89           C  
ATOM    565  C   THR A 136       2.548  44.884   9.697  1.00 30.96           C  
ATOM    566  O   THR A 136       2.170  44.960   8.526  1.00 31.54           O  
ATOM    567  CB  THR A 136       4.272  43.165  10.278  1.00 31.40           C  
ATOM    568  OG1 THR A 136       5.015  43.946  11.223  1.00 31.02           O  
ATOM    569  CG2 THR A 136       4.799  43.412   8.860  1.00 30.86           C  
ATOM    570  N   PRO A 137       2.760  45.981  10.440  1.00 31.58           N  
ATOM    571  CA  PRO A 137       2.556  47.301   9.836  1.00 33.26           C  
ATOM    572  C   PRO A 137       3.410  47.441   8.573  1.00 34.68           C  
ATOM    573  O   PRO A 137       4.513  46.908   8.498  1.00 33.21           O  
ATOM    574  CB  PRO A 137       2.991  48.260  10.950  1.00 33.46           C  
ATOM    575  CG  PRO A 137       2.605  47.519  12.196  1.00 33.10           C  
ATOM    576  CD  PRO A 137       3.064  46.098  11.880  1.00 31.49           C  
ATOM    577  N   VAL A 138       2.884  48.151   7.584  1.00 36.90           N  
ATOM    578  CA  VAL A 138       3.605  48.357   6.336  1.00 40.65           C  
ATOM    579  C   VAL A 138       5.005  48.942   6.527  1.00 41.28           C  
ATOM    580  O   VAL A 138       5.945  48.470   5.897  1.00 42.47           O  
ATOM    581  CB  VAL A 138       2.823  49.275   5.366  1.00 42.45           C  
ATOM    582  CG1 VAL A 138       3.637  49.519   4.125  1.00 42.19           C  
ATOM    583  CG2 VAL A 138       1.509  48.643   4.991  1.00 43.97           C  
ATOM    584  N   ASN A 139       5.162  49.948   7.389  1.00 42.70           N  
ATOM    585  CA  ASN A 139       6.486  50.558   7.622  1.00 43.58           C  
ATOM    586  C   ASN A 139       7.310  49.925   8.753  1.00 42.57           C  
ATOM    587  O   ASN A 139       8.257  50.543   9.250  1.00 43.46           O  
ATOM    588  CB  ASN A 139       6.344  52.054   7.937  1.00 45.82           C  
ATOM    589  CG  ASN A 139       5.650  52.824   6.834  1.00 48.50           C  
ATOM    590  OD1 ASN A 139       4.726  53.608   7.088  1.00 51.21           O  
ATOM    591  ND2 ASN A 139       6.102  52.628   5.605  1.00 51.20           N  
ATOM    592  N   SER A 140       6.974  48.714   9.178  1.00 41.04           N  
ATOM    593  CA  SER A 140       7.760  48.117  10.250  1.00 39.47           C  
ATOM    594  C   SER A 140       8.899  47.361   9.626  1.00 38.88           C  
ATOM    595  O   SER A 140       8.847  47.039   8.440  1.00 38.59           O  
ATOM    596  CB  SER A 140       6.917  47.177  11.104  1.00 38.34           C  
ATOM    597  OG  SER A 140       6.377  46.119  10.336  1.00 39.79           O  
ATOM    598  N   LEU A 141       9.929  47.084  10.414  1.00 37.52           N  
ATOM    599  CA  LEU A 141      11.085  46.371   9.903  1.00 38.84           C  
ATOM    600  C   LEU A 141      10.750  44.936   9.550  1.00 38.52           C  
ATOM    601  O   LEU A 141      11.403  44.340   8.694  1.00 36.85           O  
ATOM    602  CB  LEU A 141      12.208  46.385  10.938  1.00 39.75           C  
ATOM    603  CG  LEU A 141      12.826  47.735  11.300  1.00 40.48           C  
ATOM    604  CD1 LEU A 141      13.877  47.536  12.390  1.00 42.00           C  
ATOM    605  CD2 LEU A 141      13.440  48.369  10.064  1.00 41.31           C  
ATOM    606  N   GLU A 142       9.726  44.399  10.207  1.00 38.24           N  
ATOM    607  CA  GLU A 142       9.306  43.025   9.999  1.00 38.61           C  
ATOM    608  C   GLU A 142       8.875  42.697   8.579  1.00 37.75           C  
ATOM    609  O   GLU A 142       8.912  41.541   8.185  1.00 37.27           O  
ATOM    610  CB  GLU A 142       8.173  42.665  10.964  1.00 41.35           C  
ATOM    611  CG  GLU A 142       8.535  42.646  12.458  1.00 43.41           C  
ATOM    612  CD  GLU A 142       8.769  44.036  13.046  1.00 46.14           C  
ATOM    613  OE1 GLU A 142       8.235  45.020  12.490  1.00 47.40           O  
ATOM    614  OE2 GLU A 142       9.474  44.143  14.076  1.00 45.35           O  
ATOM    615  N   LYS A 143       8.470  43.695   7.800  1.00 37.92           N  
ATOM    616  CA  LYS A 143       8.034  43.412   6.430  1.00 38.78           C  
ATOM    617  C   LYS A 143       9.173  42.905   5.548  1.00 36.85           C  
ATOM    618  O   LYS A 143       8.940  42.230   4.550  1.00 36.93           O  
ATOM    619  CB  LYS A 143       7.422  44.658   5.777  1.00 40.69           C  
ATOM    620  CG  LYS A 143       8.421  45.763   5.485  1.00 46.04           C  
ATOM    621  CD  LYS A 143       8.009  46.562   4.258  1.00 49.94           C  
ATOM    622  CE  LYS A 143       8.808  47.844   4.156  1.00 52.19           C  
ATOM    623  NZ  LYS A 143       8.739  48.595   5.449  1.00 54.89           N  
ATOM    624  N   HIS A 144      10.402  43.237   5.919  1.00 35.40           N  
ATOM    625  CA  HIS A 144      11.573  42.825   5.154  1.00 33.91           C  
ATOM    626  C   HIS A 144      11.873  41.334   5.272  1.00 33.35           C  
ATOM    627  O   HIS A 144      11.974  40.784   6.376  1.00 32.44           O  
ATOM    628  CB  HIS A 144      12.807  43.607   5.608  1.00 34.44           C  
ATOM    629  CG  HIS A 144      12.700  45.082   5.402  1.00 35.15           C  
ATOM    630  ND1 HIS A 144      12.491  45.645   4.163  1.00 33.56           N  
ATOM    631  CD2 HIS A 144      12.795  46.115   6.275  1.00 36.92           C  
ATOM    632  CE1 HIS A 144      12.463  46.961   4.280  1.00 36.50           C  
ATOM    633  NE2 HIS A 144      12.646  47.272   5.551  1.00 37.39           N  
ATOM    634  N   SER A 145      12.039  40.694   4.121  1.00 30.87           N  
ATOM    635  CA  SER A 145      12.340  39.272   4.065  1.00 30.55           C  
ATOM    636  C   SER A 145      13.617  38.906   4.825  1.00 30.51           C  
ATOM    637  O   SER A 145      13.791  37.755   5.221  1.00 32.19           O  
ATOM    638  CB  SER A 145      12.480  38.839   2.605  1.00 31.36           C  
ATOM    639  OG  SER A 145      13.447  39.635   1.937  1.00 28.97           O  
ATOM    640  N   TRP A 146      14.506  39.872   5.040  1.00 28.40           N  
ATOM    641  CA  TRP A 146      15.759  39.587   5.740  1.00 28.88           C  
ATOM    642  C   TRP A 146      15.776  39.887   7.243  1.00 29.49           C  
ATOM    643  O   TRP A 146      16.701  39.487   7.945  1.00 28.67           O  
ATOM    644  CB  TRP A 146      16.922  40.321   5.072  1.00 25.53           C  
ATOM    645  CG  TRP A 146      16.613  41.722   4.693  1.00 25.00           C  
ATOM    646  CD1 TRP A 146      16.243  42.175   3.455  1.00 24.71           C  
ATOM    647  CD2 TRP A 146      16.639  42.869   5.547  1.00 24.88           C  
ATOM    648  NE1 TRP A 146      16.041  43.533   3.487  1.00 25.17           N  
ATOM    649  CE2 TRP A 146      16.274  43.987   4.758  1.00 22.91           C  
ATOM    650  CE3 TRP A 146      16.930  43.063   6.902  1.00 24.42           C  
ATOM    651  CZ2 TRP A 146      16.197  45.276   5.279  1.00 23.36           C  
ATOM    652  CZ3 TRP A 146      16.852  44.351   7.422  1.00 24.57           C  
ATOM    653  CH2 TRP A 146      16.487  45.442   6.608  1.00 23.28           C  
ATOM    654  N   TYR A 147      14.768  40.595   7.732  1.00 30.26           N  
ATOM    655  CA  TYR A 147      14.696  40.905   9.153  1.00 31.16           C  
ATOM    656  C   TYR A 147      13.960  39.748   9.840  1.00 30.42           C  
ATOM    657  O   TYR A 147      12.754  39.591   9.662  1.00 32.29           O  
ATOM    658  CB  TYR A 147      13.926  42.210   9.367  1.00 32.21           C  
ATOM    659  CG  TYR A 147      14.013  42.732  10.778  1.00 36.91           C  
ATOM    660  CD1 TYR A 147      15.098  43.505  11.188  1.00 38.05           C  
ATOM    661  CD2 TYR A 147      13.034  42.412  11.720  1.00 37.61           C  
ATOM    662  CE1 TYR A 147      15.210  43.946  12.498  1.00 40.95           C  
ATOM    663  CE2 TYR A 147      13.138  42.844  13.034  1.00 40.77           C  
ATOM    664  CZ  TYR A 147      14.229  43.611  13.419  1.00 41.97           C  
ATOM    665  OH  TYR A 147      14.345  44.033  14.726  1.00 43.55           O  
ATOM    666  N   HIS A 148      14.677  38.934  10.610  1.00 29.44           N  
ATOM    667  CA  HIS A 148      14.038  37.806  11.285  1.00 31.06           C  
ATOM    668  C   HIS A 148      13.667  38.105  12.733  1.00 32.76           C  
ATOM    669  O   HIS A 148      13.265  37.212  13.476  1.00 32.17           O  
ATOM    670  CB  HIS A 148      14.928  36.552  11.226  1.00 29.12           C  
ATOM    671  CG  HIS A 148      15.052  35.960   9.853  1.00 29.81           C  
ATOM    672  ND1 HIS A 148      15.206  34.607   9.636  1.00 30.59           N  
ATOM    673  CD2 HIS A 148      15.072  36.540   8.628  1.00 27.70           C  
ATOM    674  CE1 HIS A 148      15.316  34.379   8.340  1.00 30.27           C  
ATOM    675  NE2 HIS A 148      15.238  35.536   7.706  1.00 29.68           N  
ATOM    676  N   GLY A 149      13.807  39.366  13.126  1.00 35.17           N  
ATOM    677  CA  GLY A 149      13.463  39.765  14.478  1.00 37.24           C  
ATOM    678  C   GLY A 149      14.267  39.087  15.568  1.00 38.86           C  
ATOM    679  O   GLY A 149      15.460  38.828  15.399  1.00 40.39           O  
ATOM    680  N   PRO A 150      13.639  38.792  16.714  1.00 40.26           N  
ATOM    681  CA  PRO A 150      14.350  38.138  17.810  1.00 41.54           C  
ATOM    682  C   PRO A 150      14.702  36.692  17.471  1.00 42.89           C  
ATOM    683  O   PRO A 150      13.850  35.804  17.488  1.00 45.18           O  
ATOM    684  CB  PRO A 150      13.364  38.258  18.965  1.00 41.18           C  
ATOM    685  CG  PRO A 150      12.050  38.121  18.273  1.00 40.43           C  
ATOM    686  CD  PRO A 150      12.227  39.021  17.070  1.00 41.12           C  
ATOM    687  N   VAL A 151      15.969  36.478  17.146  1.00 43.49           N  
ATOM    688  CA  VAL A 151      16.489  35.167  16.794  1.00 42.68           C  
ATOM    689  C   VAL A 151      17.852  35.099  17.456  1.00 41.35           C  
ATOM    690  O   VAL A 151      18.607  36.070  17.417  1.00 41.28           O  
ATOM    691  CB  VAL A 151      16.645  35.028  15.258  1.00 44.73           C  
ATOM    692  CG1 VAL A 151      17.537  33.849  14.919  1.00 46.75           C  
ATOM    693  CG2 VAL A 151      15.283  34.842  14.617  1.00 45.88           C  
ATOM    694  N   SER A 152      18.164  33.965  18.074  1.00 39.86           N  
ATOM    695  CA  SER A 152      19.443  33.807  18.759  1.00 38.10           C  
ATOM    696  C   SER A 152      20.577  33.512  17.789  1.00 37.36           C  
ATOM    697  O   SER A 152      20.351  33.170  16.626  1.00 34.96           O  
ATOM    698  CB  SER A 152      19.365  32.671  19.777  1.00 39.01           C  
ATOM    699  OG  SER A 152      19.240  31.421  19.114  1.00 38.11           O  
ATOM    700  N   ARG A 153      21.798  33.630  18.296  1.00 35.89           N  
ATOM    701  CA  ARG A 153      23.002  33.377  17.519  1.00 36.71           C  
ATOM    702  C   ARG A 153      22.977  31.955  16.974  1.00 36.94           C  
ATOM    703  O   ARG A 153      23.244  31.725  15.789  1.00 36.90           O  
ATOM    704  CB  ARG A 153      24.236  33.570  18.407  1.00 34.53           C  
ATOM    705  CG  ARG A 153      25.573  33.401  17.704  1.00 34.03           C  
ATOM    706  CD  ARG A 153      26.692  33.339  18.729  1.00 32.39           C  
ATOM    707  NE  ARG A 153      28.009  33.125  18.137  1.00 31.90           N  
ATOM    708  CZ  ARG A 153      28.758  34.084  17.600  1.00 33.92           C  
ATOM    709  NH1 ARG A 153      28.328  35.341  17.569  1.00 31.15           N  
ATOM    710  NH2 ARG A 153      29.959  33.791  17.117  1.00 33.44           N  
ATOM    711  N   ASN A 154      22.651  31.006  17.848  1.00 36.71           N  
ATOM    712  CA  ASN A 154      22.602  29.602  17.469  1.00 36.17           C  
ATOM    713  C   ASN A 154      21.484  29.332  16.480  1.00 33.62           C  
ATOM    714  O   ASN A 154      21.681  28.610  15.508  1.00 32.30           O  
ATOM    715  CB  ASN A 154      22.426  28.718  18.705  1.00 39.14           C  
ATOM    716  CG  ASN A 154      23.461  29.006  19.778  1.00 42.86           C  
ATOM    717  OD1 ASN A 154      24.576  29.454  19.482  1.00 42.78           O  
ATOM    718  ND2 ASN A 154      23.103  28.739  21.034  1.00 42.84           N  
ATOM    719  N   ALA A 155      20.309  29.903  16.733  1.00 31.76           N  
ATOM    720  CA  ALA A 155      19.167  29.728  15.831  1.00 30.49           C  
ATOM    721  C   ALA A 155      19.556  30.268  14.453  1.00 29.20           C  
ATOM    722  O   ALA A 155      19.227  29.677  13.424  1.00 28.17           O  
ATOM    723  CB  ALA A 155      17.939  30.479  16.372  1.00 25.85           C  
ATOM    724  N   ALA A 156      20.260  31.397  14.452  1.00 28.62           N  
ATOM    725  CA  ALA A 156      20.732  32.021  13.219  1.00 29.69           C  
ATOM    726  C   ALA A 156      21.626  31.038  12.463  1.00 31.24           C  
ATOM    727  O   ALA A 156      21.505  30.893  11.244  1.00 31.47           O  
ATOM    728  CB  ALA A 156      21.517  33.295  13.539  1.00 29.02           C  
ATOM    729  N   GLU A 157      22.522  30.365  13.184  1.00 29.41           N  
ATOM    730  CA  GLU A 157      23.413  29.404  12.546  1.00 30.93           C  
ATOM    731  C   GLU A 157      22.594  28.291  11.918  1.00 29.89           C  
ATOM    732  O   GLU A 157      22.968  27.750  10.876  1.00 27.56           O  
ATOM    733  CB  GLU A 157      24.409  28.811  13.549  1.00 33.73           C  
ATOM    734  CG  GLU A 157      25.256  29.851  14.272  1.00 41.19           C  
ATOM    735  CD  GLU A 157      26.722  29.445  14.389  1.00 45.76           C  
ATOM    736  OE1 GLU A 157      27.000  28.251  14.638  1.00 48.72           O  
ATOM    737  OE2 GLU A 157      27.596  30.326  14.239  1.00 46.90           O  
ATOM    738  N   TYR A 158      21.474  27.947  12.549  1.00 27.87           N  
ATOM    739  CA  TYR A 158      20.618  26.913  11.999  1.00 26.39           C  
ATOM    740  C   TYR A 158      19.930  27.422  10.729  1.00 25.95           C  
ATOM    741  O   TYR A 158      19.879  26.726   9.725  1.00 24.17           O  
ATOM    742  CB  TYR A 158      19.537  26.481  12.988  1.00 24.76           C  
ATOM    743  CG  TYR A 158      18.571  25.539  12.329  1.00 26.50           C  
ATOM    744  CD1 TYR A 158      18.980  24.261  11.954  1.00 27.41           C  
ATOM    745  CD2 TYR A 158      17.294  25.962  11.950  1.00 26.00           C  
ATOM    746  CE1 TYR A 158      18.155  23.431  11.214  1.00 28.76           C  
ATOM    747  CE2 TYR A 158      16.454  25.134  11.199  1.00 26.70           C  
ATOM    748  CZ  TYR A 158      16.894  23.868  10.835  1.00 27.70           C  
ATOM    749  OH  TYR A 158      16.091  23.025  10.096  1.00 26.57           O  
ATOM    750  N   LEU A 159      19.387  28.632  10.793  1.00 26.87           N  
ATOM    751  CA  LEU A 159      18.701  29.220   9.649  1.00 29.31           C  
ATOM    752  C   LEU A 159      19.650  29.400   8.475  1.00 30.31           C  
ATOM    753  O   LEU A 159      19.218  29.411   7.329  1.00 32.52           O  
ATOM    754  CB  LEU A 159      18.072  30.565  10.032  1.00 26.23           C  
ATOM    755  CG  LEU A 159      16.794  30.481  10.883  1.00 28.97           C  
ATOM    756  CD1 LEU A 159      16.439  31.851  11.450  1.00 25.69           C  
ATOM    757  CD2 LEU A 159      15.646  29.951  10.021  1.00 25.86           C  
ATOM    758  N   LEU A 160      20.943  29.517   8.762  1.00 31.86           N  
ATOM    759  CA  LEU A 160      21.951  29.691   7.718  1.00 32.53           C  
ATOM    760  C   LEU A 160      22.870  28.480   7.573  1.00 33.02           C  
ATOM    761  O   LEU A 160      23.987  28.608   7.078  1.00 33.35           O  
ATOM    762  CB  LEU A 160      22.804  30.923   8.017  1.00 32.19           C  
ATOM    763  CG  LEU A 160      22.103  32.280   7.969  1.00 32.79           C  
ATOM    764  CD1 LEU A 160      23.006  33.329   8.582  1.00 30.44           C  
ATOM    765  CD2 LEU A 160      21.745  32.634   6.532  1.00 31.45           C  
ATOM    766  N   SER A 161      22.409  27.310   8.002  1.00 33.53           N  
ATOM    767  CA  SER A 161      23.233  26.104   7.916  1.00 35.02           C  
ATOM    768  C   SER A 161      23.208  25.538   6.503  1.00 36.56           C  
ATOM    769  O   SER A 161      23.877  24.544   6.202  1.00 36.47           O  
ATOM    770  CB  SER A 161      22.739  25.044   8.900  1.00 33.26           C  
ATOM    771  OG  SER A 161      21.440  24.613   8.551  1.00 36.79           O  
ATOM    772  N   SER A 162      22.419  26.172   5.645  1.00 36.06           N  
ATOM    773  CA  SER A 162      22.314  25.755   4.258  1.00 38.58           C  
ATOM    774  C   SER A 162      21.992  26.985   3.422  1.00 37.71           C  
ATOM    775  O   SER A 162      21.578  28.009   3.954  1.00 37.72           O  
ATOM    776  CB  SER A 162      21.229  24.680   4.100  1.00 40.23           C  
ATOM    777  OG  SER A 162      19.963  25.130   4.560  1.00 42.92           O  
ATOM    778  N   GLY A 163      22.207  26.895   2.116  1.00 37.46           N  
ATOM    779  CA  GLY A 163      21.934  28.033   1.259  1.00 36.58           C  
ATOM    780  C   GLY A 163      23.179  28.513   0.539  1.00 35.53           C  
ATOM    781  O   GLY A 163      24.304  28.144   0.894  1.00 31.67           O  
ATOM    782  N   ILE A 164      22.986  29.347  -0.476  1.00 35.45           N  
ATOM    783  CA  ILE A 164      24.122  29.839  -1.238  1.00 37.23           C  
ATOM    784  C   ILE A 164      24.904  30.932  -0.521  1.00 34.83           C  
ATOM    785  O   ILE A 164      24.441  31.511   0.471  1.00 32.65           O  
ATOM    786  CB  ILE A 164      23.687  30.386  -2.614  1.00 40.41           C  
ATOM    787  CG1 ILE A 164      22.848  31.640  -2.440  1.00 41.88           C  
ATOM    788  CG2 ILE A 164      22.870  29.338  -3.360  1.00 44.52           C  
ATOM    789  CD1 ILE A 164      22.603  32.351  -3.747  1.00 49.13           C  
ATOM    790  N   ASN A 165      26.104  31.197  -1.026  1.00 31.22           N  
ATOM    791  CA  ASN A 165      26.931  32.244  -0.459  1.00 29.52           C  
ATOM    792  C   ASN A 165      26.146  33.539  -0.495  1.00 26.72           C  
ATOM    793  O   ASN A 165      25.445  33.807  -1.463  1.00 29.19           O  
ATOM    794  CB  ASN A 165      28.207  32.406  -1.271  1.00 29.69           C  
ATOM    795  CG  ASN A 165      29.218  31.353  -0.953  1.00 30.29           C  
ATOM    796  OD1 ASN A 165      29.136  30.712   0.092  1.00 32.36           O  
ATOM    797  ND2 ASN A 165      30.198  31.175  -1.835  1.00 32.07           N  
ATOM    798  N   GLY A 166      26.248  34.337   0.558  1.00 24.50           N  
ATOM    799  CA  GLY A 166      25.522  35.590   0.578  1.00 22.37           C  
ATOM    800  C   GLY A 166      24.177  35.532   1.276  1.00 21.89           C  
ATOM    801  O   GLY A 166      23.498  36.556   1.390  1.00 21.82           O  
ATOM    802  N   SER A 167      23.773  34.349   1.727  1.00 20.29           N  
ATOM    803  CA  SER A 167      22.511  34.220   2.443  1.00 22.16           C  
ATOM    804  C   SER A 167      22.750  34.963   3.749  1.00 22.53           C  
ATOM    805  O   SER A 167      23.822  34.850   4.354  1.00 21.87           O  
ATOM    806  CB  SER A 167      22.185  32.751   2.733  1.00 23.76           C  
ATOM    807  OG  SER A 167      21.962  32.035   1.534  1.00 26.71           O  
ATOM    808  N   PHE A 168      21.760  35.727   4.182  1.00 21.95           N  
ATOM    809  CA  PHE A 168      21.929  36.499   5.393  1.00 24.69           C  
ATOM    810  C   PHE A 168      20.596  36.871   6.020  1.00 25.38           C  
ATOM    811  O   PHE A 168      19.529  36.698   5.423  1.00 23.31           O  
ATOM    812  CB  PHE A 168      22.671  37.796   5.082  1.00 23.02           C  
ATOM    813  CG  PHE A 168      21.796  38.835   4.431  1.00 21.35           C  
ATOM    814  CD1 PHE A 168      21.462  38.737   3.079  1.00 20.15           C  
ATOM    815  CD2 PHE A 168      21.274  39.886   5.178  1.00 19.82           C  
ATOM    816  CE1 PHE A 168      20.618  39.672   2.480  1.00 20.80           C  
ATOM    817  CE2 PHE A 168      20.426  40.833   4.593  1.00 23.25           C  
ATOM    818  CZ  PHE A 168      20.096  40.724   3.238  1.00 23.22           C  
ATOM    819  N   LEU A 169      20.683  37.427   7.220  1.00 25.40           N  
ATOM    820  CA  LEU A 169      19.506  37.859   7.936  1.00 26.84           C  
ATOM    821  C   LEU A 169      19.956  38.845   9.002  1.00 27.59           C  
ATOM    822  O   LEU A 169      21.129  38.881   9.368  1.00 24.32           O  
ATOM    823  CB  LEU A 169      18.826  36.647   8.576  1.00 27.08           C  
ATOM    824  CG  LEU A 169      19.630  35.945   9.675  1.00 29.86           C  
ATOM    825  CD1 LEU A 169      19.368  36.633  11.013  1.00 28.37           C  
ATOM    826  CD2 LEU A 169      19.224  34.487   9.757  1.00 29.56           C  
ATOM    827  N   VAL A 170      19.030  39.673   9.464  1.00 28.48           N  
ATOM    828  CA  VAL A 170      19.319  40.619  10.523  1.00 28.98           C  
ATOM    829  C   VAL A 170      18.466  40.138  11.695  1.00 31.30           C  
ATOM    830  O   VAL A 170      17.284  39.828  11.527  1.00 30.70           O  
ATOM    831  CB  VAL A 170      18.927  42.058  10.130  1.00 30.04           C  
ATOM    832  CG1 VAL A 170      18.964  42.964  11.354  1.00 27.49           C  
ATOM    833  CG2 VAL A 170      19.904  42.587   9.074  1.00 30.11           C  
ATOM    834  N   ARG A 171      19.077  40.040  12.868  1.00 32.65           N  
ATOM    835  CA  ARG A 171      18.372  39.581  14.055  1.00 35.84           C  
ATOM    836  C   ARG A 171      18.543  40.551  15.224  1.00 39.61           C  
ATOM    837  O   ARG A 171      19.526  41.294  15.298  1.00 37.11           O  
ATOM    838  CB  ARG A 171      18.883  38.192  14.458  1.00 33.49           C  
ATOM    839  CG  ARG A 171      20.382  38.124  14.758  1.00 32.17           C  
ATOM    840  CD  ARG A 171      20.821  36.685  14.941  1.00 30.72           C  
ATOM    841  NE  ARG A 171      22.273  36.526  14.982  1.00 31.75           N  
ATOM    842  CZ  ARG A 171      23.046  36.859  16.014  1.00 32.52           C  
ATOM    843  NH1 ARG A 171      22.512  37.382  17.112  1.00 30.14           N  
ATOM    844  NH2 ARG A 171      24.358  36.663  15.951  1.00 27.84           N  
ATOM    845  N   GLU A 172      17.568  40.542  16.128  1.00 45.24           N  
ATOM    846  CA  GLU A 172      17.608  41.389  17.310  1.00 51.13           C  
ATOM    847  C   GLU A 172      17.801  40.496  18.527  1.00 54.49           C  
ATOM    848  O   GLU A 172      17.625  39.279  18.451  1.00 54.16           O  
ATOM    849  CB  GLU A 172      16.302  42.170  17.477  1.00 53.68           C  
ATOM    850  CG  GLU A 172      16.290  43.060  18.730  1.00 59.28           C  
ATOM    851  CD  GLU A 172      14.927  43.668  19.032  1.00 62.74           C  
ATOM    852  OE1 GLU A 172      13.964  42.899  19.258  1.00 63.68           O  
ATOM    853  OE2 GLU A 172      14.823  44.917  19.049  1.00 64.88           O  
ATOM    854  N   SER A 173      18.162  41.106  19.648  1.00 58.39           N  
ATOM    855  CA  SER A 173      18.347  40.361  20.880  1.00 63.08           C  
ATOM    856  C   SER A 173      17.130  40.531  21.781  1.00 65.78           C  
ATOM    857  O   SER A 173      16.821  41.643  22.213  1.00 66.59           O  
ATOM    858  CB  SER A 173      19.588  40.850  21.619  1.00 63.17           C  
ATOM    859  OG  SER A 173      19.710  40.186  22.864  1.00 65.59           O  
ATOM    860  N   GLU A 174      16.432  39.430  22.048  1.00 68.89           N  
ATOM    861  CA  GLU A 174      15.265  39.469  22.922  1.00 71.86           C  
ATOM    862  C   GLU A 174      15.811  39.843  24.291  1.00 73.10           C  
ATOM    863  O   GLU A 174      15.192  40.596  25.044  1.00 73.88           O  
ATOM    864  CB  GLU A 174      14.592  38.092  22.989  1.00 72.95           C  
ATOM    865  CG  GLU A 174      13.393  38.007  23.944  1.00 74.58           C  
ATOM    866  CD  GLU A 174      12.164  38.748  23.434  1.00 75.80           C  
ATOM    867  OE1 GLU A 174      11.607  38.328  22.397  1.00 75.11           O  
ATOM    868  OE2 GLU A 174      11.755  39.749  24.066  1.00 75.52           O  
ATOM    869  N   SER A 175      16.995  39.312  24.585  1.00 74.07           N  
ATOM    870  CA  SER A 175      17.687  39.555  25.844  1.00 75.18           C  
ATOM    871  C   SER A 175      17.963  41.044  26.020  1.00 75.17           C  
ATOM    872  O   SER A 175      17.440  41.679  26.936  1.00 76.06           O  
ATOM    873  CB  SER A 175      19.006  38.779  25.858  1.00 75.94           C  
ATOM    874  OG  SER A 175      18.804  37.436  25.446  1.00 76.28           O  
ATOM    875  N   SER A 176      18.795  41.594  25.142  1.00 74.96           N  
ATOM    876  CA  SER A 176      19.132  43.012  25.190  1.00 75.21           C  
ATOM    877  C   SER A 176      18.485  43.723  24.003  1.00 74.52           C  
ATOM    878  O   SER A 176      19.122  43.923  22.969  1.00 75.08           O  
ATOM    879  CB  SER A 176      20.652  43.203  25.137  1.00 75.70           C  
ATOM    880  OG  SER A 176      21.296  42.570  26.228  1.00 77.61           O  
ATOM    881  N   PRO A 177      17.207  44.115  24.138  1.00 73.50           N  
ATOM    882  CA  PRO A 177      16.487  44.804  23.062  1.00 72.39           C  
ATOM    883  C   PRO A 177      17.308  45.924  22.427  1.00 71.48           C  
ATOM    884  O   PRO A 177      18.143  46.546  23.090  1.00 71.94           O  
ATOM    885  CB  PRO A 177      15.241  45.325  23.768  1.00 72.66           C  
ATOM    886  CG  PRO A 177      14.979  44.258  24.787  1.00 72.82           C  
ATOM    887  CD  PRO A 177      16.362  44.003  25.341  1.00 73.02           C  
ATOM    888  N   GLY A 178      17.070  46.175  21.143  1.00 69.72           N  
ATOM    889  CA  GLY A 178      17.800  47.221  20.445  1.00 66.72           C  
ATOM    890  C   GLY A 178      19.048  46.723  19.733  1.00 64.55           C  
ATOM    891  O   GLY A 178      19.276  47.061  18.568  1.00 65.00           O  
ATOM    892  N   GLN A 179      19.857  45.923  20.428  1.00 61.22           N  
ATOM    893  CA  GLN A 179      21.086  45.382  19.854  1.00 57.92           C  
ATOM    894  C   GLN A 179      20.787  44.419  18.713  1.00 53.56           C  
ATOM    895  O   GLN A 179      20.177  43.372  18.917  1.00 52.68           O  
ATOM    896  CB  GLN A 179      21.907  44.657  20.927  1.00 60.66           C  
ATOM    897  CG  GLN A 179      22.435  45.557  22.040  1.00 65.37           C  
ATOM    898  CD  GLN A 179      23.359  46.656  21.530  1.00 68.15           C  
ATOM    899  OE1 GLN A 179      24.433  46.385  20.977  1.00 70.81           O  
ATOM    900  NE2 GLN A 179      22.943  47.905  21.713  1.00 68.94           N  
ATOM    901  N   ARG A 180      21.217  44.777  17.510  1.00 48.91           N  
ATOM    902  CA  ARG A 180      20.985  43.928  16.353  1.00 45.28           C  
ATOM    903  C   ARG A 180      22.282  43.402  15.761  1.00 42.15           C  
ATOM    904  O   ARG A 180      23.364  43.944  16.007  1.00 42.34           O  
ATOM    905  CB  ARG A 180      20.190  44.683  15.288  1.00 46.09           C  
ATOM    906  CG  ARG A 180      18.861  45.183  15.794  1.00 46.98           C  
ATOM    907  CD  ARG A 180      17.883  45.371  14.662  1.00 50.53           C  
ATOM    908  NE  ARG A 180      16.624  45.940  15.132  1.00 54.06           N  
ATOM    909  CZ  ARG A 180      16.492  47.186  15.576  1.00 54.67           C  
ATOM    910  NH1 ARG A 180      17.545  47.997  15.611  1.00 54.24           N  
ATOM    911  NH2 ARG A 180      15.308  47.621  15.981  1.00 54.48           N  
ATOM    912  N   SER A 181      22.163  42.339  14.977  1.00 37.72           N  
ATOM    913  CA  SER A 181      23.319  41.712  14.360  1.00 34.82           C  
ATOM    914  C   SER A 181      23.007  41.200  12.966  1.00 34.07           C  
ATOM    915  O   SER A 181      21.846  40.998  12.599  1.00 33.55           O  
ATOM    916  CB  SER A 181      23.793  40.533  15.209  1.00 32.56           C  
ATOM    917  OG  SER A 181      24.166  40.948  16.505  1.00 34.26           O  
ATOM    918  N   ILE A 182      24.067  40.986  12.198  1.00 32.28           N  
ATOM    919  CA  ILE A 182      23.948  40.457  10.855  1.00 29.60           C  
ATOM    920  C   ILE A 182      24.602  39.091  10.874  1.00 28.37           C  
ATOM    921  O   ILE A 182      25.733  38.951  11.336  1.00 27.57           O  
ATOM    922  CB  ILE A 182      24.694  41.318   9.821  1.00 29.91           C  
ATOM    923  CG1 ILE A 182      23.982  42.659   9.647  1.00 30.50           C  
ATOM    924  CG2 ILE A 182      24.793  40.562   8.500  1.00 26.89           C  
ATOM    925  CD1 ILE A 182      24.673  43.599   8.677  1.00 31.10           C  
ATOM    926  N   SER A 183      23.876  38.082  10.410  1.00 26.51           N  
ATOM    927  CA  SER A 183      24.422  36.741  10.331  1.00 27.75           C  
ATOM    928  C   SER A 183      24.504  36.463   8.845  1.00 28.65           C  
ATOM    929  O   SER A 183      23.544  36.669   8.090  1.00 27.67           O  
ATOM    930  CB  SER A 183      23.533  35.733  11.053  1.00 28.23           C  
ATOM    931  OG  SER A 183      23.619  35.948  12.447  1.00 25.70           O  
ATOM    932  N   LEU A 184      25.674  36.000   8.433  1.00 28.41           N  
ATOM    933  CA  LEU A 184      25.946  35.781   7.033  1.00 26.58           C  
ATOM    934  C   LEU A 184      26.603  34.444   6.756  1.00 24.22           C  
ATOM    935  O   LEU A 184      27.442  33.983   7.524  1.00 23.12           O  
ATOM    936  CB  LEU A 184      26.843  36.931   6.564  1.00 27.98           C  
ATOM    937  CG  LEU A 184      27.421  37.008   5.158  1.00 30.60           C  
ATOM    938  CD1 LEU A 184      26.294  37.038   4.136  1.00 31.52           C  
ATOM    939  CD2 LEU A 184      28.272  38.277   5.049  1.00 29.79           C  
ATOM    940  N   ARG A 185      26.211  33.827   5.646  1.00 24.19           N  
ATOM    941  CA  ARG A 185      26.768  32.551   5.245  1.00 22.66           C  
ATOM    942  C   ARG A 185      27.769  32.731   4.110  1.00 24.74           C  
ATOM    943  O   ARG A 185      27.484  33.399   3.105  1.00 24.38           O  
ATOM    944  CB  ARG A 185      25.656  31.602   4.801  1.00 23.89           C  
ATOM    945  CG  ARG A 185      26.144  30.224   4.402  1.00 24.80           C  
ATOM    946  CD  ARG A 185      24.997  29.307   3.980  1.00 27.46           C  
ATOM    947  NE  ARG A 185      25.492  28.058   3.397  1.00 29.07           N  
ATOM    948  CZ  ARG A 185      25.904  26.998   4.086  1.00 30.64           C  
ATOM    949  NH1 ARG A 185      25.881  27.000   5.413  1.00 32.64           N  
ATOM    950  NH2 ARG A 185      26.365  25.940   3.438  1.00 30.73           N  
ATOM    951  N   TYR A 186      28.952  32.152   4.287  1.00 25.34           N  
ATOM    952  CA  TYR A 186      29.986  32.202   3.267  1.00 26.46           C  
ATOM    953  C   TYR A 186      30.833  30.939   3.315  1.00 27.73           C  
ATOM    954  O   TYR A 186      31.346  30.570   4.373  1.00 28.56           O  
ATOM    955  CB  TYR A 186      30.897  33.416   3.445  1.00 26.20           C  
ATOM    956  CG  TYR A 186      31.824  33.599   2.265  1.00 28.72           C  
ATOM    957  CD1 TYR A 186      31.300  33.821   0.985  1.00 29.59           C  
ATOM    958  CD2 TYR A 186      33.211  33.494   2.403  1.00 28.20           C  
ATOM    959  CE1 TYR A 186      32.121  33.926  -0.123  1.00 28.23           C  
ATOM    960  CE2 TYR A 186      34.055  33.601   1.285  1.00 29.39           C  
ATOM    961  CZ  TYR A 186      33.493  33.813   0.026  1.00 31.02           C  
ATOM    962  OH  TYR A 186      34.281  33.864  -1.105  1.00 34.18           O  
ATOM    963  N   GLU A 187      30.976  30.277   2.170  1.00 27.44           N  
ATOM    964  CA  GLU A 187      31.780  29.065   2.084  1.00 28.90           C  
ATOM    965  C   GLU A 187      31.585  28.091   3.240  1.00 30.02           C  
ATOM    966  O   GLU A 187      32.545  27.708   3.908  1.00 29.09           O  
ATOM    967  CB  GLU A 187      33.259  29.430   1.982  1.00 29.71           C  
ATOM    968  CG  GLU A 187      33.647  30.060   0.653  1.00 35.92           C  
ATOM    969  CD  GLU A 187      33.412  29.122  -0.525  1.00 39.98           C  
ATOM    970  OE1 GLU A 187      32.278  29.088  -1.062  1.00 38.49           O  
ATOM    971  OE2 GLU A 187      34.366  28.404  -0.902  1.00 42.89           O  
ATOM    972  N   GLY A 188      30.337  27.703   3.478  1.00 30.97           N  
ATOM    973  CA  GLY A 188      30.045  26.752   4.537  1.00 32.59           C  
ATOM    974  C   GLY A 188      30.070  27.251   5.971  1.00 33.16           C  
ATOM    975  O   GLY A 188      29.784  26.487   6.891  1.00 34.44           O  
ATOM    976  N   ARG A 189      30.408  28.518   6.181  1.00 32.85           N  
ATOM    977  CA  ARG A 189      30.452  29.042   7.536  1.00 31.62           C  
ATOM    978  C   ARG A 189      29.545  30.235   7.727  1.00 30.36           C  
ATOM    979  O   ARG A 189      29.252  30.977   6.784  1.00 28.67           O  
ATOM    980  CB  ARG A 189      31.883  29.422   7.925  1.00 32.08           C  
ATOM    981  CG  ARG A 189      32.844  28.235   8.001  1.00 36.34           C  
ATOM    982  CD  ARG A 189      34.241  28.688   8.415  1.00 38.44           C  
ATOM    983  NE  ARG A 189      34.252  29.232   9.774  1.00 43.31           N  
ATOM    984  CZ  ARG A 189      34.408  28.503  10.878  1.00 44.13           C  
ATOM    985  NH1 ARG A 189      34.580  27.188  10.795  1.00 41.75           N  
ATOM    986  NH2 ARG A 189      34.371  29.089  12.071  1.00 45.66           N  
ATOM    987  N   VAL A 190      29.101  30.403   8.967  1.00 29.07           N  
ATOM    988  CA  VAL A 190      28.241  31.505   9.346  1.00 27.65           C  
ATOM    989  C   VAL A 190      29.076  32.528  10.102  1.00 27.11           C  
ATOM    990  O   VAL A 190      29.847  32.178  10.986  1.00 27.38           O  
ATOM    991  CB  VAL A 190      27.086  31.023  10.241  1.00 28.57           C  
ATOM    992  CG1 VAL A 190      26.221  32.209  10.670  1.00 28.38           C  
ATOM    993  CG2 VAL A 190      26.249  30.001   9.483  1.00 26.44           C  
ATOM    994  N   TYR A 191      28.929  33.790   9.726  1.00 26.74           N  
ATOM    995  CA  TYR A 191      29.659  34.872  10.360  1.00 25.81           C  
ATOM    996  C   TYR A 191      28.642  35.807  11.013  1.00 27.12           C  
