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***  SIGNALING PROTEIN 15-JUL-04 1U19  ***

elNémo ID: 19100908220743298

Job options:

ID        	=	 19100908220743298
JOBID     	=	 SIGNALING PROTEIN 15-JUL-04 1U19
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    SIGNALING PROTEIN                       15-JUL-04   1U19              
TITLE     CRYSTAL STRUCTURE OF BOVINE RHODOPSIN AT 2.2 ANGSTROMS RESOLUTION     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RHODOPSIN;                                                 
COMPND   3 CHAIN: A, B                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913                                                 
KEYWDS    G PROTEIN-COUPLED RECEPTOR, MEMBRANE PROTEIN, RETINAL PROTEIN,        
KEYWDS   2 PHOTORECEPTOR, SIGNALING PROTEIN                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.OKADA,M.SUGIHARA,A.N.BONDAR,M.ELSTNER,P.ENTEL,V.BUSS                
REVDAT   4   25-MAR-15 1U19    1       REMARK                                   
REVDAT   3   13-JUL-11 1U19    1       VERSN                                    
REVDAT   2   24-FEB-09 1U19    1       VERSN                                    
REVDAT   1   12-OCT-04 1U19    0                                                
JRNL        AUTH   T.OKADA,M.SUGIHARA,A.N.BONDAR,M.ELSTNER,P.ENTEL,V.BUSS       
JRNL        TITL   THE RETINAL CONFORMATION AND ITS ENVIRONMENT IN RHODOPSIN IN 
JRNL        TITL 2 LIGHT OF A NEW 2.2 A CRYSTAL STRUCTURE                       
JRNL        REF    J.MOL.BIOL.                   V. 342   571 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15327956                                                     
JRNL        DOI    10.1016/J.JMB.2004.07.044                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 59552                          
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) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2839                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5498                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 384                                     
REMARK   3   SOLVENT ATOMS            : 66                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.53                            
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) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.49                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.600                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.970                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1U19 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUL-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023119.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61728                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.4                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 46.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.200                              
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 1L9H                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 6.0, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 283K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
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       75.10000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       37.55000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      112.65000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND1  HIS A    65     O    VAL A   337              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NE2  GLN A   344     O6   HTG B  1509     4564     2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 347   C   -  N   -  CA  ANGL. DEV. =   9.1 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    TYR A  10       94.72   -164.52                                   
REMARK 500    GLU A  25      -25.20   -145.41                                   
REMARK 500    VAL A 139      -73.95    -68.59                                   
REMARK 500    LYS A 141       91.59     16.27                                   
REMARK 500    ASN A 145       36.50   -177.92                                   
REMARK 500    SER A 176     -163.64     66.65                                   
REMARK 500    GLN A 184       30.66     71.64                                   
REMARK 500    HIS A 195       81.05      4.65                                   
REMARK 500    HIS A 211       53.00   -114.92                                   
REMARK 500    PHE A 212      -83.13    179.74                                   
REMARK 500    LEU A 226       41.59    -78.43                                   
REMARK 500    THR A 229     -136.01    -81.41                                   
REMARK 500    ALA A 233       94.22    -62.40                                   
REMARK 500    ALA A 235     -151.04    -93.74                                   
REMARK 500    GLN A 238      125.99     69.04                                   
REMARK 500    SER A 240       17.04    167.58                                   
REMARK 500    ALA A 241      132.21    148.69                                   
REMARK 500    HIS A 278       47.56   -143.13                                   
REMARK 500    VAL A 300      -33.74   -133.39                                   
REMARK 500    CYS A 322       31.86    -67.16                                   
REMARK 500    CYS A 323      -68.14     45.04                                   
REMARK 500    LYS A 325     -118.21   -137.50                                   
REMARK 500    ASN A 326       72.32     54.51                                   
REMARK 500    PRO A 327       27.99    -69.90                                   
REMARK 500    LEU A 328     -101.09     11.79                                   
REMARK 500    ASP A 331     -151.01     61.85                                   
REMARK 500    ALA A 333      -29.31     68.77                                   
REMARK 500    SER A 334     -161.99   -107.01                                   
REMARK 500    THR A 335      159.81    -38.78                                   
REMARK 500    SER A 338     -144.27   -176.70                                   
REMARK 500    LYS A 339      -71.43   -108.32                                   
REMARK 500    GLU A 341     -121.86    -70.18                                   
REMARK 500    THR A 342       45.44    -97.23                                   
REMARK 500    GLN A 344      107.02    -51.12                                   
REMARK 500    ALA A 346       59.91   -146.16                                   
REMARK 500    PRO A 347     -107.93    -83.03                                   
REMARK 500    TYR B  10       97.71   -161.29                                   
REMARK 500    SER B  22      130.39    -37.97                                   
REMARK 500    LEU B  68       81.99    -67.11                                   
REMARK 500    ARG B  69       26.17   -147.78                                   
REMARK 500    LYS B 141       89.33     -1.40                                   
REMARK 500    SER B 144      -62.88   -109.26                                   
REMARK 500    SER B 176     -170.27     69.39                                   
REMARK 500    HIS B 195       74.83     15.58                                   
REMARK 500    GLU B 197      -14.18    -48.88                                   
REMARK 500    THR B 198       13.44   -145.39                                   
REMARK 500    HIS B 211       33.43    -96.96                                   
REMARK 500    PHE B 212      -72.86   -161.98                                   
REMARK 500    LEU B 226       36.71    -84.32                                   
REMARK 500    THR B 229     -144.12    -70.00                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      75 RAMACHANDRAN OUTLIERS.                        
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     PLM B 1407                                                       
REMARK 610     PLM A 1410                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2011  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 195   NE2                                                    
REMARK 620 2 GLU A 197   OE1  91.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 957  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 201   OE1                                                    
REMARK 620 2 GLU A 201   OE2  60.8                                              
REMARK 620 3 GLN A 279   NE2 165.9 109.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 959  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS A 311   NZ                                                     
REMARK 620 2 ASP A 330   N   108.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 956  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 195   NE2                                                    
REMARK 620 2 GLU B 197   OE1  85.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 958  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 201   OE2                                                    
REMARK 620 2 GLN B 279   NE2  84.0                                              
REMARK 620 3 GLU B 201   OE1  57.0 139.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              HG B 906  HG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B 336   O                                                      
REMARK 620 2 VAL B 337   O    68.9                                              
REMARK 620 3 CYS B 316   SG   73.1 141.9                                        
REMARK 620 4 HIS B  65   ND1 136.5  74.3 140.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 962  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 211   ND1                                                    
REMARK 620 2 GLU A 122   OE1 101.7                                              
REMARK 620 3 TRP A 126   NE1  83.0  70.8                                        
REMARK 620 4 MET A 163   O    95.7 154.9  93.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 963  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 211   ND1                                                    
REMARK 620 2 TRP B 126   NE1  86.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              HG A 905  HG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 316   SG                                                     
REMARK 620 2 HOH A2061   O    78.5                                              
REMARK 620 3 GLN A 312   O    80.0 135.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              HG A 901  HG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 264   SG                                                     
REMARK 620 2 THR A 297   OG1  77.9                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 903                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 904                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 905                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 906                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 956                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 957                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 958                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 959                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 962                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 963                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2011                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RET A 1296                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 1322                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 1323                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RET B 1296                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM B 1322                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM B 1323                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HTO B 1401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM B 1407                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 1410                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HTG B 1506                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HTG A 1507                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HTG B 1508                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HTG B 1509                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1F88   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1HZX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1L9H   RELATED DB: PDB                                   
DBREF  1U19 A    1   348  UNP    P02699   OPSD_BOVIN       1    348             
DBREF  1U19 B    1   348  UNP    P02699   OPSD_BOVIN       1    348             
SEQRES   1 A  349  ACE MET ASN GLY THR GLU GLY PRO ASN PHE TYR VAL PRO          
SEQRES   2 A  349  PHE SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU          
SEQRES   3 A  349  ALA PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER          
SEQRES   4 A  349  MET LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY          
SEQRES   5 A  349  PHE PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN          
SEQRES   6 A  349  HIS LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU          
SEQRES   7 A  349  ASN LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY          
SEQRES   8 A  349  PHE THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE          
SEQRES   9 A  349  VAL PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE          
SEQRES  10 A  349  ALA THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL          
SEQRES  11 A  349  VAL LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO          
SEQRES  12 A  349  MET SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET          
SEQRES  13 A  349  GLY VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA          
SEQRES  14 A  349  ALA PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU          
SEQRES  15 A  349  GLY MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO          
SEQRES  16 A  349  HIS GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET          
SEQRES  17 A  349  PHE VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE          
SEQRES  18 A  349  PHE CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA          
SEQRES  19 A  349  ALA ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA          
SEQRES  20 A  349  GLU LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE          
SEQRES  21 A  349  ALA PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA          
SEQRES  22 A  349  PHE TYR ILE PHE THR HIS GLN GLY SER ASP PHE GLY PRO          
SEQRES  23 A  349  ILE PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER          
SEQRES  24 A  349  ALA VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS          
SEQRES  25 A  349  GLN PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY          
SEQRES  26 A  349  LYS ASN PRO LEU GLY ASP ASP GLU ALA SER THR THR VAL          
SEQRES  27 A  349  SER LYS THR GLU THR SER GLN VAL ALA PRO ALA                  
SEQRES   1 B  349  ACE MET ASN GLY THR GLU GLY PRO ASN PHE TYR VAL PRO          
SEQRES   2 B  349  PHE SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU          
SEQRES   3 B  349  ALA PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER          
SEQRES   4 B  349  MET LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY          
SEQRES   5 B  349  PHE PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN          
SEQRES   6 B  349  HIS LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU          
SEQRES   7 B  349  ASN LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY          
SEQRES   8 B  349  PHE THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE          
SEQRES   9 B  349  VAL PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE          
SEQRES  10 B  349  ALA THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL          
SEQRES  11 B  349  VAL LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO          
SEQRES  12 B  349  MET SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET          
SEQRES  13 B  349  GLY VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA          
SEQRES  14 B  349  ALA PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU          
SEQRES  15 B  349  GLY MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO          
SEQRES  16 B  349  HIS GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET          
SEQRES  17 B  349  PHE VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE          
SEQRES  18 B  349  PHE CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA          
SEQRES  19 B  349  ALA ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA          
SEQRES  20 B  349  GLU LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE          
SEQRES  21 B  349  ALA PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA          
SEQRES  22 B  349  PHE TYR ILE PHE THR HIS GLN GLY SER ASP PHE GLY PRO          
SEQRES  23 B  349  ILE PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER          
SEQRES  24 B  349  ALA VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS          
SEQRES  25 B  349  GLN PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY          
SEQRES  26 B  349  LYS ASN PRO LEU GLY ASP ASP GLU ALA SER THR THR VAL          
SEQRES  27 B  349  SER LYS THR GLU THR SER GLN VAL ALA PRO ALA                  
MODRES 1U19 ASN A    2  ASN  GLYCOSYLATION SITE                                 
MODRES 1U19 ASN A   15  ASN  GLYCOSYLATION SITE                                 
MODRES 1U19 ASN B    2  ASN  GLYCOSYLATION SITE                                 
MODRES 1U19 ASN B   15  ASN  GLYCOSYLATION SITE                                 
HET    ACE  A   0       3                                                       
HET    ACE  B   0       3                                                       
HET    MAN  A 503      11                                                       
HET    NAG  A 504      14                                                       
HET    NAG  A 505      14                                                       
HET    BMA  B 602      11                                                       
HET    BMA  B 603      11                                                       
HET    NAG  B 604      14                                                       
HET    NAG  B 605      14                                                       
HET    NAG  A 704      14                                                       
HET    NAG  A 705      14                                                       
HET    NAG  B 804      14                                                       
HET    NAG  B 805      14                                                       
HET     HG  A 901       1                                                       
HET     HG  B 902       1                                                       
HET     HG  A 903       1                                                       
HET     HG  B 904       1                                                       
HET     HG  A 905       1                                                       
HET     HG  B 906       1                                                       
HET     ZN  B 956       1                                                       
HET     ZN  A 957       1                                                       
HET     ZN  B 958       1                                                       
HET     ZN  A 959       1                                                       
HET     ZN  A 962       1                                                       
HET     ZN  B 963       1                                                       
HET     ZN  A2011       1                                                       
HET    RET  A1296      20                                                       
HET    PLM  A1322      17                                                       
HET    PLM  A1323      17                                                       
HET    RET  B1296      20                                                       
HET    PLM  B1322      17                                                       
HET    PLM  B1323      17                                                       
HET    HTO  B1401      10                                                       
HET    PLM  B1407      16                                                       
HET    PLM  A1410      16                                                       
HET    HTG  B1506      19                                                       
HET    HTG  A1507      19                                                       
HET    HTG  B1508      19                                                       
HET    HTG  B1509      19                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM      HG MERCURY (II) ION                                                 
HETNAM      ZN ZINC ION                                                         
HETNAM     RET RETINAL                                                          
HETNAM     PLM PALMITIC ACID                                                    
HETNAM     HTO HEPTANE-1,2,3-TRIOL                                              
HETNAM     HTG HEPTYL 1-THIOHEXOPYRANOSIDE                                      
FORMUL   1  ACE    2(C2 H4 O)                                                   
FORMUL   3  MAN    C6 H12 O6                                                    
FORMUL   3  NAG    8(C8 H15 N O6)                                               
FORMUL   4  BMA    2(C6 H12 O6)                                                 
FORMUL   7   HG    6(HG 2+)                                                     
FORMUL  13   ZN    7(ZN 2+)                                                     
FORMUL  20  RET    2(C20 H28 O)                                                 
FORMUL  21  PLM    6(C16 H32 O2)                                                
FORMUL  26  HTO    C7 H16 O3                                                    
FORMUL  29  HTG    4(C13 H26 O5 S)                                              
FORMUL  33  HOH   *66(H2 O)                                                     
HELIX    1   1 GLU A   33  HIS A   65  1                                  33    
HELIX    2   2 THR A   70  GLY A   90  1                                  21    
HELIX    3   3 GLY A   90  GLY A  101  1                                  12    
HELIX    4   4 PHE A  105  CYS A  140  1                                  36    
HELIX    5   5 GLY A  149  ALA A  169  1                                  21    
HELIX    6   6 PRO A  170  VAL A  173  5                                   4    
HELIX    7   7 HIS A  195  THR A  198  5                                   4    
HELIX    8   8 ASN A  199  HIS A  211  1                                  13    
HELIX    9   9 PHE A  212  GLY A  224  1                                  13    
HELIX   10  10 ALA A  241  HIS A  278  1                                  38    
HELIX   11  11 GLY A  284  ALA A  295  1                                  12    
HELIX   12  12 LYS A  296  ALA A  299  5                                   4    
HELIX   13  13 VAL A  300  MET A  309  1                                  10    
HELIX   14  14 ASN A  310  CYS A  322  1                                  13    
HELIX   15  15 GLU B   33  HIS B   65  1                                  33    
HELIX   16  16 THR B   70  GLY B   90  1                                  21    
HELIX   17  17 GLY B   90  GLY B  101  1                                  12    
HELIX   18  18 PHE B  105  CYS B  140  1                                  36    
HELIX   19  19 GLY B  149  ALA B  169  1                                  21    
HELIX   20  20 PRO B  170  VAL B  173  5                                   4    
HELIX   21  21 HIS B  195  THR B  198  5                                   4    
HELIX   22  22 ASN B  199  VAL B  210  1                                  12    
HELIX   23  23 PHE B  212  LEU B  226  1                                  15    
HELIX   24  24 ALA B  241  ALA B  246  1                                   6    
HELIX   25  25 GLU B  247  THR B  277  1                                  31    
HELIX   26  26 GLY B  284  LYS B  296  1                                  13    
HELIX   27  27 THR B  297  ALA B  299  5                                   3    
HELIX   28  28 VAL B  300  ASN B  310  1                                  11    
HELIX   29  29 ASN B  310  CYS B  322  1                                  13    
SHEET    1   A 2 THR A   4  GLU A   5  0                                        
SHEET    2   A 2 TYR A  10  VAL A  11 -1  O  VAL A  11   N  THR A   4           
SHEET    1   B 2 ILE A 179  GLU A 181  0                                        
SHEET    2   B 2 SER A 186  GLY A 188 -1  O  GLY A 188   N  ILE A 179           
SHEET    1   C 2 THR B   4  GLU B   5  0                                        