ATOM    997  O   TYR A 191      27.544  36.028  10.485  1.00 26.41           O  
ATOM    998  CB  TYR A 191      30.500  35.616   9.318  1.00 25.77           C  
ATOM    999  CG  TYR A 191      31.562  34.749   8.670  1.00 26.45           C  
ATOM   1000  CD1 TYR A 191      31.229  33.818   7.674  1.00 27.29           C  
ATOM   1001  CD2 TYR A 191      32.896  34.827   9.080  1.00 26.83           C  
ATOM   1002  CE1 TYR A 191      32.201  32.984   7.103  1.00 24.19           C  
ATOM   1003  CE2 TYR A 191      33.878  33.998   8.519  1.00 28.64           C  
ATOM   1004  CZ  TYR A 191      33.524  33.082   7.532  1.00 28.24           C  
ATOM   1005  OH  TYR A 191      34.494  32.281   6.977  1.00 29.12           O  
ATOM   1006  N   HIS A 192      29.003  36.346  12.169  1.00 25.24           N  
ATOM   1007  CA  HIS A 192      28.107  37.223  12.909  1.00 26.75           C  
ATOM   1008  C   HIS A 192      28.727  38.601  13.069  1.00 26.83           C  
ATOM   1009  O   HIS A 192      29.915  38.722  13.365  1.00 25.81           O  
ATOM   1010  CB  HIS A 192      27.821  36.600  14.273  1.00 26.18           C  
ATOM   1011  CG  HIS A 192      27.188  35.245  14.190  1.00 27.99           C  
ATOM   1012  ND1 HIS A 192      25.839  35.064  13.958  1.00 27.63           N  
ATOM   1013  CD2 HIS A 192      27.726  34.004  14.268  1.00 26.75           C  
ATOM   1014  CE1 HIS A 192      25.574  33.771  13.899  1.00 25.34           C  
ATOM   1015  NE2 HIS A 192      26.701  33.106  14.084  1.00 26.56           N  
ATOM   1016  N   TYR A 193      27.921  39.638  12.867  1.00 24.83           N  
ATOM   1017  CA  TYR A 193      28.422  40.993  12.968  1.00 26.78           C  
ATOM   1018  C   TYR A 193      27.495  41.875  13.773  1.00 27.74           C  
ATOM   1019  O   TYR A 193      26.295  41.945  13.511  1.00 26.93           O  
ATOM   1020  CB  TYR A 193      28.603  41.602  11.572  1.00 25.31           C  
ATOM   1021  CG  TYR A 193      29.529  40.823  10.664  1.00 25.43           C  
ATOM   1022  CD1 TYR A 193      30.910  41.050  10.666  1.00 24.30           C  
ATOM   1023  CD2 TYR A 193      29.016  39.863   9.785  1.00 23.75           C  
ATOM   1024  CE1 TYR A 193      31.757  40.336   9.800  1.00 23.79           C  
ATOM   1025  CE2 TYR A 193      29.838  39.157   8.928  1.00 23.06           C  
ATOM   1026  CZ  TYR A 193      31.202  39.393   8.932  1.00 25.09           C  
ATOM   1027  OH  TYR A 193      31.991  38.692   8.050  1.00 28.81           O  
ATOM   1028  N   ARG A 194      28.068  42.556  14.751  1.00 30.83           N  
ATOM   1029  CA  ARG A 194      27.313  43.461  15.596  1.00 34.53           C  
ATOM   1030  C   ARG A 194      27.068  44.754  14.824  1.00 33.97           C  
ATOM   1031  O   ARG A 194      27.987  45.313  14.238  1.00 34.63           O  
ATOM   1032  CB  ARG A 194      28.110  43.772  16.866  1.00 38.39           C  
ATOM   1033  CG  ARG A 194      27.392  44.663  17.870  1.00 46.51           C  
ATOM   1034  CD  ARG A 194      26.249  43.916  18.563  1.00 53.78           C  
ATOM   1035  NE  ARG A 194      26.702  42.667  19.179  1.00 59.78           N  
ATOM   1036  CZ  ARG A 194      27.685  42.581  20.074  1.00 62.91           C  
ATOM   1037  NH1 ARG A 194      28.329  43.675  20.468  1.00 64.32           N  
ATOM   1038  NH2 ARG A 194      28.032  41.400  20.576  1.00 63.76           N  
ATOM   1039  N   ILE A 195      25.821  45.210  14.802  1.00 34.30           N  
ATOM   1040  CA  ILE A 195      25.483  46.462  14.137  1.00 34.25           C  
ATOM   1041  C   ILE A 195      25.595  47.533  15.215  1.00 34.80           C  
ATOM   1042  O   ILE A 195      24.860  47.512  16.200  1.00 34.79           O  
ATOM   1043  CB  ILE A 195      24.044  46.446  13.592  1.00 33.20           C  
ATOM   1044  CG1 ILE A 195      23.938  45.429  12.453  1.00 33.72           C  
ATOM   1045  CG2 ILE A 195      23.652  47.839  13.118  1.00 32.25           C  
ATOM   1046  CD1 ILE A 195      22.545  45.263  11.895  1.00 34.00           C  
ATOM   1047  N   ASN A 196      26.524  48.458  15.033  1.00 35.42           N  
ATOM   1048  CA  ASN A 196      26.740  49.514  16.010  1.00 35.57           C  
ATOM   1049  C   ASN A 196      25.887  50.743  15.775  1.00 36.32           C  
ATOM   1050  O   ASN A 196      25.479  51.040  14.645  1.00 35.94           O  
ATOM   1051  CB  ASN A 196      28.206  49.935  16.002  1.00 35.80           C  
ATOM   1052  CG  ASN A 196      29.140  48.772  16.198  1.00 37.92           C  
ATOM   1053  OD1 ASN A 196      29.206  48.194  17.280  1.00 41.62           O  
ATOM   1054  ND2 ASN A 196      29.862  48.407  15.144  1.00 37.67           N  
ATOM   1055  N   THR A 197      25.631  51.467  16.858  1.00 36.77           N  
ATOM   1056  CA  THR A 197      24.857  52.690  16.774  1.00 38.25           C  
ATOM   1057  C   THR A 197      25.736  53.870  17.182  1.00 37.73           C  
ATOM   1058  O   THR A 197      26.325  53.875  18.260  1.00 38.01           O  
ATOM   1059  CB  THR A 197      23.618  52.630  17.688  1.00 38.03           C  
ATOM   1060  OG1 THR A 197      22.807  51.510  17.316  1.00 38.44           O  
ATOM   1061  CG2 THR A 197      22.792  53.905  17.549  1.00 38.73           C  
ATOM   1062  N   ALA A 198      25.832  54.862  16.303  1.00 39.01           N  
ATOM   1063  CA  ALA A 198      26.630  56.054  16.571  1.00 38.82           C  
ATOM   1064  C   ALA A 198      25.960  56.931  17.628  1.00 39.32           C  
ATOM   1065  O   ALA A 198      24.827  56.681  18.042  1.00 38.05           O  
ATOM   1066  CB  ALA A 198      26.820  56.846  15.292  1.00 38.78           C  
ATOM   1067  N   SER A 199      26.666  57.969  18.060  1.00 40.71           N  
ATOM   1068  CA  SER A 199      26.126  58.874  19.066  1.00 39.67           C  
ATOM   1069  C   SER A 199      24.918  59.618  18.508  1.00 39.32           C  
ATOM   1070  O   SER A 199      24.082  60.105  19.264  1.00 38.32           O  
ATOM   1071  CB  SER A 199      27.198  59.868  19.513  1.00 39.99           C  
ATOM   1072  OG  SER A 199      27.634  60.664  18.427  1.00 41.39           O  
ATOM   1073  N   ASP A 200      24.826  59.695  17.182  1.00 38.03           N  
ATOM   1074  CA  ASP A 200      23.704  60.372  16.544  1.00 37.14           C  
ATOM   1075  C   ASP A 200      22.686  59.369  15.996  1.00 36.35           C  
ATOM   1076  O   ASP A 200      21.817  59.723  15.193  1.00 33.99           O  
ATOM   1077  CB  ASP A 200      24.204  61.271  15.413  1.00 39.41           C  
ATOM   1078  CG  ASP A 200      24.758  60.484  14.246  1.00 40.16           C  
ATOM   1079  OD1 ASP A 200      25.043  59.278  14.425  1.00 38.82           O  
ATOM   1080  OD2 ASP A 200      24.915  61.075  13.153  1.00 40.74           O  
ATOM   1081  N   GLY A 201      22.812  58.112  16.414  1.00 35.04           N  
ATOM   1082  CA  GLY A 201      21.876  57.094  15.967  1.00 35.61           C  
ATOM   1083  C   GLY A 201      22.173  56.349  14.677  1.00 35.52           C  
ATOM   1084  O   GLY A 201      21.530  55.344  14.401  1.00 36.15           O  
ATOM   1085  N   LYS A 202      23.128  56.815  13.879  1.00 35.68           N  
ATOM   1086  CA  LYS A 202      23.439  56.129  12.629  1.00 35.93           C  
ATOM   1087  C   LYS A 202      23.913  54.702  12.887  1.00 35.03           C  
ATOM   1088  O   LYS A 202      24.592  54.435  13.874  1.00 35.54           O  
ATOM   1089  CB  LYS A 202      24.504  56.898  11.850  1.00 37.51           C  
ATOM   1090  CG  LYS A 202      24.057  58.277  11.371  1.00 39.86           C  
ATOM   1091  CD  LYS A 202      25.183  58.974  10.625  1.00 43.38           C  
ATOM   1092  CE  LYS A 202      24.760  60.329  10.068  1.00 44.93           C  
ATOM   1093  NZ  LYS A 202      23.642  60.214   9.087  1.00 46.71           N  
ATOM   1094  N   LEU A 203      23.542  53.783  12.001  1.00 35.54           N  
ATOM   1095  CA  LEU A 203      23.931  52.378  12.136  1.00 33.45           C  
ATOM   1096  C   LEU A 203      25.117  52.056  11.231  1.00 32.40           C  
ATOM   1097  O   LEU A 203      25.265  52.643  10.164  1.00 32.49           O  
ATOM   1098  CB  LEU A 203      22.766  51.453  11.759  1.00 33.26           C  
ATOM   1099  CG  LEU A 203      21.470  51.359  12.569  1.00 35.49           C  
ATOM   1100  CD1 LEU A 203      21.746  51.634  14.040  1.00 37.21           C  
ATOM   1101  CD2 LEU A 203      20.462  52.332  12.024  1.00 37.00           C  
ATOM   1102  N   TYR A 204      25.958  51.119  11.649  1.00 31.64           N  
ATOM   1103  CA  TYR A 204      27.102  50.750  10.828  1.00 31.40           C  
ATOM   1104  C   TYR A 204      27.797  49.485  11.300  1.00 31.84           C  
ATOM   1105  O   TYR A 204      27.685  49.088  12.462  1.00 29.04           O  
ATOM   1106  CB  TYR A 204      28.139  51.878  10.808  1.00 31.98           C  
ATOM   1107  CG  TYR A 204      28.782  52.151  12.159  1.00 33.89           C  
ATOM   1108  CD1 TYR A 204      28.183  53.014  13.084  1.00 32.97           C  
ATOM   1109  CD2 TYR A 204      29.981  51.530  12.520  1.00 35.99           C  
ATOM   1110  CE1 TYR A 204      28.759  53.249  14.331  1.00 35.11           C  
ATOM   1111  CE2 TYR A 204      30.573  51.756  13.770  1.00 36.19           C  
ATOM   1112  CZ  TYR A 204      29.953  52.616  14.669  1.00 38.78           C  
ATOM   1113  OH  TYR A 204      30.514  52.824  15.907  1.00 37.72           O  
ATOM   1114  N   VAL A 205      28.507  48.850  10.373  1.00 33.34           N  
ATOM   1115  CA  VAL A 205      29.299  47.666  10.682  1.00 36.49           C  
ATOM   1116  C   VAL A 205      30.716  48.221  10.653  1.00 38.23           C  
ATOM   1117  O   VAL A 205      31.486  48.078  11.603  1.00 36.62           O  
ATOM   1118  CB  VAL A 205      29.156  46.579   9.605  1.00 35.99           C  
ATOM   1119  CG1 VAL A 205      30.164  45.459   9.854  1.00 37.07           C  
ATOM   1120  CG2 VAL A 205      27.738  46.031   9.632  1.00 37.47           C  
ATOM   1121  N   SER A 206      31.033  48.865   9.535  1.00 40.99           N  
ATOM   1122  CA  SER A 206      32.323  49.502   9.334  1.00 44.19           C  
ATOM   1123  C   SER A 206      32.171  50.956   9.737  1.00 45.95           C  
ATOM   1124  O   SER A 206      31.295  51.656   9.233  1.00 46.70           O  
ATOM   1125  CB  SER A 206      32.726  49.421   7.869  1.00 46.59           C  
ATOM   1126  OG  SER A 206      32.929  48.069   7.492  1.00 52.32           O  
ATOM   1127  N   SER A 207      32.999  51.389  10.676  1.00 46.86           N  
ATOM   1128  CA  SER A 207      32.966  52.750  11.182  1.00 46.93           C  
ATOM   1129  C   SER A 207      32.928  53.838  10.115  1.00 47.61           C  
ATOM   1130  O   SER A 207      32.415  54.926  10.367  1.00 47.53           O  
ATOM   1131  CB  SER A 207      34.181  52.983  12.085  1.00 48.46           C  
ATOM   1132  OG  SER A 207      34.215  54.315  12.560  1.00 49.60           O  
ATOM   1133  N   GLU A 208      33.461  53.551   8.932  1.00 47.22           N  
ATOM   1134  CA  GLU A 208      33.503  54.546   7.867  1.00 48.80           C  
ATOM   1135  C   GLU A 208      32.269  54.581   6.976  1.00 47.57           C  
ATOM   1136  O   GLU A 208      32.207  55.369   6.036  1.00 47.10           O  
ATOM   1137  CB  GLU A 208      34.739  54.324   6.985  1.00 52.63           C  
ATOM   1138  CG  GLU A 208      36.024  54.047   7.748  1.00 58.54           C  
ATOM   1139  CD  GLU A 208      36.073  52.634   8.316  1.00 62.71           C  
ATOM   1140  OE1 GLU A 208      35.968  51.675   7.520  1.00 64.94           O  
ATOM   1141  OE2 GLU A 208      36.220  52.481   9.551  1.00 63.71           O  
ATOM   1142  N   SER A 209      31.291  53.731   7.259  1.00 46.48           N  
ATOM   1143  CA  SER A 209      30.082  53.689   6.442  1.00 45.19           C  
ATOM   1144  C   SER A 209      28.853  53.625   7.339  1.00 43.33           C  
ATOM   1145  O   SER A 209      28.415  52.540   7.712  1.00 43.61           O  
ATOM   1146  CB  SER A 209      30.111  52.459   5.530  1.00 47.74           C  
ATOM   1147  OG  SER A 209      31.368  52.327   4.885  1.00 48.54           O  
ATOM   1148  N   ARG A 210      28.297  54.786   7.671  1.00 39.91           N  
ATOM   1149  CA  ARG A 210      27.130  54.856   8.540  1.00 37.59           C  
ATOM   1150  C   ARG A 210      25.877  55.302   7.786  1.00 35.04           C  
ATOM   1151  O   ARG A 210      25.943  56.111   6.858  1.00 33.22           O  
ATOM   1152  CB  ARG A 210      27.430  55.798   9.710  1.00 38.17           C  
ATOM   1153  CG  ARG A 210      28.777  55.498  10.353  1.00 39.10           C  
ATOM   1154  CD  ARG A 210      29.057  56.349  11.573  1.00 38.44           C  
ATOM   1155  NE  ARG A 210      30.371  56.036  12.124  1.00 41.59           N  
ATOM   1156  CZ  ARG A 210      30.806  56.432  13.317  1.00 42.64           C  
ATOM   1157  NH1 ARG A 210      30.027  57.166  14.109  1.00 41.99           N  
ATOM   1158  NH2 ARG A 210      32.029  56.099  13.716  1.00 40.33           N  
ATOM   1159  N   PHE A 211      24.734  54.771   8.197  1.00 32.58           N  
ATOM   1160  CA  PHE A 211      23.475  55.080   7.544  1.00 32.78           C  
ATOM   1161  C   PHE A 211      22.384  55.361   8.562  1.00 32.92           C  
ATOM   1162  O   PHE A 211      22.464  54.907   9.704  1.00 33.65           O  
ATOM   1163  CB  PHE A 211      23.103  53.904   6.641  1.00 32.34           C  
ATOM   1164  CG  PHE A 211      24.153  53.599   5.625  1.00 31.03           C  
ATOM   1165  CD1 PHE A 211      24.196  54.301   4.428  1.00 32.43           C  
ATOM   1166  CD2 PHE A 211      25.168  52.690   5.907  1.00 31.57           C  
ATOM   1167  CE1 PHE A 211      25.238  54.109   3.528  1.00 32.55           C  
ATOM   1168  CE2 PHE A 211      26.212  52.493   5.015  1.00 32.32           C  
ATOM   1169  CZ  PHE A 211      26.248  53.207   3.822  1.00 31.96           C  
ATOM   1170  N   ASN A 212      21.369  56.114   8.150  1.00 33.22           N  
ATOM   1171  CA  ASN A 212      20.280  56.468   9.052  1.00 34.21           C  
ATOM   1172  C   ASN A 212      19.352  55.303   9.348  1.00 34.19           C  
ATOM   1173  O   ASN A 212      18.813  55.199  10.451  1.00 36.68           O  
ATOM   1174  CB  ASN A 212      19.435  57.614   8.476  1.00 36.00           C  
ATOM   1175  CG  ASN A 212      20.250  58.856   8.168  1.00 36.08           C  
ATOM   1176  OD1 ASN A 212      21.229  59.156   8.848  1.00 38.00           O  
ATOM   1177  ND2 ASN A 212      19.831  59.599   7.147  1.00 35.17           N  
ATOM   1178  N   THR A 213      19.155  54.435   8.360  1.00 32.78           N  
ATOM   1179  CA  THR A 213      18.255  53.305   8.521  1.00 31.35           C  
ATOM   1180  C   THR A 213      18.919  51.962   8.299  1.00 32.00           C  
ATOM   1181  O   THR A 213      19.962  51.859   7.658  1.00 31.57           O  
ATOM   1182  CB  THR A 213      17.079  53.397   7.547  1.00 33.11           C  
ATOM   1183  OG1 THR A 213      17.565  53.264   6.205  1.00 33.72           O  
ATOM   1184  CG2 THR A 213      16.359  54.745   7.697  1.00 32.85           C  
ATOM   1185  N   LEU A 214      18.287  50.927   8.831  1.00 29.83           N  
ATOM   1186  CA  LEU A 214      18.789  49.578   8.703  1.00 29.88           C  
ATOM   1187  C   LEU A 214      18.731  49.125   7.236  1.00 28.58           C  
ATOM   1188  O   LEU A 214      19.639  48.457   6.739  1.00 25.96           O  
ATOM   1189  CB  LEU A 214      17.943  48.651   9.566  1.00 31.60           C  
ATOM   1190  CG  LEU A 214      18.651  47.519  10.293  1.00 34.56           C  
ATOM   1191  CD1 LEU A 214      17.599  46.495  10.718  1.00 35.99           C  
ATOM   1192  CD2 LEU A 214      19.686  46.879   9.390  1.00 34.30           C  
ATOM   1193  N   ALA A 215      17.659  49.500   6.549  1.00 27.28           N  
ATOM   1194  CA  ALA A 215      17.484  49.127   5.151  1.00 27.68           C  
ATOM   1195  C   ALA A 215      18.593  49.715   4.277  1.00 27.77           C  
ATOM   1196  O   ALA A 215      19.036  49.093   3.309  1.00 27.39           O  
ATOM   1197  CB  ALA A 215      16.102  49.593   4.656  1.00 23.07           C  
ATOM   1198  N   GLU A 216      19.036  50.917   4.618  1.00 28.87           N  
ATOM   1199  CA  GLU A 216      20.096  51.571   3.862  1.00 31.01           C  
ATOM   1200  C   GLU A 216      21.419  50.880   4.126  1.00 30.10           C  
ATOM   1201  O   GLU A 216      22.263  50.776   3.228  1.00 31.35           O  
ATOM   1202  CB  GLU A 216      20.207  53.042   4.255  1.00 33.19           C  
ATOM   1203  CG  GLU A 216      19.158  53.924   3.642  1.00 35.31           C  
ATOM   1204  CD  GLU A 216      19.243  55.330   4.170  1.00 39.77           C  
ATOM   1205  OE1 GLU A 216      18.901  55.539   5.354  1.00 42.04           O  
ATOM   1206  OE2 GLU A 216      19.667  56.222   3.405  1.00 43.54           O  
ATOM   1207  N   LEU A 217      21.595  50.422   5.365  1.00 26.73           N  
ATOM   1208  CA  LEU A 217      22.801  49.713   5.763  1.00 25.60           C  
ATOM   1209  C   LEU A 217      22.831  48.391   4.990  1.00 25.59           C  
ATOM   1210  O   LEU A 217      23.864  47.999   4.448  1.00 26.09           O  
ATOM   1211  CB  LEU A 217      22.782  49.441   7.273  1.00 25.51           C  
ATOM   1212  CG  LEU A 217      23.948  48.642   7.875  1.00 25.80           C  
ATOM   1213  CD1 LEU A 217      25.233  49.442   7.763  1.00 28.01           C  
ATOM   1214  CD2 LEU A 217      23.663  48.338   9.326  1.00 26.56           C  
ATOM   1215  N   VAL A 218      21.690  47.711   4.939  1.00 26.14           N  
ATOM   1216  CA  VAL A 218      21.580  46.444   4.220  1.00 28.15           C  
ATOM   1217  C   VAL A 218      21.844  46.656   2.724  1.00 29.97           C  
ATOM   1218  O   VAL A 218      22.572  45.883   2.094  1.00 29.42           O  
ATOM   1219  CB  VAL A 218      20.181  45.814   4.424  1.00 27.63           C  
ATOM   1220  CG1 VAL A 218      19.918  44.727   3.377  1.00 27.72           C  
ATOM   1221  CG2 VAL A 218      20.089  45.222   5.829  1.00 26.83           C  
ATOM   1222  N   HIS A 219      21.253  47.703   2.160  1.00 31.71           N  
ATOM   1223  CA  HIS A 219      21.462  48.007   0.749  1.00 33.68           C  
ATOM   1224  C   HIS A 219      22.946  48.218   0.463  1.00 33.25           C  
ATOM   1225  O   HIS A 219      23.497  47.633  -0.468  1.00 33.41           O  
ATOM   1226  CB  HIS A 219      20.686  49.258   0.345  1.00 35.39           C  
ATOM   1227  CG  HIS A 219      20.974  49.707  -1.052  1.00 41.53           C  
ATOM   1228  ND1 HIS A 219      21.998  50.579  -1.357  1.00 43.46           N  
ATOM   1229  CD2 HIS A 219      20.433  49.332  -2.236  1.00 41.90           C  
ATOM   1230  CE1 HIS A 219      22.078  50.719  -2.668  1.00 44.56           C  
ATOM   1231  NE2 HIS A 219      21.141  49.972  -3.225  1.00 44.25           N  
ATOM   1232  N   HIS A 220      23.596  49.048   1.272  1.00 32.93           N  
ATOM   1233  CA  HIS A 220      25.018  49.317   1.083  1.00 32.97           C  
ATOM   1234  C   HIS A 220      25.843  48.035   0.992  1.00 32.75           C  
ATOM   1235  O   HIS A 220      26.612  47.851   0.046  1.00 32.88           O  
ATOM   1236  CB  HIS A 220      25.555  50.184   2.229  1.00 33.82           C  
ATOM   1237  CG  HIS A 220      27.048  50.335   2.225  1.00 35.88           C  
ATOM   1238  ND1 HIS A 220      27.733  50.932   1.189  1.00 36.01           N  
ATOM   1239  CD2 HIS A 220      27.986  49.956   3.126  1.00 36.10           C  
ATOM   1240  CE1 HIS A 220      29.028  50.915   1.452  1.00 34.08           C  
ATOM   1241  NE2 HIS A 220      29.209  50.328   2.620  1.00 33.87           N  
ATOM   1242  N   HIS A 221      25.676  47.152   1.976  1.00 31.39           N  
ATOM   1243  CA  HIS A 221      26.424  45.898   2.017  1.00 29.21           C  
ATOM   1244  C   HIS A 221      25.974  44.838   1.020  1.00 29.17           C  
ATOM   1245  O   HIS A 221      26.521  43.741   0.981  1.00 29.24           O  
ATOM   1246  CB  HIS A 221      26.424  45.344   3.440  1.00 26.63           C  
ATOM   1247  CG  HIS A 221      27.254  46.154   4.384  1.00 26.67           C  
ATOM   1248  ND1 HIS A 221      28.633  46.115   4.379  1.00 26.18           N  
ATOM   1249  CD2 HIS A 221      26.906  47.085   5.303  1.00 26.17           C  
ATOM   1250  CE1 HIS A 221      29.096  46.990   5.254  1.00 25.73           C  
ATOM   1251  NE2 HIS A 221      28.070  47.592   5.828  1.00 24.33           N  
ATOM   1252  N   SER A 222      24.969  45.155   0.217  1.00 29.96           N  
ATOM   1253  CA  SER A 222      24.550  44.216  -0.803  1.00 30.02           C  
ATOM   1254  C   SER A 222      25.313  44.632  -2.061  1.00 31.69           C  
ATOM   1255  O   SER A 222      25.409  43.868  -3.015  1.00 32.41           O  
ATOM   1256  CB  SER A 222      23.037  44.283  -1.041  1.00 29.96           C  
ATOM   1257  OG  SER A 222      22.627  45.572  -1.450  1.00 32.99           O  
ATOM   1258  N   THR A 223      25.868  45.844  -2.051  1.00 31.46           N  
ATOM   1259  CA  THR A 223      26.626  46.331  -3.202  1.00 33.29           C  
ATOM   1260  C   THR A 223      28.128  46.106  -3.014  1.00 34.39           C  
ATOM   1261  O   THR A 223      28.832  45.799  -3.972  1.00 37.33           O  
ATOM   1262  CB  THR A 223      26.357  47.843  -3.478  1.00 33.53           C  
ATOM   1263  OG1 THR A 223      26.986  48.646  -2.473  1.00 33.25           O  
ATOM   1264  CG2 THR A 223      24.857  48.126  -3.474  1.00 32.51           C  
ATOM   1265  N   VAL A 224      28.609  46.256  -1.780  1.00 35.02           N  
ATOM   1266  CA  VAL A 224      30.020  46.049  -1.450  1.00 33.79           C  
ATOM   1267  C   VAL A 224      30.155  45.431  -0.063  1.00 33.73           C  
ATOM   1268  O   VAL A 224      29.449  45.819   0.866  1.00 33.35           O  
ATOM   1269  CB  VAL A 224      30.825  47.374  -1.460  1.00 35.52           C  
ATOM   1270  CG1 VAL A 224      30.912  47.921  -2.866  1.00 35.97           C  
ATOM   1271  CG2 VAL A 224      30.170  48.395  -0.534  1.00 35.21           C  
ATOM   1272  N   ALA A 225      31.070  44.475   0.074  1.00 33.77           N  
ATOM   1273  CA  ALA A 225      31.293  43.798   1.347  1.00 34.42           C  
ATOM   1274  C   ALA A 225      31.661  44.809   2.432  1.00 35.10           C  
ATOM   1275  O   ALA A 225      31.045  44.841   3.507  1.00 34.29           O  
ATOM   1276  CB  ALA A 225      32.395  42.751   1.195  1.00 30.87           C  
ATOM   1277  N   ASP A 226      32.677  45.615   2.141  1.00 34.99           N  
ATOM   1278  CA  ASP A 226      33.142  46.672   3.040  1.00 34.92           C  
ATOM   1279  C   ASP A 226      33.141  46.317   4.524  1.00 32.46           C  
ATOM   1280  O   ASP A 226      32.472  46.970   5.320  1.00 32.15           O  
ATOM   1281  CB  ASP A 226      32.295  47.934   2.802  1.00 37.19           C  
ATOM   1282  CG  ASP A 226      32.736  49.118   3.654  1.00 40.68           C  
ATOM   1283  OD1 ASP A 226      33.953  49.262   3.922  1.00 42.26           O  
ATOM   1284  OD2 ASP A 226      31.857  49.919   4.038  1.00 41.35           O  
ATOM   1285  N   GLY A 227      33.898  45.295   4.899  1.00 31.74           N  
ATOM   1286  CA  GLY A 227      33.949  44.897   6.298  1.00 31.41           C  
ATOM   1287  C   GLY A 227      33.421  43.494   6.553  1.00 30.22           C  
ATOM   1288  O   GLY A 227      33.932  42.770   7.414  1.00 32.06           O  
ATOM   1289  N   LEU A 228      32.387  43.111   5.817  1.00 27.26           N  
ATOM   1290  CA  LEU A 228      31.820  41.781   5.960  1.00 27.12           C  
ATOM   1291  C   LEU A 228      32.687  40.823   5.149  1.00 26.75           C  
ATOM   1292  O   LEU A 228      33.480  41.261   4.303  1.00 23.73           O  
ATOM   1293  CB  LEU A 228      30.390  41.754   5.432  1.00 27.85           C  
ATOM   1294  CG  LEU A 228      29.406  42.746   6.047  1.00 27.90           C  
ATOM   1295  CD1 LEU A 228      28.034  42.574   5.382  1.00 22.62           C  
ATOM   1296  CD2 LEU A 228      29.320  42.511   7.562  1.00 27.79           C  
ATOM   1297  N   ILE A 229      32.539  39.524   5.403  1.00 24.15           N  
ATOM   1298  CA  ILE A 229      33.331  38.530   4.695  1.00 24.33           C  
ATOM   1299  C   ILE A 229      32.928  38.495   3.232  1.00 25.07           C  
ATOM   1300  O   ILE A 229      33.720  38.134   2.366  1.00 25.15           O  
ATOM   1301  CB  ILE A 229      33.153  37.124   5.297  1.00 25.11           C  
ATOM   1302  CG1 ILE A 229      34.150  36.160   4.653  1.00 24.76           C  
ATOM   1303  CG2 ILE A 229      31.733  36.625   5.080  1.00 24.20           C  
ATOM   1304  CD1 ILE A 229      35.580  36.383   5.082  1.00 27.20           C  
ATOM   1305  N   THR A 230      31.693  38.887   2.960  1.00 23.58           N  
ATOM   1306  CA  THR A 230      31.192  38.907   1.598  1.00 24.57           C  
ATOM   1307  C   THR A 230      29.960  39.802   1.549  1.00 24.01           C  
ATOM   1308  O   THR A 230      29.584  40.401   2.553  1.00 24.87           O  
ATOM   1309  CB  THR A 230      30.819  37.484   1.129  1.00 27.19           C  
ATOM   1310  OG1 THR A 230      30.434  37.524  -0.249  1.00 28.25           O  
ATOM   1311  CG2 THR A 230      29.651  36.931   1.966  1.00 23.53           C  
ATOM   1312  N   THR A 231      29.324  39.887   0.389  1.00 23.42           N  
ATOM   1313  CA  THR A 231      28.149  40.738   0.248  1.00 25.42           C  
ATOM   1314  C   THR A 231      26.851  40.077   0.681  1.00 24.94           C  
ATOM   1315  O   THR A 231      26.779  38.863   0.831  1.00 26.89           O  
ATOM   1316  CB  THR A 231      27.969  41.203  -1.207  1.00 25.92           C  
ATOM   1317  OG1 THR A 231      27.833  40.059  -2.062  1.00 25.92           O  
ATOM   1318  CG2 THR A 231      29.158  42.042  -1.640  1.00 24.57           C  
ATOM   1319  N   LEU A 232      25.827  40.901   0.876  1.00 24.87           N  
ATOM   1320  CA  LEU A 232      24.506  40.435   1.267  1.00 24.15           C  
ATOM   1321  C   LEU A 232      23.742  40.202  -0.032  1.00 26.45           C  
ATOM   1322  O   LEU A 232      23.396  41.146  -0.757  1.00 25.17           O  
ATOM   1323  CB  LEU A 232      23.825  41.497   2.126  1.00 22.82           C  
ATOM   1324  CG  LEU A 232      24.707  41.902   3.314  1.00 23.12           C  
ATOM   1325  CD1 LEU A 232      23.994  42.936   4.177  1.00 23.04           C  
ATOM   1326  CD2 LEU A 232      25.044  40.655   4.140  1.00 20.80           C  
ATOM   1327  N   HIS A 233      23.484  38.934  -0.322  1.00 27.71           N  
ATOM   1328  CA  HIS A 233      22.817  38.557  -1.558  1.00 28.49           C  
ATOM   1329  C   HIS A 233      21.393  38.048  -1.470  1.00 28.10           C  
ATOM   1330  O   HIS A 233      20.548  38.436  -2.270  1.00 28.07           O  
ATOM   1331  CB  HIS A 233      23.637  37.491  -2.280  1.00 28.61           C  
ATOM   1332  CG  HIS A 233      22.959  36.952  -3.499  1.00 34.73           C  
ATOM   1333  ND1 HIS A 233      22.638  37.745  -4.580  1.00 34.05           N  
ATOM   1334  CD2 HIS A 233      22.504  35.711  -3.792  1.00 35.39           C  
ATOM   1335  CE1 HIS A 233      22.012  37.015  -5.486  1.00 37.01           C  
ATOM   1336  NE2 HIS A 233      21.917  35.777  -5.032  1.00 36.69           N  
ATOM   1337  N   TYR A 234      21.126  37.170  -0.511  1.00 27.50           N  
ATOM   1338  CA  TYR A 234      19.803  36.580  -0.411  1.00 29.30           C  
ATOM   1339  C   TYR A 234      19.252  36.445   1.002  1.00 27.36           C  
ATOM   1340  O   TYR A 234      19.822  35.762   1.848  1.00 26.82           O  
ATOM   1341  CB  TYR A 234      19.848  35.211  -1.095  1.00 32.23           C  
ATOM   1342  CG  TYR A 234      18.595  34.377  -0.996  1.00 36.55           C  
ATOM   1343  CD1 TYR A 234      17.418  34.754  -1.650  1.00 39.29           C  
ATOM   1344  CD2 TYR A 234      18.604  33.171  -0.296  1.00 38.54           C  
ATOM   1345  CE1 TYR A 234      16.281  33.935  -1.612  1.00 41.42           C  
ATOM   1346  CE2 TYR A 234      17.480  32.351  -0.251  1.00 39.95           C  
ATOM   1347  CZ  TYR A 234      16.328  32.734  -0.909  1.00 41.50           C  
ATOM   1348  OH  TYR A 234      15.229  31.907  -0.864  1.00 45.00           O  
ATOM   1349  N   PRO A 235      18.121  37.101   1.274  1.00 29.10           N  
ATOM   1350  CA  PRO A 235      17.543  37.000   2.620  1.00 28.80           C  
ATOM   1351  C   PRO A 235      17.201  35.537   2.880  1.00 28.48           C  
ATOM   1352  O   PRO A 235      16.536  34.904   2.065  1.00 29.66           O  
ATOM   1353  CB  PRO A 235      16.295  37.871   2.526  1.00 28.56           C  
ATOM   1354  CG  PRO A 235      16.680  38.904   1.472  1.00 28.10           C  
ATOM   1355  CD  PRO A 235      17.368  38.051   0.434  1.00 27.13           C  
ATOM   1356  N   ALA A 236      17.672  34.992   3.993  1.00 27.65           N  
ATOM   1357  CA  ALA A 236      17.394  33.598   4.317  1.00 28.49           C  
ATOM   1358  C   ALA A 236      15.915  33.387   4.588  1.00 27.90           C  
ATOM   1359  O   ALA A 236      15.260  34.208   5.225  1.00 27.48           O  
ATOM   1360  CB  ALA A 236      18.210  33.167   5.521  1.00 29.41           C  
ATOM   1361  N   PRO A 237      15.367  32.273   4.103  1.00 29.63           N  
ATOM   1362  CA  PRO A 237      13.949  31.965   4.302  1.00 33.49           C  
ATOM   1363  C   PRO A 237      13.580  31.956   5.781  1.00 37.65           C  
ATOM   1364  O   PRO A 237      14.383  31.552   6.629  1.00 38.10           O  
ATOM   1365  CB  PRO A 237      13.806  30.574   3.681  1.00 30.99           C  
ATOM   1366  CG  PRO A 237      14.881  30.541   2.661  1.00 31.03           C  
ATOM   1367  CD  PRO A 237      16.038  31.188   3.372  1.00 29.50           C  
ATOM   1368  N   LYS A 238      12.365  32.398   6.085  1.00 41.94           N  
ATOM   1369  CA  LYS A 238      11.881  32.405   7.462  1.00 46.56           C  
ATOM   1370  C   LYS A 238      11.639  30.952   7.882  1.00 50.01           C  
ATOM   1371  O   LYS A 238      11.224  30.127   7.065  1.00 48.33           O  
ATOM   1372  CB  LYS A 238      10.576  33.200   7.553  1.00 45.78           C  
ATOM   1373  CG  LYS A 238      10.708  34.664   7.141  1.00 45.84           C  
ATOM   1374  CD  LYS A 238      11.560  35.442   8.125  1.00 44.61           C  
ATOM   1375  CE  LYS A 238      11.758  36.885   7.687  1.00 46.44           C  
ATOM   1376  NZ  LYS A 238      10.489  37.648   7.586  1.00 47.43           N  
ATOM   1377  N   ARG A 239      11.903  30.637   9.148  1.00 55.02           N  
ATOM   1378  CA  ARG A 239      11.709  29.276   9.641  1.00 61.31           C  
ATOM   1379  C   ARG A 239      10.358  28.714   9.219  1.00 63.07           C  
ATOM   1380  O   ARG A 239      10.282  27.816   8.373  1.00 65.36           O  
ATOM   1381  CB  ARG A 239      11.836  29.231  11.170  1.00 64.94           C  
ATOM   1382  CG  ARG A 239      11.058  30.302  11.921  1.00 69.00           C  
ATOM   1383  CD  ARG A 239      11.401  30.261  13.402  1.00 72.68           C  
ATOM   1384  NE  ARG A 239      10.895  31.430  14.117  1.00 77.10           N  
ATOM   1385  CZ  ARG A 239      11.125  31.683  15.404  1.00 78.75           C  
ATOM   1386  NH1 ARG A 239      11.856  30.848  16.136  1.00 79.35           N  
ATOM   1387  NH2 ARG A 239      10.629  32.781  15.960  1.00 78.98           N  
ATOM   1388  N   ASN A 240       9.294  29.253   9.804  1.00 63.27           N  
ATOM   1389  CA  ASN A 240       7.942  28.813   9.491  1.00 62.31           C  
ATOM   1390  C   ASN A 240       6.917  29.707  10.184  1.00 60.50           C  
ATOM   1391  O   ASN A 240       7.248  30.458  11.105  1.00 60.36           O  
ATOM   1392  CB  ASN A 240       7.747  27.356   9.930  1.00 64.70           C  
ATOM   1393  CG  ASN A 240       6.332  26.851   9.678  1.00 68.36           C  
ATOM   1394  OD1 ASN A 240       5.863  26.819   8.536  1.00 69.81           O  
ATOM   1395  ND2 ASN A 240       5.644  26.456  10.748  1.00 69.15           N  
ATOM   1396  N   LYS A 241       5.672  29.623   9.728  1.00 57.74           N  
ATOM   1397  CA  LYS A 241       4.590  30.412  10.293  1.00 54.72           C  
ATOM   1398  C   LYS A 241       4.529  30.184  11.799  1.00 52.52           C  
ATOM   1399  O   LYS A 241       4.709  29.061  12.271  1.00 51.54           O  
ATOM   1400  CB  LYS A 241       3.260  29.981   9.679  1.00 54.46           C  
ATOM   1401  CG  LYS A 241       3.301  29.776   8.183  1.00 57.43           C  
ATOM   1402  CD  LYS A 241       2.022  29.129   7.694  1.00 59.40           C  
ATOM   1403  CE  LYS A 241       2.015  28.988   6.185  1.00 60.99           C  
ATOM   1404  NZ  LYS A 241       0.745  28.368   5.713  1.00 63.43           N  
ATOM   1405  N   PRO A 242       4.300  31.254  12.578  1.00 50.72           N  
ATOM   1406  CA  PRO A 242       4.218  31.093  14.034  1.00 47.57           C  
ATOM   1407  C   PRO A 242       3.021  30.197  14.324  1.00 44.42           C  
ATOM   1408  O   PRO A 242       2.145  30.043  13.477  1.00 42.28           O  
ATOM   1409  CB  PRO A 242       3.998  32.518  14.527  1.00 48.09           C  
ATOM   1410  CG  PRO A 242       4.711  33.342  13.493  1.00 48.80           C  
ATOM   1411  CD  PRO A 242       4.300  32.679  12.201  1.00 49.43           C  
ATOM   1412  N   THR A 243       2.982  29.601  15.509  1.00 44.26           N  
ATOM   1413  CA  THR A 243       1.873  28.718  15.863  1.00 42.37           C  
ATOM   1414  C   THR A 243       0.605  29.476  16.208  1.00 38.97           C  
ATOM   1415  O   THR A 243       0.636  30.478  16.927  1.00 38.66           O  
ATOM   1416  CB  THR A 243       2.218  27.812  17.076  1.00 44.75           C  
ATOM   1417  OG1 THR A 243       3.237  26.875  16.707  1.00 47.90           O  
ATOM   1418  CG2 THR A 243       0.979  27.037  17.540  1.00 45.78           C  
ATOM   1419  N   VAL A 244      -0.514  28.998  15.680  1.00 36.06           N  
ATOM   1420  CA  VAL A 244      -1.801  29.602  15.978  1.00 33.96           C  
ATOM   1421  C   VAL A 244      -2.389  28.700  17.048  1.00 33.02           C  
ATOM   1422  O   VAL A 244      -2.548  27.499  16.830  1.00 32.36           O  
ATOM   1423  CB  VAL A 244      -2.738  29.602  14.759  1.00 35.91           C  
ATOM   1424  CG1 VAL A 244      -3.995  30.378  15.094  1.00 34.85           C  
ATOM   1425  CG2 VAL A 244      -2.031  30.206  13.546  1.00 35.24           C  
ATOM   1426  N   TYR A 245      -2.692  29.273  18.207  1.00 30.24           N  
ATOM   1427  CA  TYR A 245      -3.240  28.504  19.318  1.00 29.29           C  
ATOM   1428  C   TYR A 245      -4.748  28.267  19.186  1.00 29.51           C  