SHEET    2   C 2 TYR B  10  VAL B  11 -1  O  VAL B  11   N  THR B   4           
SHEET    1   D 2 TYR B 178  GLU B 181  0                                        
SHEET    2   D 2 SER B 186  ILE B 189 -1  O  GLY B 188   N  ILE B 179           
SSBOND   1 CYS A  110    CYS A  187                          1555   1555  2.02  
SSBOND   2 CYS B  110    CYS B  187                          1555   1555  2.03  
LINK         C15 RET A1296                 NZ  LYS A 296     1555   1555  1.33  
LINK         C1  PLM A1322                 SG  CYS A 322     1555   1555  1.86  
LINK         C1  PLM A1323                 SG  CYS A 323     1555   1555  1.89  
LINK         C15 RET B1296                 NZ  LYS B 296     1555   1555  1.34  
LINK         C1  PLM B1322                 SG  CYS B 322     1555   1555  1.89  
LINK         C1  PLM B1323                 SG  CYS B 323     1555   1555  1.90  
LINK         ND2 ASN A   2                 C1  NAG A 705     1555   1555  1.44  
LINK         ND2 ASN A  15                 C1  NAG A 505     1555   1555  1.45  
LINK         ND2 ASN B   2                 C1  NAG B 805     1555   1555  1.45  
LINK         ND2 ASN B  15                 C1  NAG B 605     1555   1555  1.44  
LINK         C1  MAN A 503                 O4  NAG A 504     1555   1555  1.40  
LINK         C1  NAG A 504                 O4  NAG A 505     1555   1555  1.40  
LINK         C1  BMA B 602                 O3  BMA B 603     1555   1555  1.40  
LINK         C1  BMA B 603                 O4  NAG B 604     1555   1555  1.38  
LINK         C1  NAG B 604                 O4  NAG B 605     1555   1555  1.38  
LINK         C1  NAG A 704                 O4  NAG A 705     1555   1555  1.38  
LINK         C1  NAG B 804                 O4  NAG B 805     1555   1555  1.39  
LINK         C   ACE A   0                 N   MET A   1     1555   1555  1.35  
LINK         C   ACE B   0                 N   MET B   1     1555   1555  1.35  
LINK         NE2 HIS A 195                ZN    ZN A2011     1555   1555  2.20  
LINK         OE1 GLU A 201                ZN    ZN A 957     1555   1555  2.31  
LINK         OE2 GLU A 201                ZN    ZN A 957     1555   1555  2.00  
LINK         NZ  LYS A 311                ZN    ZN A 959     1555   1555  1.83  
LINK         NE2 HIS B 195                ZN    ZN B 956     1555   1555  2.06  
LINK         OE1 GLU B 197                ZN    ZN B 956     1555   1555  2.09  
LINK         OE2 GLU B 201                ZN    ZN B 958     1555   1555  2.15  
LINK         NE2 GLN B 279                ZN    ZN B 958     1555   1555  1.85  
LINK         O   THR B 336                HG    HG B 906     1555   1555  2.05  
LINK         O   VAL B 337                HG    HG B 906     1555   1555  1.99  
LINK         NE2 GLN A 279                ZN    ZN A 957     1555   1555  1.72  
LINK         SG  CYS A 222                HG    HG A 903     1555   1555  2.35  
LINK         SG  CYS B 316                HG    HG B 906     1555   1555  2.37  
LINK         OE1 GLU A 197                ZN    ZN A2011     1555   1555  2.41  
LINK         N   ASP A 330                ZN    ZN A 959     1555   1555  2.43  
LINK         ND1 HIS A 211                ZN    ZN A 962     1555   1555  2.43  
LINK         OE1 GLU B 201                ZN    ZN B 958     1555   1555  2.43  
LINK         ND1 HIS B 211                ZN    ZN B 963     1555   1555  2.44  
LINK         SG  CYS A 316                HG    HG A 905     1555   1555  2.47  
LINK         NE1 TRP B 126                ZN    ZN B 963     1555   1555  2.47  
LINK        HG    HG A 905                 O   HOH A2061     1555   1555  2.60  
LINK         OE1 GLU A 122                ZN    ZN A 962     1555   1555  2.61  
LINK         NE1 TRP A 126                ZN    ZN A 962     1555   1555  2.67  
LINK         O   MET A 163                ZN    ZN A 962     1555   1555  2.67  
LINK         SG  CYS B 264                HG    HG B 902     1555   1555  2.68  
LINK         ND1 HIS B  65                HG    HG B 906     1555   1555  2.72  
LINK         SG  CYS A 264                HG    HG A 901     1555   1555  2.82  
LINK         OG1 THR A 297                HG    HG A 901     1555   1555  3.08  
LINK         O   GLN A 312                HG    HG A 905     1555   1555  3.17  
SITE     1 AC1  2 NAG A 504  LYS B  16                                          
SITE     1 AC2  3 MAN A 503  NAG A 505  LYS B  16                               
SITE     1 AC3  7 THR A   4  ASN A  15  GLY A  18  VAL A  20                    
SITE     2 AC3  7 NAG A 504  ASN B  15  NAG B 605                               
SITE     1 AC4  3 ARG B 147  PRO B 347  BMA B 603                               
SITE     1 AC5  4 LYS A  16  ARG B 147  BMA B 602  NAG B 604                    
SITE     1 AC6  4 LYS A  16  ALA B 348  BMA B 603  NAG B 605                    
SITE     1 AC7  6 NAG A 505  THR B   4  ASN B  15  GLY B  18                    
SITE     2 AC7  6 VAL B  20  NAG B 604                                          
SITE     1 AC8  2 NAG A 705  GLU B 197                                          
SITE     1 AC9  7 ASN A   2  GLY A 280  SER A 281  ASP A 282                    
SITE     2 AC9  7 NAG A 704  GLU B 197   ZN B 956                               
SITE     1 BC1  2 GLU A 197  NAG B 805                                          
SITE     1 BC2  6  ZN A2011  ASN B   2  GLY B 280  SER B 281                    
SITE     2 BC2  6 ASP B 282  NAG B 804                                          
SITE     1 BC3  3 CYS A 264  THR A 297  TYR A 301                               
SITE     1 BC4  4 ALA B 260  CYS B 264  THR B 297  TYR B 301                    
SITE     1 BC5  2 ALA A 132  CYS A 222                                          
SITE     1 BC6  3 ALA B 132  CYS B 222  TYR B 223                               
SITE     1 BC7  5 GLN A 312  CYS A 316  THR A 336  VAL A 337                    
SITE     2 BC7  5 HOH A2061                                                     
SITE     1 BC8  5 HIS B  65  CYS B 316  THR B 336  VAL B 337                    
SITE     2 BC8  5 SER B 338                                                     
SITE     1 BC9  3 NAG A 705  HIS B 195  GLU B 197                               
SITE     1 CC1  3 GLU A 201  GLN A 279  GLU B 196                               
SITE     1 CC2  3 GLU A 196  GLU B 201  GLN B 279                               
SITE     1 CC3  4 LYS A 311  GLY A 329  ASP A 330  HIS B 100                    
SITE     1 CC4  6 GLU A 122  TRP A 126  MET A 163  ALA A 164                    
SITE     2 CC4  6 CYS A 167  HIS A 211                                          
SITE     1 CC5  6 GLU B 122  TRP B 126  MET B 163  ALA B 164                    
SITE     2 CC5  6 CYS B 167  HIS B 211                                          
SITE     1 CC6  3 HIS A 195  GLU A 197  NAG B 805                               
SITE     1 CC7 12 ALA A 117  THR A 118  CYS A 187  ILE A 189                    
SITE     2 CC7 12 TYR A 191  PHE A 212  PHE A 261  TRP A 265                    
SITE     3 CC7 12 TYR A 268  ALA A 269  ALA A 292  LYS A 296                    
SITE     1 CC8  6 PRO A  53  LEU A 321  CYS A 322  PLM A1323                    
SITE     2 CC8  6 MET B  49  PHE B  52                                          
SITE     1 CC9  5 LEU A 321  CYS A 322  CYS A 323  PLM A1322                    
SITE     2 CC9  5 PHE B  88                                                     
SITE     1 DC1 12 ALA B 117  THR B 118  CYS B 187  ILE B 189                    
SITE     2 DC1 12 TYR B 191  MET B 207  PHE B 212  TRP B 265                    
SITE     3 DC1 12 TYR B 268  ALA B 269  ALA B 292  LYS B 296                    
SITE     1 DC2  5 ILE A  48  MET A  49  LEU B 321  CYS B 322                    
SITE     2 DC2  5 PLM B1323                                                     
SITE     1 DC3  6 PHE A  85  PHE A  88  LEU B 321  CYS B 322                    
SITE     2 DC3  6 CYS B 323  PLM B1322                                          
SITE     1 DC4  5 ALA A  41  LEU A  99  MET B 308  ARG B 314                    
SITE     2 DC4  5 HTG B1509                                                     
SITE     1 DC5  3 MET B  39  LEU B  46  TYR B 301                               
SITE     1 DC6  3 VAL A 300  ILE A 305  LEU B  46                               
SITE     1 DC7  3 TYR B 274  ASP B 282  PHE B 283                               
SITE     1 DC8  7 LEU A 266  PRO A 267  GLY A 270  VAL A 271                    
SITE     2 DC8  7 TYR A 274  PHE A 283  PHE A 287                               
SITE     1 DC9  8 ARG A 252  ILE A 256  VAL A 304  ILE A 305                    
SITE     2 DC9  8 MET A 309  TRP B  35  SER B  38  ALA B  42                    
SITE     1 EC1  8 LEU A  99  HIS A 100  GLN A 344  LYS B 311                    
SITE     2 EC1  8 ARG B 314  ASN B 315  ASP B 330  HTO B1401                    
CRYST1   96.680   96.680  150.200  90.00  90.00  90.00 P 41          8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010343  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010343  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006658        0.00000                         
HETATM    1  C   ACE A   0      53.553  -7.050  35.606  1.00 47.40           C  
HETATM    2  O   ACE A   0      52.916  -7.860  34.934  1.00 46.96           O  
HETATM    3  CH3 ACE A   0      54.727  -7.523  36.434  1.00 47.42           C  
ATOM      4  N   MET A   1      53.284  -5.731  35.670  1.00 47.11           N  
ATOM      5  CA  MET A   1      52.214  -5.077  34.913  1.00 46.26           C  
ATOM      6  C   MET A   1      52.674  -4.891  33.485  1.00 46.68           C  
ATOM      7  O   MET A   1      53.849  -4.563  33.283  1.00 46.86           O  
ATOM      8  CB  MET A   1      51.887  -3.719  35.536  1.00 45.60           C  
ATOM      9  CG  MET A   1      51.426  -3.792  36.982  1.00 44.48           C  
ATOM     10  SD  MET A   1      49.945  -4.797  37.183  1.00 46.06           S  
ATOM     11  CE  MET A   1      48.647  -3.745  36.534  1.00 43.77           C  
ATOM     12  N   ASN A   2      51.781  -5.083  32.508  1.00 46.50           N  
ATOM     13  CA  ASN A   2      52.150  -4.950  31.087  1.00 46.16           C  
ATOM     14  C   ASN A   2      52.395  -3.519  30.683  1.00 45.83           C  
ATOM     15  O   ASN A   2      53.065  -3.284  29.678  1.00 46.50           O  
ATOM     16  CB  ASN A   2      51.073  -5.523  30.174  1.00 46.63           C  
ATOM     17  CG  ASN A   2      50.985  -7.005  30.265  1.00 47.63           C  
ATOM     18  OD1 ASN A   2      51.963  -7.709  30.034  1.00 46.09           O  
ATOM     19  ND2 ASN A   2      49.803  -7.490  30.614  1.00 51.03           N  
ATOM     20  N   GLY A   3      51.852  -2.565  31.430  1.00 45.38           N  
ATOM     21  CA  GLY A   3      52.066  -1.173  31.079  1.00 44.72           C  
ATOM     22  C   GLY A   3      52.411  -0.330  32.284  1.00 44.42           C  
ATOM     23  O   GLY A   3      52.493  -0.830  33.401  1.00 45.22           O  
ATOM     24  N   THR A   4      52.612   0.959  32.058  1.00 43.92           N  
ATOM     25  CA  THR A   4      52.934   1.847  33.150  1.00 43.35           C  
ATOM     26  C   THR A   4      51.822   2.840  33.331  1.00 43.48           C  
ATOM     27  O   THR A   4      51.792   3.855  32.649  1.00 43.41           O  
ATOM     28  CB  THR A   4      54.234   2.605  32.893  1.00 43.38           C  
ATOM     29  OG1 THR A   4      55.307   1.673  32.708  1.00 45.14           O  
ATOM     30  CG2 THR A   4      54.550   3.501  34.066  1.00 42.82           C  
ATOM     31  N   GLU A   5      50.892   2.538  34.230  1.00 43.15           N  
ATOM     32  CA  GLU A   5      49.806   3.456  34.501  1.00 43.52           C  
ATOM     33  C   GLU A   5      50.366   4.630  35.284  1.00 43.43           C  
ATOM     34  O   GLU A   5      51.260   4.459  36.117  1.00 43.98           O  
ATOM     35  CB  GLU A   5      48.692   2.777  35.311  1.00 44.23           C  
ATOM     36  CG  GLU A   5      47.593   3.735  35.718  1.00 46.14           C  
ATOM     37  CD  GLU A   5      46.549   3.105  36.608  1.00 48.65           C  
ATOM     38  OE1 GLU A   5      46.928   2.306  37.491  1.00 50.79           O  
ATOM     39  OE2 GLU A   5      45.349   3.422  36.446  1.00 49.99           O  
ATOM     40  N   GLY A   6      49.862   5.825  34.990  1.00 43.73           N  
ATOM     41  CA  GLY A   6      50.272   7.030  35.685  1.00 42.34           C  
ATOM     42  C   GLY A   6      48.999   7.650  36.225  1.00 41.75           C  
ATOM     43  O   GLY A   6      47.890   7.161  35.969  1.00 41.59           O  
ATOM     44  N   PRO A   7      49.108   8.730  36.986  1.00 41.19           N  