ATOM   1429  O   TYR A 245      -5.553  28.857  19.911  1.00 30.08           O  
ATOM   1430  CB  TYR A 245      -2.930  29.226  20.627  1.00 26.95           C  
ATOM   1431  CG  TYR A 245      -1.455  29.490  20.816  1.00 25.35           C  
ATOM   1432  CD1 TYR A 245      -0.972  30.788  20.961  1.00 24.15           C  
ATOM   1433  CD2 TYR A 245      -0.543  28.439  20.861  1.00 25.84           C  
ATOM   1434  CE1 TYR A 245       0.381  31.033  21.144  1.00 25.70           C  
ATOM   1435  CE2 TYR A 245       0.816  28.668  21.047  1.00 26.90           C  
ATOM   1436  CZ  TYR A 245       1.274  29.967  21.186  1.00 28.42           C  
ATOM   1437  OH  TYR A 245       2.623  30.198  21.343  1.00 29.14           O  
ATOM   1438  N   GLY A 246      -5.123  27.381  18.273  1.00 28.82           N  
ATOM   1439  CA  GLY A 246      -6.528  27.102  18.053  1.00 29.30           C  
ATOM   1440  C   GLY A 246      -6.840  27.358  16.591  1.00 30.48           C  
ATOM   1441  O   GLY A 246      -5.921  27.537  15.793  1.00 30.32           O  
ATOM   1442  N   VAL A 247      -8.119  27.383  16.228  1.00 28.69           N  
ATOM   1443  CA  VAL A 247      -8.494  27.617  14.841  1.00 27.34           C  
ATOM   1444  C   VAL A 247      -9.538  28.719  14.700  1.00 27.91           C  
ATOM   1445  O   VAL A 247      -9.955  29.054  13.585  1.00 24.95           O  
ATOM   1446  CB  VAL A 247      -9.044  26.329  14.191  1.00 27.42           C  
ATOM   1447  CG1 VAL A 247      -7.991  25.237  14.216  1.00 26.14           C  
ATOM   1448  CG2 VAL A 247     -10.287  25.872  14.928  1.00 28.45           C  
ATOM   1449  N   SER A 248      -9.944  29.287  15.834  1.00 27.52           N  
ATOM   1450  CA  SER A 248     -10.954  30.336  15.854  1.00 27.84           C  
ATOM   1451  C   SER A 248     -10.581  31.546  16.701  1.00 27.39           C  
ATOM   1452  O   SER A 248      -9.979  31.412  17.760  1.00 25.23           O  
ATOM   1453  CB  SER A 248     -12.282  29.767  16.372  1.00 28.56           C  
ATOM   1454  OG  SER A 248     -13.250  30.792  16.534  1.00 30.12           O  
ATOM   1455  N   PRO A 249     -10.954  32.749  16.245  1.00 27.40           N  
ATOM   1456  CA  PRO A 249     -10.657  33.978  16.982  1.00 27.79           C  
ATOM   1457  C   PRO A 249     -11.674  34.167  18.108  1.00 28.98           C  
ATOM   1458  O   PRO A 249     -11.502  35.028  18.966  1.00 29.93           O  
ATOM   1459  CB  PRO A 249     -10.794  35.055  15.913  1.00 26.47           C  
ATOM   1460  CG  PRO A 249     -11.928  34.536  15.098  1.00 26.83           C  
ATOM   1461  CD  PRO A 249     -11.590  33.062  14.952  1.00 28.20           C  
ATOM   1462  N   ASN A 250     -12.722  33.347  18.110  1.00 29.91           N  
ATOM   1463  CA  ASN A 250     -13.766  33.468  19.122  1.00 33.42           C  
ATOM   1464  C   ASN A 250     -13.482  32.814  20.479  1.00 34.40           C  
ATOM   1465  O   ASN A 250     -12.579  31.983  20.624  1.00 32.86           O  
ATOM   1466  CB  ASN A 250     -15.101  32.981  18.546  1.00 33.97           C  
ATOM   1467  CG  ASN A 250     -15.496  33.749  17.284  1.00 35.24           C  
ATOM   1468  OD1 ASN A 250     -15.431  33.219  16.174  1.00 38.58           O  
ATOM   1469  ND2 ASN A 250     -15.883  35.006  17.452  1.00 33.82           N  
ATOM   1470  N   TYR A 251     -14.267  33.217  21.472  1.00 34.29           N  
ATOM   1471  CA  TYR A 251     -14.111  32.763  22.845  1.00 35.70           C  
ATOM   1472  C   TYR A 251     -14.438  31.295  23.085  1.00 37.00           C  
ATOM   1473  O   TYR A 251     -15.561  30.855  22.855  1.00 37.55           O  
ATOM   1474  CB  TYR A 251     -14.974  33.634  23.760  1.00 35.07           C  
ATOM   1475  CG  TYR A 251     -14.611  33.518  25.215  1.00 37.59           C  
ATOM   1476  CD1 TYR A 251     -13.494  34.170  25.720  1.00 36.64           C  
ATOM   1477  CD2 TYR A 251     -15.370  32.733  26.086  1.00 38.43           C  
ATOM   1478  CE1 TYR A 251     -13.136  34.053  27.049  1.00 38.35           C  
ATOM   1479  CE2 TYR A 251     -15.016  32.604  27.428  1.00 39.25           C  
ATOM   1480  CZ  TYR A 251     -13.897  33.271  27.901  1.00 38.89           C  
ATOM   1481  OH  TYR A 251     -13.529  33.168  29.221  1.00 38.07           O  
ATOM   1482  N   ASP A 252     -13.451  30.545  23.562  1.00 38.83           N  
ATOM   1483  CA  ASP A 252     -13.623  29.122  23.854  1.00 41.62           C  
ATOM   1484  C   ASP A 252     -14.547  28.368  22.887  1.00 42.04           C  
ATOM   1485  O   ASP A 252     -15.649  27.952  23.249  1.00 43.05           O  
ATOM   1486  CB  ASP A 252     -14.116  28.952  25.299  1.00 44.41           C  
ATOM   1487  CG  ASP A 252     -14.632  27.549  25.588  1.00 49.19           C  
ATOM   1488  OD1 ASP A 252     -13.916  26.564  25.296  1.00 51.83           O  
ATOM   1489  OD2 ASP A 252     -15.762  27.433  26.113  1.00 52.36           O  
ATOM   1490  N   LYS A 253     -14.090  28.206  21.651  1.00 41.65           N  
ATOM   1491  CA  LYS A 253     -14.838  27.485  20.629  1.00 40.25           C  
ATOM   1492  C   LYS A 253     -14.052  26.228  20.283  1.00 39.17           C  
ATOM   1493  O   LYS A 253     -13.705  26.019  19.125  1.00 41.05           O  
ATOM   1494  CB  LYS A 253     -14.996  28.343  19.366  1.00 41.14           C  
ATOM   1495  CG  LYS A 253     -16.088  29.401  19.440  1.00 42.97           C  
ATOM   1496  CD  LYS A 253     -17.464  28.755  19.570  1.00 40.77           C  
ATOM   1497  CE  LYS A 253     -18.582  29.776  19.474  1.00 41.02           C  
ATOM   1498  NZ  LYS A 253     -19.929  29.137  19.611  1.00 41.61           N  
ATOM   1499  N   TRP A 254     -13.766  25.400  21.285  1.00 37.35           N  
ATOM   1500  CA  TRP A 254     -13.006  24.176  21.064  1.00 35.07           C  
ATOM   1501  C   TRP A 254     -13.827  22.980  20.559  1.00 35.38           C  
ATOM   1502  O   TRP A 254     -13.342  22.220  19.727  1.00 32.96           O  
ATOM   1503  CB  TRP A 254     -12.259  23.783  22.341  1.00 33.38           C  
ATOM   1504  CG  TRP A 254     -11.277  24.812  22.830  1.00 33.68           C  
ATOM   1505  CD1 TRP A 254     -11.475  25.722  23.834  1.00 33.16           C  
ATOM   1506  CD2 TRP A 254      -9.934  25.024  22.357  1.00 30.05           C  
ATOM   1507  NE1 TRP A 254     -10.341  26.478  24.017  1.00 31.16           N  
ATOM   1508  CE2 TRP A 254      -9.382  26.072  23.126  1.00 30.69           C  
ATOM   1509  CE3 TRP A 254      -9.146  24.428  21.357  1.00 29.91           C  
ATOM   1510  CZ2 TRP A 254      -8.072  26.540  22.930  1.00 27.96           C  
ATOM   1511  CZ3 TRP A 254      -7.841  24.893  21.163  1.00 26.96           C  
ATOM   1512  CH2 TRP A 254      -7.322  25.938  21.947  1.00 27.93           C  
ATOM   1513  N   GLU A 255     -15.048  22.808  21.069  1.00 36.11           N  
ATOM   1514  CA  GLU A 255     -15.918  21.705  20.656  1.00 37.06           C  
ATOM   1515  C   GLU A 255     -16.072  21.650  19.139  1.00 37.96           C  
ATOM   1516  O   GLU A 255     -16.227  22.676  18.477  1.00 38.97           O  
ATOM   1517  CB  GLU A 255     -17.312  21.860  21.267  1.00 37.95           C  
ATOM   1518  CG  GLU A 255     -17.449  21.535  22.746  1.00 40.42           C  
ATOM   1519  CD  GLU A 255     -17.126  20.087  23.081  1.00 42.25           C  
ATOM   1520  OE1 GLU A 255     -17.632  19.173  22.390  1.00 42.88           O  
ATOM   1521  OE2 GLU A 255     -16.385  19.865  24.058  1.00 41.19           O  
ATOM   1522  N   MET A 256     -16.031  20.453  18.577  1.00 40.24           N  
ATOM   1523  CA  MET A 256     -16.198  20.305  17.135  1.00 44.28           C  
ATOM   1524  C   MET A 256     -17.033  19.059  16.858  1.00 44.21           C  
ATOM   1525  O   MET A 256     -17.300  18.274  17.766  1.00 43.54           O  
ATOM   1526  CB  MET A 256     -14.828  20.262  16.433  1.00 47.50           C  
ATOM   1527  CG  MET A 256     -13.879  19.198  16.924  1.00 52.60           C  
ATOM   1528  SD  MET A 256     -14.145  17.755  15.928  1.00 63.40           S  
ATOM   1529  CE  MET A 256     -13.513  18.390  14.325  1.00 59.56           C  
ATOM   1530  N   GLU A 257     -17.455  18.875  15.615  1.00 45.97           N  
ATOM   1531  CA  GLU A 257     -18.303  17.737  15.271  1.00 48.31           C  
ATOM   1532  C   GLU A 257     -17.533  16.455  14.988  1.00 46.67           C  
ATOM   1533  O   GLU A 257     -16.734  16.408  14.057  1.00 45.64           O  
ATOM   1534  CB  GLU A 257     -19.176  18.103  14.071  1.00 51.74           C  
ATOM   1535  CG  GLU A 257     -20.081  19.306  14.322  1.00 58.72           C  
ATOM   1536  CD  GLU A 257     -21.113  19.511  13.215  1.00 63.56           C  
ATOM   1537  OE1 GLU A 257     -21.396  18.544  12.468  1.00 65.60           O  
ATOM   1538  OE2 GLU A 257     -21.659  20.633  13.103  1.00 66.52           O  
ATOM   1539  N   ARG A 258     -17.777  15.423  15.795  1.00 45.80           N  
ATOM   1540  CA  ARG A 258     -17.097  14.140  15.633  1.00 46.17           C  
ATOM   1541  C   ARG A 258     -17.184  13.592  14.201  1.00 44.43           C  
ATOM   1542  O   ARG A 258     -16.235  12.987  13.708  1.00 43.76           O  
ATOM   1543  CB  ARG A 258     -17.670  13.102  16.612  1.00 47.54           C  
ATOM   1544  CG  ARG A 258     -16.887  11.783  16.642  1.00 50.23           C  
ATOM   1545  CD  ARG A 258     -17.513  10.698  17.543  1.00 52.18           C  
ATOM   1546  NE  ARG A 258     -17.443  11.012  18.971  1.00 51.98           N  
ATOM   1547  CZ  ARG A 258     -18.242  11.875  19.590  1.00 51.25           C  
ATOM   1548  NH1 ARG A 258     -19.185  12.515  18.911  1.00 51.62           N  
ATOM   1549  NH2 ARG A 258     -18.095  12.103  20.889  1.00 49.39           N  
ATOM   1550  N   THR A 259     -18.315  13.801  13.536  1.00 43.02           N  
ATOM   1551  CA  THR A 259     -18.474  13.315  12.168  1.00 44.15           C  
ATOM   1552  C   THR A 259     -17.496  14.000  11.214  1.00 44.19           C  
ATOM   1553  O   THR A 259     -17.182  13.470  10.153  1.00 43.07           O  
ATOM   1554  CB  THR A 259     -19.905  13.543  11.643  1.00 42.79           C  
ATOM   1555  OG1 THR A 259     -20.214  14.938  11.688  1.00 43.55           O  
ATOM   1556  CG2 THR A 259     -20.904  12.783  12.488  1.00 42.69           C  
ATOM   1557  N   ASP A 260     -17.017  15.178  11.595  1.00 43.70           N  
ATOM   1558  CA  ASP A 260     -16.069  15.913  10.766  1.00 45.25           C  
ATOM   1559  C   ASP A 260     -14.686  15.257  10.769  1.00 44.11           C  
ATOM   1560  O   ASP A 260     -13.797  15.660  10.014  1.00 42.05           O  
ATOM   1561  CB  ASP A 260     -15.934  17.345  11.277  1.00 49.21           C  
ATOM   1562  CG  ASP A 260     -17.223  18.135  11.164  1.00 53.61           C  
ATOM   1563  OD1 ASP A 260     -18.281  17.542  10.850  1.00 57.43           O  
ATOM   1564  OD2 ASP A 260     -17.172  19.361  11.397  1.00 54.93           O  
ATOM   1565  N   ILE A 261     -14.506  14.244  11.611  1.00 42.42           N  
ATOM   1566  CA  ILE A 261     -13.213  13.579  11.708  1.00 42.04           C  
ATOM   1567  C   ILE A 261     -13.158  12.142  11.197  1.00 42.16           C  
ATOM   1568  O   ILE A 261     -13.987  11.309  11.551  1.00 41.27           O  
ATOM   1569  CB  ILE A 261     -12.717  13.564  13.161  1.00 41.70           C  
ATOM   1570  CG1 ILE A 261     -12.713  14.986  13.731  1.00 40.61           C  
ATOM   1571  CG2 ILE A 261     -11.333  12.938  13.219  1.00 40.24           C  
ATOM   1572  CD1 ILE A 261     -11.733  15.927  13.056  1.00 40.41           C  
ATOM   1573  N   THR A 262     -12.153  11.862  10.375  1.00 43.07           N  
ATOM   1574  CA  THR A 262     -11.948  10.527   9.831  1.00 43.79           C  
ATOM   1575  C   THR A 262     -10.814   9.855  10.600  1.00 43.83           C  
ATOM   1576  O   THR A 262      -9.659  10.252  10.484  1.00 43.68           O  
ATOM   1577  CB  THR A 262     -11.574  10.585   8.335  1.00 44.94           C  
ATOM   1578  OG1 THR A 262     -12.703  11.037   7.579  1.00 47.23           O  
ATOM   1579  CG2 THR A 262     -11.153   9.215   7.833  1.00 45.43           C  
ATOM   1580  N   MET A 263     -11.152   8.841  11.390  1.00 43.89           N  
ATOM   1581  CA  MET A 263     -10.163   8.120  12.178  1.00 43.90           C  
ATOM   1582  C   MET A 263      -9.442   7.091  11.323  1.00 45.02           C  
ATOM   1583  O   MET A 263     -10.067   6.364  10.554  1.00 44.72           O  
ATOM   1584  CB  MET A 263     -10.846   7.421  13.352  1.00 43.68           C  
ATOM   1585  CG  MET A 263     -11.537   8.376  14.300  1.00 45.03           C  
ATOM   1586  SD  MET A 263     -10.354   9.487  15.097  1.00 46.26           S  
ATOM   1587  CE  MET A 263     -10.119   8.632  16.649  1.00 44.45           C  
ATOM   1588  N   LYS A 264      -8.122   7.029  11.457  1.00 45.76           N  
ATOM   1589  CA  LYS A 264      -7.343   6.072  10.689  1.00 46.22           C  
ATOM   1590  C   LYS A 264      -6.516   5.167  11.593  1.00 47.39           C  
ATOM   1591  O   LYS A 264      -6.943   4.815  12.693  1.00 48.39           O  
ATOM   1592  CB  LYS A 264      -6.451   6.806   9.694  1.00 45.71           C  
ATOM   1593  CG  LYS A 264      -7.244   7.729   8.787  1.00 47.59           C  
ATOM   1594  CD  LYS A 264      -6.511   8.060   7.497  1.00 47.64           C  
ATOM   1595  CE  LYS A 264      -5.201   8.781   7.752  1.00 50.40           C  
ATOM   1596  NZ  LYS A 264      -4.572   9.265   6.486  1.00 52.29           N  
ATOM   1597  N   HIS A 265      -5.334   4.784  11.132  1.00 48.08           N  
ATOM   1598  CA  HIS A 265      -4.478   3.901  11.909  1.00 48.22           C  
ATOM   1599  C   HIS A 265      -3.963   4.563  13.185  1.00 48.07           C  
ATOM   1600  O   HIS A 265      -3.844   5.789  13.263  1.00 48.56           O  
ATOM   1601  CB  HIS A 265      -3.297   3.442  11.051  1.00 49.44           C  
ATOM   1602  CG  HIS A 265      -2.451   4.567  10.537  1.00 51.11           C  
ATOM   1603  ND1 HIS A 265      -2.933   5.525   9.670  1.00 52.53           N  
ATOM   1604  CD2 HIS A 265      -1.157   4.889  10.771  1.00 51.57           C  
ATOM   1605  CE1 HIS A 265      -1.971   6.387   9.392  1.00 52.83           C  
ATOM   1606  NE2 HIS A 265      -0.883   6.024  10.047  1.00 51.86           N  
ATOM   1607  N   LYS A 266      -3.657   3.743  14.184  1.00 46.60           N  
ATOM   1608  CA  LYS A 266      -3.133   4.240  15.449  1.00 45.70           C  
ATOM   1609  C   LYS A 266      -1.699   4.747  15.261  1.00 44.73           C  
ATOM   1610  O   LYS A 266      -0.998   4.322  14.342  1.00 44.81           O  
ATOM   1611  CB  LYS A 266      -3.162   3.123  16.494  1.00 47.04           C  
ATOM   1612  CG  LYS A 266      -2.597   3.534  17.836  1.00 49.04           C  
ATOM   1613  CD  LYS A 266      -2.791   2.461  18.890  1.00 50.26           C  
ATOM   1614  CE  LYS A 266      -4.259   2.196  19.159  1.00 49.84           C  
ATOM   1615  NZ  LYS A 266      -4.420   1.309  20.341  1.00 50.71           N  
ATOM   1616  N   LEU A 267      -1.263   5.652  16.132  1.00 43.31           N  
ATOM   1617  CA  LEU A 267       0.087   6.213  16.041  1.00 41.54           C  
ATOM   1618  C   LEU A 267       1.065   5.648  17.067  1.00 39.29           C  
ATOM   1619  O   LEU A 267       0.696   5.375  18.200  1.00 39.56           O  
ATOM   1620  CB  LEU A 267       0.031   7.739  16.190  1.00 40.84           C  
ATOM   1621  CG  LEU A 267      -0.517   8.532  15.004  1.00 41.04           C  
ATOM   1622  CD1 LEU A 267      -0.818   9.954  15.443  1.00 41.91           C  
ATOM   1623  CD2 LEU A 267       0.499   8.523  13.863  1.00 41.88           C  
ATOM   1624  N   GLY A 268       2.318   5.484  16.656  1.00 39.43           N  
ATOM   1625  CA  GLY A 268       3.339   4.973  17.552  1.00 40.81           C  
ATOM   1626  C   GLY A 268       3.046   3.603  18.135  1.00 42.61           C  
ATOM   1627  O   GLY A 268       3.307   3.359  19.320  1.00 42.08           O  
ATOM   1628  N   GLY A 269       2.508   2.711  17.306  1.00 42.23           N  
ATOM   1629  CA  GLY A 269       2.188   1.367  17.756  1.00 41.78           C  
ATOM   1630  C   GLY A 269       1.587   1.298  19.149  1.00 41.62           C  
ATOM   1631  O   GLY A 269       1.883   0.376  19.911  1.00 42.71           O  
ATOM   1632  N   GLY A 270       0.761   2.284  19.492  1.00 40.70           N  
ATOM   1633  CA  GLY A 270       0.112   2.295  20.794  1.00 37.99           C  
ATOM   1634  C   GLY A 270       0.919   2.775  21.988  1.00 38.23           C  
ATOM   1635  O   GLY A 270       0.388   2.838  23.098  1.00 38.32           O  
ATOM   1636  N   GLN A 271       2.184   3.130  21.784  1.00 36.73           N  
ATOM   1637  CA  GLN A 271       3.014   3.579  22.898  1.00 36.10           C  
ATOM   1638  C   GLN A 271       2.553   4.891  23.539  1.00 35.90           C  
ATOM   1639  O   GLN A 271       3.041   5.262  24.609  1.00 35.48           O  
ATOM   1640  CB  GLN A 271       4.486   3.706  22.462  1.00 36.85           C  
ATOM   1641  CG  GLN A 271       4.793   4.889  21.551  1.00 40.01           C  
ATOM   1642  CD  GLN A 271       6.248   4.914  21.070  1.00 41.08           C  
ATOM   1643  OE1 GLN A 271       7.180   5.052  21.867  1.00 41.53           O  
ATOM   1644  NE2 GLN A 271       6.442   4.779  19.759  1.00 40.09           N  
ATOM   1645  N   TYR A 272       1.622   5.595  22.898  1.00 33.24           N  
ATOM   1646  CA  TYR A 272       1.129   6.853  23.454  1.00 31.82           C  
ATOM   1647  C   TYR A 272      -0.297   6.731  23.957  1.00 32.72           C  
ATOM   1648  O   TYR A 272      -0.897   7.708  24.398  1.00 32.98           O  
ATOM   1649  CB  TYR A 272       1.195   7.970  22.407  1.00 28.82           C  
ATOM   1650  CG  TYR A 272       2.579   8.188  21.861  1.00 24.68           C  
ATOM   1651  CD1 TYR A 272       2.948   7.685  20.617  1.00 25.54           C  
ATOM   1652  CD2 TYR A 272       3.532   8.871  22.605  1.00 24.65           C  
ATOM   1653  CE1 TYR A 272       4.245   7.862  20.123  1.00 26.04           C  
ATOM   1654  CE2 TYR A 272       4.827   9.048  22.129  1.00 26.46           C  
ATOM   1655  CZ  TYR A 272       5.177   8.539  20.890  1.00 24.83           C  
ATOM   1656  OH  TYR A 272       6.466   8.685  20.442  1.00 25.69           O  
ATOM   1657  N   GLY A 273      -0.844   5.528  23.898  1.00 33.88           N  
ATOM   1658  CA  GLY A 273      -2.210   5.345  24.343  1.00 34.85           C  
ATOM   1659  C   GLY A 273      -3.130   5.300  23.142  1.00 34.16           C  
ATOM   1660  O   GLY A 273      -2.716   4.898  22.059  1.00 35.23           O  
ATOM   1661  N   GLU A 274      -4.373   5.725  23.326  1.00 34.64           N  
ATOM   1662  CA  GLU A 274      -5.354   5.706  22.250  1.00 35.33           C  
ATOM   1663  C   GLU A 274      -5.220   6.914  21.329  1.00 34.51           C  
ATOM   1664  O   GLU A 274      -6.088   7.788  21.299  1.00 34.70           O  
ATOM   1665  CB  GLU A 274      -6.759   5.663  22.848  1.00 38.08           C  
ATOM   1666  CG  GLU A 274      -6.993   4.484  23.771  1.00 43.66           C  
ATOM   1667  CD  GLU A 274      -6.814   3.156  23.068  1.00 47.67           C  
ATOM   1668  OE1 GLU A 274      -7.559   2.895  22.096  1.00 50.16           O  
ATOM   1669  OE2 GLU A 274      -5.927   2.377  23.485  1.00 49.09           O  
ATOM   1670  N   VAL A 275      -4.136   6.954  20.564  1.00 33.43           N  
ATOM   1671  CA  VAL A 275      -3.903   8.071  19.664  1.00 31.55           C  
ATOM   1672  C   VAL A 275      -3.864   7.607  18.215  1.00 32.35           C  
ATOM   1673  O   VAL A 275      -3.075   6.738  17.841  1.00 32.06           O  
ATOM   1674  CB  VAL A 275      -2.596   8.793  20.040  1.00 30.53           C  
ATOM   1675  CG1 VAL A 275      -2.398  10.003  19.165  1.00 32.14           C  
ATOM   1676  CG2 VAL A 275      -2.647   9.209  21.510  1.00 28.35           C  
ATOM   1677  N   TYR A 276      -4.731   8.195  17.400  1.00 33.59           N  
ATOM   1678  CA  TYR A 276      -4.826   7.820  15.998  1.00 35.28           C  
ATOM   1679  C   TYR A 276      -4.541   8.974  15.060  1.00 35.47           C  
ATOM   1680  O   TYR A 276      -4.760  10.137  15.395  1.00 36.30           O  
ATOM   1681  CB  TYR A 276      -6.239   7.304  15.682  1.00 36.94           C  
ATOM   1682  CG  TYR A 276      -6.736   6.194  16.583  1.00 38.69           C  
ATOM   1683  CD1 TYR A 276      -7.024   6.438  17.924  1.00 39.71           C  
ATOM   1684  CD2 TYR A 276      -6.892   4.888  16.100  1.00 40.30           C  
ATOM   1685  CE1 TYR A 276      -7.450   5.416  18.771  1.00 40.47           C  
ATOM   1686  CE2 TYR A 276      -7.318   3.853  16.938  1.00 41.60           C  
ATOM   1687  CZ  TYR A 276      -7.593   4.127  18.277  1.00 42.83           C  
ATOM   1688  OH  TYR A 276      -7.991   3.119  19.136  1.00 43.72           O  
ATOM   1689  N   GLU A 277      -4.047   8.652  13.874  1.00 35.63           N  
ATOM   1690  CA  GLU A 277      -3.832   9.687  12.890  1.00 35.88           C  
ATOM   1691  C   GLU A 277      -5.243   9.904  12.356  1.00 35.60           C  
ATOM   1692  O   GLU A 277      -6.033   8.962  12.281  1.00 35.33           O  
ATOM   1693  CB  GLU A 277      -2.904   9.214  11.773  1.00 37.52           C  
ATOM   1694  CG  GLU A 277      -2.828  10.187  10.604  1.00 41.10           C  
ATOM   1695  CD  GLU A 277      -1.682   9.891   9.647  1.00 44.81           C  
ATOM   1696  OE1 GLU A 277      -1.703  10.427   8.517  1.00 45.31           O  
ATOM   1697  OE2 GLU A 277      -0.755   9.135  10.025  1.00 47.93           O  
ATOM   1698  N   GLY A 278      -5.575  11.141  12.010  1.00 35.12           N  
ATOM   1699  CA  GLY A 278      -6.911  11.410  11.515  1.00 33.44           C  
ATOM   1700  C   GLY A 278      -6.936  12.521  10.496  1.00 32.38           C  
ATOM   1701  O   GLY A 278      -5.909  13.124  10.181  1.00 30.23           O  
ATOM   1702  N   VAL A 279      -8.127  12.799   9.986  1.00 32.59           N  
ATOM   1703  CA  VAL A 279      -8.298  13.839   8.989  1.00 33.18           C  
ATOM   1704  C   VAL A 279      -9.484  14.725   9.318  1.00 33.80           C  
ATOM   1705  O   VAL A 279     -10.606  14.241   9.474  1.00 36.82           O  
ATOM   1706  CB  VAL A 279      -8.536  13.240   7.579  1.00 32.98           C  
ATOM   1707  CG1 VAL A 279      -8.743  14.364   6.570  1.00 31.31           C  
ATOM   1708  CG2 VAL A 279      -7.357  12.352   7.171  1.00 31.04           C  
ATOM   1709  N   TRP A 280      -9.229  16.021   9.443  1.00 32.91           N  
ATOM   1710  CA  TRP A 280     -10.293  16.974   9.698  1.00 33.41           C  
ATOM   1711  C   TRP A 280     -10.748  17.274   8.274  1.00 33.61           C  
ATOM   1712  O   TRP A 280     -10.216  18.168   7.621  1.00 33.31           O  
ATOM   1713  CB  TRP A 280      -9.747  18.242  10.352  1.00 30.45           C  
ATOM   1714  CG  TRP A 280     -10.823  19.102  10.922  1.00 28.64           C  
ATOM   1715  CD1 TRP A 280     -12.137  19.115  10.557  1.00 28.32           C  
ATOM   1716  CD2 TRP A 280     -10.690  20.058  11.981  1.00 29.44           C  
ATOM   1717  NE1 TRP A 280     -12.836  20.017  11.327  1.00 29.40           N  
ATOM   1718  CE2 TRP A 280     -11.972  20.608  12.211  1.00 30.28           C  
ATOM   1719  CE3 TRP A 280      -9.614  20.500  12.762  1.00 28.06           C  
ATOM   1720  CZ2 TRP A 280     -12.207  21.580  13.190  1.00 31.02           C  
ATOM   1721  CZ3 TRP A 280      -9.848  21.466  13.739  1.00 29.77           C  
ATOM   1722  CH2 TRP A 280     -11.136  21.993  13.943  1.00 31.38           C  
ATOM   1723  N   LYS A 281     -11.713  16.494   7.797  1.00 35.90           N  
ATOM   1724  CA  LYS A 281     -12.232  16.600   6.435  1.00 35.85           C  
ATOM   1725  C   LYS A 281     -12.446  17.999   5.871  1.00 35.57           C  
ATOM   1726  O   LYS A 281     -11.964  18.311   4.781  1.00 34.28           O  
ATOM   1727  CB  LYS A 281     -13.526  15.791   6.322  1.00 36.93           C  
ATOM   1728  CG  LYS A 281     -13.294  14.334   5.943  1.00 38.08           C  
ATOM   1729  CD  LYS A 281     -14.116  13.380   6.791  1.00 39.15           C  
ATOM   1730  CE  LYS A 281     -15.600  13.615   6.655  1.00 39.94           C  
ATOM   1731  NZ  LYS A 281     -16.358  12.581   7.406  1.00 38.80           N  
ATOM   1732  N   LYS A 282     -13.164  18.833   6.615  1.00 35.12           N  
ATOM   1733  CA  LYS A 282     -13.453  20.190   6.186  1.00 36.05           C  
ATOM   1734  C   LYS A 282     -12.224  20.947   5.689  1.00 37.13           C  
ATOM   1735  O   LYS A 282     -12.293  21.690   4.712  1.00 36.46           O  
ATOM   1736  CB  LYS A 282     -14.102  20.967   7.333  1.00 36.62           C  
ATOM   1737  CG  LYS A 282     -14.426  22.403   6.985  1.00 37.56           C  
ATOM   1738  CD  LYS A 282     -15.397  23.018   7.969  1.00 38.22           C  
ATOM   1739  CE  LYS A 282     -15.809  24.411   7.516  1.00 38.74           C  
ATOM   1740  NZ  LYS A 282     -16.864  24.984   8.393  1.00 37.04           N  
ATOM   1741  N   TYR A 283     -11.093  20.752   6.354  1.00 36.25           N  
ATOM   1742  CA  TYR A 283      -9.896  21.465   5.964  1.00 35.86           C  
ATOM   1743  C   TYR A 283      -8.861  20.582   5.314  1.00 36.11           C  
ATOM   1744  O   TYR A 283      -7.705  20.982   5.179  1.00 37.49           O  
ATOM   1745  CB  TYR A 283      -9.297  22.168   7.186  1.00 36.11           C  
ATOM   1746  CG  TYR A 283     -10.300  23.037   7.912  1.00 36.04           C  
ATOM   1747  CD1 TYR A 283     -11.018  22.554   9.010  1.00 36.47           C  
ATOM   1748  CD2 TYR A 283     -10.569  24.327   7.467  1.00 36.99           C  
ATOM   1749  CE1 TYR A 283     -11.985  23.347   9.645  1.00 36.79           C  
ATOM   1750  CE2 TYR A 283     -11.529  25.125   8.084  1.00 37.54           C  
ATOM   1751  CZ  TYR A 283     -12.235  24.634   9.169  1.00 39.13           C  
ATOM   1752  OH  TYR A 283     -13.191  25.439   9.755  1.00 38.01           O  
ATOM   1753  N   SER A 284      -9.264  19.382   4.905  1.00 36.71           N  
ATOM   1754  CA  SER A 284      -8.320  18.465   4.266  1.00 37.64           C  
ATOM   1755  C   SER A 284      -7.025  18.536   5.077  1.00 36.49           C  
ATOM   1756  O   SER A 284      -5.938  18.665   4.525  1.00 37.31           O  
ATOM   1757  CB  SER A 284      -8.061  18.907   2.821  1.00 35.75           C  
ATOM   1758  OG  SER A 284      -7.205  17.997   2.159  1.00 39.57           O  
ATOM   1759  N   LEU A 285      -7.171  18.452   6.396  1.00 36.70           N  
ATOM   1760  CA  LEU A 285      -6.054  18.555   7.328  1.00 35.69           C  
ATOM   1761  C   LEU A 285      -5.795  17.300   8.165  1.00 35.88           C  
ATOM   1762  O   LEU A 285      -6.698  16.782   8.829  1.00 34.97           O  
ATOM   1763  CB  LEU A 285      -6.322  19.734   8.258  1.00 34.32           C  
ATOM   1764  CG  LEU A 285      -5.307  20.125   9.330  1.00 35.51           C  
ATOM   1765  CD1 LEU A 285      -3.984  20.549   8.682  1.00 34.47           C  
ATOM   1766  CD2 LEU A 285      -5.895  21.275  10.147  1.00 32.74           C  
ATOM   1767  N   THR A 286      -4.557  16.815   8.141  1.00 35.09           N  
ATOM   1768  CA  THR A 286      -4.201  15.643   8.930  1.00 33.42           C  
ATOM   1769  C   THR A 286      -4.012  16.101  10.370  1.00 33.48           C  
ATOM   1770  O   THR A 286      -3.401  17.140  10.625  1.00 33.12           O  
ATOM   1771  CB  THR A 286      -2.896  15.014   8.442  1.00 34.81           C  
ATOM   1772  OG1 THR A 286      -3.059  14.584   7.085  1.00 39.67           O  
ATOM   1773  CG2 THR A 286      -2.523  13.816   9.308  1.00 33.26           C  
ATOM   1774  N   VAL A 287      -4.549  15.335  11.312  1.00 31.29           N  
ATOM   1775  CA  VAL A 287      -4.424  15.682  12.720  1.00 30.47           C  
ATOM   1776  C   VAL A 287      -4.196  14.428  13.549  1.00 29.55           C  
ATOM   1777  O   VAL A 287      -4.255  13.314  13.035  1.00 29.50           O  
ATOM   1778  CB  VAL A 287      -5.700  16.366  13.242  1.00 30.57           C  
ATOM   1779  CG1 VAL A 287      -5.953  17.649  12.470  1.00 29.45           C  
ATOM   1780  CG2 VAL A 287      -6.894  15.406  13.117  1.00 29.91           C  
ATOM   1781  N   ALA A 288      -3.920  14.619  14.831  1.00 29.52           N  
ATOM   1782  CA  ALA A 288      -3.726  13.500  15.741  1.00 29.33           C  
ATOM   1783  C   ALA A 288      -4.965  13.513  16.617  1.00 29.24           C  
ATOM   1784  O   ALA A 288      -5.468  14.582  16.964  1.00 31.11           O  
ATOM   1785  CB  ALA A 288      -2.480  13.701  16.575  1.00 26.83           C  
ATOM   1786  N   VAL A 289      -5.467  12.338  16.966  1.00 29.47           N  
ATOM   1787  CA  VAL A 289      -6.670  12.263  17.786  1.00 30.87           C  
ATOM   1788  C   VAL A 289      -6.530  11.256  18.916  1.00 31.25           C  
ATOM   1789  O   VAL A 289      -6.244  10.081  18.683  1.00 30.71           O  
ATOM   1790  CB  VAL A 289      -7.905  11.866  16.928  1.00 30.04           C  
ATOM   1791  CG1 VAL A 289      -9.166  11.863  17.784  1.00 28.65           C  
ATOM   1792  CG2 VAL A 289      -8.056  12.822  15.770  1.00 28.35           C  
ATOM   1793  N   LYS A 290      -6.718  11.721  20.144  1.00 33.04           N  
ATOM   1794  CA  LYS A 290      -6.643  10.830  21.285  1.00 36.08           C  
ATOM   1795  C   LYS A 290      -8.053  10.527  21.760  1.00 38.12           C  
ATOM   1796  O   LYS A 290      -8.835  11.434  22.031  1.00 37.27           O  
ATOM   1797  CB  LYS A 290      -5.847  11.449  22.429  1.00 36.09           C  
ATOM   1798  CG  LYS A 290      -6.073  10.705  23.751  1.00 39.27           C  
ATOM   1799  CD  LYS A 290      -4.782  10.273  24.416  1.00 39.89           C  
ATOM   1800  CE  LYS A 290      -4.022  11.448  24.985  1.00 39.91           C  
ATOM   1801  NZ  LYS A 290      -2.897  10.973  25.834  1.00 41.92           N  
ATOM   1802  N   THR A 291      -8.378   9.246  21.866  1.00 41.40           N  
ATOM   1803  CA  THR A 291      -9.709   8.868  22.309  1.00 46.30           C  
ATOM   1804  C   THR A 291      -9.672   8.158  23.654  1.00 48.93           C  
ATOM   1805  O   THR A 291      -8.679   7.526  24.006  1.00 48.72           O  
ATOM   1806  CB  THR A 291     -10.399   7.964  21.286  1.00 45.40           C  
ATOM   1807  OG1 THR A 291     -11.768   7.778  21.670  1.00 49.17           O  
ATOM   1808  CG2 THR A 291      -9.702   6.623  21.214  1.00 43.69           C  
ATOM   1809  N   LEU A 292     -10.761   8.262  24.403  1.00 52.95           N  
ATOM   1810  CA  LEU A 292     -10.827   7.639  25.714  1.00 58.50           C  
ATOM   1811  C   LEU A 292     -11.293   6.191  25.660  1.00 62.11           C  
ATOM   1812  O   LEU A 292     -12.292   5.876  25.017  1.00 62.13           O  
ATOM   1813  CB  LEU A 292     -11.755   8.446  26.622  1.00 58.94           C  
ATOM   1814  CG  LEU A 292     -11.929   7.951  28.061  1.00 60.64           C  
ATOM   1815  CD1 LEU A 292     -10.571   7.808  28.741  1.00 60.61           C  
ATOM   1816  CD2 LEU A 292     -12.805   8.933  28.820  1.00 60.84           C  
ATOM   1817  N   LYS A 293     -10.556   5.309  26.331  1.00 67.47           N  
ATOM   1818  CA  LYS A 293     -10.924   3.898  26.377  1.00 72.95           C  
ATOM   1819  C   LYS A 293     -12.145   3.766  27.274  1.00 75.33           C  
ATOM   1820  O   LYS A 293     -12.134   4.223  28.419  1.00 75.51           O  
ATOM   1821  CB  LYS A 293      -9.787   3.048  26.947  1.00 74.47           C  
ATOM   1822  CG  LYS A 293     -10.135   1.564  27.109  1.00 76.60           C  
ATOM   1823  CD  LYS A 293     -10.293   0.835  25.764  1.00 78.70           C  
ATOM   1824  CE  LYS A 293     -11.576   1.206  25.017  1.00 79.01           C  
ATOM   1825  NZ  LYS A 293     -11.658   0.545  23.675  1.00 79.78           N  
ATOM   1826  N   GLU A 294     -13.192   3.134  26.755  1.00 78.39           N  
ATOM   1827  CA  GLU A 294     -14.431   2.967  27.502  1.00 81.62           C  
ATOM   1828  C   GLU A 294     -14.346   1.892  28.583  1.00 82.72           C  
ATOM   1829  O   GLU A 294     -15.039   1.972  29.596  1.00 82.53           O  
ATOM   1830  CB  GLU A 294     -15.574   2.657  26.529  1.00 82.82           C  
ATOM   1831  CG  GLU A 294     -16.968   2.887  27.098  1.00 85.15           C  
ATOM   1832  CD  GLU A 294     -17.952   3.375  26.044  1.00 86.38           C  
ATOM   1833  OE1 GLU A 294     -17.774   4.508  25.538  1.00 85.68           O  
ATOM   1834  OE2 GLU A 294     -18.899   2.625  25.718  1.00 86.77           O  
ATOM   1835  N   ASP A 295     -13.484   0.901  28.374  1.00 84.71           N  
ATOM   1836  CA  ASP A 295     -13.321  -0.193  29.329  1.00 86.33           C  
ATOM   1837  C   ASP A 295     -12.884   0.281  30.710  1.00 87.06           C  
ATOM   1838  O   ASP A 295     -12.843  -0.504  31.661  1.00 86.36           O  
ATOM   1839  CB  ASP A 295     -12.318  -1.216  28.796  1.00 86.65           C  
ATOM   1840  CG  ASP A 295     -12.741  -1.800  27.464  1.00 87.49           C  
ATOM   1841  OD1 ASP A 295     -13.890  -2.282  27.367  1.00 87.07           O  
ATOM   1842  OD2 ASP A 295     -11.926  -1.777  26.517  1.00 88.07           O  
ATOM   1843  N   THR A 296     -12.551   1.563  30.818  1.00 88.39           N  
ATOM   1844  CA  THR A 296     -12.135   2.133  32.095  1.00 89.75           C  
ATOM   1845  C   THR A 296     -12.482   3.618  32.138  1.00 90.55           C  
ATOM   1846  O   THR A 296     -11.796   4.447  31.537  1.00 90.79           O  
ATOM   1847  CB  THR A 296     -10.621   1.960  32.326  1.00 89.58           C  
ATOM   1848  OG1 THR A 296     -10.245   0.605  32.046  1.00 89.37           O  
ATOM   1849  CG2 THR A 296     -10.270   2.276  33.775  1.00 89.64           C  
ATOM   1850  N   MET A 297     -13.559   3.943  32.849  1.00 91.43           N  
ATOM   1851  CA  MET A 297     -14.013   5.322  32.969  1.00 91.57           C  
ATOM   1852  C   MET A 297     -13.055   6.178  33.788  1.00 90.93           C  
ATOM   1853  O   MET A 297     -13.297   6.459  34.965  1.00 90.81           O  
ATOM   1854  CB  MET A 297     -15.414   5.380  33.595  1.00 93.47           C  
ATOM   1855  CG  MET A 297     -16.525   4.762  32.746  1.00 95.39           C  
ATOM   1856  SD  MET A 297     -16.737   5.521  31.114  1.00 97.85           S  
ATOM   1857  CE  MET A 297     -17.918   6.819  31.490  1.00 97.30           C  
ATOM   1858  N   GLU A 298     -11.955   6.575  33.158  1.00 89.50           N  
ATOM   1859  CA  GLU A 298     -10.968   7.429  33.798  1.00 87.25           C  
ATOM   1860  C   GLU A 298     -11.272   8.825  33.266  1.00 85.11           C  