ATOM     45  CA  PRO A   7      47.863   9.320  37.505  1.00 41.84           C  
ATOM     46  C   PRO A   7      47.119  10.088  36.431  1.00 42.55           C  
ATOM     47  O   PRO A   7      45.931  10.411  36.548  1.00 42.48           O  
ATOM     48  CB  PRO A   7      48.370  10.237  38.618  1.00 42.06           C  
ATOM     49  CG  PRO A   7      49.761  10.634  38.120  1.00 40.91           C  
ATOM     50  CD  PRO A   7      50.312   9.369  37.548  1.00 40.31           C  
ATOM     51  N   ASN A   8      47.841  10.286  35.344  1.00 43.66           N  
ATOM     52  CA  ASN A   8      47.426  11.107  34.234  1.00 43.35           C  
ATOM     53  C   ASN A   8      47.567  10.424  32.892  1.00 44.10           C  
ATOM     54  O   ASN A   8      47.100  10.977  31.880  1.00 43.87           O  
ATOM     55  CB  ASN A   8      48.379  12.268  34.238  1.00 43.81           C  
ATOM     56  CG  ASN A   8      47.731  13.509  33.908  1.00 45.93           C  
ATOM     57  OD1 ASN A   8      48.398  14.520  33.753  1.00 48.91           O  
ATOM     58  ND2 ASN A   8      46.399  13.482  33.800  1.00 47.02           N  
ATOM     59  N   PHE A   9      48.231   9.266  32.874  1.00 44.48           N  
ATOM     60  CA  PHE A   9      48.540   8.536  31.639  1.00 43.95           C  
ATOM     61  C   PHE A   9      48.580   7.025  31.835  1.00 44.36           C  
ATOM     62  O   PHE A   9      48.221   6.505  32.882  1.00 45.02           O  
ATOM     63  CB  PHE A   9      49.918   8.966  31.158  1.00 43.71           C  
ATOM     64  CG  PHE A   9      51.008   8.757  32.190  1.00 42.51           C  
ATOM     65  CD1 PHE A   9      51.316   9.755  33.112  1.00 42.13           C  
ATOM     66  CD2 PHE A   9      51.703   7.551  32.256  1.00 41.42           C  
ATOM     67  CE1 PHE A   9      52.306   9.555  34.090  1.00 42.10           C  
ATOM     68  CE2 PHE A   9      52.692   7.343  33.228  1.00 41.99           C  
ATOM     69  CZ  PHE A   9      52.993   8.348  34.146  1.00 41.06           C  
ATOM     70  N   TYR A  10      49.050   6.338  30.797  1.00 43.82           N  
ATOM     71  CA  TYR A  10      49.199   4.888  30.789  1.00 42.40           C  
ATOM     72  C   TYR A  10      50.099   4.537  29.625  1.00 41.15           C  
ATOM     73  O   TYR A  10      49.626   4.418  28.500  1.00 40.15           O  
ATOM     74  CB  TYR A  10      47.841   4.184  30.619  1.00 42.71           C  
ATOM     75  CG  TYR A  10      47.953   2.680  30.679  1.00 43.13           C  
ATOM     76  CD1 TYR A  10      48.026   2.018  31.909  1.00 43.63           C  
ATOM     77  CD2 TYR A  10      48.070   1.917  29.510  1.00 42.54           C  
ATOM     78  CE1 TYR A  10      48.216   0.634  31.976  1.00 42.90           C  
ATOM     79  CE2 TYR A  10      48.259   0.537  29.568  1.00 43.02           C  
ATOM     80  CZ  TYR A  10      48.330  -0.093  30.806  1.00 43.04           C  
ATOM     81  OH  TYR A  10      48.496  -1.451  30.889  1.00 44.88           O  
ATOM     82  N   VAL A  11      51.395   4.393  29.871  1.00 40.44           N  
ATOM     83  CA  VAL A  11      52.287   4.053  28.779  1.00 40.03           C  
ATOM     84  C   VAL A  11      52.197   2.565  28.521  1.00 40.67           C  
ATOM     85  O   VAL A  11      52.307   1.777  29.448  1.00 40.33           O  
ATOM     86  CB  VAL A  11      53.758   4.442  29.079  1.00 39.50           C  
ATOM     87  CG1 VAL A  11      54.618   4.187  27.848  1.00 39.72           C  
ATOM     88  CG2 VAL A  11      53.847   5.904  29.466  1.00 38.50           C  
ATOM     89  N   PRO A  12      51.963   2.171  27.257  1.00 41.71           N  
ATOM     90  CA  PRO A  12      51.848   0.771  26.838  1.00 42.42           C  
ATOM     91  C   PRO A  12      53.239   0.155  26.770  1.00 43.52           C  
ATOM     92  O   PRO A  12      53.647  -0.401  25.736  1.00 43.60           O  
ATOM     93  CB  PRO A  12      51.162   0.889  25.474  1.00 42.31           C  
ATOM     94  CG  PRO A  12      51.713   2.158  24.938  1.00 41.48           C  
ATOM     95  CD  PRO A  12      51.725   3.083  26.118  1.00 41.73           C  
ATOM     96  N   PHE A  13      53.950   0.261  27.891  1.00 44.30           N  
ATOM     97  CA  PHE A  13      55.333  -0.212  28.016  1.00 45.02           C  
ATOM     98  C   PHE A  13      55.626  -0.516  29.474  1.00 45.44           C  
ATOM     99  O   PHE A  13      55.219   0.232  30.362  1.00 45.49           O  
ATOM    100  CB  PHE A  13      56.288   0.887  27.537  1.00 45.01           C  
ATOM    101  CG  PHE A  13      57.681   0.418  27.230  1.00 44.78           C  
ATOM    102  CD1 PHE A  13      57.982  -0.149  25.984  1.00 44.85           C  
ATOM    103  CD2 PHE A  13      58.708   0.603  28.151  1.00 44.32           C  
ATOM    104  CE1 PHE A  13      59.290  -0.516  25.652  1.00 44.22           C  
ATOM    105  CE2 PHE A  13      60.016   0.241  27.835  1.00 44.63           C  
ATOM    106  CZ  PHE A  13      60.311  -0.319  26.581  1.00 44.72           C  
ATOM    107  N   SER A  14      56.354  -1.599  29.707  1.00 46.54           N  
ATOM    108  CA  SER A  14      56.692  -2.019  31.054  1.00 48.31           C  
ATOM    109  C   SER A  14      57.785  -1.128  31.617  1.00 49.77           C  
ATOM    110  O   SER A  14      58.592  -0.602  30.850  1.00 50.78           O  
ATOM    111  CB  SER A  14      57.167  -3.471  31.024  1.00 48.20           C  
ATOM    112  OG  SER A  14      57.246  -4.016  32.331  1.00 49.87           O  
ATOM    113  N   ASN A  15      57.810  -0.956  32.939  1.00 50.94           N  
ATOM    114  CA  ASN A  15      58.832  -0.135  33.587  1.00 51.08           C  
ATOM    115  C   ASN A  15      59.731  -1.029  34.442  1.00 52.19           C  
ATOM    116  O   ASN A  15      60.247  -0.577  35.471  1.00 51.78           O  
ATOM    117  CB  ASN A  15      58.179   0.945  34.454  1.00 49.76           C  
ATOM    118  CG  ASN A  15      59.129   2.060  34.782  1.00 48.97           C  
ATOM    119  OD1 ASN A  15      59.832   2.525  33.907  1.00 48.34           O  
ATOM    120  ND2 ASN A  15      59.162   2.507  36.028  1.00 49.20           N  
ATOM    121  N   LYS A  16      59.905  -2.287  34.011  1.00 54.04           N  
ATOM    122  CA  LYS A  16      60.736  -3.271  34.718  1.00 54.63           C  
ATOM    123  C   LYS A  16      62.155  -2.805  34.704  1.00 53.69           C  
ATOM    124  O   LYS A  16      62.926  -3.142  35.605  1.00 54.46           O  
ATOM    125  CB  LYS A  16      60.673  -4.654  34.057  1.00 56.68           C  
ATOM    126  CG  LYS A  16      61.525  -5.686  34.800  1.00 59.57           C  
ATOM    127  CD  LYS A  16      61.731  -7.015  34.055  1.00 62.10           C  
ATOM    128  CE  LYS A  16      62.625  -7.964  34.882  1.00 63.44           C  
ATOM    129  NZ  LYS A  16      62.719  -9.361  34.344  1.00 65.65           N  
ATOM    130  N   THR A  17      62.505  -2.039  33.681  1.00 53.00           N  
ATOM    131  CA  THR A  17      63.848  -1.499  33.561  1.00 52.95           C  
ATOM    132  C   THR A  17      63.832  -0.043  33.975  1.00 53.31           C  
ATOM    133  O   THR A  17      64.803   0.688  33.740  1.00 53.66           O  
ATOM    134  CB  THR A  17      64.328  -1.586  32.141  1.00 52.62           C  
ATOM    135  OG1 THR A  17      63.554  -0.691  31.322  1.00 52.87           O  
ATOM    136  CG2 THR A  17      64.176  -3.017  31.650  1.00 51.94           C  
ATOM    137  N   GLY A  18      62.723   0.374  34.580  1.00 53.38           N  
ATOM    138  CA  GLY A  18      62.572   1.744  35.044  1.00 52.55           C  
ATOM    139  C   GLY A  18      62.947   2.804  34.031  1.00 51.61           C  
ATOM    140  O   GLY A  18      63.367   3.885  34.408  1.00 52.42           O  
ATOM    141  N   VAL A  19      62.776   2.495  32.750  1.00 49.71           N  
ATOM    142  CA  VAL A  19      63.112   3.416  31.681  1.00 48.40           C  
ATOM    143  C   VAL A  19      61.884   4.252  31.278  1.00 47.06           C  
ATOM    144  O   VAL A  19      62.037   5.215  30.556  1.00 47.82           O  
ATOM    145  CB  VAL A  19      63.685   2.624  30.456  1.00 48.02           C  
ATOM    146  CG1 VAL A  19      62.599   1.837  29.786  1.00 48.55           C  
ATOM    147  CG2 VAL A  19      64.329   3.553  29.470  1.00 49.03           C  
ATOM    148  N   VAL A  20      60.694   3.915  31.768  1.00 45.15           N  
ATOM    149  CA  VAL A  20      59.478   4.646  31.398  1.00 43.79           C  
ATOM    150  C   VAL A  20      59.423   6.007  32.066  1.00 44.16           C  
ATOM    151  O   VAL A  20      59.819   6.127  33.209  1.00 44.75           O  
ATOM    152  CB  VAL A  20      58.205   3.833  31.756  1.00 43.31           C  
ATOM    153  CG1 VAL A  20      56.961   4.658  31.467  1.00 42.50           C  
ATOM    154  CG2 VAL A  20      58.164   2.530  30.955  1.00 42.41           C  
ATOM    155  N   ARG A  21      58.911   7.015  31.352  1.00 44.75           N  
ATOM    156  CA  ARG A  21      58.828   8.402  31.848  1.00 44.75           C  
ATOM    157  C   ARG A  21      57.547   9.106  31.407  1.00 42.99           C  
ATOM    158  O   ARG A  21      57.187   8.988  30.241  1.00 42.68           O  
ATOM    159  CB  ARG A  21      60.010   9.191  31.307  1.00 46.93           C  
ATOM    160  CG  ARG A  21      61.353   8.607  31.683  1.00 51.12           C  
ATOM    161  CD  ARG A  21      62.197   9.698  32.291  1.00 54.40           C  
ATOM    162  NE  ARG A  21      61.432  10.420  33.309  1.00 57.11           N  
ATOM    163  CZ  ARG A  21      61.717  11.653  33.734  1.00 58.83           C  
ATOM    164  NH1 ARG A  21      62.763  12.312  33.223  1.00 59.50           N  
ATOM    165  NH2 ARG A  21      60.949  12.233  34.666  1.00 59.07           N  
ATOM    166  N   SER A  22      56.903   9.862  32.305  1.00 41.77           N  
ATOM    167  CA  SER A  22      55.651  10.597  32.008  1.00 41.01           C  
ATOM    168  C   SER A  22      55.704  11.282  30.658  1.00 40.64           C  
ATOM    169  O   SER A  22      56.594  12.087  30.430  1.00 41.06           O  
ATOM    170  CB  SER A  22      55.389  11.662  33.072  1.00 41.13           C  
ATOM    171  OG  SER A  22      54.229  12.418  32.757  1.00 42.28           O  
ATOM    172  N   PRO A  23      54.732  11.009  29.760  1.00 40.80           N  
ATOM    173  CA  PRO A  23      54.726  11.630  28.430  1.00 40.56           C  
ATOM    174  C   PRO A  23      54.341  13.082  28.483  1.00 41.56           C  
ATOM    175  O   PRO A  23      54.016  13.667  27.469  1.00 43.00           O  
ATOM    176  CB  PRO A  23      53.735  10.777  27.663  1.00 39.64           C  
ATOM    177  CG  PRO A  23      52.723  10.464  28.702  1.00 38.93           C  
ATOM    178  CD  PRO A  23      53.532  10.174  29.948  1.00 39.84           C  
ATOM    179  N   PHE A  24      54.360  13.647  29.686  1.00 42.39           N  
ATOM    180  CA  PHE A  24      54.078  15.063  29.913  1.00 42.72           C  
ATOM    181  C   PHE A  24      55.315  15.645  30.541  1.00 44.07           C  
ATOM    182  O   PHE A  24      55.250  16.738  31.071  1.00 45.15           O  
ATOM    183  CB  PHE A  24      52.938  15.260  30.909  1.00 41.45           C  
ATOM    184  CG  PHE A  24      51.590  14.858  30.397  1.00 40.52           C  
ATOM    185  CD1 PHE A  24      51.072  15.428  29.239  1.00 39.67           C  
ATOM    186  CD2 PHE A  24      50.818  13.943  31.102  1.00 39.26           C  
ATOM    187  CE1 PHE A  24      49.808  15.099  28.794  1.00 39.12           C  
ATOM    188  CE2 PHE A  24      49.552  13.605  30.665  1.00 38.85           C  
ATOM    189  CZ  PHE A  24      49.046  14.186  29.508  1.00 39.03           C  
ATOM    190  N   GLU A  25      56.429  14.918  30.486  1.00 44.94           N  
ATOM    191  CA  GLU A  25      57.647  15.378  31.113  1.00 45.77           C  
ATOM    192  C   GLU A  25      58.918  14.995  30.361  1.00 45.53           C  
ATOM    193  O   GLU A  25      59.924  15.683  30.529  1.00 46.05           O  
ATOM    194  CB  GLU A  25      57.708  14.825  32.526  1.00 48.16           C  
ATOM    195  CG  GLU A  25      56.917  15.584  33.548  1.00 52.84           C  
ATOM    196  CD  GLU A  25      56.531  14.693  34.719  1.00 57.72           C  
ATOM    197  OE1 GLU A  25      57.301  13.750  35.062  1.00 59.35           O  
ATOM    198  OE2 GLU A  25      55.446  14.935  35.303  1.00 60.82           O  
ATOM    199  N   ALA A  26      58.924  13.930  29.564  1.00 44.99           N  
ATOM    200  CA  ALA A  26      60.165  13.571  28.858  1.00 44.91           C  
ATOM    201  C   ALA A  26      59.896  12.837  27.550  1.00 44.95           C  