ATOM   1861  O   GLU A 298     -10.424   9.719  33.289  1.00 85.35           O  
ATOM   1862  CB  GLU A 298      -9.557   7.014  33.391  1.00 88.45           C  
ATOM   1863  CG  GLU A 298      -9.305   7.114  31.899  1.00 89.97           C  
ATOM   1864  CD  GLU A 298      -7.841   6.979  31.548  1.00 91.52           C  
ATOM   1865  OE1 GLU A 298      -7.249   5.925  31.866  1.00 92.45           O  
ATOM   1866  OE2 GLU A 298      -7.282   7.928  30.955  1.00 91.57           O  
ATOM   1867  N   VAL A 299     -12.501   8.979  32.780  1.00 81.70           N  
ATOM   1868  CA  VAL A 299     -12.997  10.227  32.212  1.00 78.45           C  
ATOM   1869  C   VAL A 299     -12.440  11.475  32.888  1.00 75.88           C  
ATOM   1870  O   VAL A 299     -12.011  12.409  32.216  1.00 74.58           O  
ATOM   1871  CB  VAL A 299     -14.539  10.271  32.271  1.00 78.30           C  
ATOM   1872  CG1 VAL A 299     -15.054  11.525  31.588  1.00 78.56           C  
ATOM   1873  CG2 VAL A 299     -15.114   9.036  31.602  1.00 78.01           C  
ATOM   1874  N   GLU A 300     -12.449  11.489  34.215  1.00 73.87           N  
ATOM   1875  CA  GLU A 300     -11.937  12.631  34.960  1.00 72.18           C  
ATOM   1876  C   GLU A 300     -10.518  12.981  34.533  1.00 69.40           C  
ATOM   1877  O   GLU A 300     -10.195  14.148  34.323  1.00 69.30           O  
ATOM   1878  CB  GLU A 300     -11.975  12.343  36.462  1.00 74.43           C  
ATOM   1879  CG  GLU A 300     -13.372  12.397  37.058  1.00 79.10           C  
ATOM   1880  CD  GLU A 300     -13.986  13.788  36.976  1.00 82.46           C  
ATOM   1881  OE1 GLU A 300     -13.451  14.716  37.627  1.00 83.14           O  
ATOM   1882  OE2 GLU A 300     -14.999  13.955  36.258  1.00 83.73           O  
ATOM   1883  N   GLU A 301      -9.676  11.964  34.401  1.00 66.34           N  
ATOM   1884  CA  GLU A 301      -8.290  12.159  33.994  1.00 62.55           C  
ATOM   1885  C   GLU A 301      -8.238  12.745  32.579  1.00 58.50           C  
ATOM   1886  O   GLU A 301      -7.610  13.777  32.347  1.00 57.65           O  
ATOM   1887  CB  GLU A 301      -7.553  10.817  34.026  1.00 65.28           C  
ATOM   1888  CG  GLU A 301      -6.051  10.904  33.792  1.00 70.10           C  
ATOM   1889  CD  GLU A 301      -5.251  10.937  35.088  1.00 73.06           C  
ATOM   1890  OE1 GLU A 301      -5.421  11.892  35.880  1.00 74.77           O  
ATOM   1891  OE2 GLU A 301      -4.451  10.002  35.316  1.00 73.53           O  
ATOM   1892  N   PHE A 302      -8.908  12.075  31.644  1.00 53.44           N  
ATOM   1893  CA  PHE A 302      -8.956  12.494  30.243  1.00 49.11           C  
ATOM   1894  C   PHE A 302      -9.456  13.936  30.115  1.00 46.78           C  
ATOM   1895  O   PHE A 302      -8.843  14.766  29.442  1.00 43.78           O  
ATOM   1896  CB  PHE A 302      -9.885  11.558  29.466  1.00 46.96           C  
ATOM   1897  CG  PHE A 302      -9.820  11.726  27.976  1.00 44.99           C  
ATOM   1898  CD1 PHE A 302      -8.821  11.104  27.236  1.00 43.51           C  
ATOM   1899  CD2 PHE A 302     -10.766  12.498  27.308  1.00 43.73           C  
ATOM   1900  CE1 PHE A 302      -8.764  11.244  25.852  1.00 42.50           C  
ATOM   1901  CE2 PHE A 302     -10.717  12.644  25.925  1.00 43.57           C  
ATOM   1902  CZ  PHE A 302      -9.710  12.012  25.195  1.00 42.79           C  
ATOM   1903  N   LEU A 303     -10.579  14.218  30.763  1.00 44.97           N  
ATOM   1904  CA  LEU A 303     -11.172  15.545  30.737  1.00 43.84           C  
ATOM   1905  C   LEU A 303     -10.203  16.592  31.260  1.00 43.02           C  
ATOM   1906  O   LEU A 303     -10.114  17.688  30.715  1.00 43.95           O  
ATOM   1907  CB  LEU A 303     -12.458  15.559  31.568  1.00 43.08           C  
ATOM   1908  CG  LEU A 303     -13.781  15.601  30.792  1.00 44.09           C  
ATOM   1909  CD1 LEU A 303     -13.740  14.674  29.588  1.00 43.21           C  
ATOM   1910  CD2 LEU A 303     -14.915  15.215  31.732  1.00 45.03           C  
ATOM   1911  N   LYS A 304      -9.476  16.254  32.316  1.00 42.32           N  
ATOM   1912  CA  LYS A 304      -8.510  17.183  32.892  1.00 41.81           C  
ATOM   1913  C   LYS A 304      -7.432  17.534  31.875  1.00 39.40           C  
ATOM   1914  O   LYS A 304      -6.976  18.676  31.817  1.00 37.08           O  
ATOM   1915  CB  LYS A 304      -7.846  16.575  34.131  1.00 45.16           C  
ATOM   1916  CG  LYS A 304      -8.772  16.370  35.317  1.00 50.32           C  
ATOM   1917  CD  LYS A 304      -8.048  15.656  36.457  1.00 53.27           C  
ATOM   1918  CE  LYS A 304      -8.981  15.401  37.635  1.00 56.63           C  
ATOM   1919  NZ  LYS A 304      -8.315  14.639  38.736  1.00 59.05           N  
ATOM   1920  N   GLU A 305      -7.023  16.549  31.080  1.00 38.44           N  
ATOM   1921  CA  GLU A 305      -5.983  16.767  30.072  1.00 39.08           C  
ATOM   1922  C   GLU A 305      -6.476  17.755  29.013  1.00 38.75           C  
ATOM   1923  O   GLU A 305      -5.733  18.637  28.579  1.00 37.56           O  
ATOM   1924  CB  GLU A 305      -5.572  15.435  29.423  1.00 39.62           C  
ATOM   1925  CG  GLU A 305      -4.477  15.556  28.363  1.00 43.43           C  
ATOM   1926  CD  GLU A 305      -3.830  14.216  28.012  1.00 46.32           C  
ATOM   1927  OE1 GLU A 305      -3.117  13.651  28.868  1.00 48.31           O  
ATOM   1928  OE2 GLU A 305      -4.031  13.724  26.880  1.00 47.79           O  
ATOM   1929  N   ALA A 306      -7.739  17.616  28.620  1.00 36.95           N  
ATOM   1930  CA  ALA A 306      -8.321  18.508  27.633  1.00 35.63           C  
ATOM   1931  C   ALA A 306      -8.286  19.936  28.166  1.00 35.45           C  
ATOM   1932  O   ALA A 306      -7.838  20.854  27.475  1.00 35.80           O  
ATOM   1933  CB  ALA A 306      -9.752  18.096  27.337  1.00 33.09           C  
ATOM   1934  N   ALA A 307      -8.753  20.122  29.398  1.00 34.55           N  
ATOM   1935  CA  ALA A 307      -8.766  21.449  30.006  1.00 34.40           C  
ATOM   1936  C   ALA A 307      -7.362  22.071  30.041  1.00 34.21           C  
ATOM   1937  O   ALA A 307      -7.162  23.203  29.599  1.00 34.53           O  
ATOM   1938  CB  ALA A 307      -9.344  21.369  31.414  1.00 34.37           C  
ATOM   1939  N   VAL A 308      -6.394  21.331  30.566  1.00 33.31           N  
ATOM   1940  CA  VAL A 308      -5.021  21.820  30.638  1.00 32.51           C  
ATOM   1941  C   VAL A 308      -4.545  22.255  29.260  1.00 32.07           C  
ATOM   1942  O   VAL A 308      -3.994  23.349  29.087  1.00 32.71           O  
ATOM   1943  CB  VAL A 308      -4.056  20.722  31.161  1.00 32.27           C  
ATOM   1944  CG1 VAL A 308      -2.604  21.118  30.888  1.00 29.20           C  
ATOM   1945  CG2 VAL A 308      -4.268  20.514  32.648  1.00 30.54           C  
ATOM   1946  N   MET A 309      -4.773  21.396  28.275  1.00 31.17           N  
ATOM   1947  CA  MET A 309      -4.341  21.674  26.918  1.00 31.32           C  
ATOM   1948  C   MET A 309      -4.897  22.965  26.347  1.00 31.35           C  
ATOM   1949  O   MET A 309      -4.211  23.679  25.614  1.00 31.45           O  
ATOM   1950  CB  MET A 309      -4.678  20.490  26.025  1.00 32.28           C  
ATOM   1951  CG  MET A 309      -3.880  19.272  26.428  1.00 35.41           C  
ATOM   1952  SD  MET A 309      -3.642  18.159  25.088  1.00 40.33           S  
ATOM   1953  CE  MET A 309      -2.317  18.980  24.221  1.00 38.25           C  
ATOM   1954  N   LYS A 310      -6.136  23.275  26.692  1.00 30.69           N  
ATOM   1955  CA  LYS A 310      -6.740  24.500  26.221  1.00 30.92           C  
ATOM   1956  C   LYS A 310      -5.899  25.681  26.673  1.00 31.74           C  
ATOM   1957  O   LYS A 310      -5.798  26.685  25.966  1.00 31.99           O  
ATOM   1958  CB  LYS A 310      -8.163  24.622  26.763  1.00 30.26           C  
ATOM   1959  CG  LYS A 310      -9.108  23.585  26.186  1.00 30.69           C  
ATOM   1960  CD  LYS A 310     -10.506  23.682  26.775  1.00 32.06           C  
ATOM   1961  CE  LYS A 310     -11.410  22.616  26.172  1.00 33.10           C  
ATOM   1962  NZ  LYS A 310     -12.789  22.653  26.723  1.00 35.66           N  
ATOM   1963  N   GLU A 311      -5.269  25.547  27.838  1.00 33.64           N  
ATOM   1964  CA  GLU A 311      -4.452  26.627  28.399  1.00 35.35           C  
ATOM   1965  C   GLU A 311      -3.002  26.674  27.935  1.00 32.87           C  
ATOM   1966  O   GLU A 311      -2.346  27.700  28.079  1.00 32.37           O  
ATOM   1967  CB  GLU A 311      -4.469  26.567  29.933  1.00 39.06           C  
ATOM   1968  CG  GLU A 311      -5.847  26.746  30.545  1.00 46.82           C  
ATOM   1969  CD  GLU A 311      -6.550  27.989  30.029  1.00 52.74           C  
ATOM   1970  OE1 GLU A 311      -6.090  29.112  30.345  1.00 55.51           O  
ATOM   1971  OE2 GLU A 311      -7.559  27.842  29.299  1.00 55.66           O  
ATOM   1972  N   ILE A 312      -2.497  25.575  27.389  1.00 30.29           N  
ATOM   1973  CA  ILE A 312      -1.114  25.535  26.937  1.00 29.95           C  
ATOM   1974  C   ILE A 312      -0.892  26.310  25.642  1.00 27.96           C  
ATOM   1975  O   ILE A 312      -1.493  25.998  24.612  1.00 28.95           O  
ATOM   1976  CB  ILE A 312      -0.648  24.089  26.708  1.00 32.77           C  
ATOM   1977  CG1 ILE A 312      -0.751  23.282  28.011  1.00 33.81           C  
ATOM   1978  CG2 ILE A 312       0.774  24.092  26.165  1.00 33.59           C  
ATOM   1979  CD1 ILE A 312       0.122  23.795  29.139  1.00 35.32           C  
ATOM   1980  N   LYS A 313      -0.026  27.317  25.694  1.00 25.57           N  
ATOM   1981  CA  LYS A 313       0.287  28.133  24.514  1.00 26.38           C  
ATOM   1982  C   LYS A 313       1.787  28.386  24.393  1.00 25.15           C  
ATOM   1983  O   LYS A 313       2.321  29.308  25.007  1.00 25.24           O  
ATOM   1984  CB  LYS A 313      -0.437  29.484  24.571  1.00 24.01           C  
ATOM   1985  CG  LYS A 313      -1.949  29.399  24.569  1.00 25.78           C  
ATOM   1986  CD  LYS A 313      -2.551  30.796  24.665  1.00 29.15           C  
ATOM   1987  CE  LYS A 313      -4.064  30.743  24.782  1.00 29.93           C  
ATOM   1988  NZ  LYS A 313      -4.639  32.116  24.796  1.00 32.38           N  
ATOM   1989  N   HIS A 314       2.463  27.563  23.601  1.00 24.62           N  
ATOM   1990  CA  HIS A 314       3.898  27.706  23.398  1.00 23.02           C  
ATOM   1991  C   HIS A 314       4.272  27.020  22.088  1.00 23.96           C  
ATOM   1992  O   HIS A 314       3.784  25.925  21.787  1.00 24.19           O  
ATOM   1993  CB  HIS A 314       4.672  27.089  24.573  1.00 22.60           C  
ATOM   1994  CG  HIS A 314       6.144  27.330  24.509  1.00 22.20           C  
ATOM   1995  ND1 HIS A 314       6.975  26.634  23.656  1.00 22.25           N  
ATOM   1996  CD2 HIS A 314       6.924  28.245  25.135  1.00 21.03           C  
ATOM   1997  CE1 HIS A 314       8.203  27.112  23.761  1.00 23.71           C  
ATOM   1998  NE2 HIS A 314       8.198  28.090  24.651  1.00 20.98           N  
ATOM   1999  N   PRO A 315       5.142  27.659  21.292  1.00 21.93           N  
ATOM   2000  CA  PRO A 315       5.611  27.163  19.996  1.00 22.92           C  
ATOM   2001  C   PRO A 315       6.107  25.724  19.986  1.00 24.00           C  
ATOM   2002  O   PRO A 315       6.030  25.055  18.959  1.00 23.36           O  
ATOM   2003  CB  PRO A 315       6.739  28.131  19.632  1.00 21.90           C  
ATOM   2004  CG  PRO A 315       6.338  29.384  20.304  1.00 26.90           C  
ATOM   2005  CD  PRO A 315       5.839  28.905  21.650  1.00 24.25           C  
ATOM   2006  N   ASN A 316       6.619  25.251  21.120  1.00 23.46           N  
ATOM   2007  CA  ASN A 316       7.167  23.904  21.179  1.00 23.69           C  
ATOM   2008  C   ASN A 316       6.437  22.886  22.046  1.00 24.65           C  
ATOM   2009  O   ASN A 316       7.028  21.902  22.494  1.00 25.82           O  
ATOM   2010  CB  ASN A 316       8.636  23.973  21.584  1.00 21.88           C  
ATOM   2011  CG  ASN A 316       9.413  24.948  20.741  1.00 22.97           C  
ATOM   2012  OD1 ASN A 316       9.615  26.101  21.131  1.00 23.11           O  
ATOM   2013  ND2 ASN A 316       9.843  24.502  19.563  1.00 25.46           N  
ATOM   2014  N   LEU A 317       5.160  23.137  22.300  1.00 24.70           N  
ATOM   2015  CA  LEU A 317       4.322  22.204  23.040  1.00 24.95           C  
ATOM   2016  C   LEU A 317       3.213  21.882  22.037  1.00 25.79           C  
ATOM   2017  O   LEU A 317       2.701  22.785  21.376  1.00 25.67           O  
ATOM   2018  CB  LEU A 317       3.765  22.853  24.312  1.00 22.86           C  
ATOM   2019  CG  LEU A 317       4.802  22.877  25.444  1.00 24.07           C  
ATOM   2020  CD1 LEU A 317       4.328  23.733  26.606  1.00 23.34           C  
ATOM   2021  CD2 LEU A 317       5.060  21.450  25.895  1.00 22.58           C  
ATOM   2022  N   VAL A 318       2.867  20.606  21.888  1.00 25.16           N  
ATOM   2023  CA  VAL A 318       1.842  20.236  20.917  1.00 26.30           C  
ATOM   2024  C   VAL A 318       0.534  20.982  21.164  1.00 26.77           C  
ATOM   2025  O   VAL A 318      -0.035  20.941  22.256  1.00 25.39           O  
ATOM   2026  CB  VAL A 318       1.609  18.708  20.900  1.00 26.06           C  
ATOM   2027  CG1 VAL A 318       0.608  18.340  19.805  1.00 24.79           C  
ATOM   2028  CG2 VAL A 318       2.928  18.005  20.635  1.00 23.68           C  
ATOM   2029  N   GLN A 319       0.073  21.667  20.120  1.00 26.45           N  
ATOM   2030  CA  GLN A 319      -1.126  22.489  20.178  1.00 24.84           C  
ATOM   2031  C   GLN A 319      -2.454  21.774  19.998  1.00 26.03           C  
ATOM   2032  O   GLN A 319      -2.614  20.937  19.109  1.00 27.96           O  
ATOM   2033  CB  GLN A 319      -1.029  23.604  19.130  1.00 23.88           C  
ATOM   2034  CG  GLN A 319      -2.215  24.555  19.118  1.00 23.61           C  
ATOM   2035  CD  GLN A 319      -2.467  25.155  20.495  1.00 24.33           C  
ATOM   2036  OE1 GLN A 319      -1.526  25.494  21.214  1.00 26.89           O  
ATOM   2037  NE2 GLN A 319      -3.730  25.295  20.861  1.00 21.05           N  
ATOM   2038  N   LEU A 320      -3.410  22.138  20.847  1.00 26.45           N  
ATOM   2039  CA  LEU A 320      -4.756  21.599  20.796  1.00 27.86           C  
ATOM   2040  C   LEU A 320      -5.495  22.303  19.652  1.00 28.96           C  
ATOM   2041  O   LEU A 320      -5.321  23.510  19.450  1.00 29.68           O  
ATOM   2042  CB  LEU A 320      -5.470  21.885  22.117  1.00 26.47           C  
ATOM   2043  CG  LEU A 320      -6.942  21.470  22.252  1.00 26.79           C  
ATOM   2044  CD1 LEU A 320      -7.049  19.950  22.314  1.00 24.26           C  
ATOM   2045  CD2 LEU A 320      -7.533  22.088  23.523  1.00 24.84           C  
ATOM   2046  N   LEU A 321      -6.301  21.558  18.900  1.00 28.78           N  
ATOM   2047  CA  LEU A 321      -7.076  22.147  17.806  1.00 30.18           C  
ATOM   2048  C   LEU A 321      -8.576  22.108  18.125  1.00 30.79           C  
ATOM   2049  O   LEU A 321      -9.331  22.981  17.702  1.00 32.55           O  
ATOM   2050  CB  LEU A 321      -6.817  21.410  16.490  1.00 29.68           C  
ATOM   2051  CG  LEU A 321      -5.399  21.429  15.910  1.00 28.91           C  
ATOM   2052  CD1 LEU A 321      -5.430  20.729  14.563  1.00 26.90           C  
ATOM   2053  CD2 LEU A 321      -4.885  22.862  15.754  1.00 28.17           C  
ATOM   2054  N   GLY A 322      -8.998  21.097  18.878  1.00 30.28           N  
ATOM   2055  CA  GLY A 322     -10.399  20.976  19.236  1.00 30.37           C  
ATOM   2056  C   GLY A 322     -10.679  19.776  20.119  1.00 31.50           C  
ATOM   2057  O   GLY A 322      -9.776  18.991  20.408  1.00 31.64           O  
ATOM   2058  N   VAL A 323     -11.929  19.635  20.553  1.00 32.55           N  
ATOM   2059  CA  VAL A 323     -12.328  18.514  21.403  1.00 32.90           C  
ATOM   2060  C   VAL A 323     -13.768  18.073  21.130  1.00 34.06           C  
ATOM   2061  O   VAL A 323     -14.569  18.826  20.579  1.00 33.74           O  
ATOM   2062  CB  VAL A 323     -12.249  18.875  22.911  1.00 32.81           C  
ATOM   2063  CG1 VAL A 323     -10.837  19.305  23.283  1.00 32.24           C  
ATOM   2064  CG2 VAL A 323     -13.264  19.968  23.243  1.00 27.60           C  
ATOM   2065  N   CYS A 324     -14.080  16.842  21.519  1.00 35.09           N  
ATOM   2066  CA  CYS A 324     -15.429  16.292  21.385  1.00 38.72           C  
ATOM   2067  C   CYS A 324     -15.710  15.708  22.757  1.00 40.74           C  
ATOM   2068  O   CYS A 324     -15.419  14.539  23.012  1.00 40.29           O  
ATOM   2069  CB  CYS A 324     -15.484  15.184  20.329  1.00 38.48           C  
ATOM   2070  SG  CYS A 324     -15.131  15.741  18.644  1.00 42.22           S  
ATOM   2071  N   THR A 325     -16.256  16.537  23.642  1.00 44.46           N  
ATOM   2072  CA  THR A 325     -16.549  16.116  25.008  1.00 48.98           C  
ATOM   2073  C   THR A 325     -18.031  16.211  25.367  1.00 51.89           C  
ATOM   2074  O   THR A 325     -18.420  15.971  26.510  1.00 52.88           O  
ATOM   2075  CB  THR A 325     -15.736  16.954  26.013  1.00 48.55           C  
ATOM   2076  OG1 THR A 325     -16.149  18.323  25.936  1.00 49.91           O  
ATOM   2077  CG2 THR A 325     -14.244  16.869  25.693  1.00 47.48           C  
ATOM   2078  N   ARG A 326     -18.855  16.557  24.387  1.00 56.06           N  
ATOM   2079  CA  ARG A 326     -20.295  16.672  24.596  1.00 59.02           C  
ATOM   2080  C   ARG A 326     -20.891  15.314  24.953  1.00 59.42           C  
ATOM   2081  O   ARG A 326     -21.756  15.207  25.824  1.00 60.63           O  
ATOM   2082  CB  ARG A 326     -20.960  17.212  23.327  1.00 61.83           C  
ATOM   2083  CG  ARG A 326     -20.880  18.724  23.172  1.00 65.20           C  
ATOM   2084  CD  ARG A 326     -21.933  19.400  24.032  1.00 69.15           C  
ATOM   2085  NE  ARG A 326     -23.261  18.863  23.744  1.00 72.00           N  
ATOM   2086  CZ  ARG A 326     -24.380  19.258  24.346  1.00 74.17           C  
ATOM   2087  NH1 ARG A 326     -24.341  20.205  25.278  1.00 74.08           N  
ATOM   2088  NH2 ARG A 326     -25.540  18.697  24.022  1.00 75.35           N  
ATOM   2089  N   GLU A 327     -20.417  14.277  24.274  1.00 59.64           N  
ATOM   2090  CA  GLU A 327     -20.886  12.917  24.492  1.00 59.16           C  
ATOM   2091  C   GLU A 327     -19.808  11.932  24.059  1.00 57.81           C  
ATOM   2092  O   GLU A 327     -18.902  12.294  23.311  1.00 58.60           O  
ATOM   2093  CB  GLU A 327     -22.167  12.669  23.692  1.00 61.52           C  
ATOM   2094  CG  GLU A 327     -22.119  13.192  22.259  1.00 64.88           C  
ATOM   2095  CD  GLU A 327     -22.594  12.165  21.240  1.00 67.82           C  
ATOM   2096  OE1 GLU A 327     -23.583  11.454  21.520  1.00 68.91           O  
ATOM   2097  OE2 GLU A 327     -21.988  12.078  20.150  1.00 68.85           O  
ATOM   2098  N   PRO A 328     -19.879  10.680  24.537  1.00 55.70           N  
ATOM   2099  CA  PRO A 328     -18.893   9.654  24.183  1.00 52.86           C  
ATOM   2100  C   PRO A 328     -18.991   9.223  22.724  1.00 50.67           C  
ATOM   2101  O   PRO A 328     -20.066   9.276  22.127  1.00 51.41           O  
ATOM   2102  CB  PRO A 328     -19.233   8.512  25.138  1.00 53.58           C  
ATOM   2103  CG  PRO A 328     -19.829   9.212  26.312  1.00 54.26           C  
ATOM   2104  CD  PRO A 328     -20.726  10.217  25.646  1.00 55.52           C  
ATOM   2105  N   PRO A 329     -17.864   8.799  22.129  1.00 47.98           N  
ATOM   2106  CA  PRO A 329     -16.539   8.719  22.756  1.00 46.12           C  
ATOM   2107  C   PRO A 329     -15.875  10.095  22.761  1.00 42.77           C  
ATOM   2108  O   PRO A 329     -15.977  10.840  21.788  1.00 40.34           O  
ATOM   2109  CB  PRO A 329     -15.783   7.733  21.857  1.00 45.78           C  
ATOM   2110  CG  PRO A 329     -16.861   6.988  21.138  1.00 46.89           C  
ATOM   2111  CD  PRO A 329     -17.866   8.063  20.858  1.00 47.09           C  
ATOM   2112  N   PHE A 330     -15.191  10.420  23.851  1.00 40.39           N  
ATOM   2113  CA  PHE A 330     -14.517  11.705  23.970  1.00 39.48           C  
ATOM   2114  C   PHE A 330     -13.245  11.791  23.132  1.00 36.95           C  
ATOM   2115  O   PHE A 330     -12.466  10.841  23.066  1.00 34.99           O  
ATOM   2116  CB  PHE A 330     -14.198  11.983  25.439  1.00 40.55           C  
ATOM   2117  CG  PHE A 330     -15.413  12.280  26.276  1.00 44.92           C  
ATOM   2118  CD1 PHE A 330     -15.333  12.283  27.667  1.00 46.04           C  
ATOM   2119  CD2 PHE A 330     -16.634  12.587  25.677  1.00 45.53           C  
ATOM   2120  CE1 PHE A 330     -16.449  12.589  28.447  1.00 46.34           C  
ATOM   2121  CE2 PHE A 330     -17.754  12.896  26.449  1.00 45.70           C  
ATOM   2122  CZ  PHE A 330     -17.660  12.897  27.834  1.00 45.97           C  
ATOM   2123  N   TYR A 331     -13.049  12.941  22.493  1.00 36.00           N  
ATOM   2124  CA  TYR A 331     -11.874  13.179  21.657  1.00 36.83           C  
ATOM   2125  C   TYR A 331     -11.078  14.405  22.094  1.00 36.29           C  
ATOM   2126  O   TYR A 331     -11.625  15.341  22.680  1.00 35.48           O  
ATOM   2127  CB  TYR A 331     -12.264  13.441  20.200  1.00 37.57           C  
ATOM   2128  CG  TYR A 331     -12.715  12.267  19.363  1.00 39.62           C  
ATOM   2129  CD1 TYR A 331     -12.979  12.446  18.000  1.00 40.92           C  
ATOM   2130  CD2 TYR A 331     -12.890  11.001  19.908  1.00 39.28           C  
ATOM   2131  CE1 TYR A 331     -13.404  11.399  17.201  1.00 42.34           C  
ATOM   2132  CE2 TYR A 331     -13.320   9.938  19.114  1.00 43.15           C  
ATOM   2133  CZ  TYR A 331     -13.574  10.149  17.758  1.00 43.79           C  
ATOM   2134  OH  TYR A 331     -13.987   9.116  16.951  1.00 44.18           O  
ATOM   2135  N   ILE A 332      -9.783  14.373  21.784  1.00 35.31           N  
ATOM   2136  CA  ILE A 332      -8.859  15.477  22.014  1.00 34.16           C  
ATOM   2137  C   ILE A 332      -8.108  15.540  20.682  1.00 33.87           C  
ATOM   2138  O   ILE A 332      -7.345  14.633  20.362  1.00 34.57           O  
ATOM   2139  CB  ILE A 332      -7.847  15.201  23.138  1.00 33.31           C  
ATOM   2140  CG1 ILE A 332      -8.539  15.236  24.500  1.00 33.86           C  
ATOM   2141  CG2 ILE A 332      -6.756  16.259  23.105  1.00 30.58           C  
ATOM   2142  CD1 ILE A 332      -7.595  14.987  25.672  1.00 30.91           C  
ATOM   2143  N   ILE A 333      -8.347  16.594  19.905  1.00 32.59           N  
ATOM   2144  CA  ILE A 333      -7.722  16.756  18.594  1.00 30.68           C  
ATOM   2145  C   ILE A 333      -6.611  17.801  18.603  1.00 29.06           C  
ATOM   2146  O   ILE A 333      -6.816  18.940  19.033  1.00 28.42           O  
ATOM   2147  CB  ILE A 333      -8.759  17.174  17.522  1.00 33.01           C  
ATOM   2148  CG1 ILE A 333      -9.911  16.169  17.472  1.00 35.27           C  
ATOM   2149  CG2 ILE A 333      -8.095  17.242  16.157  1.00 33.93           C  
ATOM   2150  CD1 ILE A 333     -10.943  16.345  18.569  1.00 38.54           C  
ATOM   2151  N   THR A 334      -5.441  17.408  18.107  1.00 26.34           N  
ATOM   2152  CA  THR A 334      -4.287  18.292  18.064  1.00 26.37           C  
ATOM   2153  C   THR A 334      -3.657  18.300  16.682  1.00 27.20           C  
ATOM   2154  O   THR A 334      -4.051  17.534  15.800  1.00 27.59           O  
ATOM   2155  CB  THR A 334      -3.200  17.842  19.059  1.00 26.83           C  
ATOM   2156  OG1 THR A 334      -2.572  16.654  18.568  1.00 26.31           O  
ATOM   2157  CG2 THR A 334      -3.804  17.537  20.416  1.00 27.62           C  
ATOM   2158  N   GLU A 335      -2.667  19.167  16.505  1.00 27.92           N  
ATOM   2159  CA  GLU A 335      -1.951  19.256  15.242  1.00 28.50           C  
ATOM   2160  C   GLU A 335      -1.180  17.945  15.061  1.00 29.15           C  
ATOM   2161  O   GLU A 335      -0.856  17.254  16.034  1.00 29.37           O  
ATOM   2162  CB  GLU A 335      -0.970  20.429  15.268  1.00 29.60           C  
ATOM   2163  CG  GLU A 335      -0.012  20.390  16.460  1.00 34.00           C  
ATOM   2164  CD  GLU A 335       1.036  21.496  16.443  1.00 35.71           C  
ATOM   2165  OE1 GLU A 335       1.631  21.761  17.514  1.00 35.87           O  
ATOM   2166  OE2 GLU A 335       1.275  22.087  15.368  1.00 37.34           O  
ATOM   2167  N   PHE A 336      -0.891  17.603  13.815  1.00 27.59           N  
ATOM   2168  CA  PHE A 336      -0.164  16.386  13.520  1.00 28.51           C  
ATOM   2169  C   PHE A 336       1.307  16.700  13.255  1.00 29.18           C  
ATOM   2170  O   PHE A 336       1.623  17.497  12.377  1.00 30.13           O  
ATOM   2171  CB  PHE A 336      -0.778  15.707  12.293  1.00 29.03           C  
ATOM   2172  CG  PHE A 336      -0.106  14.420  11.909  1.00 30.38           C  
ATOM   2173  CD1 PHE A 336      -0.342  13.252  12.629  1.00 31.02           C  
ATOM   2174  CD2 PHE A 336       0.768  14.375  10.830  1.00 30.56           C  
ATOM   2175  CE1 PHE A 336       0.283  12.056  12.276  1.00 31.32           C  
ATOM   2176  CE2 PHE A 336       1.396  13.186  10.471  1.00 31.33           C  
ATOM   2177  CZ  PHE A 336       1.151  12.025  11.197  1.00 29.31           C  
ATOM   2178  N   MET A 337       2.202  16.101  14.036  1.00 28.62           N  
ATOM   2179  CA  MET A 337       3.630  16.297  13.830  1.00 29.46           C  
ATOM   2180  C   MET A 337       3.966  15.214  12.802  1.00 30.82           C  
ATOM   2181  O   MET A 337       3.875  14.013  13.088  1.00 28.43           O  
ATOM   2182  CB  MET A 337       4.394  16.081  15.136  1.00 29.01           C  
ATOM   2183  CG  MET A 337       3.983  17.036  16.255  1.00 30.80           C  
ATOM   2184  SD  MET A 337       3.994  18.803  15.770  1.00 31.45           S  
ATOM   2185  CE  MET A 337       5.720  19.028  15.359  1.00 26.03           C  
ATOM   2186  N   THR A 338       4.344  15.645  11.603  1.00 29.94           N  
ATOM   2187  CA  THR A 338       4.605  14.718  10.503  1.00 33.05           C  
ATOM   2188  C   THR A 338       5.788  13.756  10.577  1.00 31.86           C  
ATOM   2189  O   THR A 338       5.768  12.714   9.925  1.00 30.90           O  
ATOM   2190  CB  THR A 338       4.704  15.482   9.169  1.00 32.57           C  
ATOM   2191  OG1 THR A 338       5.855  16.331   9.195  1.00 38.66           O  
ATOM   2192  CG2 THR A 338       3.481  16.354   8.967  1.00 33.92           C  
ATOM   2193  N   TYR A 339       6.813  14.062  11.360  1.00 32.04           N  
ATOM   2194  CA  TYR A 339       7.945  13.152  11.392  1.00 31.24           C  
ATOM   2195  C   TYR A 339       8.101  12.216  12.582  1.00 30.45           C  
ATOM   2196  O   TYR A 339       9.185  11.687  12.811  1.00 33.14           O  
ATOM   2197  CB  TYR A 339       9.232  13.933  11.163  1.00 35.37           C  
ATOM   2198  CG  TYR A 339       9.261  14.595   9.805  1.00 40.93           C  
ATOM   2199  CD1 TYR A 339       8.724  15.870   9.613  1.00 41.05           C  
ATOM   2200  CD2 TYR A 339       9.775  13.924   8.693  1.00 43.76           C  
ATOM   2201  CE1 TYR A 339       8.696  16.459   8.347  1.00 44.35           C  
ATOM   2202  CE2 TYR A 339       9.749  14.505   7.421  1.00 45.12           C  
ATOM   2203  CZ  TYR A 339       9.208  15.769   7.258  1.00 45.93           C  
ATOM   2204  OH  TYR A 339       9.168  16.343   6.005  1.00 49.51           O  
ATOM   2205  N   GLY A 340       7.029  11.977  13.326  1.00 26.90           N  
ATOM   2206  CA  GLY A 340       7.136  11.071  14.458  1.00 26.21           C  
ATOM   2207  C   GLY A 340       7.972  11.589  15.612  1.00 27.75           C  
ATOM   2208  O   GLY A 340       8.266  12.784  15.689  1.00 28.51           O  
ATOM   2209  N   ASN A 341       8.372  10.691  16.510  1.00 27.81           N  
ATOM   2210  CA  ASN A 341       9.145  11.095  17.676  1.00 27.48           C  
ATOM   2211  C   ASN A 341      10.632  11.316  17.399  1.00 28.11           C  
ATOM   2212  O   ASN A 341      11.198  10.761  16.457  1.00 27.92           O  
ATOM   2213  CB  ASN A 341       8.955  10.083  18.814  1.00 29.29           C  
ATOM   2214  CG  ASN A 341       9.618   8.744  18.532  1.00 29.63           C  
ATOM   2215  OD1 ASN A 341      10.846   8.646  18.458  1.00 30.06           O  
ATOM   2216  ND2 ASN A 341       8.806   7.707  18.375  1.00 28.43           N  
ATOM   2217  N   LEU A 342      11.254  12.137  18.241  1.00 27.63           N  
ATOM   2218  CA  LEU A 342      12.660  12.482  18.107  1.00 26.29           C  
ATOM   2219  C   LEU A 342      13.604  11.301  18.230  1.00 26.58           C  
ATOM   2220  O   LEU A 342      14.667  11.303  17.622  1.00 26.10           O  
ATOM   2221  CB  LEU A 342      13.034  13.549  19.141  1.00 26.50           C  
ATOM   2222  CG  LEU A 342      14.461  14.102  19.131  1.00 26.25           C  
ATOM   2223  CD1 LEU A 342      14.764  14.813  17.809  1.00 24.83           C  
ATOM   2224  CD2 LEU A 342      14.613  15.060  20.292  1.00 25.08           C  
ATOM   2225  N   LEU A 343      13.227  10.294  19.012  1.00 26.84           N  
ATOM   2226  CA  LEU A 343      14.086   9.133  19.176  1.00 28.48           C  
ATOM   2227  C   LEU A 343      14.276   8.394  17.846  1.00 29.06           C  
ATOM   2228  O   LEU A 343      15.404   8.135  17.429  1.00 26.20           O  
ATOM   2229  CB  LEU A 343      13.510   8.182  20.236  1.00 30.87           C  
ATOM   2230  CG  LEU A 343      14.354   6.928  20.535  1.00 34.14           C  
ATOM   2231  CD1 LEU A 343      15.770   7.332  20.928  1.00 34.25           C  
ATOM   2232  CD2 LEU A 343      13.711   6.115  21.655  1.00 34.52           C  
ATOM   2233  N   ASP A 344      13.173   8.060  17.180  1.00 29.49           N  
ATOM   2234  CA  ASP A 344      13.256   7.367  15.905  1.00 29.64           C  
ATOM   2235  C   ASP A 344      13.921   8.264  14.861  1.00 30.07           C  
ATOM   2236  O   ASP A 344      14.713   7.792  14.036  1.00 29.57           O  
ATOM   2237  CB  ASP A 344      11.859   6.957  15.404  1.00 32.23           C  
ATOM   2238  CG  ASP A 344      11.179   5.928  16.303  1.00 33.17           C  
ATOM   2239  OD1 ASP A 344      11.861   5.004  16.798  1.00 34.63           O  
ATOM   2240  OD2 ASP A 344       9.950   6.034  16.501  1.00 35.48           O  
ATOM   2241  N   TYR A 345      13.601   9.556  14.896  1.00 28.26           N  
ATOM   2242  CA  TYR A 345      14.171  10.499  13.932  1.00 29.07           C  
ATOM   2243  C   TYR A 345      15.688  10.536  14.013  1.00 28.27           C  
ATOM   2244  O   TYR A 345      16.367  10.484  12.990  1.00 26.73           O  
ATOM   2245  CB  TYR A 345      13.642  11.914  14.161  1.00 30.19           C  
ATOM   2246  CG  TYR A 345      14.123  12.897  13.115  1.00 30.36           C  
ATOM   2247  CD1 TYR A 345      13.449  13.041  11.900  1.00 30.79           C  
ATOM   2248  CD2 TYR A 345      15.277  13.656  13.323  1.00 31.50           C  
ATOM   2249  CE1 TYR A 345      13.919  13.922  10.913  1.00 31.72           C  
ATOM   2250  CE2 TYR A 345      15.755  14.537  12.346  1.00 31.09           C  
ATOM   2251  CZ  TYR A 345      15.072  14.663  11.146  1.00 31.93           C  
ATOM   2252  OH  TYR A 345      15.545  15.521  10.181  1.00 33.07           O  
ATOM   2253  N   LEU A 346      16.208  10.640  15.234  1.00 28.33           N  
ATOM   2254  CA  LEU A 346      17.652  10.684  15.476  1.00 29.92           C  
ATOM   2255  C   LEU A 346      18.344   9.430  14.955  1.00 32.04           C  
ATOM   2256  O   LEU A 346      19.440   9.500  14.399  1.00 32.01           O  
ATOM   2257  CB  LEU A 346      17.943  10.813  16.975  1.00 26.75           C  
ATOM   2258  CG  LEU A 346      17.593  12.135  17.664  1.00 27.96           C  
ATOM   2259  CD1 LEU A 346      17.655  11.966  19.188  1.00 27.47           C  
ATOM   2260  CD2 LEU A 346      18.557  13.211  17.210  1.00 25.93           C  
ATOM   2261  N   ARG A 347      17.694   8.287  15.138  1.00 33.46           N  
ATOM   2262  CA  ARG A 347      18.255   7.013  14.716  1.00 35.21           C  
ATOM   2263  C   ARG A 347      18.251   6.758  13.214  1.00 35.65           C  
ATOM   2264  O   ARG A 347      19.077   6.001  12.712  1.00 36.13           O  
ATOM   2265  CB  ARG A 347      17.519   5.870  15.422  1.00 35.85           C  
ATOM   2266  CG  ARG A 347      17.789   5.795  16.912  1.00 36.46           C  
ATOM   2267  CD  ARG A 347      16.946   4.724  17.590  1.00 36.51           C  
ATOM   2268  NE  ARG A 347      17.232   4.653  19.021  1.00 37.22           N  
ATOM   2269  CZ  ARG A 347      16.680   3.780  19.861  1.00 41.33           C  
ATOM   2270  NH1 ARG A 347      15.797   2.891  19.419  1.00 40.95           N  
ATOM   2271  NH2 ARG A 347      17.020   3.787  21.149  1.00 40.03           N  
ATOM   2272  N   GLU A 348      17.336   7.398  12.499  1.00 36.53           N  
ATOM   2273  CA  GLU A 348      17.209   7.195  11.063  1.00 38.87           C  
ATOM   2274  C   GLU A 348      17.680   8.364  10.206  1.00 39.52           C  
ATOM   2275  O   GLU A 348      17.727   8.257   8.980  1.00 40.25           O  
ATOM   2276  CB  GLU A 348      15.743   6.919  10.720  1.00 40.68           C  
ATOM   2277  CG  GLU A 348      15.121   5.757  11.470  1.00 46.18           C  
ATOM   2278  CD  GLU A 348      13.600   5.767  11.396  1.00 50.32           C  
ATOM   2279  OE1 GLU A 348      13.051   5.771  10.268  1.00 51.71           O  
ATOM   2280  OE2 GLU A 348      12.952   5.772  12.468  1.00 51.89           O  
ATOM   2281  N   CYS A 349      18.027   9.476  10.839  1.00 37.48           N  
ATOM   2282  CA  CYS A 349      18.431  10.655  10.094  1.00 36.59           C  
ATOM   2283  C   CYS A 349      19.790  10.570   9.432  1.00 37.53           C  
ATOM   2284  O   CYS A 349      20.640   9.765   9.803  1.00 37.45           O  
ATOM   2285  CB  CYS A 349      18.431  11.880  11.007  1.00 35.23           C  
ATOM   2286  SG  CYS A 349      19.866  11.945  12.124  1.00 35.67           S  
ATOM   2287  N   ASN A 350      19.976  11.434   8.443  1.00 38.83           N  
ATOM   2288  CA  ASN A 350      21.234  11.559   7.726  1.00 38.54           C  
ATOM   2289  C   ASN A 350      22.041  12.513   8.608  1.00 38.61           C  
ATOM   2290  O   ASN A 350      21.750  13.708   8.673  1.00 38.16           O  
ATOM   2291  CB  ASN A 350      20.971  12.180   6.358  1.00 39.72           C  
ATOM   2292  CG  ASN A 350      22.242  12.562   5.630  1.00 42.05           C  
ATOM   2293  OD1 ASN A 350      23.343  12.473   6.172  1.00 47.02           O  
ATOM   2294  ND2 ASN A 350      22.092  13.007   4.391  1.00 43.96           N  
ATOM   2295  N   ARG A 351      23.048  11.981   9.290  1.00 39.54           N  
ATOM   2296  CA  ARG A 351      23.859  12.779  10.202  1.00 39.49           C  
ATOM   2297  C   ARG A 351      24.634  13.942   9.609  1.00 41.66           C  
ATOM   2298  O   ARG A 351      25.182  14.767  10.345  1.00 39.33           O  
ATOM   2299  CB  ARG A 351      24.800  11.867  10.977  1.00 37.72           C  
ATOM   2300  CG  ARG A 351      24.043  10.837  11.790  1.00 37.52           C  
ATOM   2301  CD  ARG A 351      24.940  10.108  12.744  1.00 36.05           C  
ATOM   2302  NE  ARG A 351      24.243   8.976  13.330  1.00 38.36           N  
ATOM   2303  CZ  ARG A 351      24.794   8.138  14.196  1.00 38.96           C  
ATOM   2304  NH1 ARG A 351      26.053   8.316  14.574  1.00 39.28           N  
ATOM   2305  NH2 ARG A 351      24.093   7.123  14.677  1.00 38.06           N  
ATOM   2306  N   GLN A 352      24.685  14.020   8.286  1.00 44.16           N  
ATOM   2307  CA  GLN A 352      25.388  15.122   7.650  1.00 47.02           C  
ATOM   2308  C   GLN A 352      24.436  16.310   7.600  1.00 47.16           C  
ATOM   2309  O   GLN A 352      24.853  17.458   7.742  1.00 48.22           O  
ATOM   2310  CB  GLN A 352      25.836  14.731   6.242  1.00 49.86           C  
ATOM   2311  CG  GLN A 352      26.779  13.538   6.210  1.00 57.15           C  
ATOM   2312  CD  GLN A 352      28.060  13.761   7.014  1.00 60.58           C  
ATOM   2313  OE1 GLN A 352      28.910  12.871   7.105  1.00 62.49           O  
ATOM   2314  NE2 GLN A 352      28.204  14.948   7.596  1.00 61.66           N  
ATOM   2315  N   GLU A 353      23.153  16.023   7.398  1.00 45.77           N  
ATOM   2316  CA  GLU A 353      22.129  17.061   7.354  1.00 44.45           C  
ATOM   2317  C   GLU A 353      21.807  17.475   8.785  1.00 42.25           C  
ATOM   2318  O   GLU A 353      21.690  18.662   9.096  1.00 43.25           O  
ATOM   2319  CB  GLU A 353      20.854  16.535   6.685  1.00 45.77           C  
ATOM   2320  CG  GLU A 353      19.632  17.427   6.923  1.00 51.64           C  
ATOM   2321  CD  GLU A 353      18.309  16.776   6.518  1.00 53.33           C  
ATOM   2322  OE1 GLU A 353      17.240  17.358   6.817  1.00 53.65           O  
ATOM   2323  OE2 GLU A 353      18.337  15.689   5.903  1.00 54.16           O  
ATOM   2324  N   VAL A 354      21.663  16.481   9.652  1.00 38.55           N  
ATOM   2325  CA  VAL A 354      21.347  16.725  11.051  1.00 35.55           C  
ATOM   2326  C   VAL A 354      22.647  16.768  11.837  1.00 35.84           C  
ATOM   2327  O   VAL A 354      22.953  15.855  12.610  1.00 36.14           O  
ATOM   2328  CB  VAL A 354      20.434  15.608  11.600  1.00 33.45           C  
ATOM   2329  CG1 VAL A 354      20.026  15.906  13.024  1.00 32.20           C  
ATOM   2330  CG2 VAL A 354      19.209  15.479  10.717  1.00 32.50           C  
ATOM   2331  N   ASN A 355      23.419  17.831  11.627  1.00 34.69           N  
ATOM   2332  CA  ASN A 355      24.696  17.977  12.314  1.00 33.84           C  
ATOM   2333  C   ASN A 355      24.536  18.599  13.691  1.00 30.92           C  
ATOM   2334  O   ASN A 355      23.417  18.798  14.167  1.00 32.91           O  
ATOM   2335  CB  ASN A 355      25.675  18.809  11.475  1.00 34.95           C  
ATOM   2336  CG  ASN A 355      25.131  20.176  11.130  1.00 39.39           C  
ATOM   2337  OD1 ASN A 355      24.606  20.890  11.990  1.00 39.38           O  
ATOM   2338  ND2 ASN A 355      25.258  20.555   9.862  1.00 40.85           N  
ATOM   2339  N   ALA A 356      25.664  18.905  14.320  1.00 29.14           N  
ATOM   2340  CA  ALA A 356      25.680  19.480  15.660  1.00 28.28           C  
ATOM   2341  C   ALA A 356      24.842  20.746  15.805  1.00 27.25           C  
ATOM   2342  O   ALA A 356      24.201  20.947  16.835  1.00 26.42           O  
ATOM   2343  CB  ALA A 356      27.125  19.749  16.093  1.00 28.28           C  
ATOM   2344  N   VAL A 357      24.858  21.607  14.788  1.00 26.82           N  
ATOM   2345  CA  VAL A 357      24.079  22.844  14.830  1.00 23.79           C  
ATOM   2346  C   VAL A 357      22.588  22.531  15.004  1.00 24.29           C  
ATOM   2347  O   VAL A 357      21.875  23.233  15.735  1.00 22.60           O  
ATOM   2348  CB  VAL A 357      24.288  23.679  13.538  1.00 26.17           C  
ATOM   2349  CG1 VAL A 357      23.102  24.625  13.308  1.00 22.26           C  
ATOM   2350  CG2 VAL A 357      25.576  24.487  13.651  1.00 26.73           C  
ATOM   2351  N   VAL A 358      22.125  21.479  14.332  1.00 22.27           N  
ATOM   2352  CA  VAL A 358      20.721  21.062  14.413  1.00 22.76           C  
ATOM   2353  C   VAL A 358      20.383  20.430  15.767  1.00 21.66           C  
ATOM   2354  O   VAL A 358      19.319  20.677  16.331  1.00 20.79           O  
ATOM   2355  CB  VAL A 358      20.373  20.022  13.331  1.00 23.53           C  
ATOM   2356  CG1 VAL A 358      18.888  19.710  13.396  1.00 21.84           C  
ATOM   2357  CG2 VAL A 358      20.782  20.529  11.944  1.00 19.35           C  
ATOM   2358  N   LEU A 359      21.281  19.592  16.273  1.00 21.81           N  
ATOM   2359  CA  LEU A 359      21.059  18.951  17.561  1.00 22.94           C  
ATOM   2360  C   LEU A 359      20.857  20.040  18.618  1.00 24.08           C  
ATOM   2361  O   LEU A 359      19.928  19.974  19.422  1.00 25.14           O  
ATOM   2362  CB  LEU A 359      22.258  18.063  17.928  1.00 22.37           C  
ATOM   2363  CG  LEU A 359      22.515  16.840  17.030  1.00 26.15           C  
ATOM   2364  CD1 LEU A 359      23.589  15.943  17.652  1.00 24.21           C  
ATOM   2365  CD2 LEU A 359      21.217  16.052  16.853  1.00 23.29           C  
ATOM   2366  N   LEU A 360      21.720  21.051  18.596  1.00 24.50           N  
ATOM   2367  CA  LEU A 360      21.639  22.159  19.547  1.00 25.06           C  
ATOM   2368  C   LEU A 360      20.325  22.899  19.365  1.00 25.23           C  
ATOM   2369  O   LEU A 360      19.672  23.302  20.336  1.00 25.66           O  
ATOM   2370  CB  LEU A 360      22.800  23.118  19.319  1.00 27.48           C  
ATOM   2371  CG  LEU A 360      22.943  24.336  20.229  1.00 27.65           C  
ATOM   2372  CD1 LEU A 360      23.248  23.893  21.661  1.00 29.61           C  
ATOM   2373  CD2 LEU A 360      24.068  25.191  19.701  1.00 27.18           C  
ATOM   2374  N   TYR A 361      19.945  23.081  18.108  1.00 24.26           N  
ATOM   2375  CA  TYR A 361      18.702  23.760  17.781  1.00 24.87           C  
ATOM   2376  C   TYR A 361      17.538  23.013  18.438  1.00 24.41           C  
ATOM   2377  O   TYR A 361      16.674  23.614  19.079  1.00 23.62           O  
ATOM   2378  CB  TYR A 361      18.521  23.799  16.253  1.00 25.73           C  
ATOM   2379  CG  TYR A 361      17.265  24.510  15.784  1.00 28.34           C  
ATOM   2380  CD1 TYR A 361      16.967  25.795  16.224  1.00 29.32           C  
ATOM   2381  CD2 TYR A 361      16.391  23.905  14.879  1.00 28.62           C  
ATOM   2382  CE1 TYR A 361      15.837  26.463  15.774  1.00 31.43           C  
ATOM   2383  CE2 TYR A 361      15.253  24.568  14.421  1.00 27.16           C  
ATOM   2384  CZ  TYR A 361      14.986  25.844  14.872  1.00 31.25           C  
ATOM   2385  OH  TYR A 361      13.877  26.526  14.421  1.00 35.34           O  
ATOM   2386  N   MET A 362      17.532  21.695  18.279  1.00 24.86           N  
ATOM   2387  CA  MET A 362      16.475  20.872  18.842  1.00 26.47           C  
ATOM   2388  C   MET A 362      16.534  20.814  20.365  1.00 25.50           C  
ATOM   2389  O   MET A 362      15.502  20.848  21.023  1.00 26.33           O  
ATOM   2390  CB  MET A 362      16.542  19.461  18.246  1.00 28.83           C  
ATOM   2391  CG  MET A 362      16.477  19.464  16.717  1.00 32.62           C  
ATOM   2392  SD  MET A 362      16.308  17.826  15.956  1.00 41.54           S  
ATOM   2393  CE  MET A 362      17.771  17.033  16.583  1.00 31.94           C  
ATOM   2394  N   ALA A 363      17.733  20.731  20.931  1.00 24.42           N  
ATOM   2395  CA  ALA A 363      17.849  20.672  22.382  1.00 25.77           C  
ATOM   2396  C   ALA A 363      17.367  21.990  22.985  1.00 26.66           C  
ATOM   2397  O   ALA A 363      16.790  22.016  24.075  1.00 28.57           O  
ATOM   2398  CB  ALA A 363      19.300  20.400  22.791  1.00 24.81           C  
ATOM   2399  N   THR A 364      17.602  23.085  22.266  1.00 25.47           N  
ATOM   2400  CA  THR A 364      17.194  24.392  22.741  1.00 25.14           C  
ATOM   2401  C   THR A 364      15.677  24.547  22.706  1.00 24.64           C  
ATOM   2402  O   THR A 364      15.085  25.113  23.623  1.00 24.28           O  
ATOM   2403  CB  THR A 364      17.871  25.499  21.912  1.00 25.11           C  
ATOM   2404  OG1 THR A 364      19.295  25.350  22.020  1.00 26.96           O  
ATOM   2405  CG2 THR A 364      17.478  26.880  22.425  1.00 23.28           C  
ATOM   2406  N   GLN A 365      15.044  24.038  21.654  1.00 25.70           N  
ATOM   2407  CA  GLN A 365      13.589  24.126  21.549  1.00 24.75           C  
ATOM   2408  C   GLN A 365      12.938  23.375  22.700  1.00 23.96           C  
ATOM   2409  O   GLN A 365      11.947  23.835  23.260  1.00 23.89           O  
ATOM   2410  CB  GLN A 365      13.094  23.517  20.239  1.00 24.81           C  
ATOM   2411  CG  GLN A 365      13.428  24.308  19.003  1.00 24.21           C  
ATOM   2412  CD  GLN A 365      12.979  23.586  17.754  1.00 23.79           C  
ATOM   2413  OE1 GLN A 365      11.799  23.598  17.402  1.00 24.19           O  
ATOM   2414  NE2 GLN A 365      13.918  22.935  17.084  1.00 24.80           N  
ATOM   2415  N   ILE A 366      13.482  22.204  23.030  1.00 23.38           N  
ATOM   2416  CA  ILE A 366      12.932  21.405  24.121  1.00 24.64           C  
ATOM   2417  C   ILE A 366      13.081  22.095  25.477  1.00 24.63           C  
ATOM   2418  O   ILE A 366      12.183  22.026  26.311  1.00 26.43           O  
ATOM   2419  CB  ILE A 366      13.593  20.017  24.191  1.00 23.24           C  
ATOM   2420  CG1 ILE A 366      13.293  19.246  22.906  1.00 25.66           C  
ATOM   2421  CG2 ILE A 366      13.067  19.251  25.399  1.00 22.14           C  
ATOM   2422  CD1 ILE A 366      13.977  17.893  22.810  1.00 25.15           C  
ATOM   2423  N   SER A 367      14.206  22.763  25.702  1.00 24.08           N  
ATOM   2424  CA  SER A 367      14.401  23.444  26.980  1.00 24.72           C  
ATOM   2425  C   SER A 367      13.412  24.604  27.083  1.00 25.10           C  
ATOM   2426  O   SER A 367      12.921  24.918  28.170  1.00 25.05           O  
ATOM   2427  CB  SER A 367      15.834  23.968  27.099  1.00 23.46           C  
ATOM   2428  OG  SER A 367      16.129  24.867  26.042  1.00 25.25           O  
ATOM   2429  N   SER A 368      13.121  25.234  25.944  1.00 23.54           N  
ATOM   2430  CA  SER A 368      12.191  26.350  25.922  1.00 23.05           C  
ATOM   2431  C   SER A 368      10.807  25.857  26.347  1.00 23.21           C  
ATOM   2432  O   SER A 368      10.114  26.523  27.115  1.00 22.62           O  
ATOM   2433  CB  SER A 368      12.136  26.978  24.521  1.00 22.76           C  
ATOM   2434  OG  SER A 368      11.349  28.163  24.514  1.00 21.78           O  
ATOM   2435  N   ALA A 369      10.403  24.692  25.852  1.00 22.12           N  
ATOM   2436  CA  ALA A 369       9.104  24.140  26.226  1.00 22.62           C  
ATOM   2437  C   ALA A 369       9.053  23.892  27.736  1.00 22.68           C  
ATOM   2438  O   ALA A 369       8.088  24.256  28.402  1.00 22.96           O  
ATOM   2439  CB  ALA A 369       8.844  22.835  25.474  1.00 20.37           C  
ATOM   2440  N   MET A 370      10.094  23.265  28.273  1.00 23.32           N  
ATOM   2441  CA  MET A 370      10.144  22.980  29.704  1.00 24.00           C  
ATOM   2442  C   MET A 370      10.207  24.249  30.549  1.00 25.28           C  
ATOM   2443  O   MET A 370       9.657  24.290  31.656  1.00 25.88           O  
ATOM   2444  CB  MET A 370      11.335  22.077  30.020  1.00 25.22           C  
ATOM   2445  CG  MET A 370      11.237  20.698  29.368  1.00 25.82           C  
ATOM   2446  SD  MET A 370       9.645  19.899  29.676  1.00 26.86           S  
ATOM   2447  CE  MET A 370       9.688  19.717  31.475  1.00 23.67           C  
ATOM   2448  N   GLU A 371      10.874  25.287  30.048  1.00 25.51           N  
ATOM   2449  CA  GLU A 371      10.928  26.540  30.803  1.00 27.41           C  
ATOM   2450  C   GLU A 371       9.508  27.086  30.949  1.00 27.05           C  
ATOM   2451  O   GLU A 371       9.136  27.607  32.000  1.00 28.44           O  
ATOM   2452  CB  GLU A 371      11.793  27.595  30.099  1.00 29.45           C  
ATOM   2453  CG  GLU A 371      11.911  28.897  30.899  1.00 31.96           C  
ATOM   2454  CD  GLU A 371      12.674  30.003  30.166  1.00 37.21           C  
ATOM   2455  OE1 GLU A 371      12.890  31.078  30.777  1.00 38.91           O  
ATOM   2456  OE2 GLU A 371      13.057  29.811  28.987  1.00 35.72           O  
ATOM   2457  N   TYR A 372       8.718  26.969  29.886  1.00 25.35           N  
ATOM   2458  CA  TYR A 372       7.336  27.445  29.907  1.00 24.85           C  
ATOM   2459  C   TYR A 372       6.534  26.665  30.960  1.00 25.31           C  
ATOM   2460  O   TYR A 372       5.859  27.264  31.788  1.00 26.31           O  
ATOM   2461  CB  TYR A 372       6.704  27.266  28.530  1.00 21.91           C  
ATOM   2462  CG  TYR A 372       5.231  27.612  28.459  1.00 21.66           C  
ATOM   2463  CD1 TYR A 372       4.807  28.918  28.208  1.00 21.82           C  
ATOM   2464  CD2 TYR A 372       4.258  26.621  28.623  1.00 23.65           C  
ATOM   2465  CE1 TYR A 372       3.439  29.232  28.114  1.00 22.78           C  
ATOM   2466  CE2 TYR A 372       2.893  26.921  28.535  1.00 24.04           C  
ATOM   2467  CZ  TYR A 372       2.496  28.227  28.278  1.00 23.02           C  
ATOM   2468  OH  TYR A 372       1.166  28.510  28.171  1.00 21.65           O  
ATOM   2469  N   LEU A 373       6.610  25.335  30.925  1.00 23.85           N  
ATOM   2470  CA  LEU A 373       5.896  24.519  31.907  1.00 26.26           C  
ATOM   2471  C   LEU A 373       6.384  24.861  33.307  1.00 25.84           C  
ATOM   2472  O   LEU A 373       5.590  24.964  34.229  1.00 25.02           O  
ATOM   2473  CB  LEU A 373       6.109  23.019  31.650  1.00 24.56           C  
ATOM   2474  CG  LEU A 373       5.532  22.471  30.343  1.00 24.01           C  
ATOM   2475  CD1 LEU A 373       5.855  20.982  30.208  1.00 22.53           C  
ATOM   2476  CD2 LEU A 373       4.026  22.699  30.329  1.00 22.83           C  
ATOM   2477  N   GLU A 374       7.693  25.044  33.455  1.00 28.30           N  
ATOM   2478  CA  GLU A 374       8.273  25.381  34.752  1.00 30.69           C  
ATOM   2479  C   GLU A 374       7.575  26.600  35.358  1.00 31.04           C  
ATOM   2480  O   GLU A 374       7.088  26.549  36.487  1.00 32.90           O  
ATOM   2481  CB  GLU A 374       9.778  25.650  34.604  1.00 31.63           C  
ATOM   2482  CG  GLU A 374      10.514  25.968  35.907  1.00 34.24           C  
ATOM   2483  CD  GLU A 374      12.040  25.988  35.735  1.00 38.94           C  
ATOM   2484  OE1 GLU A 374      12.562  26.887  35.024  1.00 38.10           O  
ATOM   2485  OE2 GLU A 374      12.719  25.095  36.305  1.00 36.34           O  
ATOM   2486  N   LYS A 375       7.495  27.687  34.600  1.00 30.93           N  
ATOM   2487  CA  LYS A 375       6.869  28.890  35.119  1.00 31.99           C  
ATOM   2488  C   LYS A 375       5.353  28.793  35.235  1.00 32.78           C  
ATOM   2489  O   LYS A 375       4.741  29.554  35.983  1.00 32.39           O  
ATOM   2490  CB  LYS A 375       7.261  30.110  34.278  1.00 36.02           C  
ATOM   2491  CG  LYS A 375       6.538  30.264  32.967  1.00 41.17           C  
ATOM   2492  CD  LYS A 375       6.836  31.634  32.370  1.00 44.99           C  
ATOM   2493  CE  LYS A 375       6.111  31.841  31.046  1.00 49.48           C  
ATOM   2494  NZ  LYS A 375       6.447  33.159  30.425  1.00 52.32           N  
ATOM   2495  N   LYS A 376       4.744  27.859  34.509  1.00 32.26           N  
ATOM   2496  CA  LYS A 376       3.297  27.687  34.583  1.00 32.82           C  
ATOM   2497  C   LYS A 376       2.928  26.688  35.677  1.00 33.43           C  
ATOM   2498  O   LYS A 376       1.767  26.301  35.808  1.00 34.11           O  
ATOM   2499  CB  LYS A 376       2.739  27.209  33.237  1.00 32.73           C  
ATOM   2500  CG  LYS A 376       2.823  28.243  32.124  1.00 33.94           C  
ATOM   2501  CD  LYS A 376       2.099  29.526  32.518  1.00 35.57           C  
ATOM   2502  CE  LYS A 376       2.145  30.554  31.404  1.00 36.99           C  
ATOM   2503  NZ  LYS A 376       1.311  31.751  31.713  1.00 38.72           N  
ATOM   2504  N   ASN A 377       3.924  26.261  36.448  1.00 33.42           N  
ATOM   2505  CA  ASN A 377       3.706  25.315  37.540  1.00 33.97           C  
ATOM   2506  C   ASN A 377       3.177  23.940  37.133  1.00 34.37           C  
ATOM   2507  O   ASN A 377       2.263  23.416  37.766  1.00 35.88           O  
ATOM   2508  CB  ASN A 377       2.756  25.919  38.571  1.00 33.35           C  
ATOM   2509  CG  ASN A 377       3.292  27.185  39.168  1.00 35.06           C  
ATOM   2510  OD1 ASN A 377       4.341  27.181  39.811  1.00 36.14           O  
ATOM   2511  ND2 ASN A 377       2.578  28.289  38.959  1.00 37.51           N  
ATOM   2512  N   PHE A 378       3.745  23.360  36.081  1.00 34.00           N  
ATOM   2513  CA  PHE A 378       3.344  22.028  35.627  1.00 32.10           C  
ATOM   2514  C   PHE A 378       4.572  21.131  35.653  1.00 32.04           C  
ATOM   2515  O   PHE A 378       5.696  21.618  35.498  1.00 32.23           O  
ATOM   2516  CB  PHE A 378       2.856  22.052  34.175  1.00 31.74           C  
ATOM   2517  CG  PHE A 378       1.475  22.602  33.988  1.00 31.86           C  
ATOM   2518  CD1 PHE A 378       1.282  23.806  33.321  1.00 30.28           C  
ATOM   2519  CD2 PHE A 378       0.361  21.894  34.434  1.00 31.39           C  
ATOM   2520  CE1 PHE A 378       0.003  24.299  33.097  1.00 31.70           C  
ATOM   2521  CE2 PHE A 378      -0.924  22.377  34.215  1.00 29.55           C  
ATOM   2522  CZ  PHE A 378      -1.104  23.583  33.545  1.00 30.38           C  
ATOM   2523  N   ILE A 379       4.370  19.834  35.859  1.00 30.07           N  
ATOM   2524  CA  ILE A 379       5.483  18.896  35.794  1.00 31.16           C  
ATOM   2525  C   ILE A 379       5.070  17.873  34.741  1.00 30.94           C  
ATOM   2526  O   ILE A 379       3.878  17.678  34.504  1.00 30.10           O  
ATOM   2527  CB  ILE A 379       5.800  18.194  37.148  1.00 31.45           C  
ATOM   2528  CG1 ILE A 379       4.597  17.415  37.657  1.00 31.14           C  
ATOM   2529  CG2 ILE A 379       6.265  19.222  38.170  1.00 28.41           C  
ATOM   2530  CD1 ILE A 379       4.913  16.651  38.929  1.00 29.88           C  
ATOM   2531  N   HIS A 380       6.051  17.239  34.103  1.00 30.40           N  
ATOM   2532  CA  HIS A 380       5.794  16.273  33.042  1.00 31.19           C  
ATOM   2533  C   HIS A 380       5.908  14.807  33.474  1.00 31.39           C  
ATOM   2534  O   HIS A 380       4.943  14.047  33.369  1.00 32.04           O  
ATOM   2535  CB  HIS A 380       6.744  16.555  31.882  1.00 31.53           C  
ATOM   2536  CG  HIS A 380       6.396  15.822  30.629  1.00 33.00           C  
ATOM   2537  ND1 HIS A 380       6.485  14.452  30.520  1.00 33.66           N  
ATOM   2538  CD2 HIS A 380       5.942  16.267  29.434  1.00 33.88           C  
ATOM   2539  CE1 HIS A 380       6.098  14.084  29.313  1.00 33.89           C  
ATOM   2540  NE2 HIS A 380       5.763  15.164  28.634  1.00 32.90           N  
ATOM   2541  N   ARG A 381       7.095  14.413  33.930  1.00 30.67           N  
ATOM   2542  CA  ARG A 381       7.356  13.058  34.413  1.00 31.36           C  
ATOM   2543  C   ARG A 381       7.615  11.999  33.347  1.00 31.17           C  
ATOM   2544  O   ARG A 381       7.912  10.853  33.678  1.00 31.06           O  
ATOM   2545  CB  ARG A 381       6.217  12.591  35.333  1.00 30.41           C  
ATOM   2546  CG  ARG A 381       6.008  13.470  36.557  1.00 33.83           C  
ATOM   2547  CD  ARG A 381       4.766  13.043  37.325  1.00 38.79           C  
ATOM   2548  NE  ARG A 381       3.584  13.089  36.470  1.00 45.41           N  
ATOM   2549  CZ  ARG A 381       2.593  12.206  36.518  1.00 48.21           C  
ATOM   2550  NH1 ARG A 381       2.642  11.203  37.388  1.00 49.58           N  
ATOM   2551  NH2 ARG A 381       1.560  12.315  35.686  1.00 48.68           N  
ATOM   2552  N   ASN A 382       7.506  12.361  32.075  1.00 30.89           N  
ATOM   2553  CA  ASN A 382       7.769  11.394  31.009  1.00 30.69           C  
ATOM   2554  C   ASN A 382       8.649  12.026  29.931  1.00 27.94           C  
ATOM   2555  O   ASN A 382       8.565  11.675  28.762  1.00 26.82           O  
ATOM   2556  CB  ASN A 382       6.448  10.902  30.400  1.00 34.24           C  
ATOM   2557  CG  ASN A 382       5.733   9.867  31.274  1.00 37.19           C  
ATOM   2558  OD1 ASN A 382       4.509   9.730  31.212  1.00 40.76           O  
ATOM   2559  ND2 ASN A 382       6.493   9.128  32.071  1.00 35.62           N  
ATOM   2560  N   LEU A 383       9.501  12.960  30.335  1.00 26.31           N  
ATOM   2561  CA  LEU A 383      10.374  13.647  29.389  1.00 24.65           C  
ATOM   2562  C   LEU A 383      11.437  12.701  28.855  1.00 24.67           C  
ATOM   2563  O   LEU A 383      12.218  12.143  29.619  1.00 26.56           O  
ATOM   2564  CB  LEU A 383      11.031  14.851  30.069  1.00 24.44           C  
ATOM   2565  CG  LEU A 383      11.816  15.835  29.196  1.00 26.68           C  
ATOM   2566  CD1 LEU A 383      10.983  16.273  27.979  1.00 24.46           C  
ATOM   2567  CD2 LEU A 383      12.201  17.036  30.037  1.00 24.13           C  
ATOM   2568  N   ALA A 384      11.451  12.517  27.541  1.00 21.94           N  
ATOM   2569  CA  ALA A 384      12.412  11.638  26.880  1.00 23.26           C  
ATOM   2570  C   ALA A 384      12.359  11.893  25.382  1.00 22.63           C  
ATOM   2571  O   ALA A 384      11.417  12.499  24.891  1.00 23.09           O  
ATOM   2572  CB  ALA A 384      12.079  10.161  27.169  1.00 19.70           C  
ATOM   2573  N   ALA A 385      13.361  11.419  24.650  1.00 24.82           N  
ATOM   2574  CA  ALA A 385      13.376  11.623  23.206  1.00 25.98           C  
ATOM   2575  C   ALA A 385      12.099  11.099  22.549  1.00 25.39           C  
ATOM   2576  O   ALA A 385      11.537  11.758  21.678  1.00 27.27           O  
ATOM   2577  CB  ALA A 385      14.594  10.953  22.592  1.00 25.97           C  
ATOM   2578  N   ARG A 386      11.642   9.924  22.976  1.00 26.14           N  
ATOM   2579  CA  ARG A 386      10.437   9.299  22.421  1.00 27.22           C  
ATOM   2580  C   ARG A 386       9.174  10.119  22.657  1.00 26.23           C  
ATOM   2581  O   ARG A 386       8.160   9.932  21.971  1.00 23.53           O  
ATOM   2582  CB  ARG A 386      10.224   7.899  23.015  1.00 30.13           C  
ATOM   2583  CG  ARG A 386      10.090   7.905  24.531  1.00 37.40           C  
ATOM   2584  CD  ARG A 386       9.710   6.530  25.114  1.00 41.56           C  
ATOM   2585  NE  ARG A 386       9.732   6.569  26.580  1.00 43.79           N  
ATOM   2586  CZ  ARG A 386      10.840   6.532  27.321  1.00 44.35           C  
ATOM   2587  NH1 ARG A 386      12.034   6.437  26.743  1.00 42.33           N  
ATOM   2588  NH2 ARG A 386      10.756   6.630  28.643  1.00 45.52           N  
ATOM   2589  N   ASN A 387       9.215  11.015  23.636  1.00 24.71           N  
ATOM   2590  CA  ASN A 387       8.044  11.824  23.896  1.00 24.04           C  
ATOM   2591  C   ASN A 387       8.176  13.240  23.352  1.00 24.09           C  
ATOM   2592  O   ASN A 387       7.503  14.164  23.812  1.00 23.06           O  
ATOM   2593  CB  ASN A 387       7.708  11.805  25.385  1.00 24.15           C  
ATOM   2594  CG  ASN A 387       7.259  10.424  25.848  1.00 25.03           C  
ATOM   2595  OD1 ASN A 387       6.523   9.740  25.143  1.00 26.90           O  
ATOM   2596  ND2 ASN A 387       7.692  10.016  27.028  1.00 23.92           N  
ATOM   2597  N   CYS A 388       9.049  13.385  22.357  1.00 21.11           N  
ATOM   2598  CA  CYS A 388       9.251  14.658  21.670  1.00 24.40           C  
ATOM   2599  C   CYS A 388       8.891  14.367  20.221  1.00 24.55           C  
ATOM   2600  O   CYS A 388       9.166  13.275  19.717  1.00 25.13           O  
ATOM   2601  CB  CYS A 388      10.708  15.134  21.779  1.00 24.46           C  
ATOM   2602  SG  CYS A 388      11.151  15.736  23.424  1.00 26.64           S  
ATOM   2603  N   LEU A 389       8.285  15.337  19.553  1.00 23.26           N  
ATOM   2604  CA  LEU A 389       7.851  15.130  18.183  1.00 24.81           C  
ATOM   2605  C   LEU A 389       8.490  16.095  17.200  1.00 24.37           C  
ATOM   2606  O   LEU A 389       8.700  17.269  17.503  1.00 25.15           O  
ATOM   2607  CB  LEU A 389       6.330  15.229  18.134  1.00 24.30           C  
ATOM   2608  CG  LEU A 389       5.647  14.221  19.067  1.00 26.02           C  
ATOM   2609  CD1 LEU A 389       4.151  14.501  19.145  1.00 25.09           C  
ATOM   2610  CD2 LEU A 389       5.903  12.800  18.565  1.00 26.99           C  
ATOM   2611  N   VAL A 390       8.794  15.592  16.013  1.00 24.44           N  
ATOM   2612  CA  VAL A 390       9.446  16.403  14.994  1.00 24.25           C  
ATOM   2613  C   VAL A 390       8.527  16.831  13.851  1.00 25.75           C  
ATOM   2614  O   VAL A 390       7.789  16.023  13.296  1.00 25.38           O  
ATOM   2615  CB  VAL A 390      10.643  15.634  14.402  1.00 24.37           C  
ATOM   2616  CG1 VAL A 390      11.351  16.487  13.358  1.00 24.35           C  
ATOM   2617  CG2 VAL A 390      11.596  15.213  15.525  1.00 22.19           C  
ATOM   2618  N   GLY A 391       8.585  18.114  13.508  1.00 27.29           N  
ATOM   2619  CA  GLY A 391       7.791  18.644  12.415  1.00 28.79           C  
ATOM   2620  C   GLY A 391       8.706  19.181  11.327  1.00 32.26           C  
ATOM   2621  O   GLY A 391       9.890  18.860  11.299  1.00 31.92           O  
ATOM   2622  N   GLU A 392       8.176  20.005  10.430  1.00 33.78           N  
ATOM   2623  CA  GLU A 392       8.983  20.566   9.353  1.00 36.11           C  
ATOM   2624  C   GLU A 392      10.110  21.465   9.864  1.00 36.74           C  
ATOM   2625  O   GLU A 392       9.978  22.122  10.899  1.00 35.33           O  
ATOM   2626  CB  GLU A 392       8.097  21.370   8.400  1.00 39.86           C  
ATOM   2627  CG  GLU A 392       6.986  20.559   7.761  1.00 45.28           C  
ATOM   2628  CD  GLU A 392       7.504  19.410   6.905  1.00 47.44           C  
ATOM   2629  OE1 GLU A 392       8.736  19.264   6.760  1.00 50.71           O  
ATOM   2630  OE2 GLU A 392       6.670  18.648   6.371  1.00 49.86           O  
ATOM   2631  N   ASN A 393      11.212  21.495   9.118  1.00 36.95           N  
ATOM   2632  CA  ASN A 393      12.365  22.331   9.454  1.00 36.31           C  
ATOM   2633  C   ASN A 393      12.922  22.085  10.854  1.00 34.31           C  
ATOM   2634  O   ASN A 393      13.214  23.025  11.600  1.00 34.62           O  
ATOM   2635  CB  ASN A 393      12.009  23.820   9.303  1.00 38.08           C  
ATOM   2636  CG  ASN A 393      11.544  24.174   7.895  1.00 40.61           C  
ATOM   2637  OD1 ASN A 393      12.225  23.873   6.915  1.00 41.80           O  
ATOM   2638  ND2 ASN A 393      10.382  24.820   7.792  1.00 40.67           N  
ATOM   2639  N   HIS A 394      13.063  20.814  11.205  1.00 31.65           N  
ATOM   2640  CA  HIS A 394      13.594  20.416  12.501  1.00 29.40           C  
ATOM   2641  C   HIS A 394      12.945  21.080  13.696  1.00 27.44           C  
ATOM   2642  O   HIS A 394      13.587  21.330  14.710  1.00 27.35           O  
ATOM   2643  CB  HIS A 394      15.105  20.621  12.533  1.00 28.45           C  
ATOM   2644  CG  HIS A 394      15.815  19.882  11.445  1.00 28.62           C  
ATOM   2645  ND1 HIS A 394      16.152  20.469  10.244  1.00 30.04           N  
ATOM   2646  CD2 HIS A 394      16.161  18.577  11.336  1.00 28.14           C  
ATOM   2647  CE1 HIS A 394      16.673  19.557   9.441  1.00 29.75           C  
ATOM   2648  NE2 HIS A 394      16.689  18.401  10.080  1.00 30.60           N  
ATOM   2649  N   LEU A 395      11.658  21.363  13.562  1.00 27.26           N  
ATOM   2650  CA  LEU A 395      10.880  21.934  14.647  1.00 28.29           C  
ATOM   2651  C   LEU A 395      10.574  20.777  15.613  1.00 26.75           C  
ATOM   2652  O   LEU A 395      10.178  19.695  15.192  1.00 25.81           O  
ATOM   2653  CB  LEU A 395       9.568  22.499  14.105  1.00 30.27           C  
ATOM   2654  CG  LEU A 395       8.541  22.921  15.160  1.00 33.07           C  
ATOM   2655  CD1 LEU A 395       9.060  24.132  15.909  1.00 33.15           C  
ATOM   2656  CD2 LEU A 395       7.207  23.244  14.490  1.00 34.01           C  
ATOM   2657  N   VAL A 396      10.780  20.986  16.902  1.00 26.38           N  
ATOM   2658  CA  VAL A 396      10.483  19.938  17.857  1.00 25.05           C  
ATOM   2659  C   VAL A 396       9.510  20.439  18.906  1.00 26.44           C  
ATOM   2660  O   VAL A 396       9.586  21.588  19.348  1.00 26.43           O  
ATOM   2661  CB  VAL A 396      11.750  19.419  18.546  1.00 24.86           C  
ATOM   2662  CG1 VAL A 396      11.378  18.296  19.506  1.00 24.43           C  
ATOM   2663  CG2 VAL A 396      12.732  18.902  17.498  1.00 26.00           C  
ATOM   2664  N   LYS A 397       8.577  19.574  19.283  1.00 25.92           N  
ATOM   2665  CA  LYS A 397       7.583  19.920  20.279  1.00 26.78           C  
ATOM   2666  C   LYS A 397       7.501  18.781  21.272  1.00 28.73           C  
ATOM   2667  O   LYS A 397       7.552  17.601  20.899  1.00 29.51           O  
ATOM   2668  CB  LYS A 397       6.208  20.142  19.637  1.00 25.09           C  
ATOM   2669  CG  LYS A 397       6.173  21.287  18.619  1.00 28.04           C  
ATOM   2670  CD  LYS A 397       4.749  21.681  18.237  1.00 24.33           C  
ATOM   2671  CE  LYS A 397       4.771  22.821  17.227  1.00 26.80           C  
ATOM   2672  NZ  LYS A 397       3.434  23.445  17.033  1.00 24.73           N  
ATOM   2673  N   VAL A 398       7.385  19.140  22.541  1.00 27.10           N  
ATOM   2674  CA  VAL A 398       7.284  18.146  23.590  1.00 27.47           C  
ATOM   2675  C   VAL A 398       5.830  17.692  23.640  1.00 26.19           C  
ATOM   2676  O   VAL A 398       4.919  18.494  23.446  1.00 24.78           O  
ATOM   2677  CB  VAL A 398       7.699  18.755  24.957  1.00 25.46           C  
ATOM   2678  CG1 VAL A 398       7.475  17.751  26.072  1.00 26.15           C  
ATOM   2679  CG2 VAL A 398       9.166  19.175  24.910  1.00 21.70           C  
ATOM   2680  N   ALA A 399       5.617  16.404  23.862  1.00 27.23           N  
ATOM   2681  CA  ALA A 399       4.261  15.867  23.965  1.00 28.81           C  
ATOM   2682  C   ALA A 399       3.758  16.268  25.350  1.00 31.74           C  
ATOM   2683  O   ALA A 399       4.336  15.869  26.356  1.00 32.79           O  
ATOM   2684  CB  ALA A 399       4.292  14.356  23.835  1.00 27.78           C  
ATOM   2685  N   ASP A 400       2.689  17.059  25.408  1.00 33.77           N  
ATOM   2686  CA  ASP A 400       2.161  17.522  26.693  1.00 36.02           C  
ATOM   2687  C   ASP A 400       1.020  16.708  27.285  1.00 35.38           C  
ATOM   2688  O   ASP A 400       0.049  17.268  27.797  1.00 35.99           O  
ATOM   2689  CB  ASP A 400       1.729  18.996  26.604  1.00 38.64           C  
ATOM   2690  CG  ASP A 400       1.038  19.325  25.295  1.00 41.66           C  
ATOM   2691  OD1 ASP A 400       0.408  18.414  24.710  1.00 42.64           O  
ATOM   2692  OD2 ASP A 400       1.121  20.496  24.855  1.00 44.88           O  
ATOM   2693  N   PHE A 401       1.135  15.388  27.224  1.00 34.35           N  
ATOM   2694  CA  PHE A 401       0.109  14.533  27.807  1.00 33.95           C  
ATOM   2695  C   PHE A 401       0.498  14.263  29.268  1.00 32.40           C  
ATOM   2696  O   PHE A 401       1.667  14.360  29.635  1.00 32.47           O  
ATOM   2697  CB  PHE A 401      -0.006  13.210  27.016  1.00 32.89           C  
ATOM   2698  CG  PHE A 401       1.254  12.365  27.030  1.00 34.59           C  
ATOM   2699  CD1 PHE A 401       1.643  11.678  28.181  1.00 33.26           C  
ATOM   2700  CD2 PHE A 401       2.063  12.280  25.896  1.00 33.78           C  
ATOM   2701  CE1 PHE A 401       2.824  10.920  28.202  1.00 34.95           C  
ATOM   2702  CE2 PHE A 401       3.251  11.525  25.905  1.00 32.07           C  
ATOM   2703  CZ  PHE A 401       3.631  10.846  27.058  1.00 33.50           C  
ATOM   2704  N   GLY A 402      -0.491  13.957  30.098  1.00 31.87           N  
ATOM   2705  CA  GLY A 402      -0.228  13.639  31.489  1.00 31.83           C  
ATOM   2706  C   GLY A 402       0.395  14.708  32.362  1.00 32.35           C  
ATOM   2707  O   GLY A 402       1.053  14.388  33.351  1.00 32.20           O  
ATOM   2708  N   LEU A 403       0.186  15.974  32.015  1.00 32.29           N  
ATOM   2709  CA  LEU A 403       0.738  17.074  32.801  1.00 31.75           C  
ATOM   2710  C   LEU A 403       0.031  17.219  34.145  1.00 33.84           C  
ATOM   2711  O   LEU A 403      -1.176  16.985  34.251  1.00 32.73           O  
ATOM   2712  CB  LEU A 403       0.612  18.390  32.034  1.00 31.29           C  
ATOM   2713  CG  LEU A 403       1.553  18.593  30.852  1.00 30.76           C  
ATOM   2714  CD1 LEU A 403       1.241  19.911  30.166  1.00 29.20           C  
ATOM   2715  CD2 LEU A 403       2.991  18.568  31.352  1.00 30.84           C  
ATOM   2716  N   SER A 404       0.789  17.608  35.169  1.00 35.05           N  
ATOM   2717  CA  SER A 404       0.233  17.806  36.508  1.00 37.62           C  
ATOM   2718  C   SER A 404       0.557  19.198  37.037  1.00 38.42           C  
ATOM   2719  O   SER A 404       1.659  19.703  36.844  1.00 37.23           O  
ATOM   2720  CB  SER A 404       0.775  16.760  37.487  1.00 37.89           C  
ATOM   2721  OG  SER A 404       0.299  15.463  37.173  1.00 41.82           O  
ATOM   2722  N   ARG A 405      -0.413  19.815  37.702  1.00 40.96           N  
ATOM   2723  CA  ARG A 405      -0.219  21.147  38.263  1.00 42.86           C  
ATOM   2724  C   ARG A 405       0.440  20.997  39.621  1.00 42.45           C  