ATOM    202  O   ALA A  26      58.817  12.291  27.380  1.00 45.80           O  
ATOM    203  CB  ALA A  26      61.046  12.712  29.765  1.00 44.63           C  
ATOM    204  N   PRO A  27      60.866  12.836  26.606  1.00 44.41           N  
ATOM    205  CA  PRO A  27      60.715  12.152  25.320  1.00 44.33           C  
ATOM    206  C   PRO A  27      60.406  10.708  25.576  1.00 44.85           C  
ATOM    207  O   PRO A  27      60.808  10.194  26.609  1.00 45.98           O  
ATOM    208  CB  PRO A  27      62.080  12.331  24.674  1.00 43.15           C  
ATOM    209  CG  PRO A  27      62.468  13.651  25.137  1.00 42.69           C  
ATOM    210  CD  PRO A  27      62.109  13.619  26.604  1.00 43.52           C  
ATOM    211  N   GLN A  28      59.715  10.059  24.641  1.00 45.43           N  
ATOM    212  CA  GLN A  28      59.331   8.658  24.776  1.00 45.56           C  
ATOM    213  C   GLN A  28      60.120   7.781  23.799  1.00 46.39           C  
ATOM    214  O   GLN A  28      59.625   6.738  23.392  1.00 46.18           O  
ATOM    215  CB  GLN A  28      57.828   8.535  24.505  1.00 44.55           C  
ATOM    216  CG  GLN A  28      56.966   9.492  25.319  1.00 43.69           C  
ATOM    217  CD  GLN A  28      56.926   9.146  26.804  1.00 44.58           C  
ATOM    218  OE1 GLN A  28      56.602   8.027  27.172  1.00 46.04           O  
ATOM    219  NE2 GLN A  28      57.247  10.108  27.660  1.00 44.47           N  
ATOM    220  N   TYR A  29      61.344   8.173  23.459  1.00 47.80           N  
ATOM    221  CA  TYR A  29      62.138   7.425  22.485  1.00 49.27           C  
ATOM    222  C   TYR A  29      62.484   6.064  22.939  1.00 49.23           C  
ATOM    223  O   TYR A  29      63.082   5.310  22.189  1.00 50.24           O  
ATOM    224  CB  TYR A  29      63.405   8.189  22.124  1.00 50.88           C  
ATOM    225  CG  TYR A  29      63.067   9.537  21.556  1.00 52.45           C  
ATOM    226  CD1 TYR A  29      61.981   9.687  20.703  1.00 53.03           C  
ATOM    227  CD2 TYR A  29      63.785  10.669  21.913  1.00 53.07           C  
ATOM    228  CE1 TYR A  29      61.609  10.919  20.227  1.00 53.77           C  
ATOM    229  CE2 TYR A  29      63.422  11.917  21.435  1.00 54.32           C  
ATOM    230  CZ  TYR A  29      62.330  12.036  20.592  1.00 54.49           C  
ATOM    231  OH  TYR A  29      61.960  13.271  20.101  1.00 55.76           O  
ATOM    232  N   TYR A  30      62.125   5.725  24.159  1.00 48.54           N  
ATOM    233  CA  TYR A  30      62.433   4.402  24.617  1.00 48.23           C  
ATOM    234  C   TYR A  30      61.305   3.496  24.187  1.00 48.90           C  
ATOM    235  O   TYR A  30      61.389   2.304  24.393  1.00 50.63           O  
ATOM    236  CB  TYR A  30      62.600   4.419  26.136  1.00 47.12           C  
ATOM    237  CG  TYR A  30      61.363   4.854  26.851  1.00 45.37           C  
ATOM    238  CD1 TYR A  30      60.302   3.979  27.005  1.00 45.53           C  
ATOM    239  CD2 TYR A  30      61.223   6.153  27.324  1.00 45.07           C  
ATOM    240  CE1 TYR A  30      59.129   4.378  27.603  1.00 45.82           C  
ATOM    241  CE2 TYR A  30      60.041   6.569  27.936  1.00 44.88           C  
ATOM    242  CZ  TYR A  30      58.999   5.666  28.066  1.00 45.10           C  
ATOM    243  OH  TYR A  30      57.805   6.014  28.647  1.00 45.98           O  
ATOM    244  N   LEU A  31      60.262   4.072  23.589  1.00 49.37           N  
ATOM    245  CA  LEU A  31      59.087   3.329  23.116  1.00 49.46           C  
ATOM    246  C   LEU A  31      59.256   2.971  21.676  1.00 50.18           C  
ATOM    247  O   LEU A  31      58.658   2.005  21.199  1.00 50.31           O  
ATOM    248  CB  LEU A  31      57.832   4.188  23.165  1.00 48.71           C  
ATOM    249  CG  LEU A  31      57.191   4.654  24.449  1.00 47.86           C  
ATOM    250  CD1 LEU A  31      55.960   5.418  24.083  1.00 48.50           C  
ATOM    251  CD2 LEU A  31      56.826   3.480  25.315  1.00 49.10           C  
ATOM    252  N   ALA A  32      60.037   3.786  20.978  1.00 51.31           N  
ATOM    253  CA  ALA A  32      60.261   3.617  19.558  1.00 52.13           C  
ATOM    254  C   ALA A  32      61.471   4.419  19.137  1.00 52.81           C  
ATOM    255  O   ALA A  32      61.936   5.278  19.885  1.00 53.90           O  
ATOM    256  CB  ALA A  32      59.030   4.098  18.803  1.00 52.26           C  
ATOM    257  N   GLU A  33      61.964   4.152  17.932  1.00 53.21           N  
ATOM    258  CA  GLU A  33      63.119   4.851  17.385  1.00 53.37           C  
ATOM    259  C   GLU A  33      62.800   6.314  17.187  1.00 53.01           C  
ATOM    260  O   GLU A  33      61.661   6.665  16.872  1.00 53.66           O  
ATOM    261  CB  GLU A  33      63.494   4.241  16.045  1.00 55.32           C  
ATOM    262  CG  GLU A  33      63.499   2.755  16.104  1.00 60.15           C  
ATOM    263  CD  GLU A  33      64.373   2.274  17.232  1.00 63.21           C  
ATOM    264  OE1 GLU A  33      65.610   2.358  17.067  1.00 65.05           O  
ATOM    265  OE2 GLU A  33      63.833   1.838  18.285  1.00 65.24           O  
ATOM    266  N   PRO A  34      63.793   7.197  17.374  1.00 52.11           N  
ATOM    267  CA  PRO A  34      63.543   8.626  17.189  1.00 51.15           C  
ATOM    268  C   PRO A  34      63.112   9.007  15.777  1.00 51.04           C  
ATOM    269  O   PRO A  34      62.327   9.949  15.614  1.00 52.47           O  
ATOM    270  CB  PRO A  34      64.869   9.251  17.599  1.00 50.49           C  
ATOM    271  CG  PRO A  34      65.290   8.358  18.716  1.00 50.93           C  
ATOM    272  CD  PRO A  34      65.045   6.987  18.127  1.00 51.49           C  
ATOM    273  N   TRP A  35      63.589   8.287  14.765  1.00 50.33           N  
ATOM    274  CA  TRP A  35      63.213   8.603  13.389  1.00 49.69           C  
ATOM    275  C   TRP A  35      61.724   8.407  13.166  1.00 49.03           C  
ATOM    276  O   TRP A  35      61.135   9.090  12.330  1.00 49.88           O  
ATOM    277  CB  TRP A  35      63.991   7.742  12.390  1.00 50.26           C  
ATOM    278  CG  TRP A  35      63.684   6.279  12.420  1.00 49.95           C  
ATOM    279  CD1 TRP A  35      64.343   5.317  13.124  1.00 50.75           C  
ATOM    280  CD2 TRP A  35      62.660   5.605  11.681  1.00 50.07           C  
ATOM    281  NE1 TRP A  35      63.798   4.078  12.866  1.00 50.41           N  
ATOM    282  CE2 TRP A  35      62.763   4.229  11.983  1.00 49.98           C  
ATOM    283  CE3 TRP A  35      61.668   6.030  10.792  1.00 50.78           C  
ATOM    284  CZ2 TRP A  35      61.914   3.277  11.428  1.00 50.01           C  
ATOM    285  CZ3 TRP A  35      60.822   5.082  10.240  1.00 50.53           C  
ATOM    286  CH2 TRP A  35      60.951   3.721  10.560  1.00 50.23           C  
ATOM    287  N   GLN A  36      61.123   7.482  13.904  1.00 47.39           N  
ATOM    288  CA  GLN A  36      59.707   7.207  13.778  1.00 45.84           C  
ATOM    289  C   GLN A  36      58.915   8.385  14.301  1.00 44.09           C  
ATOM    290  O   GLN A  36      57.848   8.663  13.803  1.00 43.39           O  
ATOM    291  CB  GLN A  36      59.390   5.919  14.526  1.00 47.26           C  
ATOM    292  CG  GLN A  36      60.213   4.738  13.997  1.00 49.06           C  
ATOM    293  CD  GLN A  36      59.927   3.422  14.708  1.00 50.37           C  
ATOM    294  OE1 GLN A  36      60.240   3.254  15.883  1.00 51.24           O  
ATOM    295  NE2 GLN A  36      59.327   2.480  13.985  1.00 51.74           N  
ATOM    296  N   PHE A  37      59.426   9.088  15.296  1.00 42.51           N  
ATOM    297  CA  PHE A  37      58.703  10.249  15.755  1.00 41.69           C  
ATOM    298  C   PHE A  37      58.813  11.294  14.690  1.00 42.67           C  
ATOM    299  O   PHE A  37      57.878  12.051  14.491  1.00 43.09           O  
ATOM    300  CB  PHE A  37      59.285  10.795  17.038  1.00 41.03           C  
ATOM    301  CG  PHE A  37      58.918  10.006  18.239  1.00 40.89           C  
ATOM    302  CD1 PHE A  37      59.589   8.841  18.553  1.00 42.12           C  
ATOM    303  CD2 PHE A  37      57.881  10.413  19.053  1.00 40.26           C  
ATOM    304  CE1 PHE A  37      59.228   8.093  19.664  1.00 41.77           C  
ATOM    305  CE2 PHE A  37      57.515   9.676  20.159  1.00 40.28           C  
ATOM    306  CZ  PHE A  37      58.186   8.519  20.466  1.00 41.93           C  
ATOM    307  N   SER A  38      59.958  11.336  14.007  1.00 43.24           N  
ATOM    308  CA  SER A  38      60.202  12.297  12.924  1.00 43.83           C  
ATOM    309  C   SER A  38      59.207  12.064  11.819  1.00 44.03           C  
ATOM    310  O   SER A  38      58.798  12.997  11.127  1.00 43.65           O  
ATOM    311  CB  SER A  38      61.613  12.116  12.372  1.00 44.42           C  
ATOM    312  OG  SER A  38      62.578  12.342  13.381  1.00 45.67           O  
ATOM    313  N   MET A  39      58.852  10.797  11.652  1.00 44.42           N  
ATOM    314  CA  MET A  39      57.880  10.365  10.672  1.00 45.11           C  
ATOM    315  C   MET A  39      56.569  11.008  11.016  1.00 43.72           C  
ATOM    316  O   MET A  39      55.965  11.657  10.169  1.00 43.83           O  
ATOM    317  CB  MET A  39      57.726   8.857  10.749  1.00 49.83           C  
ATOM    318  CG  MET A  39      58.821   8.082  10.078  1.00 55.09           C  
ATOM    319  SD  MET A  39      58.428   7.998   8.334  1.00 64.91           S  
ATOM    320  CE  MET A  39      59.203   9.645   7.679  1.00 61.65           C  
ATOM    321  N   LEU A  40      56.126  10.812  12.256  1.00 41.69           N  
ATOM    322  CA  LEU A  40      54.883  11.397  12.726  1.00 39.43           C  
ATOM    323  C   LEU A  40      54.941  12.869  12.486  1.00 39.28           C  
ATOM    324  O   LEU A  40      53.994  13.427  11.947  1.00 39.74           O  
ATOM    325  CB  LEU A  40      54.710  11.156  14.218  1.00 38.47           C  
ATOM    326  CG  LEU A  40      54.629   9.703  14.663  1.00 37.65           C  
ATOM    327  CD1 LEU A  40      54.509   9.621  16.174  1.00 36.12           C  
ATOM    328  CD2 LEU A  40      53.443   9.071  13.996  1.00 36.72           C  
ATOM    329  N   ALA A  41      56.058  13.490  12.869  1.00 38.51           N  
ATOM    330  CA  ALA A  41      56.248  14.930  12.709  1.00 38.38           C  
ATOM    331  C   ALA A  41      56.185  15.316  11.245  1.00 38.70           C  
ATOM    332  O   ALA A  41      55.431  16.217  10.886  1.00 39.91           O  
ATOM    333  CB  ALA A  41      57.568  15.358  13.316  1.00 37.42           C  
ATOM    334  N   ALA A  42      56.970  14.655  10.401  1.00 38.10           N  
ATOM    335  CA  ALA A  42      56.963  14.953   8.971  1.00 37.99           C  
ATOM    336  C   ALA A  42      55.532  14.826   8.451  1.00 38.10           C  
ATOM    337  O   ALA A  42      55.035  15.692   7.747  1.00 38.96           O  
ATOM    338  CB  ALA A  42      57.867  13.978   8.243  1.00 37.25           C  
ATOM    339  N   TYR A  43      54.882  13.732   8.821  1.00 38.21           N  
ATOM    340  CA  TYR A  43      53.511  13.441   8.435  1.00 38.19           C  
ATOM    341  C   TYR A  43      52.536  14.547   8.875  1.00 39.26           C  
ATOM    342  O   TYR A  43      51.799  15.103   8.040  1.00 39.81           O  
ATOM    343  CB  TYR A  43      53.117  12.121   9.067  1.00 36.82           C  
ATOM    344  CG  TYR A  43      51.668  11.756   8.935  1.00 35.03           C  
ATOM    345  CD1 TYR A  43      51.130  11.391   7.712  1.00 35.25           C  
ATOM    346  CD2 TYR A  43      50.857  11.683  10.058  1.00 35.02           C  
ATOM    347  CE1 TYR A  43      49.820  10.941   7.616  1.00 35.63           C  
ATOM    348  CE2 TYR A  43      49.551  11.243   9.982  1.00 35.31           C  
ATOM    349  CZ  TYR A  43      49.039  10.862   8.762  1.00 36.38           C  
ATOM    350  OH  TYR A  43      47.766  10.328   8.707  1.00 38.88           O  
ATOM    351  N   MET A  44      52.507  14.863  10.169  1.00 39.54           N  
ATOM    352  CA  MET A  44      51.590  15.896  10.653  1.00 39.27           C  
ATOM    353  C   MET A  44      51.838  17.168   9.921  1.00 40.04           C  
ATOM    354  O   MET A  44      50.926  17.948   9.709  1.00 39.78           O  
ATOM    355  CB  MET A  44      51.761  16.131  12.150  1.00 38.24           C  
ATOM    356  CG  MET A  44      51.219  15.010  13.012  1.00 39.39           C  
ATOM    357  SD  MET A  44      49.615  14.319  12.414  1.00 42.50           S  
ATOM    358  CE  MET A  44      48.565  15.793  12.245  1.00 40.90           C  