ATOM   2725  O   ARG A 405      -0.126  20.391  40.522  1.00 43.07           O  
ATOM   2726  CB  ARG A 405      -1.566  21.857  38.419  1.00 43.89           C  
ATOM   2727  CG  ARG A 405      -2.381  21.930  37.136  1.00 47.37           C  
ATOM   2728  CD  ARG A 405      -3.782  22.443  37.395  1.00 49.85           C  
ATOM   2729  NE  ARG A 405      -4.593  22.483  36.182  1.00 53.90           N  
ATOM   2730  CZ  ARG A 405      -4.556  23.465  35.283  1.00 56.75           C  
ATOM   2731  NH1 ARG A 405      -3.745  24.506  35.456  1.00 56.67           N  
ATOM   2732  NH2 ARG A 405      -5.331  23.403  34.205  1.00 57.69           N  
ATOM   2733  N   LEU A 406       1.642  21.538  39.761  1.00 43.85           N  
ATOM   2734  CA  LEU A 406       2.361  21.460  41.026  1.00 46.86           C  
ATOM   2735  C   LEU A 406       3.069  22.779  41.260  1.00 50.33           C  
ATOM   2736  O   LEU A 406       3.985  23.137  40.523  1.00 51.61           O  
ATOM   2737  CB  LEU A 406       3.389  20.324  40.996  1.00 44.82           C  
ATOM   2738  CG  LEU A 406       4.119  19.994  42.303  1.00 43.68           C  
ATOM   2739  CD1 LEU A 406       3.142  19.436  43.332  1.00 39.52           C  
ATOM   2740  CD2 LEU A 406       5.210  18.982  42.022  1.00 41.92           C  
ATOM   2741  N   MET A 407       2.640  23.516  42.276  1.00 54.36           N  
ATOM   2742  CA  MET A 407       3.273  24.790  42.569  1.00 59.36           C  
ATOM   2743  C   MET A 407       4.760  24.548  42.795  1.00 62.97           C  
ATOM   2744  O   MET A 407       5.134  23.727  43.638  1.00 63.91           O  
ATOM   2745  CB  MET A 407       2.626  25.425  43.796  1.00 59.83           C  
ATOM   2746  CG  MET A 407       1.187  25.866  43.552  1.00 61.97           C  
ATOM   2747  SD  MET A 407       1.000  26.885  42.049  1.00 62.12           S  
ATOM   2748  CE  MET A 407       2.079  28.276  42.449  1.00 61.28           C  
ATOM   2749  N   THR A 408       5.594  25.262  42.035  1.00 66.42           N  
ATOM   2750  CA  THR A 408       7.052  25.123  42.095  1.00 69.48           C  
ATOM   2751  C   THR A 408       7.553  24.796  43.496  1.00 70.99           C  
ATOM   2752  O   THR A 408       8.441  23.952  43.666  1.00 70.91           O  
ATOM   2753  CB  THR A 408       7.735  26.394  41.582  1.00 70.93           C  
ATOM   2754  OG1 THR A 408       7.333  26.626  40.226  1.00 71.82           O  
ATOM   2755  CG2 THR A 408       9.250  26.253  41.628  1.00 70.93           C  
ATOM   2756  N   GLY A 409       6.985  25.468  44.493  1.00 71.73           N  
ATOM   2757  CA  GLY A 409       7.350  25.202  45.870  1.00 72.53           C  
ATOM   2758  C   GLY A 409       6.488  24.075  46.404  1.00 73.01           C  
ATOM   2759  O   GLY A 409       5.645  24.311  47.267  1.00 73.43           O  
ATOM   2760  N   ASP A 410       6.702  22.856  45.901  1.00 72.24           N  
ATOM   2761  CA  ASP A 410       5.896  21.707  46.320  1.00 71.28           C  
ATOM   2762  C   ASP A 410       6.313  20.453  45.522  1.00 69.73           C  
ATOM   2763  O   ASP A 410       6.924  20.565  44.455  1.00 68.67           O  
ATOM   2764  CB  ASP A 410       4.416  22.012  46.053  1.00 72.87           C  
ATOM   2765  CG  ASP A 410       3.482  21.339  47.047  1.00 74.43           C  
ATOM   2766  OD1 ASP A 410       3.885  20.336  47.689  1.00 74.78           O  
ATOM   2767  OD2 ASP A 410       2.333  21.812  47.181  1.00 75.62           O  
ATOM   2768  N   THR A 411       5.990  19.266  46.041  1.00 67.60           N  
ATOM   2769  CA  THR A 411       6.314  18.028  45.332  1.00 65.29           C  
ATOM   2770  C   THR A 411       5.116  17.077  45.198  1.00 63.19           C  
ATOM   2771  O   THR A 411       4.153  17.120  45.975  1.00 62.13           O  
ATOM   2772  CB  THR A 411       7.496  17.256  45.990  1.00 65.88           C  
ATOM   2773  OG1 THR A 411       7.024  16.005  46.510  1.00 67.01           O  
ATOM   2774  CG2 THR A 411       8.112  18.070  47.132  1.00 64.86           C  
ATOM   2775  N   TYR A 412       5.209  16.211  44.197  1.00 61.45           N  
ATOM   2776  CA  TYR A 412       4.169  15.246  43.848  1.00 60.54           C  
ATOM   2777  C   TYR A 412       4.563  13.821  44.214  1.00 60.30           C  
ATOM   2778  O   TYR A 412       5.729  13.461  44.112  1.00 59.38           O  
ATOM   2779  CB  TYR A 412       3.947  15.365  42.348  1.00 60.73           C  
ATOM   2780  CG  TYR A 412       3.023  14.369  41.708  1.00 62.39           C  
ATOM   2781  CD1 TYR A 412       1.662  14.633  41.595  1.00 64.38           C  
ATOM   2782  CD2 TYR A 412       3.520  13.203  41.129  1.00 62.90           C  
ATOM   2783  CE1 TYR A 412       0.816  13.770  40.916  1.00 64.67           C  
ATOM   2784  CE2 TYR A 412       2.679  12.327  40.447  1.00 64.08           C  
ATOM   2785  CZ  TYR A 412       1.326  12.620  40.341  1.00 64.87           C  
ATOM   2786  OH  TYR A 412       0.487  11.762  39.658  1.00 66.73           O  
ATOM   2787  N   THR A 413       3.594  13.012  44.636  1.00 60.51           N  
ATOM   2788  CA  THR A 413       3.857  11.619  44.996  1.00 60.83           C  
ATOM   2789  C   THR A 413       3.018  10.661  44.161  1.00 61.92           C  
ATOM   2790  O   THR A 413       1.793  10.725  44.177  1.00 62.76           O  
ATOM   2791  CB  THR A 413       3.556  11.348  46.480  1.00 59.79           C  
ATOM   2792  OG1 THR A 413       4.382  12.187  47.294  1.00 59.55           O  
ATOM   2793  CG2 THR A 413       3.833   9.888  46.821  1.00 59.24           C  
ATOM   2794  N   ALA A 414       3.681   9.772  43.432  1.00 63.93           N  
ATOM   2795  CA  ALA A 414       2.981   8.806  42.592  1.00 66.91           C  
ATOM   2796  C   ALA A 414       2.388   7.671  43.422  1.00 69.03           C  
ATOM   2797  O   ALA A 414       2.730   7.491  44.592  1.00 69.14           O  
ATOM   2798  CB  ALA A 414       3.928   8.241  41.539  1.00 65.64           C  
ATOM   2799  N   HIS A 415       1.494   6.909  42.802  1.00 71.88           N  
ATOM   2800  CA  HIS A 415       0.849   5.786  43.467  1.00 74.42           C  
ATOM   2801  C   HIS A 415       1.835   4.652  43.675  1.00 74.17           C  
ATOM   2802  O   HIS A 415       2.522   4.238  42.741  1.00 74.21           O  
ATOM   2803  CB  HIS A 415      -0.328   5.278  42.630  1.00 76.93           C  
ATOM   2804  CG  HIS A 415      -1.432   6.275  42.476  1.00 80.11           C  
ATOM   2805  ND1 HIS A 415      -2.085   6.833  43.555  1.00 81.72           N  
ATOM   2806  CD2 HIS A 415      -2.001   6.813  41.372  1.00 81.29           C  
ATOM   2807  CE1 HIS A 415      -3.009   7.672  43.122  1.00 82.71           C  
ATOM   2808  NE2 HIS A 415      -2.979   7.678  41.801  1.00 83.03           N  
ATOM   2809  N   ALA A 416       1.905   4.152  44.904  1.00 73.84           N  
ATOM   2810  CA  ALA A 416       2.799   3.049  45.210  1.00 73.29           C  
ATOM   2811  C   ALA A 416       2.421   1.900  44.285  1.00 73.00           C  
ATOM   2812  O   ALA A 416       1.241   1.585  44.127  1.00 73.17           O  
ATOM   2813  CB  ALA A 416       2.639   2.632  46.664  1.00 73.28           C  
ATOM   2814  N   GLY A 417       3.420   1.286  43.662  1.00 72.57           N  
ATOM   2815  CA  GLY A 417       3.150   0.182  42.760  1.00 72.00           C  
ATOM   2816  C   GLY A 417       3.292   0.580  41.305  1.00 71.36           C  
ATOM   2817  O   GLY A 417       3.375  -0.280  40.426  1.00 71.10           O  
ATOM   2818  N   ALA A 418       3.312   1.885  41.050  1.00 70.24           N  
ATOM   2819  CA  ALA A 418       3.457   2.404  39.693  1.00 69.38           C  
ATOM   2820  C   ALA A 418       4.916   2.279  39.252  1.00 68.16           C  
ATOM   2821  O   ALA A 418       5.830   2.638  39.998  1.00 67.37           O  
ATOM   2822  CB  ALA A 418       3.013   3.862  39.644  1.00 70.10           C  
ATOM   2823  N   LYS A 419       5.127   1.766  38.043  1.00 66.88           N  
ATOM   2824  CA  LYS A 419       6.474   1.582  37.509  1.00 65.63           C  
ATOM   2825  C   LYS A 419       6.983   2.828  36.786  1.00 63.29           C  
ATOM   2826  O   LYS A 419       6.197   3.647  36.303  1.00 63.76           O  
ATOM   2827  CB  LYS A 419       6.505   0.384  36.556  1.00 67.75           C  
ATOM   2828  CG  LYS A 419       5.571   0.510  35.364  1.00 70.41           C  
ATOM   2829  CD  LYS A 419       5.742  -0.654  34.398  1.00 72.80           C  
ATOM   2830  CE  LYS A 419       4.856  -0.489  33.166  1.00 74.42           C  
ATOM   2831  NZ  LYS A 419       5.114  -1.538  32.136  1.00 74.76           N  
ATOM   2832  N   PHE A 420       8.304   2.958  36.707  1.00 59.38           N  
ATOM   2833  CA  PHE A 420       8.931   4.110  36.066  1.00 54.88           C  
ATOM   2834  C   PHE A 420      10.001   3.697  35.061  1.00 52.00           C  
ATOM   2835  O   PHE A 420      10.625   2.647  35.198  1.00 52.37           O  
ATOM   2836  CB  PHE A 420       9.616   4.991  37.118  1.00 53.34           C  
ATOM   2837  CG  PHE A 420       8.733   5.386  38.268  1.00 52.75           C  
ATOM   2838  CD1 PHE A 420       9.234   5.384  39.568  1.00 51.22           C  
ATOM   2839  CD2 PHE A 420       7.417   5.790  38.054  1.00 53.20           C  
ATOM   2840  CE1 PHE A 420       8.439   5.778  40.642  1.00 51.85           C  
ATOM   2841  CE2 PHE A 420       6.610   6.187  39.121  1.00 52.50           C  
ATOM   2842  CZ  PHE A 420       7.123   6.181  40.419  1.00 53.54           C  
ATOM   2843  N   PRO A 421      10.216   4.517  34.022  1.00 48.82           N  
ATOM   2844  CA  PRO A 421      11.252   4.173  33.043  1.00 46.70           C  
ATOM   2845  C   PRO A 421      12.578   4.513  33.744  1.00 44.38           C  
ATOM   2846  O   PRO A 421      13.098   5.629  33.641  1.00 44.52           O  
ATOM   2847  CB  PRO A 421      10.927   5.089  31.862  1.00 46.72           C  
ATOM   2848  CG  PRO A 421      10.313   6.284  32.517  1.00 48.03           C  
ATOM   2849  CD  PRO A 421       9.428   5.679  33.581  1.00 48.05           C  
ATOM   2850  N   ILE A 422      13.089   3.532  34.486  1.00 41.35           N  
ATOM   2851  CA  ILE A 422      14.307   3.662  35.284  1.00 37.07           C  
ATOM   2852  C   ILE A 422      15.413   4.597  34.797  1.00 34.37           C  
ATOM   2853  O   ILE A 422      15.801   5.519  35.508  1.00 30.72           O  
ATOM   2854  CB  ILE A 422      14.935   2.278  35.546  1.00 36.90           C  
ATOM   2855  CG1 ILE A 422      13.908   1.350  36.204  1.00 38.05           C  
ATOM   2856  CG2 ILE A 422      16.134   2.420  36.453  1.00 34.64           C  
ATOM   2857  CD1 ILE A 422      13.399   1.836  37.536  1.00 37.76           C  
ATOM   2858  N   LYS A 423      15.921   4.353  33.595  1.00 33.32           N  
ATOM   2859  CA  LYS A 423      17.016   5.144  33.037  1.00 33.04           C  
ATOM   2860  C   LYS A 423      16.805   6.660  32.956  1.00 30.31           C  
ATOM   2861  O   LYS A 423      17.770   7.414  32.865  1.00 28.96           O  
ATOM   2862  CB  LYS A 423      17.384   4.598  31.652  1.00 36.39           C  
ATOM   2863  CG  LYS A 423      17.982   3.187  31.674  1.00 43.31           C  
ATOM   2864  CD  LYS A 423      18.001   2.562  30.269  1.00 47.24           C  
ATOM   2865  CE  LYS A 423      18.708   1.209  30.265  1.00 49.06           C  
ATOM   2866  NZ  LYS A 423      18.607   0.508  28.947  1.00 49.46           N  
ATOM   2867  N   TRP A 424      15.558   7.111  32.991  1.00 28.48           N  
ATOM   2868  CA  TRP A 424      15.271   8.543  32.909  1.00 26.75           C  
ATOM   2869  C   TRP A 424      14.775   9.112  34.241  1.00 27.49           C  
ATOM   2870  O   TRP A 424      14.572  10.316  34.373  1.00 27.59           O  
ATOM   2871  CB  TRP A 424      14.190   8.800  31.854  1.00 25.35           C  
ATOM   2872  CG  TRP A 424      14.620   8.676  30.420  1.00 25.73           C  
ATOM   2873  CD1 TRP A 424      14.871   9.702  29.549  1.00 25.14           C  
ATOM   2874  CD2 TRP A 424      14.813   7.462  29.675  1.00 25.36           C  
ATOM   2875  NE1 TRP A 424      15.205   9.202  28.308  1.00 25.99           N  
ATOM   2876  CE2 TRP A 424      15.177   7.833  28.356  1.00 25.04           C  
ATOM   2877  CE3 TRP A 424      14.717   6.098  29.994  1.00 26.05           C  
ATOM   2878  CZ2 TRP A 424      15.440   6.890  27.353  1.00 26.97           C  
ATOM   2879  CZ3 TRP A 424      14.982   5.154  28.993  1.00 26.90           C  
ATOM   2880  CH2 TRP A 424      15.337   5.558  27.690  1.00 27.93           C  
ATOM   2881  N   THR A 425      14.600   8.248  35.229  1.00 25.47           N  
ATOM   2882  CA  THR A 425      14.052   8.669  36.503  1.00 24.82           C  
ATOM   2883  C   THR A 425      15.061   9.085  37.551  1.00 23.59           C  
ATOM   2884  O   THR A 425      16.054   8.400  37.773  1.00 25.32           O  
ATOM   2885  CB  THR A 425      13.156   7.554  37.053  1.00 26.74           C  
ATOM   2886  OG1 THR A 425      12.183   7.215  36.054  1.00 30.99           O  
ATOM   2887  CG2 THR A 425      12.451   7.993  38.316  1.00 25.80           C  
ATOM   2888  N   ALA A 426      14.780  10.208  38.209  1.00 22.16           N  
ATOM   2889  CA  ALA A 426      15.653  10.750  39.248  1.00 24.17           C  
ATOM   2890  C   ALA A 426      15.696   9.886  40.513  1.00 24.62           C  
ATOM   2891  O   ALA A 426      14.766   9.142  40.804  1.00 23.87           O  
ATOM   2892  CB  ALA A 426      15.204  12.167  39.613  1.00 21.54           C  
ATOM   2893  N   PRO A 427      16.790   9.984  41.284  1.00 27.22           N  
ATOM   2894  CA  PRO A 427      16.944   9.214  42.518  1.00 28.40           C  
ATOM   2895  C   PRO A 427      15.734   9.333  43.449  1.00 29.51           C  
ATOM   2896  O   PRO A 427      15.136   8.323  43.824  1.00 29.43           O  
ATOM   2897  CB  PRO A 427      18.204   9.808  43.127  1.00 27.61           C  
ATOM   2898  CG  PRO A 427      19.022  10.092  41.923  1.00 29.65           C  
ATOM   2899  CD  PRO A 427      18.032  10.711  40.968  1.00 28.48           C  
ATOM   2900  N   GLU A 428      15.371  10.563  43.807  1.00 28.88           N  
ATOM   2901  CA  GLU A 428      14.243  10.786  44.705  1.00 31.26           C  
ATOM   2902  C   GLU A 428      12.975  10.116  44.164  1.00 32.95           C  
ATOM   2903  O   GLU A 428      12.112   9.682  44.927  1.00 33.08           O  
ATOM   2904  CB  GLU A 428      13.989  12.287  44.897  1.00 32.51           C  
ATOM   2905  CG  GLU A 428      13.436  12.993  43.661  1.00 32.63           C  
ATOM   2906  CD  GLU A 428      14.523  13.621  42.801  1.00 33.70           C  
ATOM   2907  OE1 GLU A 428      15.693  13.179  42.882  1.00 30.99           O  
ATOM   2908  OE2 GLU A 428      14.202  14.558  42.035  1.00 35.50           O  
ATOM   2909  N   SER A 429      12.869  10.020  42.845  1.00 32.50           N  
ATOM   2910  CA  SER A 429      11.696   9.402  42.244  1.00 31.81           C  
ATOM   2911  C   SER A 429      11.765   7.876  42.335  1.00 31.14           C  
ATOM   2912  O   SER A 429      10.761   7.212  42.585  1.00 29.59           O  
ATOM   2913  CB  SER A 429      11.566   9.849  40.785  1.00 32.31           C  
ATOM   2914  OG  SER A 429      11.447  11.261  40.699  1.00 30.45           O  
ATOM   2915  N   LEU A 430      12.957   7.327  42.147  1.00 31.18           N  
ATOM   2916  CA  LEU A 430      13.146   5.885  42.207  1.00 32.86           C  
ATOM   2917  C   LEU A 430      13.008   5.339  43.623  1.00 33.19           C  
ATOM   2918  O   LEU A 430      12.634   4.188  43.811  1.00 34.09           O  
ATOM   2919  CB  LEU A 430      14.532   5.507  41.673  1.00 32.58           C  
ATOM   2920  CG  LEU A 430      14.825   5.717  40.189  1.00 32.04           C  
ATOM   2921  CD1 LEU A 430      16.302   5.522  39.948  1.00 35.24           C  
ATOM   2922  CD2 LEU A 430      14.023   4.744  39.351  1.00 34.25           C  
ATOM   2923  N   ALA A 431      13.308   6.170  44.615  1.00 34.57           N  
ATOM   2924  CA  ALA A 431      13.260   5.749  46.008  1.00 33.65           C  
ATOM   2925  C   ALA A 431      12.025   6.163  46.791  1.00 33.83           C  
ATOM   2926  O   ALA A 431      11.588   5.431  47.672  1.00 32.40           O  
ATOM   2927  CB  ALA A 431      14.502   6.246  46.732  1.00 32.15           C  
ATOM   2928  N   TYR A 432      11.456   7.323  46.481  1.00 34.87           N  
ATOM   2929  CA  TYR A 432      10.290   7.787  47.228  1.00 36.57           C  
ATOM   2930  C   TYR A 432       9.065   8.106  46.394  1.00 36.49           C  
ATOM   2931  O   TYR A 432       8.071   8.609  46.916  1.00 35.43           O  
ATOM   2932  CB  TYR A 432      10.667   9.014  48.056  1.00 39.96           C  
ATOM   2933  CG  TYR A 432      11.952   8.833  48.823  1.00 43.41           C  
ATOM   2934  CD1 TYR A 432      13.065   9.625  48.546  1.00 46.96           C  
ATOM   2935  CD2 TYR A 432      12.069   7.848  49.803  1.00 44.75           C  
ATOM   2936  CE1 TYR A 432      14.269   9.441  49.228  1.00 48.70           C  
ATOM   2937  CE2 TYR A 432      13.270   7.654  50.492  1.00 47.31           C  
ATOM   2938  CZ  TYR A 432      14.363   8.455  50.197  1.00 49.08           C  
ATOM   2939  OH  TYR A 432      15.555   8.271  50.861  1.00 53.29           O  
ATOM   2940  N   ASN A 433       9.129   7.809  45.101  1.00 37.75           N  
ATOM   2941  CA  ASN A 433       8.012   8.084  44.214  1.00 38.80           C  
ATOM   2942  C   ASN A 433       7.676   9.568  44.218  1.00 39.15           C  
ATOM   2943  O   ASN A 433       6.534   9.948  43.970  1.00 41.05           O  
ATOM   2944  CB  ASN A 433       6.792   7.273  44.647  1.00 40.12           C  
ATOM   2945  CG  ASN A 433       6.861   5.838  44.180  1.00 42.49           C  
ATOM   2946  OD1 ASN A 433       7.947   5.288  43.980  1.00 42.59           O  
ATOM   2947  ND2 ASN A 433       5.702   5.217  44.006  1.00 45.38           N  
ATOM   2948  N   LYS A 434       8.669  10.403  44.509  1.00 37.70           N  
ATOM   2949  CA  LYS A 434       8.459  11.847  44.532  1.00 38.67           C  
ATOM   2950  C   LYS A 434       8.916  12.495  43.220  1.00 36.71           C  
ATOM   2951  O   LYS A 434       9.974  12.172  42.685  1.00 37.58           O  
ATOM   2952  CB  LYS A 434       9.210  12.483  45.710  1.00 39.58           C  
ATOM   2953  CG  LYS A 434       8.737  12.032  47.085  1.00 41.11           C  
ATOM   2954  CD  LYS A 434       9.469  12.802  48.186  1.00 45.67           C  
ATOM   2955  CE  LYS A 434       9.026  12.375  49.581  1.00 47.06           C  
ATOM   2956  NZ  LYS A 434       7.556  12.567  49.822  1.00 49.10           N  
ATOM   2957  N   PHE A 435       8.101  13.404  42.700  1.00 35.40           N  
ATOM   2958  CA  PHE A 435       8.424  14.095  41.461  1.00 31.66           C  
ATOM   2959  C   PHE A 435       8.241  15.590  41.628  1.00 30.00           C  
ATOM   2960  O   PHE A 435       7.411  16.041  42.418  1.00 30.68           O  
ATOM   2961  CB  PHE A 435       7.529  13.605  40.324  1.00 31.24           C  
ATOM   2962  CG  PHE A 435       7.692  12.148  40.009  1.00 31.02           C  
ATOM   2963  CD1 PHE A 435       7.162  11.176  40.849  1.00 28.68           C  
ATOM   2964  CD2 PHE A 435       8.386  11.747  38.872  1.00 28.42           C  
ATOM   2965  CE1 PHE A 435       7.325   9.821  40.557  1.00 27.85           C  
ATOM   2966  CE2 PHE A 435       8.551  10.397  38.577  1.00 29.11           C  
ATOM   2967  CZ  PHE A 435       8.019   9.435  39.422  1.00 25.83           C  
ATOM   2968  N   SER A 436       9.026  16.349  40.875  1.00 29.05           N  
ATOM   2969  CA  SER A 436       8.976  17.807  40.890  1.00 27.80           C  
ATOM   2970  C   SER A 436       9.560  18.258  39.561  1.00 27.94           C  
ATOM   2971  O   SER A 436       9.978  17.422  38.753  1.00 28.43           O  
ATOM   2972  CB  SER A 436       9.839  18.368  42.018  1.00 29.12           C  
ATOM   2973  OG  SER A 436      11.220  18.196  41.728  1.00 27.00           O  
ATOM   2974  N   ILE A 437       9.608  19.569  39.336  1.00 27.26           N  
ATOM   2975  CA  ILE A 437      10.168  20.090  38.095  1.00 25.92           C  
ATOM   2976  C   ILE A 437      11.648  19.693  38.029  1.00 25.79           C  
ATOM   2977  O   ILE A 437      12.217  19.496  36.954  1.00 25.74           O  
ATOM   2978  CB  ILE A 437      10.002  21.635  38.015  1.00 28.25           C  
ATOM   2979  CG1 ILE A 437      10.487  22.135  36.657  1.00 26.95           C  
ATOM   2980  CG2 ILE A 437      10.756  22.319  39.148  1.00 28.59           C  
ATOM   2981  CD1 ILE A 437       9.631  21.650  35.488  1.00 26.78           C  
ATOM   2982  N   LYS A 438      12.267  19.540  39.194  1.00 25.17           N  
ATOM   2983  CA  LYS A 438      13.666  19.136  39.240  1.00 25.72           C  
ATOM   2984  C   LYS A 438      13.891  17.704  38.734  1.00 25.65           C  
ATOM   2985  O   LYS A 438      14.980  17.382  38.255  1.00 23.33           O  
ATOM   2986  CB  LYS A 438      14.214  19.247  40.651  1.00 27.58           C  
ATOM   2987  CG  LYS A 438      14.300  20.665  41.154  1.00 28.21           C  
ATOM   2988  CD  LYS A 438      15.138  21.522  40.239  1.00 27.25           C  
ATOM   2989  CE  LYS A 438      15.280  22.917  40.807  1.00 28.55           C  
ATOM   2990  NZ  LYS A 438      16.159  23.743  39.941  1.00 29.60           N  
ATOM   2991  N   SER A 439      12.885  16.835  38.861  1.00 24.43           N  
ATOM   2992  CA  SER A 439      13.048  15.473  38.353  1.00 26.02           C  
ATOM   2993  C   SER A 439      12.856  15.537  36.841  1.00 25.93           C  
ATOM   2994  O   SER A 439      13.366  14.688  36.101  1.00 25.39           O  
ATOM   2995  CB  SER A 439      12.081  14.465  39.017  1.00 29.46           C  
ATOM   2996  OG  SER A 439      10.729  14.865  38.971  1.00 37.99           O  
ATOM   2997  N   ASP A 440      12.124  16.548  36.371  1.00 24.47           N  
ATOM   2998  CA  ASP A 440      11.968  16.716  34.931  1.00 24.55           C  
ATOM   2999  C   ASP A 440      13.347  17.143  34.421  1.00 22.63           C  
ATOM   3000  O   ASP A 440      13.787  16.705  33.354  1.00 23.46           O  
ATOM   3001  CB  ASP A 440      10.940  17.798  34.599  1.00 29.15           C  
ATOM   3002  CG  ASP A 440       9.496  17.268  34.574  1.00 34.42           C  
ATOM   3003  OD1 ASP A 440       9.249  16.074  34.893  1.00 35.05           O  
ATOM   3004  OD2 ASP A 440       8.593  18.065  34.230  1.00 36.96           O  
ATOM   3005  N   VAL A 441      14.015  17.995  35.200  1.00 19.45           N  
ATOM   3006  CA  VAL A 441      15.356  18.493  34.871  1.00 19.54           C  
ATOM   3007  C   VAL A 441      16.341  17.333  34.752  1.00 21.07           C  
ATOM   3008  O   VAL A 441      17.174  17.296  33.836  1.00 18.53           O  
ATOM   3009  CB  VAL A 441      15.877  19.470  35.952  1.00 14.66           C  
ATOM   3010  CG1 VAL A 441      17.379  19.723  35.761  1.00 13.57           C  
ATOM   3011  CG2 VAL A 441      15.111  20.779  35.870  1.00 16.04           C  
ATOM   3012  N   TRP A 442      16.248  16.394  35.694  1.00 22.38           N  
ATOM   3013  CA  TRP A 442      17.109  15.221  35.682  1.00 21.29           C  
ATOM   3014  C   TRP A 442      16.853  14.460  34.384  1.00 20.39           C  
ATOM   3015  O   TRP A 442      17.786  13.975  33.735  1.00 17.98           O  
ATOM   3016  CB  TRP A 442      16.798  14.297  36.872  1.00 23.15           C  
ATOM   3017  CG  TRP A 442      17.585  13.006  36.818  1.00 22.72           C  
ATOM   3018  CD1 TRP A 442      17.409  11.982  35.941  1.00 21.99           C  
ATOM   3019  CD2 TRP A 442      18.730  12.662  37.615  1.00 23.12           C  
ATOM   3020  NE1 TRP A 442      18.375  11.024  36.131  1.00 25.57           N  
ATOM   3021  CE2 TRP A 442      19.198  11.413  37.153  1.00 23.92           C  
ATOM   3022  CE3 TRP A 442      19.404  13.291  38.676  1.00 22.01           C  
ATOM   3023  CZ2 TRP A 442      20.316  10.770  37.713  1.00 24.05           C  
ATOM   3024  CZ3 TRP A 442      20.513  12.657  39.233  1.00 22.92           C  
ATOM   3025  CH2 TRP A 442      20.959  11.405  38.750  1.00 23.25           C  
ATOM   3026  N   ALA A 443      15.576  14.337  34.028  1.00 21.55           N  
ATOM   3027  CA  ALA A 443      15.190  13.629  32.806  1.00 24.14           C  
ATOM   3028  C   ALA A 443      15.727  14.359  31.571  1.00 24.67           C  
ATOM   3029  O   ALA A 443      16.219  13.726  30.628  1.00 26.21           O  
ATOM   3030  CB  ALA A 443      13.662  13.505  32.724  1.00 23.66           C  
ATOM   3031  N   PHE A 444      15.640  15.686  31.579  1.00 23.58           N  
ATOM   3032  CA  PHE A 444      16.126  16.459  30.448  1.00 25.42           C  
ATOM   3033  C   PHE A 444      17.584  16.123  30.182  1.00 25.65           C  
ATOM   3034  O   PHE A 444      17.995  15.974  29.030  1.00 23.78           O  
ATOM   3035  CB  PHE A 444      16.010  17.958  30.699  1.00 25.07           C  
ATOM   3036  CG  PHE A 444      16.516  18.780  29.559  1.00 26.48           C  
ATOM   3037  CD1 PHE A 444      15.765  18.911  28.398  1.00 26.37           C  
ATOM   3038  CD2 PHE A 444      17.768  19.372  29.617  1.00 26.50           C  
ATOM   3039  CE1 PHE A 444      16.253  19.620  27.306  1.00 27.89           C  
ATOM   3040  CE2 PHE A 444      18.271  20.087  28.527  1.00 28.70           C  
ATOM   3041  CZ  PHE A 444      17.513  20.211  27.371  1.00 28.63           C  
ATOM   3042  N   GLY A 445      18.354  16.007  31.263  1.00 25.38           N  
ATOM   3043  CA  GLY A 445      19.763  15.675  31.151  1.00 22.79           C  
ATOM   3044  C   GLY A 445      19.949  14.363  30.419  1.00 23.08           C  
ATOM   3045  O   GLY A 445      20.862  14.231  29.597  1.00 21.79           O  
ATOM   3046  N   VAL A 446      19.090  13.385  30.705  1.00 21.81           N  
ATOM   3047  CA  VAL A 446      19.198  12.095  30.024  1.00 24.16           C  
ATOM   3048  C   VAL A 446      18.815  12.280  28.558  1.00 24.44           C  
ATOM   3049  O   VAL A 446      19.468  11.758  27.660  1.00 25.19           O  
ATOM   3050  CB  VAL A 446      18.265  11.024  30.641  1.00 25.46           C  
ATOM   3051  CG1 VAL A 446      18.490   9.691  29.951  1.00 20.73           C  
ATOM   3052  CG2 VAL A 446      18.512  10.905  32.137  1.00 25.18           C  
ATOM   3053  N   LEU A 447      17.748  13.030  28.318  1.00 25.87           N  
ATOM   3054  CA  LEU A 447      17.304  13.291  26.957  1.00 26.04           C  
ATOM   3055  C   LEU A 447      18.427  14.002  26.175  1.00 26.94           C  
ATOM   3056  O   LEU A 447      18.635  13.734  24.995  1.00 25.49           O  
ATOM   3057  CB  LEU A 447      16.034  14.147  27.004  1.00 29.03           C  
ATOM   3058  CG  LEU A 447      15.248  14.564  25.759  1.00 31.57           C  
ATOM   3059  CD1 LEU A 447      13.975  15.291  26.201  1.00 32.87           C  
ATOM   3060  CD2 LEU A 447      16.078  15.484  24.893  1.00 33.20           C  
ATOM   3061  N   LEU A 448      19.152  14.898  26.842  1.00 26.00           N  
ATOM   3062  CA  LEU A 448      20.244  15.636  26.208  1.00 26.38           C  
ATOM   3063  C   LEU A 448      21.297  14.650  25.715  1.00 26.72           C  
ATOM   3064  O   LEU A 448      21.915  14.843  24.669  1.00 27.92           O  
ATOM   3065  CB  LEU A 448      20.899  16.597  27.208  1.00 26.50           C  
ATOM   3066  CG  LEU A 448      21.319  17.976  26.687  1.00 28.95           C  
ATOM   3067  CD1 LEU A 448      22.353  18.578  27.636  1.00 28.70           C  
ATOM   3068  CD2 LEU A 448      21.893  17.864  25.291  1.00 28.03           C  
ATOM   3069  N   TRP A 449      21.508  13.601  26.502  1.00 24.62           N  
ATOM   3070  CA  TRP A 449      22.471  12.557  26.177  1.00 22.74           C  
ATOM   3071  C   TRP A 449      21.981  11.764  24.957  1.00 22.01           C  
ATOM   3072  O   TRP A 449      22.777  11.355  24.115  1.00 21.08           O  
ATOM   3073  CB  TRP A 449      22.621  11.613  27.378  1.00 21.86           C  
ATOM   3074  CG  TRP A 449      23.734  10.642  27.265  1.00 22.42           C  
ATOM   3075  CD1 TRP A 449      25.028  10.835  27.645  1.00 23.57           C  
ATOM   3076  CD2 TRP A 449      23.665   9.320  26.720  1.00 23.48           C  
ATOM   3077  NE1 TRP A 449      25.773   9.713  27.374  1.00 25.14           N  
ATOM   3078  CE2 TRP A 449      24.961   8.766  26.808  1.00 24.50           C  
ATOM   3079  CE3 TRP A 449      22.630   8.546  26.171  1.00 24.58           C  
ATOM   3080  CZ2 TRP A 449      25.257   7.467  26.361  1.00 25.63           C  
ATOM   3081  CZ3 TRP A 449      22.921   7.255  25.729  1.00 25.68           C  
ATOM   3082  CH2 TRP A 449      24.227   6.729  25.830  1.00 24.34           C  
ATOM   3083  N   GLU A 450      20.672  11.534  24.879  1.00 22.18           N  
ATOM   3084  CA  GLU A 450      20.109  10.793  23.758  1.00 25.91           C  
ATOM   3085  C   GLU A 450      20.344  11.609  22.494  1.00 25.16           C  
ATOM   3086  O   GLU A 450      20.657  11.066  21.436  1.00 27.08           O  
ATOM   3087  CB  GLU A 450      18.596  10.570  23.932  1.00 26.51           C  
ATOM   3088  CG  GLU A 450      18.177   9.764  25.153  1.00 28.73           C  
ATOM   3089  CD  GLU A 450      16.668   9.510  25.190  1.00 32.13           C  
ATOM   3090  OE1 GLU A 450      16.186   8.644  24.424  1.00 32.72           O  
ATOM   3091  OE2 GLU A 450      15.957  10.185  25.971  1.00 32.50           O  
ATOM   3092  N   ILE A 451      20.187  12.920  22.607  1.00 23.17           N  
ATOM   3093  CA  ILE A 451      20.390  13.778  21.460  1.00 25.08           C  
ATOM   3094  C   ILE A 451      21.854  13.755  21.022  1.00 26.65           C  
ATOM   3095  O   ILE A 451      22.142  13.586  19.835  1.00 25.93           O  
ATOM   3096  CB  ILE A 451      19.930  15.212  21.771  1.00 23.70           C  
ATOM   3097  CG1 ILE A 451      18.397  15.227  21.900  1.00 22.18           C  
ATOM   3098  CG2 ILE A 451      20.414  16.170  20.689  1.00 22.82           C  
ATOM   3099  CD1 ILE A 451      17.796  16.563  22.346  1.00 21.14           C  
ATOM   3100  N   ALA A 452      22.767  13.870  21.984  1.00 25.71           N  
ATOM   3101  CA  ALA A 452      24.197  13.880  21.689  1.00 28.70           C  
ATOM   3102  C   ALA A 452      24.734  12.578  21.088  1.00 29.21           C  
ATOM   3103  O   ALA A 452      25.772  12.579  20.429  1.00 31.53           O  
ATOM   3104  CB  ALA A 452      24.985  14.240  22.946  1.00 26.30           C  
ATOM   3105  N   THR A 453      24.023  11.477  21.302  1.00 28.28           N  
ATOM   3106  CA  THR A 453      24.444  10.179  20.784  1.00 26.01           C  
ATOM   3107  C   THR A 453      23.622   9.709  19.589  1.00 25.24           C  
ATOM   3108  O   THR A 453      23.812   8.599  19.098  1.00 25.01           O  
ATOM   3109  CB  THR A 453      24.341   9.101  21.873  1.00 26.96           C  
ATOM   3110  OG1 THR A 453      22.971   8.974  22.279  1.00 23.18           O  
ATOM   3111  CG2 THR A 453      25.210   9.477  23.090  1.00 25.67           C  
ATOM   3112  N   TYR A 454      22.705  10.550  19.127  1.00 27.11           N  
ATOM   3113  CA  TYR A 454      21.848  10.212  17.989  1.00 28.47           C  
ATOM   3114  C   TYR A 454      20.914   9.031  18.263  1.00 28.85           C  
ATOM   3115  O   TYR A 454      20.651   8.220  17.377  1.00 28.54           O  
ATOM   3116  CB  TYR A 454      22.691   9.928  16.733  1.00 29.35           C  
ATOM   3117  CG  TYR A 454      23.192  11.171  16.022  1.00 31.69           C  
ATOM   3118  CD1 TYR A 454      22.329  11.963  15.260  1.00 32.16           C  
ATOM   3119  CD2 TYR A 454      24.528  11.565  16.121  1.00 33.51           C  
ATOM   3120  CE1 TYR A 454      22.782  13.119  14.614  1.00 31.78           C  
ATOM   3121  CE2 TYR A 454      24.992  12.720  15.480  1.00 33.57           C  
ATOM   3122  CZ  TYR A 454      24.116  13.488  14.729  1.00 33.74           C  
ATOM   3123  OH  TYR A 454      24.590  14.615  14.090  1.00 35.68           O  
ATOM   3124  N   GLY A 455      20.417   8.932  19.494  1.00 29.11           N  
ATOM   3125  CA  GLY A 455      19.487   7.869  19.819  1.00 29.11           C  
ATOM   3126  C   GLY A 455      19.954   6.638  20.578  1.00 29.39           C  
ATOM   3127  O   GLY A 455      19.174   5.701  20.741  1.00 28.46           O  
ATOM   3128  N   MET A 456      21.197   6.611  21.042  1.00 28.03           N  
ATOM   3129  CA  MET A 456      21.662   5.445  21.787  1.00 32.37           C  
ATOM   3130  C   MET A 456      20.793   5.197  23.024  1.00 32.02           C  
ATOM   3131  O   MET A 456      20.111   6.102  23.504  1.00 30.82           O  
ATOM   3132  CB  MET A 456      23.121   5.626  22.225  1.00 35.65           C  
ATOM   3133  CG  MET A 456      24.142   5.268  21.159  1.00 40.50           C  
ATOM   3134  SD  MET A 456      25.840   5.413  21.780  1.00 50.11           S  
ATOM   3135  CE  MET A 456      25.862   4.061  23.038  1.00 46.28           C  
ATOM   3136  N   SER A 457      20.814   3.966  23.529  1.00 31.99           N  
ATOM   3137  CA  SER A 457      20.051   3.616  24.724  1.00 32.75           C  
ATOM   3138  C   SER A 457      20.887   4.062  25.935  1.00 32.31           C  
ATOM   3139  O   SER A 457      22.085   3.794  25.996  1.00 33.97           O  
ATOM   3140  CB  SER A 457      19.812   2.107  24.757  1.00 34.69           C  
ATOM   3141  OG  SER A 457      18.872   1.763  25.756  1.00 41.22           O  
ATOM   3142  N   PRO A 458      20.271   4.752  26.911  1.00 32.63           N  
ATOM   3143  CA  PRO A 458      21.011   5.219  28.093  1.00 32.48           C  
ATOM   3144  C   PRO A 458      21.728   4.130  28.891  1.00 32.77           C  
ATOM   3145  O   PRO A 458      21.362   2.955  28.836  1.00 33.26           O  
ATOM   3146  CB  PRO A 458      19.938   5.921  28.929  1.00 31.87           C  
ATOM   3147  CG  PRO A 458      18.902   6.310  27.931  1.00 32.28           C  
ATOM   3148  CD  PRO A 458      18.847   5.113  27.016  1.00 32.23           C  
ATOM   3149  N   TYR A 459      22.747   4.548  29.637  1.00 34.36           N  
ATOM   3150  CA  TYR A 459      23.556   3.663  30.476  1.00 33.92           C  
ATOM   3151  C   TYR A 459      23.938   2.340  29.808  1.00 34.61           C  
ATOM   3152  O   TYR A 459      23.568   1.265  30.278  1.00 35.04           O  
ATOM   3153  CB  TYR A 459      22.835   3.376  31.804  1.00 31.87           C  
ATOM   3154  CG  TYR A 459      22.527   4.608  32.629  1.00 29.12           C  
ATOM   3155  CD1 TYR A 459      21.288   5.245  32.533  1.00 27.78           C  
ATOM   3156  CD2 TYR A 459      23.479   5.150  33.490  1.00 27.62           C  