ATOM    359  N   PHE A  45      53.083  17.379   9.532  1.00 40.44           N  
ATOM    360  CA  PHE A  45      53.430  18.575   8.820  1.00 41.68           C  
ATOM    361  C   PHE A  45      52.747  18.605   7.457  1.00 42.48           C  
ATOM    362  O   PHE A  45      52.119  19.616   7.119  1.00 42.51           O  
ATOM    363  CB  PHE A  45      54.938  18.646   8.638  1.00 43.09           C  
ATOM    364  CG  PHE A  45      55.374  19.750   7.720  1.00 44.36           C  
ATOM    365  CD1 PHE A  45      55.552  21.035   8.197  1.00 45.21           C  
ATOM    366  CD2 PHE A  45      55.553  19.511   6.357  1.00 45.08           C  
ATOM    367  CE1 PHE A  45      55.899  22.066   7.334  1.00 46.18           C  
ATOM    368  CE2 PHE A  45      55.900  20.538   5.485  1.00 45.37           C  
ATOM    369  CZ  PHE A  45      56.073  21.815   5.970  1.00 45.74           C  
ATOM    370  N   LEU A  46      52.872  17.524   6.679  1.00 42.88           N  
ATOM    371  CA  LEU A  46      52.277  17.452   5.333  1.00 43.04           C  
ATOM    372  C   LEU A  46      50.786  17.547   5.395  1.00 43.92           C  
ATOM    373  O   LEU A  46      50.198  18.142   4.495  1.00 45.21           O  
ATOM    374  CB  LEU A  46      52.652  16.157   4.628  1.00 42.25           C  
ATOM    375  CG  LEU A  46      54.142  15.948   4.372  1.00 41.88           C  
ATOM    376  CD1 LEU A  46      54.372  14.584   3.706  1.00 40.66           C  
ATOM    377  CD2 LEU A  46      54.659  17.091   3.513  1.00 41.13           C  
ATOM    378  N   LEU A  47      50.172  16.953   6.425  1.00 44.06           N  
ATOM    379  CA  LEU A  47      48.713  17.013   6.612  1.00 43.95           C  
ATOM    380  C   LEU A  47      48.253  18.466   6.861  1.00 44.22           C  
ATOM    381  O   LEU A  47      47.184  18.866   6.406  1.00 44.58           O  
ATOM    382  CB  LEU A  47      48.273  16.162   7.815  1.00 43.00           C  
ATOM    383  CG  LEU A  47      47.751  14.736   7.677  1.00 41.74           C  
ATOM    384  CD1 LEU A  47      47.138  14.306   9.018  1.00 41.03           C  
ATOM    385  CD2 LEU A  47      46.702  14.664   6.591  1.00 41.45           C  
ATOM    386  N   ILE A  48      49.035  19.242   7.603  1.00 44.86           N  
ATOM    387  CA  ILE A  48      48.662  20.616   7.875  1.00 45.04           C  
ATOM    388  C   ILE A  48      48.820  21.416   6.613  1.00 45.85           C  
ATOM    389  O   ILE A  48      48.043  22.320   6.372  1.00 46.88           O  
ATOM    390  CB  ILE A  48      49.530  21.215   8.998  1.00 44.97           C  
ATOM    391  CG1 ILE A  48      49.202  20.514  10.317  1.00 45.10           C  
ATOM    392  CG2 ILE A  48      49.287  22.706   9.109  1.00 43.90           C  
ATOM    393  CD1 ILE A  48      50.081  20.897  11.472  1.00 44.94           C  
ATOM    394  N   MET A  49      49.799  21.064   5.791  1.00 46.45           N  
ATOM    395  CA  MET A  49      50.048  21.782   4.544  1.00 47.22           C  
ATOM    396  C   MET A  49      48.975  21.500   3.491  1.00 46.97           C  
ATOM    397  O   MET A  49      48.766  22.319   2.593  1.00 46.84           O  
ATOM    398  CB  MET A  49      51.426  21.407   4.012  1.00 48.66           C  
ATOM    399  CG  MET A  49      51.777  22.105   2.744  1.00 50.95           C  
ATOM    400  SD  MET A  49      53.529  22.137   2.566  1.00 55.48           S  
ATOM    401  CE  MET A  49      53.893  23.393   3.818  1.00 55.02           C  
ATOM    402  N   LEU A  50      48.315  20.351   3.595  1.00 46.90           N  
ATOM    403  CA  LEU A  50      47.246  19.952   2.673  1.00 46.07           C  
ATOM    404  C   LEU A  50      45.904  20.379   3.223  1.00 45.63           C  
ATOM    405  O   LEU A  50      45.088  20.933   2.507  1.00 45.93           O  
ATOM    406  CB  LEU A  50      47.220  18.436   2.515  1.00 46.86           C  
ATOM    407  CG  LEU A  50      47.988  17.804   1.370  1.00 47.61           C  
ATOM    408  CD1 LEU A  50      48.027  16.299   1.554  1.00 47.21           C  
ATOM    409  CD2 LEU A  50      47.311  18.196   0.064  1.00 48.87           C  
ATOM    410  N   GLY A  51      45.691  20.102   4.505  1.00 45.22           N  
ATOM    411  CA  GLY A  51      44.435  20.420   5.156  1.00 44.90           C  
ATOM    412  C   GLY A  51      44.049  21.871   5.256  1.00 44.75           C  
ATOM    413  O   GLY A  51      42.870  22.199   5.207  1.00 44.76           O  
ATOM    414  N   PHE A  52      45.032  22.746   5.412  1.00 45.13           N  
ATOM    415  CA  PHE A  52      44.713  24.152   5.517  1.00 45.65           C  
ATOM    416  C   PHE A  52      44.201  24.678   4.186  1.00 45.91           C  
ATOM    417  O   PHE A  52      43.029  25.083   4.107  1.00 45.90           O  
ATOM    418  CB  PHE A  52      45.916  24.974   5.976  1.00 46.43           C  
ATOM    419  CG  PHE A  52      45.694  26.449   5.846  1.00 48.61           C  
ATOM    420  CD1 PHE A  52      44.473  27.017   6.255  1.00 49.02           C  
ATOM    421  CD2 PHE A  52      46.650  27.264   5.240  1.00 49.50           C  
ATOM    422  CE1 PHE A  52      44.200  28.375   6.053  1.00 49.51           C  
ATOM    423  CE2 PHE A  52      46.388  28.628   5.031  1.00 50.33           C  
ATOM    424  CZ  PHE A  52      45.155  29.182   5.438  1.00 49.77           C  
ATOM    425  N   PRO A  53      45.045  24.669   3.123  1.00 45.76           N  
ATOM    426  CA  PRO A  53      44.569  25.176   1.829  1.00 45.16           C  
ATOM    427  C   PRO A  53      43.280  24.546   1.317  1.00 45.13           C  
ATOM    428  O   PRO A  53      42.361  25.270   0.954  1.00 46.49           O  
ATOM    429  CB  PRO A  53      45.765  24.937   0.894  1.00 44.98           C  
ATOM    430  CG  PRO A  53      46.507  23.808   1.528  1.00 44.93           C  
ATOM    431  CD  PRO A  53      46.424  24.155   3.000  1.00 45.16           C  
ATOM    432  N   ILE A  54      43.195  23.220   1.313  1.00 44.04           N  
ATOM    433  CA  ILE A  54      42.011  22.517   0.810  1.00 42.97           C  
ATOM    434  C   ILE A  54      40.750  22.872   1.563  1.00 42.53           C  
ATOM    435  O   ILE A  54      39.717  23.037   0.949  1.00 41.95           O  
ATOM    436  CB  ILE A  54      42.215  20.968   0.850  1.00 43.05           C  
ATOM    437  CG1 ILE A  54      43.234  20.555  -0.226  1.00 44.10           C  
ATOM    438  CG2 ILE A  54      40.887  20.264   0.639  1.00 42.79           C  
ATOM    439  CD1 ILE A  54      43.793  19.149  -0.115  1.00 43.42           C  
ATOM    440  N   ASN A  55      40.829  22.991   2.881  1.00 42.93           N  
ATOM    441  CA  ASN A  55      39.651  23.294   3.669  1.00 43.96           C  
ATOM    442  C   ASN A  55      39.294  24.752   3.612  1.00 44.87           C  
ATOM    443  O   ASN A  55      38.102  25.083   3.615  1.00 44.95           O  
ATOM    444  CB  ASN A  55      39.861  22.838   5.108  1.00 43.31           C  
ATOM    445  CG  ASN A  55      39.597  21.357   5.282  1.00 43.14           C  
ATOM    446  OD1 ASN A  55      38.467  20.899   5.108  1.00 43.36           O  
ATOM    447  ND2 ASN A  55      40.635  20.597   5.613  1.00 42.94           N  
ATOM    448  N   PHE A  56      40.295  25.627   3.561  1.00 45.63           N  
ATOM    449  CA  PHE A  56      40.019  27.058   3.489  1.00 46.70           C  
ATOM    450  C   PHE A  56      39.431  27.412   2.119  1.00 47.32           C  
ATOM    451  O   PHE A  56      38.491  28.211   2.036  1.00 47.65           O  
ATOM    452  CB  PHE A  56      41.286  27.886   3.718  1.00 46.89           C  
ATOM    453  CG  PHE A  56      41.034  29.359   3.661  1.00 47.40           C  
ATOM    454  CD1 PHE A  56      40.389  30.008   4.713  1.00 48.11           C  
ATOM    455  CD2 PHE A  56      41.328  30.088   2.507  1.00 47.41           C  
ATOM    456  CE1 PHE A  56      40.034  31.362   4.610  1.00 47.76           C  
ATOM    457  CE2 PHE A  56      40.972  31.447   2.395  1.00 46.49           C  
ATOM    458  CZ  PHE A  56      40.327  32.079   3.441  1.00 47.16           C  
ATOM    459  N   LEU A  57      39.993  26.829   1.062  1.00 47.21           N  
ATOM    460  CA  LEU A  57      39.537  27.053  -0.310  1.00 47.39           C  
ATOM    461  C   LEU A  57      38.080  26.645  -0.409  1.00 47.92           C  
ATOM    462  O   LEU A  57      37.267  27.389  -0.923  1.00 49.30           O  
ATOM    463  CB  LEU A  57      40.369  26.204  -1.265  1.00 47.19           C  
ATOM    464  CG  LEU A  57      40.606  26.676  -2.686  1.00 46.88           C  
ATOM    465  CD1 LEU A  57      40.678  25.449  -3.565  1.00 48.01           C  
ATOM    466  CD2 LEU A  57      39.489  27.589  -3.143  1.00 47.33           C  
ATOM    467  N   THR A  58      37.766  25.453   0.087  1.00 47.99           N  
ATOM    468  CA  THR A  58      36.406  24.912   0.098  1.00 47.06           C  
ATOM    469  C   THR A  58      35.471  25.905   0.742  1.00 47.93           C  
ATOM    470  O   THR A  58      34.384  26.186   0.245  1.00 48.07           O  
ATOM    471  CB  THR A  58      36.339  23.643   0.937  1.00 46.49           C  
ATOM    472  OG1 THR A  58      37.081  22.602   0.300  1.00 45.36           O  
ATOM    473  CG2 THR A  58      34.902  23.217   1.130  1.00 46.10           C  
ATOM    474  N   LEU A  59      35.908  26.411   1.881  1.00 49.29           N  
ATOM    475  CA  LEU A  59      35.161  27.379   2.658  1.00 50.60           C  
ATOM    476  C   LEU A  59      34.949  28.671   1.868  1.00 51.13           C  
ATOM    477  O   LEU A  59      33.832  29.172   1.789  1.00 50.82           O  
ATOM    478  CB  LEU A  59      35.945  27.650   3.935  1.00 51.06           C  
ATOM    479  CG  LEU A  59      35.625  28.919   4.703  1.00 51.08           C  
ATOM    480  CD1 LEU A  59      34.196  28.872   5.209  1.00 51.10           C  
ATOM    481  CD2 LEU A  59      36.621  29.034   5.848  1.00 51.43           C  
ATOM    482  N   TYR A  60      36.022  29.192   1.282  1.00 51.69           N  
ATOM    483  CA  TYR A  60      35.964  30.433   0.521  1.00 51.92           C  
ATOM    484  C   TYR A  60      35.049  30.292  -0.682  1.00 51.11           C  
ATOM    485  O   TYR A  60      34.232  31.165  -0.936  1.00 51.40           O  
ATOM    486  CB  TYR A  60      37.379  30.824   0.086  1.00 53.48           C  
ATOM    487  CG  TYR A  60      37.521  32.209  -0.511  1.00 55.64           C  
ATOM    488  CD1 TYR A  60      37.026  32.502  -1.783  1.00 57.21           C  
ATOM    489  CD2 TYR A  60      38.157  33.233   0.198  1.00 57.36           C  
ATOM    490  CE1 TYR A  60      37.162  33.793  -2.339  1.00 59.13           C  
ATOM    491  CE2 TYR A  60      38.302  34.527  -0.345  1.00 58.91           C  
ATOM    492  CZ  TYR A  60      37.799  34.802  -1.611  1.00 59.55           C  
ATOM    493  OH  TYR A  60      37.912  36.077  -2.139  1.00 59.68           O  
ATOM    494  N   VAL A  61      35.159  29.204  -1.421  1.00 49.86           N  
ATOM    495  CA  VAL A  61      34.306  29.048  -2.582  1.00 49.23           C  
ATOM    496  C   VAL A  61      32.830  29.017  -2.179  1.00 50.23           C  
ATOM    497  O   VAL A  61      32.022  29.742  -2.754  1.00 50.34           O  
ATOM    498  CB  VAL A  61      34.676  27.773  -3.369  1.00 47.84           C  
ATOM    499  CG1 VAL A  61      33.586  27.446  -4.395  1.00 46.90           C  
ATOM    500  CG2 VAL A  61      36.018  27.984  -4.073  1.00 46.42           C  
ATOM    501  N   THR A  62      32.484  28.212  -1.182  1.00 51.03           N  
ATOM    502  CA  THR A  62      31.093  28.080  -0.754  1.00 52.03           C  
ATOM    503  C   THR A  62      30.473  29.420  -0.465  1.00 53.52           C  
ATOM    504  O   THR A  62      29.366  29.709  -0.905  1.00 54.27           O  
ATOM    505  CB  THR A  62      30.982  27.219   0.516  1.00 50.96           C  
ATOM    506  OG1 THR A  62      31.647  25.972   0.299  1.00 50.00           O  
ATOM    507  CG2 THR A  62      29.523  26.945   0.855  1.00 50.10           C  
ATOM    508  N   VAL A  63      31.186  30.248   0.272  1.00 54.09           N  
ATOM    509  CA  VAL A  63      30.656  31.536   0.650  1.00 54.78           C  
ATOM    510  C   VAL A  63      30.508  32.461  -0.526  1.00 56.02           C  
ATOM    511  O   VAL A  63      29.432  33.020  -0.741  1.00 56.05           O  
ATOM    512  CB  VAL A  63      31.554  32.180   1.694  1.00 53.72           C  
ATOM    513  CG1 VAL A  63      31.172  33.621   1.888  1.00 53.98           C  
ATOM    514  CG2 VAL A  63      31.428  31.425   2.995  1.00 53.21           C  
ATOM    515  N   GLN A  64      31.581  32.622  -1.284  1.00 57.46           N  
ATOM    516  CA  GLN A  64      31.587  33.520  -2.429  1.00 58.69           C  