ATOM   3157  CE1 TYR A 459      21.004   6.390  33.272  1.00 26.27           C  
ATOM   3158  CE2 TYR A 459      23.203   6.302  34.236  1.00 28.69           C  
ATOM   3159  CZ  TYR A 459      21.962   6.916  34.120  1.00 27.42           C  
ATOM   3160  OH  TYR A 459      21.684   8.057  34.846  1.00 26.80           O  
ATOM   3161  N   PRO A 460      24.695   2.404  28.704  1.00 35.74           N  
ATOM   3162  CA  PRO A 460      25.097   1.173  28.018  1.00 38.63           C  
ATOM   3163  C   PRO A 460      25.959   0.279  28.911  1.00 40.95           C  
ATOM   3164  O   PRO A 460      26.840   0.765  29.626  1.00 41.25           O  
ATOM   3165  CB  PRO A 460      25.856   1.691  26.803  1.00 38.24           C  
ATOM   3166  CG  PRO A 460      26.464   2.988  27.321  1.00 36.55           C  
ATOM   3167  CD  PRO A 460      25.311   3.589  28.080  1.00 36.44           C  
ATOM   3168  N   GLY A 461      25.682  -1.022  28.873  1.00 43.54           N  
ATOM   3169  CA  GLY A 461      26.432  -1.974  29.670  1.00 47.05           C  
ATOM   3170  C   GLY A 461      26.093  -1.938  31.149  1.00 49.82           C  
ATOM   3171  O   GLY A 461      26.955  -2.188  31.992  1.00 52.35           O  
ATOM   3172  N   ILE A 462      24.842  -1.631  31.474  1.00 49.89           N  
ATOM   3173  CA  ILE A 462      24.420  -1.565  32.868  1.00 50.42           C  
ATOM   3174  C   ILE A 462      22.986  -2.054  33.020  1.00 51.54           C  
ATOM   3175  O   ILE A 462      22.087  -1.600  32.310  1.00 52.06           O  
ATOM   3176  CB  ILE A 462      24.515  -0.119  33.406  1.00 49.99           C  
ATOM   3177  CG1 ILE A 462      25.953   0.391  33.260  1.00 49.06           C  
ATOM   3178  CG2 ILE A 462      24.064  -0.071  34.860  1.00 48.09           C  
ATOM   3179  CD1 ILE A 462      26.140   1.841  33.632  1.00 47.60           C  
ATOM   3180  N   ASP A 463      22.776  -2.985  33.945  1.00 51.96           N  
ATOM   3181  CA  ASP A 463      21.443  -3.523  34.178  1.00 52.47           C  
ATOM   3182  C   ASP A 463      20.645  -2.634  35.131  1.00 50.74           C  
ATOM   3183  O   ASP A 463      21.155  -2.167  36.153  1.00 49.86           O  
ATOM   3184  CB  ASP A 463      21.526  -4.975  34.694  1.00 57.39           C  
ATOM   3185  CG  ASP A 463      22.630  -5.182  35.724  1.00 61.95           C  
ATOM   3186  OD1 ASP A 463      23.801  -4.830  35.443  1.00 64.22           O  
ATOM   3187  OD2 ASP A 463      22.327  -5.714  36.816  1.00 65.62           O  
ATOM   3188  N   LEU A 464      19.387  -2.401  34.771  1.00 47.76           N  
ATOM   3189  CA  LEU A 464      18.494  -1.546  35.535  1.00 46.95           C  
ATOM   3190  C   LEU A 464      18.514  -1.743  37.043  1.00 46.88           C  
ATOM   3191  O   LEU A 464      18.247  -0.806  37.798  1.00 46.47           O  
ATOM   3192  CB  LEU A 464      17.065  -1.713  35.026  1.00 47.66           C  
ATOM   3193  CG  LEU A 464      16.876  -1.553  33.517  1.00 49.00           C  
ATOM   3194  CD1 LEU A 464      15.396  -1.608  33.196  1.00 49.08           C  
ATOM   3195  CD2 LEU A 464      17.468  -0.243  33.044  1.00 49.45           C  
ATOM   3196  N   SER A 465      18.825  -2.957  37.484  1.00 45.87           N  
ATOM   3197  CA  SER A 465      18.857  -3.264  38.911  1.00 44.33           C  
ATOM   3198  C   SER A 465      20.052  -2.639  39.624  1.00 42.45           C  
ATOM   3199  O   SER A 465      20.111  -2.634  40.848  1.00 43.34           O  
ATOM   3200  CB  SER A 465      18.872  -4.782  39.120  1.00 45.12           C  
ATOM   3201  OG  SER A 465      19.981  -5.374  38.458  1.00 45.77           O  
ATOM   3202  N   GLN A 466      21.006  -2.122  38.858  1.00 41.01           N  
ATOM   3203  CA  GLN A 466      22.185  -1.496  39.443  1.00 40.54           C  
ATOM   3204  C   GLN A 466      22.252   0.021  39.234  1.00 37.99           C  
ATOM   3205  O   GLN A 466      23.077   0.696  39.853  1.00 37.43           O  
ATOM   3206  CB  GLN A 466      23.459  -2.134  38.881  1.00 43.33           C  
ATOM   3207  CG  GLN A 466      23.600  -3.615  39.188  1.00 48.22           C  
ATOM   3208  CD  GLN A 466      24.980  -4.156  38.843  1.00 52.22           C  
ATOM   3209  OE1 GLN A 466      25.216  -5.369  38.895  1.00 52.68           O  
ATOM   3210  NE2 GLN A 466      25.904  -3.255  38.495  1.00 51.86           N  
ATOM   3211  N   VAL A 467      21.389   0.558  38.374  1.00 35.08           N  
ATOM   3212  CA  VAL A 467      21.394   1.992  38.101  1.00 33.03           C  
ATOM   3213  C   VAL A 467      21.385   2.845  39.369  1.00 31.21           C  
ATOM   3214  O   VAL A 467      22.293   3.655  39.576  1.00 29.77           O  
ATOM   3215  CB  VAL A 467      20.202   2.408  37.200  1.00 32.92           C  
ATOM   3216  CG1 VAL A 467      20.197   3.924  36.993  1.00 29.65           C  
ATOM   3217  CG2 VAL A 467      20.312   1.712  35.852  1.00 33.27           C  
ATOM   3218  N   TYR A 468      20.376   2.667  40.216  1.00 28.25           N  
ATOM   3219  CA  TYR A 468      20.299   3.447  41.446  1.00 29.43           C  
ATOM   3220  C   TYR A 468      21.560   3.311  42.285  1.00 31.38           C  
ATOM   3221  O   TYR A 468      22.104   4.304  42.764  1.00 31.59           O  
ATOM   3222  CB  TYR A 468      19.112   3.023  42.305  1.00 29.52           C  
ATOM   3223  CG  TYR A 468      18.873   3.966  43.467  1.00 28.59           C  
ATOM   3224  CD1 TYR A 468      18.076   5.101  43.312  1.00 28.00           C  
ATOM   3225  CD2 TYR A 468      19.463   3.741  44.713  1.00 27.31           C  
ATOM   3226  CE1 TYR A 468      17.867   5.988  44.368  1.00 28.51           C  
ATOM   3227  CE2 TYR A 468      19.260   4.623  45.779  1.00 27.44           C  
ATOM   3228  CZ  TYR A 468      18.460   5.743  45.596  1.00 28.56           C  
ATOM   3229  OH  TYR A 468      18.251   6.623  46.629  1.00 31.02           O  
ATOM   3230  N   GLU A 469      22.012   2.075  42.469  1.00 31.70           N  
ATOM   3231  CA  GLU A 469      23.216   1.806  43.247  1.00 33.60           C  
ATOM   3232  C   GLU A 469      24.404   2.596  42.695  1.00 31.92           C  
ATOM   3233  O   GLU A 469      25.153   3.226  43.446  1.00 29.84           O  
ATOM   3234  CB  GLU A 469      23.511   0.299  43.228  1.00 37.66           C  
ATOM   3235  CG  GLU A 469      24.917  -0.097  43.654  1.00 42.98           C  
ATOM   3236  CD  GLU A 469      25.146  -1.598  43.544  1.00 48.57           C  
ATOM   3237  OE1 GLU A 469      26.322  -2.029  43.565  1.00 50.15           O  
ATOM   3238  OE2 GLU A 469      24.148  -2.348  43.442  1.00 49.48           O  
ATOM   3239  N   LEU A 470      24.574   2.565  41.378  1.00 31.39           N  
ATOM   3240  CA  LEU A 470      25.666   3.296  40.744  1.00 31.09           C  
ATOM   3241  C   LEU A 470      25.509   4.805  40.916  1.00 30.22           C  
ATOM   3242  O   LEU A 470      26.461   5.493  41.270  1.00 29.96           O  
ATOM   3243  CB  LEU A 470      25.745   2.944  39.262  1.00 31.36           C  
ATOM   3244  CG  LEU A 470      26.264   1.535  38.989  1.00 32.03           C  
ATOM   3245  CD1 LEU A 470      26.047   1.169  37.534  1.00 33.33           C  
ATOM   3246  CD2 LEU A 470      27.739   1.475  39.351  1.00 32.34           C  
ATOM   3247  N   LEU A 471      24.306   5.318  40.677  1.00 28.97           N  
ATOM   3248  CA  LEU A 471      24.062   6.751  40.821  1.00 28.71           C  
ATOM   3249  C   LEU A 471      24.406   7.211  42.235  1.00 29.23           C  
ATOM   3250  O   LEU A 471      25.014   8.262  42.432  1.00 30.08           O  
ATOM   3251  CB  LEU A 471      22.593   7.085  40.515  1.00 26.12           C  
ATOM   3252  CG  LEU A 471      22.127   6.920  39.065  1.00 27.23           C  
ATOM   3253  CD1 LEU A 471      20.647   7.260  38.943  1.00 25.40           C  
ATOM   3254  CD2 LEU A 471      22.961   7.829  38.167  1.00 25.05           C  
ATOM   3255  N   GLU A 472      24.018   6.411  43.217  1.00 31.06           N  
ATOM   3256  CA  GLU A 472      24.269   6.735  44.614  1.00 32.59           C  
ATOM   3257  C   GLU A 472      25.766   6.848  44.950  1.00 30.69           C  
ATOM   3258  O   GLU A 472      26.134   7.534  45.899  1.00 29.23           O  
ATOM   3259  CB  GLU A 472      23.584   5.697  45.502  1.00 36.28           C  
ATOM   3260  CG  GLU A 472      23.669   5.990  46.984  1.00 44.60           C  
ATOM   3261  CD  GLU A 472      22.792   5.061  47.796  1.00 48.19           C  
ATOM   3262  OE1 GLU A 472      22.923   3.826  47.643  1.00 50.65           O  
ATOM   3263  OE2 GLU A 472      21.970   5.568  48.589  1.00 50.41           O  
ATOM   3264  N   LYS A 473      26.618   6.186  44.171  1.00 29.48           N  
ATOM   3265  CA  LYS A 473      28.069   6.258  44.378  1.00 31.59           C  
ATOM   3266  C   LYS A 473      28.645   7.325  43.444  1.00 29.67           C  
ATOM   3267  O   LYS A 473      29.822   7.300  43.094  1.00 28.30           O  
ATOM   3268  CB  LYS A 473      28.746   4.913  44.074  1.00 32.93           C  
ATOM   3269  CG  LYS A 473      28.322   3.756  44.971  1.00 38.71           C  
ATOM   3270  CD  LYS A 473      29.058   2.468  44.573  1.00 44.09           C  
ATOM   3271  CE  LYS A 473      28.671   1.286  45.466  1.00 47.73           C  
ATOM   3272  NZ  LYS A 473      28.892   1.581  46.919  1.00 48.79           N  
ATOM   3273  N   ASP A 474      27.786   8.247  43.030  1.00 29.20           N  
ATOM   3274  CA  ASP A 474      28.159   9.345  42.146  1.00 28.28           C  
ATOM   3275  C   ASP A 474      28.604   8.942  40.737  1.00 25.84           C  
ATOM   3276  O   ASP A 474      29.270   9.712  40.055  1.00 26.68           O  
ATOM   3277  CB  ASP A 474      29.245  10.215  42.788  1.00 29.11           C  
ATOM   3278  CG  ASP A 474      29.355  11.578  42.126  1.00 32.92           C  
ATOM   3279  OD1 ASP A 474      30.485  12.063  41.925  1.00 32.64           O  
ATOM   3280  OD2 ASP A 474      28.300  12.170  41.809  1.00 34.99           O  
ATOM   3281  N   TYR A 475      28.258   7.742  40.296  1.00 23.79           N  
ATOM   3282  CA  TYR A 475      28.607   7.346  38.939  1.00 23.32           C  
ATOM   3283  C   TYR A 475      27.600   8.032  37.994  1.00 26.01           C  
ATOM   3284  O   TYR A 475      26.433   8.238  38.364  1.00 22.44           O  
ATOM   3285  CB  TYR A 475      28.492   5.837  38.767  1.00 24.24           C  
ATOM   3286  CG  TYR A 475      28.521   5.407  37.320  1.00 27.71           C  
ATOM   3287  CD1 TYR A 475      29.728   5.186  36.663  1.00 27.29           C  
ATOM   3288  CD2 TYR A 475      27.338   5.299  36.584  1.00 29.69           C  
ATOM   3289  CE1 TYR A 475      29.765   4.879  35.310  1.00 29.65           C  
ATOM   3290  CE2 TYR A 475      27.358   4.992  35.224  1.00 29.63           C  
ATOM   3291  CZ  TYR A 475      28.579   4.787  34.593  1.00 32.04           C  
ATOM   3292  OH  TYR A 475      28.623   4.525  33.238  1.00 32.13           O  
ATOM   3293  N   ARG A 476      28.052   8.374  36.787  1.00 24.54           N  
ATOM   3294  CA  ARG A 476      27.204   9.020  35.782  1.00 26.56           C  
ATOM   3295  C   ARG A 476      27.675   8.628  34.373  1.00 26.96           C  
ATOM   3296  O   ARG A 476      28.841   8.310  34.173  1.00 27.24           O  
ATOM   3297  CB  ARG A 476      27.278  10.546  35.919  1.00 23.12           C  
ATOM   3298  CG  ARG A 476      26.762  11.112  37.231  1.00 25.22           C  
ATOM   3299  CD  ARG A 476      25.245  11.021  37.366  1.00 23.71           C  
ATOM   3300  NE  ARG A 476      24.779  11.737  38.554  1.00 23.55           N  
ATOM   3301  CZ  ARG A 476      24.812  11.252  39.793  1.00 24.61           C  
ATOM   3302  NH1 ARG A 476      25.281  10.032  40.016  1.00 22.60           N  
ATOM   3303  NH2 ARG A 476      24.394  11.997  40.814  1.00 20.22           N  
ATOM   3304  N   MET A 477      26.773   8.653  33.400  1.00 28.60           N  
ATOM   3305  CA  MET A 477      27.147   8.319  32.028  1.00 30.71           C  
ATOM   3306  C   MET A 477      28.345   9.138  31.559  1.00 31.03           C  
ATOM   3307  O   MET A 477      28.500  10.301  31.927  1.00 30.50           O  
ATOM   3308  CB  MET A 477      25.972   8.550  31.076  1.00 30.45           C  
ATOM   3309  CG  MET A 477      24.895   7.481  31.153  1.00 31.21           C  
ATOM   3310  SD  MET A 477      23.620   7.688  29.894  1.00 34.28           S  
ATOM   3311  CE  MET A 477      22.599   8.902  30.729  1.00 30.11           C  
ATOM   3312  N   GLU A 478      29.192   8.514  30.748  1.00 33.20           N  
ATOM   3313  CA  GLU A 478      30.389   9.157  30.213  1.00 35.19           C  
ATOM   3314  C   GLU A 478      30.039  10.182  29.136  1.00 34.85           C  
ATOM   3315  O   GLU A 478      28.958  10.128  28.541  1.00 33.70           O  
ATOM   3316  CB  GLU A 478      31.322   8.102  29.616  1.00 38.07           C  
ATOM   3317  CG  GLU A 478      31.796   7.052  30.608  1.00 45.71           C  
ATOM   3318  CD  GLU A 478      32.524   5.902  29.927  1.00 51.22           C  
ATOM   3319  OE1 GLU A 478      33.550   6.162  29.255  1.00 53.47           O  
ATOM   3320  OE2 GLU A 478      32.067   4.740  30.062  1.00 52.20           O  
ATOM   3321  N   ARG A 479      30.958  11.109  28.884  1.00 32.66           N  
ATOM   3322  CA  ARG A 479      30.739  12.130  27.872  1.00 33.71           C  
ATOM   3323  C   ARG A 479      30.665  11.529  26.466  1.00 33.51           C  
ATOM   3324  O   ARG A 479      31.611  10.901  25.988  1.00 34.70           O  
ATOM   3325  CB  ARG A 479      31.852  13.178  27.927  1.00 34.04           C  
ATOM   3326  CG  ARG A 479      31.736  14.265  26.864  1.00 36.46           C  
ATOM   3327  CD  ARG A 479      32.733  15.391  27.118  1.00 38.28           C  
ATOM   3328  NE  ARG A 479      34.116  14.949  26.973  1.00 42.00           N  
ATOM   3329  CZ  ARG A 479      34.688  14.649  25.811  1.00 43.48           C  
ATOM   3330  NH1 ARG A 479      33.996  14.751  24.681  1.00 44.12           N  
ATOM   3331  NH2 ARG A 479      35.948  14.231  25.779  1.00 43.45           N  
ATOM   3332  N   PRO A 480      29.529  11.713  25.785  1.00 33.04           N  
ATOM   3333  CA  PRO A 480      29.366  11.177  24.427  1.00 33.07           C  
ATOM   3334  C   PRO A 480      30.501  11.616  23.483  1.00 34.25           C  
ATOM   3335  O   PRO A 480      31.056  12.709  23.610  1.00 30.08           O  
ATOM   3336  CB  PRO A 480      28.009  11.733  23.994  1.00 30.98           C  
ATOM   3337  CG  PRO A 480      27.269  11.863  25.296  1.00 34.22           C  
ATOM   3338  CD  PRO A 480      28.319  12.428  26.225  1.00 30.19           C  
ATOM   3339  N   GLU A 481      30.833  10.746  22.537  1.00 36.71           N  
ATOM   3340  CA  GLU A 481      31.887  11.007  21.564  1.00 39.21           C  
ATOM   3341  C   GLU A 481      31.621  12.313  20.813  1.00 38.38           C  
ATOM   3342  O   GLU A 481      30.524  12.532  20.303  1.00 38.65           O  
ATOM   3343  CB  GLU A 481      31.950   9.845  20.571  1.00 42.50           C  
ATOM   3344  CG  GLU A 481      33.063   9.919  19.547  1.00 47.64           C  
ATOM   3345  CD  GLU A 481      32.889   8.874  18.453  1.00 52.73           C  
ATOM   3346  OE1 GLU A 481      32.593   7.702  18.789  1.00 54.11           O  
ATOM   3347  OE2 GLU A 481      33.049   9.222  17.260  1.00 53.43           O  
ATOM   3348  N   GLY A 482      32.632  13.172  20.750  1.00 37.71           N  
ATOM   3349  CA  GLY A 482      32.493  14.437  20.053  1.00 35.67           C  
ATOM   3350  C   GLY A 482      31.649  15.480  20.765  1.00 35.45           C  
ATOM   3351  O   GLY A 482      31.540  16.617  20.295  1.00 33.90           O  
ATOM   3352  N   CYS A 483      31.056  15.117  21.898  1.00 34.98           N  
ATOM   3353  CA  CYS A 483      30.226  16.071  22.624  1.00 34.63           C  
ATOM   3354  C   CYS A 483      31.076  17.112  23.324  1.00 34.03           C  
ATOM   3355  O   CYS A 483      31.899  16.783  24.171  1.00 34.63           O  
ATOM   3356  CB  CYS A 483      29.344  15.365  23.657  1.00 33.71           C  
ATOM   3357  SG  CYS A 483      28.408  16.502  24.722  1.00 34.90           S  
ATOM   3358  N   PRO A 484      30.887  18.391  22.974  1.00 33.62           N  
ATOM   3359  CA  PRO A 484      31.670  19.452  23.613  1.00 34.04           C  
ATOM   3360  C   PRO A 484      31.538  19.464  25.141  1.00 33.64           C  
ATOM   3361  O   PRO A 484      30.450  19.289  25.697  1.00 32.76           O  
ATOM   3362  CB  PRO A 484      31.153  20.726  22.939  1.00 33.40           C  
ATOM   3363  CG  PRO A 484      29.804  20.356  22.451  1.00 33.43           C  
ATOM   3364  CD  PRO A 484      29.960  18.945  21.977  1.00 32.83           C  
ATOM   3365  N   GLU A 485      32.671  19.656  25.807  1.00 35.53           N  
ATOM   3366  CA  GLU A 485      32.736  19.668  27.263  1.00 37.12           C  
ATOM   3367  C   GLU A 485      31.646  20.521  27.904  1.00 36.34           C  
ATOM   3368  O   GLU A 485      31.075  20.133  28.919  1.00 37.49           O  
ATOM   3369  CB  GLU A 485      34.127  20.140  27.710  1.00 40.17           C  
ATOM   3370  CG  GLU A 485      34.351  20.245  29.225  1.00 45.83           C  
ATOM   3371  CD  GLU A 485      34.168  18.922  29.969  1.00 49.86           C  
ATOM   3372  OE1 GLU A 485      34.485  17.854  29.394  1.00 52.01           O  
ATOM   3373  OE2 GLU A 485      33.721  18.954  31.139  1.00 51.14           O  
ATOM   3374  N   LYS A 486      31.350  21.674  27.312  1.00 35.40           N  
ATOM   3375  CA  LYS A 486      30.319  22.557  27.851  1.00 34.71           C  
ATOM   3376  C   LYS A 486      28.951  21.888  27.919  1.00 33.59           C  
ATOM   3377  O   LYS A 486      28.182  22.109  28.853  1.00 31.12           O  
ATOM   3378  CB  LYS A 486      30.218  23.831  27.008  1.00 36.90           C  
ATOM   3379  CG  LYS A 486      31.259  24.897  27.363  1.00 41.36           C  
ATOM   3380  CD  LYS A 486      31.302  26.022  26.327  1.00 44.65           C  
ATOM   3381  CE  LYS A 486      31.972  27.279  26.883  1.00 46.50           C  
ATOM   3382  NZ  LYS A 486      33.283  26.986  27.534  1.00 49.08           N  
ATOM   3383  N   VAL A 487      28.644  21.068  26.925  1.00 32.31           N  
ATOM   3384  CA  VAL A 487      27.359  20.397  26.898  1.00 30.82           C  
ATOM   3385  C   VAL A 487      27.314  19.264  27.921  1.00 31.48           C  
ATOM   3386  O   VAL A 487      26.294  19.059  28.591  1.00 31.02           O  
ATOM   3387  CB  VAL A 487      27.058  19.877  25.482  1.00 30.16           C  
ATOM   3388  CG1 VAL A 487      25.721  19.135  25.456  1.00 28.91           C  
ATOM   3389  CG2 VAL A 487      27.024  21.064  24.517  1.00 29.30           C  
ATOM   3390  N   TYR A 488      28.425  18.546  28.058  1.00 31.37           N  
ATOM   3391  CA  TYR A 488      28.499  17.456  29.019  1.00 31.78           C  
ATOM   3392  C   TYR A 488      28.382  17.999  30.449  1.00 30.96           C  
ATOM   3393  O   TYR A 488      27.798  17.358  31.320  1.00 30.33           O  
ATOM   3394  CB  TYR A 488      29.814  16.686  28.855  1.00 31.71           C  
ATOM   3395  CG  TYR A 488      29.955  15.516  29.805  1.00 34.98           C  
ATOM   3396  CD1 TYR A 488      29.023  14.481  29.808  1.00 34.67           C  
ATOM   3397  CD2 TYR A 488      31.002  15.460  30.726  1.00 35.74           C  
ATOM   3398  CE1 TYR A 488      29.126  13.421  30.709  1.00 37.40           C  
ATOM   3399  CE2 TYR A 488      31.116  14.402  31.632  1.00 35.14           C  
ATOM   3400  CZ  TYR A 488      30.174  13.391  31.622  1.00 36.47           C  
ATOM   3401  OH  TYR A 488      30.252  12.368  32.539  1.00 36.65           O  
ATOM   3402  N   GLU A 489      28.918  19.187  30.689  1.00 31.12           N  
ATOM   3403  CA  GLU A 489      28.841  19.756  32.025  1.00 33.18           C  
ATOM   3404  C   GLU A 489      27.406  20.150  32.367  1.00 33.34           C  
ATOM   3405  O   GLU A 489      27.022  20.173  33.543  1.00 32.81           O  
ATOM   3406  CB  GLU A 489      29.767  20.968  32.162  1.00 36.42           C  
ATOM   3407  CG  GLU A 489      31.253  20.644  31.995  1.00 40.99           C  
ATOM   3408  CD  GLU A 489      32.170  21.713  32.605  1.00 45.65           C  
ATOM   3409  OE1 GLU A 489      31.735  22.887  32.714  1.00 45.71           O  
ATOM   3410  OE2 GLU A 489      33.328  21.377  32.965  1.00 44.88           O  
ATOM   3411  N   LEU A 490      26.606  20.460  31.349  1.00 29.80           N  
ATOM   3412  CA  LEU A 490      25.218  20.823  31.607  1.00 28.08           C  
ATOM   3413  C   LEU A 490      24.483  19.542  32.025  1.00 26.44           C  
ATOM   3414  O   LEU A 490      23.637  19.559  32.929  1.00 23.11           O  
ATOM   3415  CB  LEU A 490      24.566  21.414  30.357  1.00 30.20           C  
ATOM   3416  CG  LEU A 490      23.457  22.451  30.580  1.00 31.61           C  
ATOM   3417  CD1 LEU A 490      22.553  22.478  29.355  1.00 31.85           C  
ATOM   3418  CD2 LEU A 490      22.644  22.118  31.812  1.00 32.13           C  
ATOM   3419  N   MET A 491      24.812  18.436  31.357  1.00 24.38           N  
ATOM   3420  CA  MET A 491      24.211  17.146  31.676  1.00 25.62           C  
ATOM   3421  C   MET A 491      24.490  16.827  33.139  1.00 24.58           C  
ATOM   3422  O   MET A 491      23.580  16.482  33.895  1.00 26.24           O  
ATOM   3423  CB  MET A 491      24.806  16.026  30.815  1.00 26.90           C  
ATOM   3424  CG  MET A 491      24.434  16.045  29.351  1.00 28.18           C  
ATOM   3425  SD  MET A 491      25.271  14.696  28.460  1.00 30.96           S  
ATOM   3426  CE  MET A 491      25.110  15.241  26.786  1.00 29.50           C  
ATOM   3427  N   ARG A 492      25.755  16.952  33.529  1.00 23.10           N  
ATOM   3428  CA  ARG A 492      26.168  16.668  34.897  1.00 23.14           C  
ATOM   3429  C   ARG A 492      25.482  17.558  35.913  1.00 22.93           C  
ATOM   3430  O   ARG A 492      25.269  17.158  37.063  1.00 22.88           O  
ATOM   3431  CB  ARG A 492      27.690  16.800  35.032  1.00 23.08           C  
ATOM   3432  CG  ARG A 492      28.454  15.628  34.424  1.00 30.13           C  
ATOM   3433  CD  ARG A 492      29.968  15.846  34.441  1.00 36.74           C  
ATOM   3434  NE  ARG A 492      30.536  15.782  35.788  1.00 44.43           N  
ATOM   3435  CZ  ARG A 492      31.808  16.056  36.081  1.00 46.84           C  
ATOM   3436  NH1 ARG A 492      32.652  16.419  35.119  1.00 46.76           N  
ATOM   3437  NH2 ARG A 492      32.238  15.961  37.336  1.00 46.15           N  
ATOM   3438  N   ALA A 493      25.139  18.771  35.503  1.00 21.90           N  
ATOM   3439  CA  ALA A 493      24.467  19.685  36.411  1.00 21.45           C  
ATOM   3440  C   ALA A 493      23.024  19.214  36.599  1.00 22.28           C  
ATOM   3441  O   ALA A 493      22.467  19.333  37.687  1.00 23.71           O  
ATOM   3442  CB  ALA A 493      24.502  21.097  35.860  1.00 20.52           C  
ATOM   3443  N   CYS A 494      22.432  18.667  35.539  1.00 20.83           N  
ATOM   3444  CA  CYS A 494      21.063  18.159  35.589  1.00 22.76           C  
ATOM   3445  C   CYS A 494      21.022  16.880  36.425  1.00 24.58           C  
ATOM   3446  O   CYS A 494      19.994  16.535  37.008  1.00 26.19           O  
ATOM   3447  CB  CYS A 494      20.551  17.844  34.178  1.00 22.97           C  
ATOM   3448  SG  CYS A 494      20.358  19.288  33.067  1.00 25.99           S  
ATOM   3449  N   TRP A 495      22.148  16.178  36.484  1.00 24.88           N  
ATOM   3450  CA  TRP A 495      22.225  14.937  37.239  1.00 24.60           C  
ATOM   3451  C   TRP A 495      22.789  15.096  38.634  1.00 23.03           C  
ATOM   3452  O   TRP A 495      23.442  14.185  39.133  1.00 23.45           O  
ATOM   3453  CB  TRP A 495      23.073  13.903  36.497  1.00 25.32           C  
ATOM   3454  CG  TRP A 495      22.566  13.562  35.144  1.00 25.66           C  
ATOM   3455  CD1 TRP A 495      21.260  13.513  34.741  1.00 25.39           C  
ATOM   3456  CD2 TRP A 495      23.349  13.158  34.020  1.00 24.32           C  
ATOM   3457  NE1 TRP A 495      21.185  13.099  33.433  1.00 25.32           N  
ATOM   3458  CE2 TRP A 495      22.454  12.873  32.967  1.00 25.30           C  
ATOM   3459  CE3 TRP A 495      24.722  13.004  33.801  1.00 23.85           C  
ATOM   3460  CZ2 TRP A 495      22.891  12.442  31.711  1.00 24.55           C  
ATOM   3461  CZ3 TRP A 495      25.154  12.574  32.552  1.00 23.49           C  
ATOM   3462  CH2 TRP A 495      24.241  12.299  31.526  1.00 23.95           C  
ATOM   3463  N   GLN A 496      22.577  16.250  39.255  1.00 23.12           N  
ATOM   3464  CA  GLN A 496      23.070  16.440  40.617  1.00 23.25           C  
ATOM   3465  C   GLN A 496      22.161  15.593  41.498  1.00 23.72           C  
ATOM   3466  O   GLN A 496      20.949  15.541  41.277  1.00 23.22           O  
ATOM   3467  CB  GLN A 496      22.993  17.921  41.034  1.00 23.52           C  
ATOM   3468  CG  GLN A 496      24.084  18.810  40.416  1.00 21.91           C  
ATOM   3469  CD  GLN A 496      25.482  18.329  40.778  1.00 24.42           C  
ATOM   3470  OE1 GLN A 496      25.900  18.435  41.934  1.00 24.81           O  
ATOM   3471  NE2 GLN A 496      26.204  17.781  39.795  1.00 18.18           N  
ATOM   3472  N   TRP A 497      22.737  14.922  42.486  1.00 24.30           N  
ATOM   3473  CA  TRP A 497      21.941  14.077  43.371  1.00 24.74           C  
ATOM   3474  C   TRP A 497      20.799  14.829  44.048  1.00 25.12           C  
ATOM   3475  O   TRP A 497      19.661  14.365  44.036  1.00 26.00           O  
ATOM   3476  CB  TRP A 497      22.825  13.425  44.428  1.00 23.18           C  
ATOM   3477  CG  TRP A 497      22.062  12.531  45.339  1.00 25.66           C  
ATOM   3478  CD1 TRP A 497      21.446  12.881  46.511  1.00 21.28           C  
ATOM   3479  CD2 TRP A 497      21.768  11.143  45.125  1.00 24.71           C  
ATOM   3480  NE1 TRP A 497      20.788  11.795  47.036  1.00 24.80           N  
ATOM   3481  CE2 TRP A 497      20.971  10.715  46.208  1.00 24.46           C  
ATOM   3482  CE3 TRP A 497      22.103  10.219  44.122  1.00 27.27           C  
ATOM   3483  CZ2 TRP A 497      20.499   9.402  46.320  1.00 25.49           C  
ATOM   3484  CZ3 TRP A 497      21.631   8.907  44.231  1.00 27.72           C  
ATOM   3485  CH2 TRP A 497      20.841   8.513  45.326  1.00 27.03           C  
ATOM   3486  N   ASN A 498      21.088  15.979  44.645  1.00 24.55           N  
ATOM   3487  CA  ASN A 498      20.027  16.749  45.296  1.00 28.29           C  
ATOM   3488  C   ASN A 498      19.254  17.532  44.250  1.00 29.47           C  
ATOM   3489  O   ASN A 498      19.839  18.232  43.419  1.00 30.01           O  
ATOM   3490  CB  ASN A 498      20.601  17.731  46.317  1.00 28.75           C  
ATOM   3491  CG  ASN A 498      21.528  17.062  47.308  1.00 33.01           C  
ATOM   3492  OD1 ASN A 498      21.204  16.013  47.868  1.00 35.14           O  
ATOM   3493  ND2 ASN A 498      22.686  17.668  47.534  1.00 29.44           N  
ATOM   3494  N   PRO A 499      17.923  17.420  44.264  1.00 30.26           N  
ATOM   3495  CA  PRO A 499      17.176  18.177  43.257  1.00 29.00           C  
ATOM   3496  C   PRO A 499      17.406  19.690  43.316  1.00 28.59           C  
ATOM   3497  O   PRO A 499      17.473  20.350  42.276  1.00 27.95           O  
ATOM   3498  CB  PRO A 499      15.715  17.777  43.520  1.00 30.36           C  
ATOM   3499  CG  PRO A 499      15.717  17.229  44.947  1.00 30.80           C  
ATOM   3500  CD  PRO A 499      17.044  16.513  45.024  1.00 29.89           C  
ATOM   3501  N   SER A 500      17.542  20.246  44.518  1.00 27.43           N  
ATOM   3502  CA  SER A 500      17.755  21.688  44.632  1.00 28.50           C  
ATOM   3503  C   SER A 500      19.115  22.119  44.052  1.00 27.90           C  
ATOM   3504  O   SER A 500      19.303  23.286  43.726  1.00 26.38           O  
ATOM   3505  CB  SER A 500      17.653  22.145  46.090  1.00 28.37           C  
ATOM   3506  OG  SER A 500      18.788  21.717  46.831  1.00 35.47           O  
ATOM   3507  N   ASP A 501      20.059  21.186  43.934  1.00 26.72           N  
ATOM   3508  CA  ASP A 501      21.369  21.512  43.375  1.00 26.91           C  
ATOM   3509  C   ASP A 501      21.339  21.485  41.851  1.00 27.71           C  
ATOM   3510  O   ASP A 501      22.346  21.781  41.197  1.00 26.40           O  
ATOM   3511  CB  ASP A 501      22.444  20.529  43.851  1.00 26.75           C  
ATOM   3512  CG  ASP A 501      22.934  20.822  45.256  1.00 26.47           C  
ATOM   3513  OD1 ASP A 501      22.945  22.002  45.657  1.00 24.78           O  
ATOM   3514  OD2 ASP A 501      23.335  19.863  45.953  1.00 30.04           O  
ATOM   3515  N   ARG A 502      20.192  21.109  41.291  1.00 24.89           N  
ATOM   3516  CA  ARG A 502      20.029  21.041  39.846  1.00 25.27           C  
ATOM   3517  C   ARG A 502      19.560  22.397  39.311  1.00 24.73           C  
ATOM   3518  O   ARG A 502      18.804  23.107  39.967  1.00 24.99           O  
ATOM   3519  CB  ARG A 502      19.007  19.960  39.479  1.00 25.30           C  
ATOM   3520  CG  ARG A 502      19.407  18.552  39.887  1.00 24.94           C  
ATOM   3521  CD  ARG A 502      18.254  17.558  39.729  1.00 23.87           C  
ATOM   3522  NE  ARG A 502      18.479  16.357  40.539  1.00 25.49           N  
ATOM   3523  CZ  ARG A 502      17.525  15.521  40.943  1.00 26.41           C  
ATOM   3524  NH1 ARG A 502      16.250  15.739  40.613  1.00 24.00           N  
ATOM   3525  NH2 ARG A 502      17.845  14.472  41.699  1.00 22.93           N  
ATOM   3526  N   PRO A 503      20.005  22.768  38.107  1.00 22.49           N  
ATOM   3527  CA  PRO A 503      19.602  24.050  37.525  1.00 22.68           C  
ATOM   3528  C   PRO A 503      18.127  24.045  37.155  1.00 22.90           C  
ATOM   3529  O   PRO A 503      17.521  22.982  37.039  1.00 23.33           O  
ATOM   3530  CB  PRO A 503      20.501  24.164  36.300  1.00 22.57           C  
ATOM   3531  CG  PRO A 503      20.671  22.711  35.882  1.00 22.98           C  
ATOM   3532  CD  PRO A 503      20.920  22.040  37.213  1.00 23.11           C  
ATOM   3533  N   SER A 504      17.546  25.231  37.004  1.00 21.94           N  
ATOM   3534  CA  SER A 504      16.147  25.351  36.604  1.00 22.42           C  
ATOM   3535  C   SER A 504      16.133  25.314  35.077  1.00 21.93           C  
ATOM   3536  O   SER A 504      17.181  25.434  34.438  1.00 21.15           O  
ATOM   3537  CB  SER A 504      15.567  26.692  37.054  1.00 21.52           C  
ATOM   3538  OG  SER A 504      16.207  27.749  36.365  1.00 23.46           O  
ATOM   3539  N   PHE A 505      14.953  25.160  34.493  1.00 21.73           N  
ATOM   3540  CA  PHE A 505      14.860  25.137  33.044  1.00 24.30           C  
ATOM   3541  C   PHE A 505      15.165  26.522  32.466  1.00 25.20           C  
ATOM   3542  O   PHE A 505      15.692  26.637  31.360  1.00 25.29           O  
ATOM   3543  CB  PHE A 505      13.476  24.632  32.613  1.00 22.85           C  
ATOM   3544  CG  PHE A 505      13.377  23.128  32.579  1.00 24.67           C  
ATOM   3545  CD1 PHE A 505      14.178  22.391  31.706  1.00 24.53           C  
ATOM   3546  CD2 PHE A 505      12.520  22.450  33.432  1.00 24.50           C  
ATOM   3547  CE1 PHE A 505      14.128  21.010  31.683  1.00 25.68           C  
ATOM   3548  CE2 PHE A 505      12.459  21.059  33.421  1.00 27.27           C  
ATOM   3549  CZ  PHE A 505      13.266  20.335  32.544  1.00 27.27           C  
ATOM   3550  N   ALA A 506      14.862  27.573  33.226  1.00 25.09           N  
ATOM   3551  CA  ALA A 506      15.153  28.927  32.764  1.00 25.42           C  
ATOM   3552  C   ALA A 506      16.660  29.055  32.622  1.00 26.60           C  
ATOM   3553  O   ALA A 506      17.167  29.644  31.662  1.00 28.39           O  
ATOM   3554  CB  ALA A 506      14.642  29.948  33.755  1.00 23.35           C  
ATOM   3555  N   GLU A 507      17.382  28.482  33.576  1.00 27.07           N  
ATOM   3556  CA  GLU A 507      18.830  28.546  33.537  1.00 27.07           C  
ATOM   3557  C   GLU A 507      19.404  27.643  32.455  1.00 26.63           C  
ATOM   3558  O   GLU A 507      20.437  27.955  31.861  1.00 26.12           O  
ATOM   3559  CB  GLU A 507      19.403  28.193  34.907  1.00 29.66           C  
ATOM   3560  CG  GLU A 507      18.988  29.189  35.989  1.00 35.11           C  
ATOM   3561  CD  GLU A 507      19.512  28.822  37.362  1.00 38.61           C  
ATOM   3562  OE1 GLU A 507      19.304  27.670  37.792  1.00 41.72           O  
ATOM   3563  OE2 GLU A 507      20.132  29.687  38.014  1.00 42.46           O  
ATOM   3564  N   ILE A 508      18.729  26.534  32.181  1.00 25.85           N  
ATOM   3565  CA  ILE A 508      19.200  25.610  31.159  1.00 25.98           C  
ATOM   3566  C   ILE A 508      19.104  26.246  29.770  1.00 26.75           C  
ATOM   3567  O   ILE A 508      20.047  26.167  28.978  1.00 27.54           O  
ATOM   3568  CB  ILE A 508      18.380  24.294  31.174  1.00 24.25           C  
ATOM   3569  CG1 ILE A 508      18.822  23.426  32.352  1.00 23.53           C  
ATOM   3570  CG2 ILE A 508      18.563  23.523  29.860  1.00 21.39           C  
ATOM   3571  CD1 ILE A 508      17.924  22.235  32.591  1.00 22.71           C  
ATOM   3572  N   HIS A 509      17.968  26.874  29.485  1.00 25.61           N  
ATOM   3573  CA  HIS A 509      17.746  27.503  28.191  1.00 29.12           C  
ATOM   3574  C   HIS A 509      18.734  28.642  27.961  1.00 29.23           C  
ATOM   3575  O   HIS A 509      19.278  28.787  26.868  1.00 29.33           O  
ATOM   3576  CB  HIS A 509      16.294  28.010  28.093  1.00 30.12           C  
ATOM   3577  CG  HIS A 509      15.959  28.654  26.781  1.00 30.08           C  
ATOM   3578  ND1 HIS A 509      15.814  30.018  26.636  1.00 29.76           N  
ATOM   3579  CD2 HIS A 509      15.724  28.119  25.558  1.00 30.21           C  
ATOM   3580  CE1 HIS A 509      15.500  30.295  25.382  1.00 29.13           C  
ATOM   3581  NE2 HIS A 509      15.440  29.160  24.707  1.00 30.36           N  
ATOM   3582  N   GLN A 510      18.974  29.439  28.994  1.00 29.77           N  
ATOM   3583  CA  GLN A 510      19.914  30.552  28.880  1.00 32.54           C  
ATOM   3584  C   GLN A 510      21.326  30.009  28.633  1.00 31.62           C  
ATOM   3585  O   GLN A 510      22.099  30.568  27.847  1.00 31.10           O  
ATOM   3586  CB  GLN A 510      19.884  31.398  30.160  1.00 34.44           C  
ATOM   3587  CG  GLN A 510      20.889  32.544  30.184  1.00 39.91           C  
ATOM   3588  CD  GLN A 510      20.619  33.610  29.128  1.00 41.93           C  