ATOM    517  C   GLN A  64      30.488  33.246  -3.438  1.00 58.45           C  
ATOM    518  O   GLN A  64      29.975  34.196  -4.018  1.00 58.89           O  
ATOM    519  CB  GLN A  64      32.938  33.447  -3.108  1.00 59.96           C  
ATOM    520  CG  GLN A  64      32.952  33.957  -4.514  1.00 62.27           C  
ATOM    521  CD  GLN A  64      34.357  33.970  -5.066  1.00 63.48           C  
ATOM    522  OE1 GLN A  64      35.168  34.839  -4.711  1.00 64.32           O  
ATOM    523  NE2 GLN A  64      34.671  32.992  -5.922  1.00 63.50           N  
ATOM    524  N   HIS A  65      30.127  31.987  -3.663  1.00 58.02           N  
ATOM    525  CA  HIS A  65      29.089  31.684  -4.637  1.00 57.75           C  
ATOM    526  C   HIS A  65      27.749  31.633  -3.981  1.00 57.12           C  
ATOM    527  O   HIS A  65      27.326  30.612  -3.466  1.00 57.06           O  
ATOM    528  CB  HIS A  65      29.435  30.395  -5.351  1.00 58.33           C  
ATOM    529  CG  HIS A  65      30.654  30.519  -6.198  1.00 59.05           C  
ATOM    530  ND1 HIS A  65      30.625  30.396  -7.570  1.00 60.95           N  
ATOM    531  CD2 HIS A  65      31.930  30.826  -5.874  1.00 58.96           C  
ATOM    532  CE1 HIS A  65      31.833  30.618  -8.054  1.00 60.45           C  
ATOM    533  NE2 HIS A  65      32.643  30.882  -7.045  1.00 59.58           N  
ATOM    534  N   LYS A  66      27.079  32.773  -4.042  1.00 57.17           N  
ATOM    535  CA  LYS A  66      25.783  32.997  -3.422  1.00 57.71           C  
ATOM    536  C   LYS A  66      24.726  31.956  -3.707  1.00 56.77           C  
ATOM    537  O   LYS A  66      23.707  31.954  -3.023  1.00 56.67           O  
ATOM    538  CB  LYS A  66      25.277  34.394  -3.798  1.00 59.76           C  
ATOM    539  CG  LYS A  66      25.815  35.500  -2.884  1.00 61.99           C  
ATOM    540  CD  LYS A  66      27.345  35.509  -2.815  1.00 64.98           C  
ATOM    541  CE  LYS A  66      27.867  36.339  -1.624  1.00 66.82           C  
ATOM    542  NZ  LYS A  66      29.376  36.392  -1.524  1.00 67.87           N  
ATOM    543  N   LYS A  67      24.933  31.065  -4.663  1.00 56.05           N  
ATOM    544  CA  LYS A  67      23.881  30.092  -4.935  1.00 55.60           C  
ATOM    545  C   LYS A  67      24.197  28.736  -4.347  1.00 54.38           C  
ATOM    546  O   LYS A  67      23.323  27.886  -4.311  1.00 54.67           O  
ATOM    547  CB  LYS A  67      23.617  29.973  -6.444  1.00 57.47           C  
ATOM    548  CG  LYS A  67      23.480  31.325  -7.194  1.00 59.32           C  
ATOM    549  CD  LYS A  67      22.312  32.210  -6.702  1.00 60.15           C  
ATOM    550  CE  LYS A  67      20.954  31.525  -6.895  1.00 60.70           C  
ATOM    551  NZ  LYS A  67      20.772  30.980  -8.287  1.00 60.40           N  
ATOM    552  N   LEU A  68      25.424  28.517  -3.894  1.00 52.58           N  
ATOM    553  CA  LEU A  68      25.761  27.234  -3.288  1.00 50.90           C  
ATOM    554  C   LEU A  68      25.120  27.216  -1.894  1.00 50.80           C  
ATOM    555  O   LEU A  68      25.815  27.355  -0.886  1.00 50.71           O  
ATOM    556  CB  LEU A  68      27.285  27.099  -3.198  1.00 49.12           C  
ATOM    557  CG  LEU A  68      28.065  27.034  -4.514  1.00 46.92           C  
ATOM    558  CD1 LEU A  68      29.549  27.218  -4.235  1.00 46.53           C  
ATOM    559  CD2 LEU A  68      27.804  25.715  -5.202  1.00 45.78           C  
ATOM    560  N   ARG A  69      23.800  27.037  -1.840  1.00 50.49           N  
ATOM    561  CA  ARG A  69      23.087  27.072  -0.561  1.00 51.13           C  
ATOM    562  C   ARG A  69      22.188  25.868  -0.298  1.00 52.12           C  
ATOM    563  O   ARG A  69      21.192  26.011   0.419  1.00 52.49           O  
ATOM    564  CB  ARG A  69      22.255  28.345  -0.497  1.00 49.63           C  
ATOM    565  CG  ARG A  69      23.087  29.577  -0.650  1.00 47.89           C  
ATOM    566  CD  ARG A  69      23.937  29.726   0.560  1.00 45.64           C  
ATOM    567  NE  ARG A  69      24.826  30.874   0.479  1.00 44.55           N  
ATOM    568  CZ  ARG A  69      26.014  30.867  -0.118  1.00 45.26           C  
ATOM    569  NH1 ARG A  69      26.463  29.761  -0.699  1.00 46.04           N  
ATOM    570  NH2 ARG A  69      26.768  31.961  -0.110  1.00 44.86           N  
ATOM    571  N   THR A  70      22.528  24.699  -0.832  1.00 52.18           N  
ATOM    572  CA  THR A  70      21.717  23.500  -0.609  1.00 52.88           C  
ATOM    573  C   THR A  70      22.059  22.902   0.737  1.00 53.40           C  
ATOM    574  O   THR A  70      23.028  23.330   1.369  1.00 54.03           O  
ATOM    575  CB  THR A  70      21.994  22.429  -1.684  1.00 53.03           C  
ATOM    576  OG1 THR A  70      23.349  21.989  -1.600  1.00 52.24           O  
ATOM    577  CG2 THR A  70      21.793  23.003  -3.048  1.00 53.58           C  
ATOM    578  N   PRO A  71      21.272  21.919   1.209  1.00 53.34           N  
ATOM    579  CA  PRO A  71      21.602  21.327   2.502  1.00 52.72           C  
ATOM    580  C   PRO A  71      23.014  20.754   2.436  1.00 52.40           C  
ATOM    581  O   PRO A  71      23.737  20.788   3.426  1.00 52.57           O  
ATOM    582  CB  PRO A  71      20.535  20.251   2.657  1.00 52.87           C  
ATOM    583  CG  PRO A  71      19.354  20.888   2.020  1.00 52.95           C  
ATOM    584  CD  PRO A  71      19.966  21.425   0.739  1.00 53.66           C  
ATOM    585  N   LEU A  72      23.402  20.254   1.262  1.00 51.28           N  
ATOM    586  CA  LEU A  72      24.734  19.683   1.060  1.00 50.35           C  
ATOM    587  C   LEU A  72      25.827  20.753   1.072  1.00 50.75           C  
ATOM    588  O   LEU A  72      26.909  20.518   1.613  1.00 51.05           O  
ATOM    589  CB  LEU A  72      24.799  18.931  -0.263  1.00 49.30           C  
ATOM    590  CG  LEU A  72      26.192  18.367  -0.560  1.00 48.89           C  
ATOM    591  CD1 LEU A  72      26.503  17.258   0.421  1.00 48.52           C  
ATOM    592  CD2 LEU A  72      26.268  17.832  -1.964  1.00 49.08           C  
ATOM    593  N   ASN A  73      25.566  21.904   0.462  1.00 50.95           N  
ATOM    594  CA  ASN A  73      26.550  22.977   0.444  1.00 51.39           C  
ATOM    595  C   ASN A  73      26.784  23.438   1.867  1.00 51.63           C  
ATOM    596  O   ASN A  73      27.880  23.910   2.173  1.00 52.65           O  
ATOM    597  CB  ASN A  73      26.076  24.165  -0.412  1.00 51.88           C  
ATOM    598  CG  ASN A  73      26.010  23.836  -1.898  1.00 52.44           C  
ATOM    599  OD1 ASN A  73      26.941  23.264  -2.463  1.00 52.20           O  
ATOM    600  ND2 ASN A  73      24.910  24.214  -2.539  1.00 52.35           N  
ATOM    601  N   TYR A  74      25.773  23.317   2.727  1.00 50.85           N  
ATOM    602  CA  TYR A  74      25.919  23.718   4.123  1.00 50.94           C  
ATOM    603  C   TYR A  74      26.755  22.703   4.866  1.00 51.04           C  
ATOM    604  O   TYR A  74      27.777  23.065   5.436  1.00 51.67           O  
ATOM    605  CB  TYR A  74      24.562  23.830   4.804  1.00 50.49           C  
ATOM    606  CG  TYR A  74      23.913  25.152   4.575  1.00 51.17           C  
ATOM    607  CD1 TYR A  74      24.028  26.176   5.508  1.00 51.00           C  
ATOM    608  CD2 TYR A  74      23.232  25.411   3.386  1.00 52.42           C  
ATOM    609  CE1 TYR A  74      23.481  27.435   5.253  1.00 51.51           C  
ATOM    610  CE2 TYR A  74      22.682  26.661   3.122  1.00 51.79           C  
ATOM    611  CZ  TYR A  74      22.814  27.662   4.055  1.00 51.69           C  
ATOM    612  OH  TYR A  74      22.297  28.892   3.764  1.00 52.66           O  
ATOM    613  N   ILE A  75      26.326  21.443   4.854  1.00 50.14           N  
ATOM    614  CA  ILE A  75      27.014  20.369   5.557  1.00 48.96           C  
ATOM    615  C   ILE A  75      28.470  20.308   5.201  1.00 48.51           C  
ATOM    616  O   ILE A  75      29.293  20.035   6.070  1.00 49.55           O  
ATOM    617  CB  ILE A  75      26.334  19.005   5.277  1.00 49.74           C  
ATOM    618  CG1 ILE A  75      25.084  18.887   6.152  1.00 49.32           C  
ATOM    619  CG2 ILE A  75      27.307  17.856   5.515  1.00 49.57           C  
ATOM    620  CD1 ILE A  75      25.318  19.308   7.620  1.00 50.51           C  
ATOM    621  N   LEU A  76      28.813  20.560   3.946  1.00 47.28           N  
ATOM    622  CA  LEU A  76      30.214  20.505   3.589  1.00 46.46           C  
ATOM    623  C   LEU A  76      30.938  21.758   3.994  1.00 45.97           C  
ATOM    624  O   LEU A  76      32.143  21.717   4.153  1.00 46.60           O  
ATOM    625  CB  LEU A  76      30.399  20.177   2.112  1.00 46.57           C  
ATOM    626  CG  LEU A  76      30.610  18.652   2.095  1.00 47.04           C  
ATOM    627  CD1 LEU A  76      29.364  17.952   1.609  1.00 46.91           C  
ATOM    628  CD2 LEU A  76      31.798  18.297   1.253  1.00 47.00           C  
ATOM    629  N   LEU A  77      30.237  22.868   4.172  1.00 45.16           N  
ATOM    630  CA  LEU A  77      30.916  24.075   4.641  1.00 45.05           C  
ATOM    631  C   LEU A  77      31.237  23.819   6.100  1.00 44.75           C  
ATOM    632  O   LEU A  77      32.309  24.161   6.588  1.00 45.61           O  
ATOM    633  CB  LEU A  77      30.006  25.307   4.521  1.00 45.31           C  
ATOM    634  CG  LEU A  77      30.605  26.607   5.071  1.00 45.03           C  
ATOM    635  CD1 LEU A  77      32.001  26.853   4.527  1.00 45.06           C  
ATOM    636  CD2 LEU A  77      29.692  27.736   4.703  1.00 44.86           C  
ATOM    637  N   ASN A  78      30.280  23.202   6.781  1.00 44.05           N  
ATOM    638  CA  ASN A  78      30.388  22.834   8.182  1.00 43.70           C  
ATOM    639  C   ASN A  78      31.632  21.957   8.328  1.00 43.59           C  
ATOM    640  O   ASN A  78      32.489  22.238   9.157  1.00 44.16           O  
ATOM    641  CB  ASN A  78      29.095  22.086   8.571  1.00 44.36           C  
ATOM    642  CG  ASN A  78      29.113  21.514   9.981  1.00 43.95           C  
ATOM    643  OD1 ASN A  78      29.474  22.196  10.948  1.00 42.89           O  
ATOM    644  ND2 ASN A  78      28.688  20.250  10.103  1.00 44.26           N  
ATOM    645  N   LEU A  79      31.746  20.925   7.498  1.00 42.41           N  
ATOM    646  CA  LEU A  79      32.885  20.029   7.558  1.00 40.88           C  
ATOM    647  C   LEU A  79      34.202  20.756   7.342  1.00 40.84           C  
ATOM    648  O   LEU A  79      35.183  20.421   8.006  1.00 40.77           O  
ATOM    649  CB  LEU A  79      32.722  18.928   6.527  1.00 40.93           C  
ATOM    650  CG  LEU A  79      32.017  17.658   6.999  1.00 40.99           C  
ATOM    651  CD1 LEU A  79      31.441  17.820   8.410  1.00 41.38           C  
ATOM    652  CD2 LEU A  79      30.956  17.315   5.969  1.00 40.67           C  
ATOM    653  N   ALA A  80      34.241  21.733   6.437  1.00 40.56           N  
ATOM    654  CA  ALA A  80      35.476  22.472   6.163  1.00 40.21           C  
ATOM    655  C   ALA A  80      35.868  23.269   7.392  1.00 40.35           C  
ATOM    656  O   ALA A  80      37.042  23.387   7.712  1.00 40.96           O  
ATOM    657  CB  ALA A  80      35.290  23.409   4.946  1.00 39.75           C  
ATOM    658  N   VAL A  81      34.890  23.811   8.094  1.00 40.28           N  
ATOM    659  CA  VAL A  81      35.185  24.585   9.287  1.00 40.28           C  
ATOM    660  C   VAL A  81      35.723  23.669  10.382  1.00 40.81           C  
ATOM    661  O   VAL A  81      36.739  23.963  11.003  1.00 40.13           O  
ATOM    662  CB  VAL A  81      33.919  25.300   9.751  1.00 39.83           C  
ATOM    663  CG1 VAL A  81      34.185  26.097  11.001  1.00 39.65           C  
ATOM    664  CG2 VAL A  81      33.436  26.197   8.641  1.00 38.79           C  
ATOM    665  N   ALA A  82      35.037  22.556  10.600  1.00 41.39           N  
ATOM    666  CA  ALA A  82      35.434  21.596  11.604  1.00 41.75           C  
ATOM    667  C   ALA A  82      36.826  21.046  11.284  1.00 42.80           C  
ATOM    668  O   ALA A  82      37.581  20.750  12.204  1.00 43.38           O  
ATOM    669  CB  ALA A  82      34.407  20.471  11.666  1.00 40.80           C  
ATOM    670  N   ASP A  83      37.169  20.930   9.998  1.00 44.01           N  
ATOM    671  CA  ASP A  83      38.472  20.407   9.549  1.00 43.99           C  
ATOM    672  C   ASP A  83      39.557  21.458   9.781  1.00 44.44           C  
ATOM    673  O   ASP A  83      40.721  21.094   9.991  1.00 45.71           O  