ATOM   3589  OE1 GLN A 510      21.471  34.450  28.861  1.00 44.08           O  
ATOM   3590  NE2 GLN A 510      19.430  33.583  28.534  1.00 42.99           N  
ATOM   3591  N   ALA A 511      21.648  28.903  29.293  1.00 29.30           N  
ATOM   3592  CA  ALA A 511      22.956  28.289  29.150  1.00 28.83           C  
ATOM   3593  C   ALA A 511      23.258  27.934  27.699  1.00 30.18           C  
ATOM   3594  O   ALA A 511      24.386  28.095  27.238  1.00 29.41           O  
ATOM   3595  CB  ALA A 511      23.041  27.048  30.013  1.00 26.67           C  
ATOM   3596  N   PHE A 512      22.255  27.440  26.979  1.00 32.59           N  
ATOM   3597  CA  PHE A 512      22.449  27.067  25.579  1.00 34.91           C  
ATOM   3598  C   PHE A 512      22.700  28.269  24.669  1.00 35.88           C  
ATOM   3599  O   PHE A 512      23.552  28.215  23.787  1.00 37.27           O  
ATOM   3600  CB  PHE A 512      21.234  26.293  25.054  1.00 34.37           C  
ATOM   3601  CG  PHE A 512      21.197  24.845  25.471  1.00 33.79           C  
ATOM   3602  CD1 PHE A 512      22.239  23.979  25.133  1.00 32.02           C  
ATOM   3603  CD2 PHE A 512      20.100  24.335  26.167  1.00 32.59           C  
ATOM   3604  CE1 PHE A 512      22.189  22.620  25.479  1.00 30.64           C  
ATOM   3605  CE2 PHE A 512      20.041  22.981  26.516  1.00 30.30           C  
ATOM   3606  CZ  PHE A 512      21.089  22.123  26.170  1.00 28.27           C  
ATOM   3607  N   GLU A 513      21.956  29.350  24.886  1.00 38.18           N  
ATOM   3608  CA  GLU A 513      22.080  30.554  24.060  1.00 40.60           C  
ATOM   3609  C   GLU A 513      23.419  31.268  24.217  1.00 41.14           C  
ATOM   3610  O   GLU A 513      23.876  31.954  23.299  1.00 40.96           O  
ATOM   3611  CB  GLU A 513      20.944  31.531  24.381  1.00 41.96           C  
ATOM   3612  CG  GLU A 513      19.543  30.927  24.243  1.00 44.42           C  
ATOM   3613  CD  GLU A 513      19.131  30.683  22.798  1.00 47.65           C  
ATOM   3614  OE1 GLU A 513      19.890  30.021  22.053  1.00 47.98           O  
ATOM   3615  OE2 GLU A 513      18.036  31.150  22.407  1.00 49.19           O  
ATOM   3616  N   THR A 514      24.051  31.096  25.374  1.00 40.51           N  
ATOM   3617  CA  THR A 514      25.329  31.746  25.641  1.00 39.31           C  
ATOM   3618  C   THR A 514      26.468  30.741  25.648  1.00 39.71           C  
ATOM   3619  O   THR A 514      27.570  31.049  26.096  1.00 38.82           O  
ATOM   3620  CB  THR A 514      25.303  32.463  27.009  1.00 39.28           C  
ATOM   3621  OG1 THR A 514      25.200  31.490  28.059  1.00 33.95           O  
ATOM   3622  CG2 THR A 514      24.108  33.417  27.086  1.00 37.42           C  
ATOM   3623  N   MET A 515      26.202  29.547  25.129  1.00 40.72           N  
ATOM   3624  CA  MET A 515      27.196  28.475  25.106  1.00 42.41           C  
ATOM   3625  C   MET A 515      28.228  28.547  23.983  1.00 43.35           C  
ATOM   3626  O   MET A 515      29.360  28.098  24.160  1.00 42.46           O  
ATOM   3627  CB  MET A 515      26.490  27.115  25.070  1.00 41.79           C  
ATOM   3628  CG  MET A 515      27.389  25.936  25.398  1.00 42.18           C  
ATOM   3629  SD  MET A 515      26.442  24.445  25.812  1.00 43.30           S  
ATOM   3630  CE  MET A 515      25.995  24.815  27.506  1.00 38.13           C  
ATOM   3631  N   PHE A 516      27.850  29.093  22.830  1.00 44.43           N  
ATOM   3632  CA  PHE A 516      28.795  29.204  21.716  1.00 46.28           C  
ATOM   3633  C   PHE A 516      28.719  30.592  21.087  1.00 48.26           C  
ATOM   3634  O   PHE A 516      28.420  30.734  19.902  1.00 49.08           O  
ATOM   3635  CB  PHE A 516      28.515  28.131  20.653  1.00 44.90           C  
ATOM   3636  CG  PHE A 516      28.381  26.739  21.212  1.00 45.22           C  
ATOM   3637  CD1 PHE A 516      27.161  26.287  21.710  1.00 44.91           C  
ATOM   3638  CD2 PHE A 516      29.474  25.877  21.239  1.00 45.29           C  
ATOM   3639  CE1 PHE A 516      27.028  24.997  22.222  1.00 44.54           C  
ATOM   3640  CE2 PHE A 516      29.354  24.585  21.750  1.00 44.11           C  
ATOM   3641  CZ  PHE A 516      28.127  24.143  22.241  1.00 44.19           C  
ATOM   3642  N   GLN A 517      28.995  31.612  21.894  1.00 51.28           N  
ATOM   3643  CA  GLN A 517      28.948  32.991  21.438  1.00 54.10           C  
ATOM   3644  C   GLN A 517      30.224  33.421  20.738  1.00 55.55           C  
ATOM   3645  O   GLN A 517      30.267  34.492  20.128  1.00 56.10           O  
ATOM   3646  CB  GLN A 517      28.687  33.922  22.618  1.00 55.95           C  
ATOM   3647  CG  GLN A 517      27.616  33.440  23.562  1.00 58.11           C  
ATOM   3648  CD  GLN A 517      27.380  34.411  24.698  1.00 60.07           C  
ATOM   3649  OE1 GLN A 517      26.418  35.185  24.678  1.00 61.51           O  
ATOM   3650  NE2 GLN A 517      28.269  34.392  25.693  1.00 58.13           N  
ATOM   3651  N   GLU A 518      31.265  32.599  20.825  1.00 56.80           N  
ATOM   3652  CA  GLU A 518      32.514  32.948  20.171  1.00 59.38           C  
ATOM   3653  C   GLU A 518      32.807  32.092  18.948  1.00 59.70           C  
ATOM   3654  O   GLU A 518      33.137  32.620  17.883  1.00 61.37           O  
ATOM   3655  CB  GLU A 518      33.675  32.897  21.156  1.00 62.15           C  
ATOM   3656  CG  GLU A 518      33.581  33.995  22.221  1.00 66.12           C  
ATOM   3657  CD  GLU A 518      33.313  35.370  21.624  1.00 67.39           C  
ATOM   3658  OE1 GLU A 518      34.106  35.804  20.761  1.00 67.61           O  
ATOM   3659  OE2 GLU A 518      32.317  36.017  22.018  1.00 68.23           O  
ATOM   3660  N   SER A 519      32.681  30.779  19.097  1.00 59.15           N  
ATOM   3661  CA  SER A 519      32.904  29.876  17.971  1.00 57.35           C  
ATOM   3662  C   SER A 519      31.585  29.145  17.710  1.00 55.90           C  
ATOM   3663  O   SER A 519      30.574  29.458  18.320  1.00 55.63           O  
ATOM   3664  CB  SER A 519      34.018  28.875  18.296  1.00 57.38           C  
ATOM   3665  OG  SER A 519      33.657  28.012  19.360  1.00 58.99           O  
ATOM   3666  N   SER A 520      31.582  28.185  16.796  1.00 53.76           N  
ATOM   3667  CA  SER A 520      30.369  27.431  16.508  1.00 51.79           C  
ATOM   3668  C   SER A 520      30.510  26.053  17.129  1.00 48.72           C  
ATOM   3669  O   SER A 520      31.610  25.499  17.228  1.00 48.05           O  
ATOM   3670  CB  SER A 520      30.159  27.296  15.000  1.00 52.32           C  
ATOM   3671  OG  SER A 520      31.157  26.493  14.390  1.00 55.90           O  
ATOM   3672  N   ILE A 521      29.379  25.512  17.556  1.00 45.15           N  
ATOM   3673  CA  ILE A 521      29.348  24.202  18.170  1.00 42.31           C  
ATOM   3674  C   ILE A 521      30.018  23.186  17.253  1.00 42.31           C  
ATOM   3675  O   ILE A 521      30.531  22.170  17.710  1.00 41.84           O  
ATOM   3676  CB  ILE A 521      27.886  23.757  18.497  1.00 40.08           C  
ATOM   3677  CG1 ILE A 521      27.910  22.419  19.245  1.00 39.33           C  
ATOM   3678  CG2 ILE A 521      27.063  23.643  17.217  1.00 37.87           C  
ATOM   3679  CD1 ILE A 521      26.592  22.017  19.822  1.00 38.44           C  
ATOM   3680  N   SER A 522      30.028  23.475  15.958  1.00 43.29           N  
ATOM   3681  CA  SER A 522      30.653  22.588  14.976  1.00 45.74           C  
ATOM   3682  C   SER A 522      32.173  22.534  15.173  1.00 46.88           C  
ATOM   3683  O   SER A 522      32.778  21.457  15.135  1.00 46.07           O  
ATOM   3684  CB  SER A 522      30.355  23.080  13.562  1.00 47.14           C  
ATOM   3685  OG  SER A 522      28.986  23.406  13.427  1.00 51.36           O  
ATOM   3686  N   ASP A 523      32.786  23.701  15.371  1.00 47.16           N  
ATOM   3687  CA  ASP A 523      34.228  23.776  15.577  1.00 48.36           C  
ATOM   3688  C   ASP A 523      34.590  23.090  16.890  1.00 48.24           C  
ATOM   3689  O   ASP A 523      35.620  22.424  16.989  1.00 47.36           O  
ATOM   3690  CB  ASP A 523      34.688  25.237  15.593  1.00 49.42           C  
ATOM   3691  CG  ASP A 523      34.329  25.973  14.313  1.00 51.96           C  
ATOM   3692  OD1 ASP A 523      34.514  25.395  13.220  1.00 52.92           O  
ATOM   3693  OD2 ASP A 523      33.865  27.130  14.397  1.00 53.98           O  
ATOM   3694  N   GLU A 524      33.732  23.257  17.894  1.00 48.69           N  
ATOM   3695  CA  GLU A 524      33.939  22.639  19.197  1.00 48.97           C  
ATOM   3696  C   GLU A 524      33.943  21.131  19.026  1.00 48.07           C  
ATOM   3697  O   GLU A 524      34.800  20.437  19.563  1.00 46.91           O  
ATOM   3698  CB  GLU A 524      32.821  23.030  20.163  1.00 51.44           C  
ATOM   3699  CG  GLU A 524      32.965  24.411  20.758  1.00 56.71           C  
ATOM   3700  CD  GLU A 524      34.128  24.501  21.722  1.00 60.51           C  
ATOM   3701  OE1 GLU A 524      34.086  23.823  22.774  1.00 63.00           O  
ATOM   3702  OE2 GLU A 524      35.088  25.246  21.424  1.00 63.39           O  
ATOM   3703  N   VAL A 525      32.969  20.631  18.277  1.00 48.99           N  
ATOM   3704  CA  VAL A 525      32.861  19.204  18.029  1.00 49.52           C  
ATOM   3705  C   VAL A 525      34.101  18.759  17.281  1.00 53.41           C  
ATOM   3706  O   VAL A 525      34.634  17.678  17.529  1.00 53.38           O  
ATOM   3707  CB  VAL A 525      31.609  18.869  17.183  1.00 47.25           C  
ATOM   3708  CG1 VAL A 525      31.623  17.401  16.773  1.00 43.10           C  
ATOM   3709  CG2 VAL A 525      30.356  19.179  17.979  1.00 43.54           C  
ATOM   3710  N   GLU A 526      34.568  19.610  16.373  1.00 57.56           N  
ATOM   3711  CA  GLU A 526      35.746  19.296  15.583  1.00 61.43           C  
ATOM   3712  C   GLU A 526      36.970  19.091  16.471  1.00 62.56           C  
ATOM   3713  O   GLU A 526      37.803  18.230  16.196  1.00 62.83           O  
ATOM   3714  CB  GLU A 526      36.013  20.408  14.569  1.00 64.31           C  
ATOM   3715  CG  GLU A 526      37.005  20.006  13.491  1.00 70.29           C  
ATOM   3716  CD  GLU A 526      37.292  21.123  12.506  1.00 73.31           C  
ATOM   3717  OE1 GLU A 526      36.329  21.645  11.898  1.00 74.30           O  
ATOM   3718  OE2 GLU A 526      38.483  21.471  12.341  1.00 74.48           O  
ATOM   3719  N   LYS A 527      37.080  19.879  17.536  1.00 63.68           N  
ATOM   3720  CA  LYS A 527      38.209  19.751  18.451  1.00 65.80           C  
ATOM   3721  C   LYS A 527      38.095  18.510  19.328  1.00 66.40           C  
ATOM   3722  O   LYS A 527      39.093  17.844  19.599  1.00 67.30           O  
ATOM   3723  CB  LYS A 527      38.334  20.994  19.337  1.00 67.29           C  
ATOM   3724  CG  LYS A 527      39.115  22.135  18.697  1.00 69.70           C  
ATOM   3725  CD  LYS A 527      39.211  23.351  19.614  1.00 70.98           C  
ATOM   3726  CE  LYS A 527      37.868  24.052  19.758  1.00 72.29           C  
ATOM   3727  NZ  LYS A 527      37.962  25.277  20.605  1.00 73.92           N  
ATOM   3728  N   GLU A 528      36.880  18.202  19.774  1.00 67.04           N  
ATOM   3729  CA  GLU A 528      36.656  17.033  20.619  1.00 67.52           C  
ATOM   3730  C   GLU A 528      37.018  15.756  19.876  1.00 67.68           C  
ATOM   3731  O   GLU A 528      37.431  14.773  20.487  1.00 68.07           O  
ATOM   3732  CB  GLU A 528      35.193  16.954  21.069  1.00 67.56           C  
ATOM   3733  CG  GLU A 528      34.774  17.991  22.101  1.00 68.85           C  
ATOM   3734  CD  GLU A 528      35.648  17.975  23.344  1.00 70.04           C  
ATOM   3735  OE1 GLU A 528      36.270  16.925  23.621  1.00 68.87           O  
ATOM   3736  OE2 GLU A 528      35.698  19.012  24.048  1.00 69.89           O  
ATOM   3737  N   LEU A 529      36.851  15.770  18.558  1.00 67.98           N  
ATOM   3738  CA  LEU A 529      37.169  14.605  17.741  1.00 68.85           C  
ATOM   3739  C   LEU A 529      38.608  14.680  17.251  1.00 70.13           C  
ATOM   3740  O   LEU A 529      39.432  13.828  17.578  1.00 70.51           O  
ATOM   3741  CB  LEU A 529      36.227  14.519  16.538  1.00 67.28           C  
ATOM   3742  CG  LEU A 529      34.740  14.315  16.826  1.00 66.05           C  
ATOM   3743  CD1 LEU A 529      33.983  14.173  15.521  1.00 65.58           C  
ATOM   3744  CD2 LEU A 529      34.550  13.077  17.674  1.00 66.79           C  
ATOM   3745  N   GLY A 530      38.899  15.710  16.465  1.00 71.51           N  
ATOM   3746  CA  GLY A 530      40.236  15.888  15.934  1.00 72.90           C  
ATOM   3747  C   GLY A 530      40.267  16.964  14.866  1.00 73.85           C  
ATOM   3748  O   GLY A 530      41.035  17.940  15.020  1.00 73.59           O  
TER    3749      GLY A 530                                                      
HETATM 3750  C1  MYR A 701      31.436   8.197  14.434  1.00 76.12           C  
HETATM 3751  O1  MYR A 701      32.235   7.784  13.350  1.00 77.49           O  
HETATM 3752  C2  MYR A 701      31.334   9.722  14.477  1.00 74.44           C  
HETATM 3753  C3  MYR A 701      30.335  10.218  15.532  1.00 72.46           C  
HETATM 3754  C4  MYR A 701      30.422  11.733  15.762  1.00 68.76           C  
HETATM 3755  C5  MYR A 701      29.101  12.345  16.265  1.00 65.07           C  
HETATM 3756  C6  MYR A 701      29.192  13.865  16.493  1.00 60.16           C  
HETATM 3757  C7  MYR A 701      28.861  14.264  17.925  1.00 54.07           C  
HETATM 3758  C8  MYR A 701      27.733  15.280  18.008  1.00 49.46           C  
HETATM 3759  C9  MYR A 701      27.826  16.136  19.259  1.00 46.28           C  
HETATM 3760  C10 MYR A 701      26.708  17.156  19.360  1.00 43.17           C  
HETATM 3761  C11 MYR A 701      26.395  17.546  20.796  1.00 38.61           C  
HETATM 3762  C12 MYR A 701      25.404  18.699  20.860  1.00 37.75           C  
HETATM 3763  C13 MYR A 701      24.058  18.300  21.454  1.00 36.73           C  
HETATM 3764  C14 MYR A 701      23.169  19.502  21.770  1.00 33.68           C  
HETATM 3765  O1  P16 A 702       3.106   8.696  11.186  1.00 45.73           O  
HETATM 3766  C2  P16 A 702       4.314   8.947  11.865  1.00 39.94           C  
HETATM 3767  C3  P16 A 702       4.140   9.435  13.313  1.00 32.81           C  
HETATM 3768  C4  P16 A 702       4.557   8.600  14.416  1.00 32.53           C  
HETATM 3769  C5  P16 A 702       4.401   9.049  15.757  1.00 29.69           C  
HETATM 3770  C6  P16 A 702       3.831  10.325  16.044  1.00 28.59           C  
HETATM 3771  C7  P16 A 702       3.405  11.179  14.961  1.00 29.16           C  
HETATM 3772  N9  P16 A 702       2.801  12.465  15.130  1.00 28.27           N  
HETATM 3773  C10 P16 A 702       2.089  12.959  16.224  1.00 28.18           C  
HETATM 3774  N11 P16 A 702       1.565  14.252  16.074  1.00 27.68           N  
HETATM 3775  C12 P16 A 702       0.834  14.748  17.100  1.00 27.27           C  
HETATM 3776  C13 P16 A 702       0.584  14.010  18.310  1.00 27.97           C  
HETATM 3777  C16 P16 A 702      -0.216  14.501  19.426  1.00 28.25           C  
HETATM 3778  C17 P16 A 702      -0.404  13.732  20.560  1.00 29.41           C  
HETATM 3779  C18 P16 A 702       0.216  12.363  20.662  1.00 29.45           C  
HETATM 3780  O21 P16 A 702       0.114  11.614  21.625  1.00 31.05           O  
HETATM 3781  N19 P16 A 702       1.011  11.903  19.524  1.00 29.52           N  
HETATM 3782  C14 P16 A 702       1.183  12.687  18.372  1.00 27.40           C  
HETATM 3783  N15 P16 A 702       1.914  12.201  17.326  1.00 29.70           N  
HETATM 3784  C20 P16 A 702       1.639  10.559  19.564  1.00 25.51           C  
HETATM 3785  C22 P16 A 702      -1.237  14.190  21.708  1.00 31.71           C  
HETATM 3786  C27 P16 A 702      -0.662  14.762  22.905  1.00 34.91           C  
HETATM 3787 CL28 P16 A 702       1.062  14.959  23.084  1.00 42.89          CL  
HETATM 3788  C26 P16 A 702      -1.502  15.187  23.989  1.00 35.03           C  
HETATM 3789  C25 P16 A 702      -2.919  15.050  23.898  1.00 32.53           C  
HETATM 3790  C24 P16 A 702      -3.514  14.495  22.738  1.00 29.96           C  
HETATM 3791  C23 P16 A 702      -2.683  14.073  21.663  1.00 30.58           C  
HETATM 3792 CL29 P16 A 702      -3.506  13.396  20.258  1.00 31.05          CL  
HETATM 3793  C8  P16 A 702       3.567  10.715  13.592  1.00 28.73           C  
HETATM 3794  C1  GOL A 703      13.032  18.024   7.066  1.00 44.41           C  
HETATM 3795  O1  GOL A 703      11.974  18.982   6.941  1.00 48.20           O  
HETATM 3796  C2  GOL A 703      12.724  16.946   8.129  1.00 42.37           C  
HETATM 3797  O2  GOL A 703      13.581  15.811   7.933  1.00 41.43           O  
HETATM 3798  C3  GOL A 703      12.939  17.486   9.547  1.00 38.41           C  
HETATM 3799  O3  GOL A 703      12.125  18.616   9.805  1.00 36.33           O  
HETATM 3800  C1  GOL A 704      27.554  55.949  21.208  1.00 81.45           C  
HETATM 3801  O1  GOL A 704      27.980  54.869  20.382  1.00 81.28           O  
HETATM 3802  C2  GOL A 704      26.215  55.658  21.921  1.00 82.09           C  
HETATM 3803  O2  GOL A 704      25.304  55.028  21.011  1.00 82.24           O  
HETATM 3804  C3  GOL A 704      26.418  54.743  23.130  1.00 82.49           C  
HETATM 3805  O3  GOL A 704      27.310  55.311  24.075  1.00 82.92           O  
HETATM 3806  O   HOH A 538      17.856   6.794  36.643  1.00 20.48           O  
HETATM 3807  O   HOH A 539      -3.936  26.311  23.682  1.00 24.73           O  
HETATM 3808  O   HOH A 540      25.676  11.673  43.094  1.00 24.00           O  
HETATM 3809  O   HOH A 541      13.661   8.272  24.798  1.00 25.95           O  
HETATM 3810  O   HOH A 542      27.938  11.045  19.710  1.00 30.71           O  
HETATM 3811  O   HOH A 543     -14.347  30.496  13.800  1.00 24.57           O  
HETATM 3812  O   HOH A 544       2.470  24.863  19.531  1.00 38.08           O  
HETATM 3813  O   HOH A 545      29.426  57.077   6.031  1.00 40.50           O  
HETATM 3814  O   HOH A 546       0.606  30.936  28.601  1.00 30.05           O  
HETATM 3815  O   HOH A 547      18.935   8.555  34.888  1.00 21.23           O  
HETATM 3816  O   HOH A 548      23.991   9.504  34.066  1.00 27.41           O  
HETATM 3817  O   HOH A 549      25.013   2.407  46.203  1.00 35.25           O  
HETATM 3818  O   HOH A 550      20.568  27.647  21.204  1.00 29.58           O  
HETATM 3819  O   HOH A 551      -3.399  33.660  16.515  1.00 36.32           O  
HETATM 3820  O   HOH A 552      16.450  29.814   6.531  1.00 37.26           O  
HETATM 3821  O   HOH A 553       1.750  32.497  17.878  1.00 37.67           O  
HETATM 3822  O   HOH A 554      28.822  49.575   7.946  1.00 25.97           O  
HETATM 3823  O   HOH A 555       8.374   7.763  15.434  1.00 25.68           O  
HETATM 3824  O   HOH A 556      23.692  42.042  -3.421  1.00 33.30           O  
HETATM 3825  O   HOH A 557      -0.083   5.354  20.652  1.00 25.12           O  
HETATM 3826  O   HOH A 558     -14.874  18.102   8.594  1.00 31.47           O  
HETATM 3827  O   HOH A 559      26.335  21.075  42.455  1.00 34.19           O  
HETATM 3828  O   HOH A 560      -2.127  19.191  11.978  1.00 29.81           O  
HETATM 3829  O   HOH A 561      25.596  15.398  42.905  1.00 24.34           O  
HETATM 3830  O   HOH A 562      -2.962  31.932  18.726  1.00 27.25           O  
HETATM 3831  O   HOH A 563      10.919  28.914  33.905  1.00 23.21           O  
HETATM 3832  O   HOH A 564      10.145  13.705  32.912  1.00 27.90           O  
HETATM 3833  O   HOH A 565      13.227  42.533  16.852  1.00 44.26           O  
HETATM 3834  O   HOH A 566      -2.800  16.610  32.571  1.00 31.06           O  
HETATM 3835  O   HOH A 567      32.031  29.672  21.527  1.00 44.11           O  
HETATM 3836  O   HOH A 568       5.419  37.280  13.475  1.00 33.01           O  
HETATM 3837  O   HOH A 569       6.730  23.398  37.665  1.00 33.37           O  
HETATM 3838  O   HOH A 570     -11.997  23.461  17.134  1.00 29.31           O  
HETATM 3839  O   HOH A 571      29.862  28.441  10.882  1.00 32.91           O  
HETATM 3840  O   HOH A 572      17.366   6.144  23.881  1.00 26.66           O  
HETATM 3841  O   HOH A 573      29.935  30.220  13.001  1.00 32.15           O  
HETATM 3842  O   HOH A 574     -12.657  21.449   1.972  1.00 31.18           O  
HETATM 3843  O   HOH A 575       9.604  14.261  36.621  1.00 40.06           O  
HETATM 3844  O   HOH A 576      -7.226  38.201   0.939  1.00 52.93           O  
HETATM 3845  O   HOH A 577       8.100  21.139  41.052  1.00 33.99           O  
HETATM 3846  O   HOH A 578      17.805  12.906   8.013  1.00 44.61           O  
HETATM 3847  O   HOH A 579      23.113   1.482  25.354  1.00 54.52           O  
HETATM 3848  O   HOH A 580      25.521  26.632  10.419  1.00 33.17           O  
HETATM 3849  O   HOH A 581      33.164  11.052  30.655  1.00 41.08           O  
HETATM 3850  O   HOH A 582      26.133  52.950  -0.500  1.00 42.36           O  
HETATM 3851  O   HOH A 583      12.394  49.981   5.953  1.00 37.53           O  
HETATM 3852  O   HOH A 584     -13.600  25.269  27.421  1.00 43.44           O  
HETATM 3853  O   HOH A 585     -17.113  25.074  19.905  1.00 46.65           O  
HETATM 3854  O   HOH A 586      10.484   9.803  13.818  1.00 35.04           O  
HETATM 3855  O   HOH A 587     -15.967  27.895  12.281  1.00 39.09           O  
HETATM 3856  O   HOH A 588       3.475  51.263   8.962  1.00 36.55           O  
HETATM 3857  O   HOH A 589     -13.111  43.915  14.894  1.00 35.04           O  
HETATM 3858  O   HOH A 590      14.905  50.493   7.602  1.00 32.92           O  
HETATM 3859  O   HOH A 591      32.946  43.926  -2.354  1.00 40.10           O  
HETATM 3860  O   HOH A 592      -0.572  12.135   6.854  1.00 57.48           O  
HETATM 3861  O   HOH A 593      -6.696  33.593  26.096  1.00 35.20           O  
HETATM 3862  O   HOH A 594      23.992  -3.907  30.502  1.00 57.45           O  
HETATM 3863  O   HOH A 595       0.267  18.662  10.122  1.00 53.75           O  
HETATM 3864  O   HOH A 596      31.755  35.832  13.146  1.00 48.05           O  
HETATM 3865  O   HOH A 597      18.266   0.717  39.936  1.00 35.53           O  
HETATM 3866  O   HOH A 598       3.394  40.835  14.019  1.00 43.71           O  
HETATM 3867  O   HOH A 599       1.814  20.838  12.926  1.00 51.35           O  
HETATM 3868  O   HOH A 600     -12.443  44.318  19.965  1.00 32.10           O  
HETATM 3869  O   HOH A 601      19.657  26.688  18.547  1.00 28.72           O  
HETATM 3870  O   HOH A 602       3.141  25.503  14.623  1.00 45.85           O  
HETATM 3871  O   HOH A 603      22.083  47.427  16.501  1.00 40.56           O  
HETATM 3872  O   HOH A 604      -5.297  43.088  -0.517  1.00 41.05           O  
HETATM 3873  O   HOH A 605      26.460  14.663  37.720  1.00 31.15           O  
HETATM 3874  O   HOH A 606      -1.755  17.316  29.839  1.00 40.49           O  
HETATM 3875  O   HOH A 607      14.606  29.224  21.929  1.00 35.74           O  
HETATM 3876  O   HOH A 608      20.523  -0.278  41.883  1.00 28.48           O  
HETATM 3877  O   HOH A 609      23.886  22.603  39.084  1.00 31.49           O  
HETATM 3878  O   HOH A 610     -13.568  37.153  20.829  1.00 32.66           O  
HETATM 3879  O   HOH A 611      27.076  29.741  -3.276  1.00 32.12           O  
HETATM 3880  O   HOH A 612     -14.932  -2.511  31.531  1.00 39.23           O  
HETATM 3881  O   HOH A 613     -13.567  24.200  15.093  1.00 32.30           O  
HETATM 3882  O   HOH A 614       9.706  29.790  26.958  1.00 35.30           O  
HETATM 3883  O   HOH A 615      -1.189  35.982  17.226  1.00 40.75           O  
HETATM 3884  O   HOH A 616      26.464  34.110  -3.951  1.00 28.08           O  
HETATM 3885  O   HOH A 617      -2.402  25.626  14.986  1.00 39.68           O  
HETATM 3886  O   HOH A 618      20.589  25.073  41.260  1.00 36.55           O  
HETATM 3887  O   HOH A 619      -2.276   1.372  23.353  1.00 53.33           O  
HETATM 3888  O   HOH A 620      33.491  37.685  12.106  1.00 44.19           O  
HETATM 3889  O   HOH A 621     -13.262  26.076  12.934  1.00 41.55           O  
HETATM 3890  O   HOH A 622       4.688  31.343  24.815  1.00 46.98           O  
HETATM 3891  O   HOH A 623      22.937  52.280   0.443  1.00 40.30           O  
HETATM 3892  O   HOH A 624      25.306  23.723   9.581  1.00 37.88           O  
HETATM 3893  O   HOH A 625      -2.609  28.299   6.957  1.00 45.14           O  
HETATM 3894  O   HOH A 626      -2.713  30.490  28.799  1.00 48.39           O  
HETATM 3895  O   HOH A 627      18.860  26.850  40.401  1.00 34.87           O  
HETATM 3896  O   HOH A 628      29.163  30.920  16.356  1.00 47.31           O  
HETATM 3897  O   HOH A 629      -2.250  22.197  12.012  1.00 40.28           O  
HETATM 3898  O   HOH A 630      16.787  29.963  20.453  1.00 36.96           O  
HETATM 3899  O   HOH A 631      26.698  27.042  17.266  1.00 30.40           O  
HETATM 3900  O   HOH A 632      21.807  25.870  16.709  1.00 40.00           O  
HETATM 3901  O   HOH A 633      -2.268  23.122  22.972  1.00 45.82           O  
HETATM 3902  O   HOH A 634       0.966   8.934  39.432  1.00 43.38           O  
HETATM 3903  O   HOH A 635     -15.936   9.879   9.958  1.00 43.57           O  
HETATM 3904  O   HOH A 636      -4.479  26.299  13.748  1.00 48.63           O  
HETATM 3905  O   HOH A 637       3.303  12.973  31.550  1.00 56.07           O  
HETATM 3906  O   HOH A 638      17.230  25.441  43.753  1.00 44.55           O  
HETATM 3907  O   HOH A 639       8.174   7.662  12.793  1.00 44.65           O  
HETATM 3908  O   HOH A 640      15.942  32.111  18.701  1.00 43.11           O  
HETATM 3909  O   HOH A 641     -10.628  23.014   1.470  1.00 43.91           O  
HETATM 3910  O   HOH A 642       9.970  53.083   8.640  1.00 52.78           O  
HETATM 3911  O   HOH A 643      -4.661  27.422   8.713  1.00 46.53           O  
HETATM 3912  O   HOH A 644      12.431  29.861  26.209  1.00 36.28           O  
HETATM 3913  O   HOH A 645      30.475  31.210  24.120  1.00 44.76           O  
HETATM 3914  O   HOH A 646      29.902  54.992  17.806  1.00 47.38           O  
HETATM 3915  O   HOH A 647      32.775  10.802  41.611  1.00 39.52           O  
HETATM 3916  O   HOH A 648      15.851   3.952  24.181  1.00 39.46           O  
HETATM 3917  O   HOH A 649      -0.512  27.158  13.272  1.00 58.97           O  
HETATM 3918  O   HOH A 650      21.880  40.702  17.918  1.00 40.77           O  
HETATM 3919  O   HOH A 651      31.382  36.161  16.151  1.00 52.59           O  
HETATM 3920  O   HOH A 652      35.091  12.851  21.703  1.00 39.30           O  
HETATM 3921  O   HOH A 653      27.986  28.575   1.396  1.00 35.76           O  
HETATM 3922  O   HOH A 654      13.454  24.908  39.079  1.00 49.25           O  
HETATM 3923  O   HOH A 655      15.145  10.219  10.651  1.00 49.62           O  
HETATM 3924  O   HOH A 656       1.218   2.611  14.633  1.00 44.00           O  
HETATM 3925  O   HOH A 657      15.809  31.211  29.561  1.00 49.84           O  
HETATM 3926  O   HOH A 658      26.658  29.835  17.683  1.00 49.13           O  
HETATM 3927  O   HOH A 659      23.208  40.078  -5.154  1.00 43.84           O  
HETATM 3928  O   HOH A 660      22.246  31.630  20.953  1.00 29.67           O  
HETATM 3929  O   HOH A 661      29.976  57.553  17.608  1.00 44.36           O  
HETATM 3930  O   HOH A 662      20.348  39.669  -4.804  1.00 47.85           O  
HETATM 3931  O   HOH A 663      13.577  43.376  -7.252  1.00 39.40           O  
HETATM 3932  O   HOH A 664     -18.338  18.321  20.092  1.00 31.73           O  
HETATM 3933  O   HOH A 665      -2.487  24.038   9.749  1.00 47.45           O  
HETATM 3934  O   HOH A 666      -9.436  25.168  30.525  1.00 52.16           O  
HETATM 3935  O   HOH A 667      12.147  15.923  42.739  1.00 40.24           O  
HETATM 3936  O   HOH A 668      34.826  15.296  29.623  1.00 54.97           O  
HETATM 3937  O   HOH A 669      28.200   6.070  29.496  1.00 46.17           O  
HETATM 3938  O   HOH A 670      26.891   4.027  30.739  1.00 34.65           O  
HETATM 3939  O   HOH A 671      17.670  12.767  45.056  1.00 42.31           O  
HETATM 3940  O   HOH A 672       5.395  21.253  11.135  1.00 43.89           O  
HETATM 3941  O   HOH A 673      27.028  14.976  12.850  1.00 44.70           O  
HETATM 3942  O   HOH A 674      -3.939  27.748  11.414  1.00 38.89           O  
HETATM 3943  O   HOH A 675     -14.679   9.858  14.414  1.00 51.09           O  
HETATM 3944  O   HOH A 676      -0.379  34.851  22.162  1.00 43.50           O  
HETATM 3945  O   HOH A 677      27.615  27.085  11.867  1.00 43.76           O  
HETATM 3946  O   HOH A 678      -9.858  28.121  25.963  1.00 51.57           O  
HETATM 3947  O   HOH A 679      -7.559  29.098  25.221  1.00 29.52           O  
HETATM 3948  O   HOH A 680      14.082  44.001   1.400  1.00 50.79           O  
HETATM 3949  O   HOH A 681      23.763  17.116  45.044  1.00 25.41           O  
HETATM 3950  O   HOH A 682       0.920  25.172  22.855  1.00 24.45           O  
CONECT   33   39                                                                
CONECT   39   33   40                                                           
CONECT   40   39   41   43                                                      
CONECT   41   40   42                                                           
CONECT   42   41   45                                                           
CONECT   43   40   44   49                                                      
CONECT   44   43                                                                
CONECT   45   42   46   47   48                                                 
CONECT   46   45                                                                
CONECT   47   45                                                                
CONECT   48   45                                                                
CONECT   49   43                                                                
CONECT 3750 3751 3752                                                           
CONECT 3751 3750                                                                
CONECT 3752 3750 3753                                                           
CONECT 3753 3752 3754                                                           
CONECT 3754 3753 3755                                                           
CONECT 3755 3754 3756                                                           
CONECT 3756 3755 3757                                                           
CONECT 3757 3756 3758                                                           
CONECT 3758 3757 3759                                                           
CONECT 3759 3758 3760                                                           
CONECT 3760 3759 3761                                                           
CONECT 3761 3760 3762                                                           
CONECT 3762 3761 3763                                                           
CONECT 3763 3762 3764                                                           
CONECT 3764 3763                                                                
CONECT 3765 3766                                                                
CONECT 3766 3765 3767                                                           
CONECT 3767 3766 3768 3793                                                      
CONECT 3768 3767 3769                                                           
CONECT 3769 3768 3770                                                           
CONECT 3770 3769 3771                                                           
CONECT 3771 3770 3772 3793                                                      
CONECT 3772 3771 3773                                                           
CONECT 3773 3772 3774 3783                                                      
CONECT 3774 3773 3775                                                           
CONECT 3775 3774 3776                                                           
CONECT 3776 3775 3777 3782                                                      
CONECT 3777 3776 3778                                                           
CONECT 3778 3777 3779 3785                                                      
CONECT 3779 3778 3780 3781                                                      
CONECT 3780 3779                                                                
CONECT 3781 3779 3782 3784                                                      
CONECT 3782 3776 3781 3783                                                      
CONECT 3783 3773 3782                                                           
CONECT 3784 3781                                                                
CONECT 3785 3778 3786 3791                                                      
CONECT 3786 3785 3787 3788                                                      
CONECT 3787 3786                                                                
CONECT 3788 3786 3789                                                           
CONECT 3789 3788 3790                                                           
CONECT 3790 3789 3791                                                           
CONECT 3791 3785 3790 3792                                                      
CONECT 3792 3791                                                                
CONECT 3793 3767 3771                                                           
CONECT 3794 3795 3796                                                           
CONECT 3795 3794                                                                
CONECT 3796 3794 3797 3798                                                      
CONECT 3797 3796                                                                
CONECT 3798 3796 3799                                                           
CONECT 3799 3798                                                                
CONECT 3800 3801 3802                                                           
CONECT 3801 3800                                                                
CONECT 3802 3800 3803 3804                                                      
CONECT 3803 3802                                                                
CONECT 3804 3802 3805                                                           
CONECT 3805 3804                                                                
MASTER      332    0    5   21   24    0    8    6 3949    1   68   39          
END                                                                             