ATOM    674  CB  ASP A  83      38.462  20.026   8.056  1.00 44.02           C  
ATOM    675  CG  ASP A  83      37.573  18.838   7.742  1.00 43.73           C  
ATOM    676  OD1 ASP A  83      37.126  18.132   8.660  1.00 43.57           O  
ATOM    677  OD2 ASP A  83      37.323  18.602   6.550  1.00 43.85           O  
ATOM    678  N   LEU A  84      39.197  22.740   9.724  1.00 43.64           N  
ATOM    679  CA  LEU A  84      40.169  23.806   9.967  1.00 42.71           C  
ATOM    680  C   LEU A  84      40.443  23.885  11.462  1.00 43.09           C  
ATOM    681  O   LEU A  84      41.531  24.298  11.855  1.00 43.70           O  
ATOM    682  CB  LEU A  84      39.659  25.154   9.430  1.00 42.24           C  
ATOM    683  CG  LEU A  84      39.790  25.391   7.912  1.00 40.63           C  
ATOM    684  CD1 LEU A  84      38.895  26.542   7.491  1.00 40.06           C  
ATOM    685  CD2 LEU A  84      41.233  25.674   7.539  1.00 39.38           C  
ATOM    686  N   PHE A  85      39.467  23.499  12.288  1.00 42.95           N  
ATOM    687  CA  PHE A  85      39.668  23.473  13.736  1.00 43.35           C  
ATOM    688  C   PHE A  85      40.601  22.326  14.051  1.00 43.03           C  
ATOM    689  O   PHE A  85      41.421  22.412  14.947  1.00 42.63           O  
ATOM    690  CB  PHE A  85      38.345  23.280  14.469  1.00 44.35           C  
ATOM    691  CG  PHE A  85      37.628  24.559  14.749  1.00 45.15           C  
ATOM    692  CD1 PHE A  85      38.246  25.565  15.488  1.00 45.69           C  
ATOM    693  CD2 PHE A  85      36.339  24.769  14.271  1.00 45.61           C  
ATOM    694  CE1 PHE A  85      37.582  26.780  15.753  1.00 46.18           C  
ATOM    695  CE2 PHE A  85      35.667  25.967  14.522  1.00 45.34           C  
ATOM    696  CZ  PHE A  85      36.288  26.979  15.266  1.00 45.44           C  
ATOM    697  N   MET A  86      40.461  21.245  13.306  1.00 42.72           N  
ATOM    698  CA  MET A  86      41.331  20.103  13.474  1.00 43.14           C  
ATOM    699  C   MET A  86      42.761  20.534  13.195  1.00 43.77           C  
ATOM    700  O   MET A  86      43.621  20.361  14.041  1.00 45.48           O  
ATOM    701  CB  MET A  86      40.935  18.984  12.504  1.00 43.69           C  
ATOM    702  CG  MET A  86      39.535  18.452  12.733  1.00 44.57           C  
ATOM    703  SD  MET A  86      39.137  16.991  11.762  1.00 46.25           S  
ATOM    704  CE  MET A  86      39.972  15.752  12.693  1.00 43.20           C  
ATOM    705  N   VAL A  87      42.996  21.107  12.017  1.00 43.22           N  
ATOM    706  CA  VAL A  87      44.326  21.540  11.591  1.00 41.86           C  
ATOM    707  C   VAL A  87      44.966  22.489  12.573  1.00 42.70           C  
ATOM    708  O   VAL A  87      46.048  22.226  13.080  1.00 43.40           O  
ATOM    709  CB  VAL A  87      44.267  22.237  10.220  1.00 40.07           C  
ATOM    710  CG1 VAL A  87      45.640  22.673   9.806  1.00 38.91           C  
ATOM    711  CG2 VAL A  87      43.674  21.315   9.190  1.00 38.64           C  
ATOM    712  N   PHE A  88      44.304  23.600  12.845  1.00 43.08           N  
ATOM    713  CA  PHE A  88      44.868  24.598  13.749  1.00 44.04           C  
ATOM    714  C   PHE A  88      44.629  24.247  15.203  1.00 43.44           C  
ATOM    715  O   PHE A  88      45.496  24.502  16.040  1.00 43.33           O  
ATOM    716  CB  PHE A  88      44.292  25.979  13.425  1.00 46.07           C  
ATOM    717  CG  PHE A  88      44.708  26.508  12.079  1.00 47.73           C  
ATOM    718  CD1 PHE A  88      46.048  26.756  11.801  1.00 49.33           C  
ATOM    719  CD2 PHE A  88      43.766  26.706  11.065  1.00 48.02           C  
ATOM    720  CE1 PHE A  88      46.450  27.192  10.523  1.00 50.24           C  
ATOM    721  CE2 PHE A  88      44.158  27.141   9.787  1.00 48.37           C  
ATOM    722  CZ  PHE A  88      45.498  27.381   9.515  1.00 49.38           C  
ATOM    723  N   GLY A  89      43.480  23.654  15.502  1.00 42.32           N  
ATOM    724  CA  GLY A  89      43.179  23.294  16.874  1.00 41.13           C  
ATOM    725  C   GLY A  89      44.055  22.222  17.508  1.00 40.24           C  
ATOM    726  O   GLY A  89      44.655  22.447  18.546  1.00 39.99           O  
ATOM    727  N   GLY A  90      44.141  21.051  16.896  1.00 39.51           N  
ATOM    728  CA  GLY A  90      44.943  20.013  17.504  1.00 38.76           C  
ATOM    729  C   GLY A  90      46.161  19.576  16.740  1.00 38.72           C  
ATOM    730  O   GLY A  90      47.115  19.165  17.353  1.00 40.10           O  
ATOM    731  N   PHE A  91      46.133  19.669  15.415  1.00 38.41           N  
ATOM    732  CA  PHE A  91      47.253  19.227  14.577  1.00 38.45           C  
ATOM    733  C   PHE A  91      48.484  20.004  14.841  1.00 39.35           C  
ATOM    734  O   PHE A  91      49.584  19.512  14.631  1.00 40.01           O  
ATOM    735  CB  PHE A  91      46.893  19.315  13.105  1.00 37.74           C  
ATOM    736  CG  PHE A  91      45.960  18.236  12.664  1.00 37.36           C  
ATOM    737  CD1 PHE A  91      45.235  17.507  13.600  1.00 37.59           C  
ATOM    738  CD2 PHE A  91      45.808  17.938  11.314  1.00 36.40           C  
ATOM    739  CE1 PHE A  91      44.380  16.501  13.200  1.00 37.98           C  
ATOM    740  CE2 PHE A  91      44.952  16.927  10.903  1.00 37.14           C  
ATOM    741  CZ  PHE A  91      44.236  16.204  11.844  1.00 37.01           C  
ATOM    742  N   THR A  92      48.312  21.225  15.303  1.00 38.69           N  
ATOM    743  CA  THR A  92      49.444  22.058  15.624  1.00 38.89           C  
ATOM    744  C   THR A  92      50.146  21.465  16.853  1.00 39.29           C  
ATOM    745  O   THR A  92      51.373  21.421  16.935  1.00 39.23           O  
ATOM    746  CB  THR A  92      48.933  23.469  15.883  1.00 39.14           C  
ATOM    747  OG1 THR A  92      47.778  23.401  16.729  1.00 41.00           O  
ATOM    748  CG2 THR A  92      48.518  24.120  14.569  1.00 39.56           C  
ATOM    749  N   THR A  93      49.360  20.981  17.802  1.00 39.63           N  
ATOM    750  CA  THR A  93      49.926  20.388  18.993  1.00 40.57           C  
ATOM    751  C   THR A  93      50.468  19.009  18.679  1.00 41.11           C  
ATOM    752  O   THR A  93      51.507  18.646  19.215  1.00 42.70           O  
ATOM    753  CB  THR A  93      48.881  20.254  20.117  1.00 41.08           C  
ATOM    754  OG1 THR A  93      48.595  21.546  20.658  1.00 41.36           O  
ATOM    755  CG2 THR A  93      49.401  19.349  21.233  1.00 42.23           C  
ATOM    756  N   THR A  94      49.794  18.235  17.832  1.00 40.59           N  
ATOM    757  CA  THR A  94      50.294  16.897  17.540  1.00 39.16           C  
ATOM    758  C   THR A  94      51.595  16.932  16.752  1.00 38.71           C  
ATOM    759  O   THR A  94      52.394  16.019  16.857  1.00 38.34           O  
ATOM    760  CB  THR A  94      49.245  16.034  16.813  1.00 38.75           C  
ATOM    761  OG1 THR A  94      49.913  15.010  16.063  1.00 38.79           O  
ATOM    762  CG2 THR A  94      48.389  16.862  15.923  1.00 37.55           C  
ATOM    763  N   LEU A  95      51.816  17.984  15.982  1.00 38.95           N  
ATOM    764  CA  LEU A  95      53.072  18.091  15.261  1.00 38.48           C  
ATOM    765  C   LEU A  95      54.101  18.583  16.238  1.00 38.97           C  
ATOM    766  O   LEU A  95      55.233  18.137  16.215  1.00 39.01           O  
ATOM    767  CB  LEU A  95      52.975  19.085  14.110  1.00 37.78           C  
ATOM    768  CG  LEU A  95      54.327  19.491  13.512  1.00 36.87           C  
ATOM    769  CD1 LEU A  95      55.087  18.277  13.016  1.00 37.07           C  
ATOM    770  CD2 LEU A  95      54.083  20.446  12.376  1.00 36.69           C  
ATOM    771  N   TYR A  96      53.704  19.506  17.102  1.00 39.20           N  
ATOM    772  CA  TYR A  96      54.617  20.049  18.086  1.00 40.11           C  
ATOM    773  C   TYR A  96      55.055  18.965  19.038  1.00 40.78           C  
ATOM    774  O   TYR A  96      56.213  18.940  19.449  1.00 41.85           O  
ATOM    775  CB  TYR A  96      53.940  21.140  18.889  1.00 41.92           C  
ATOM    776  CG  TYR A  96      54.903  21.858  19.787  1.00 45.17           C  
ATOM    777  CD1 TYR A  96      55.786  22.799  19.267  1.00 46.93           C  
ATOM    778  CD2 TYR A  96      54.961  21.584  21.151  1.00 46.94           C  
ATOM    779  CE1 TYR A  96      56.711  23.461  20.073  1.00 48.34           C  
ATOM    780  CE2 TYR A  96      55.885  22.241  21.977  1.00 49.53           C  
ATOM    781  CZ  TYR A  96      56.763  23.184  21.427  1.00 50.08           C  
ATOM    782  OH  TYR A  96      57.698  23.847  22.210  1.00 53.51           O  
ATOM    783  N   THR A  97      54.122  18.092  19.406  1.00 40.08           N  
ATOM    784  CA  THR A  97      54.373  16.991  20.321  1.00 39.55           C  
ATOM    785  C   THR A  97      55.240  15.922  19.668  1.00 39.94           C  
ATOM    786  O   THR A  97      56.152  15.406  20.303  1.00 40.27           O  
ATOM    787  CB  THR A  97      53.053  16.383  20.741  1.00 39.67           C  
ATOM    788  OG1 THR A  97      52.332  17.344  21.522  1.00 40.97           O  
ATOM    789  CG2 THR A  97      53.273  15.111  21.521  1.00 39.33           C  
ATOM    790  N   SER A  98      54.949  15.574  18.417  1.00 40.39           N  
ATOM    791  CA  SER A  98      55.732  14.573  17.711  1.00 40.18           C  
ATOM    792  C   SER A  98      57.153  15.036  17.638  1.00 41.32           C  
ATOM    793  O   SER A  98      58.057  14.224  17.802  1.00 42.60           O  
ATOM    794  CB  SER A  98      55.207  14.373  16.297  1.00 38.90           C  
ATOM    795  OG  SER A  98      53.973  13.717  16.329  1.00 38.62           O  
ATOM    796  N   LEU A  99      57.352  16.338  17.403  1.00 42.19           N  
ATOM    797  CA  LEU A  99      58.700  16.944  17.275  1.00 42.27           C  
ATOM    798  C   LEU A  99      59.522  16.848  18.536  1.00 42.49           C  
ATOM    799  O   LEU A  99      60.732  16.907  18.448  1.00 43.81           O  
ATOM    800  CB  LEU A  99      58.612  18.422  16.865  1.00 40.98           C  
ATOM    801  CG  LEU A  99      58.346  18.689  15.382  1.00 40.58           C  
ATOM    802  CD1 LEU A  99      58.062  20.146  15.174  1.00 39.57           C  
ATOM    803  CD2 LEU A  99      59.532  18.223  14.548  1.00 39.74           C  
ATOM    804  N   HIS A 100      58.891  16.708  19.693  1.00 42.42           N  
ATOM    805  CA  HIS A 100      59.630  16.621  20.941  1.00 41.56           C  
ATOM    806  C   HIS A 100      59.559  15.233  21.537  1.00 41.28           C  
ATOM    807  O   HIS A 100      60.275  14.955  22.493  1.00 41.98           O  
ATOM    808  CB  HIS A 100      59.091  17.667  21.910  1.00 42.53           C  
ATOM    809  CG  HIS A 100      59.284  19.071  21.424  1.00 45.43           C  
ATOM    810  ND1 HIS A 100      60.531  19.655  21.300  1.00 47.16           N  
ATOM    811  CD2 HIS A 100      58.395  20.005  21.014  1.00 46.79           C  
ATOM    812  CE1 HIS A 100      60.401  20.886  20.840  1.00 47.33           C  
ATOM    813  NE2 HIS A 100      59.114  21.125  20.659  1.00 48.54           N  
ATOM    814  N   GLY A 101      58.719  14.365  20.972  1.00 40.51           N  
ATOM    815  CA  GLY A 101      58.589  13.016  21.489  1.00 39.14           C  
ATOM    816  C   GLY A 101      57.705  12.924  22.722  1.00 39.04           C  
ATOM    817  O   GLY A 101      57.713  11.913  23.402  1.00 39.19           O  
ATOM    818  N   TYR A 102      56.949  13.980  23.019  1.00 39.70           N  
ATOM    819  CA  TYR A 102      56.048  13.997  24.179  1.00 39.93           C  
ATOM    820  C   TYR A 102      55.266  15.307  24.238  1.00 39.31           C  
ATOM    821  O   TYR A 102      55.601  16.273  23.545  1.00 39.55           O  
ATOM    822  CB  TYR A 102      56.830  13.797  25.500  1.00 41.85           C  
ATOM    823  CG  TYR A 102      57.514  15.044  26.063  1.00 42.10           C  
ATOM    824  CD1 TYR A 102      58.713  15.527  25.524  1.00 42.02           C  
ATOM    825  CD2 TYR A 102      56.947  15.742  27.128  1.00 43.00           C  
ATOM    826  CE1 TYR A 102      59.329  16.674  26.032  1.00 42.00           C  
ATOM    827  CE2 TYR A 102      57.546  16.886  27.645  1.00 43.54           C  
ATOM    828  CZ  TYR A 102      58.737  17.353  27.095  1.00 43.24           C  
ATOM    829  OH  TYR A 102      59.308  18.501  27.616  1.00 43.00           O  
ATOM    830  N   PHE A 103      54.242  15.326  25.087  1.00 38.37           N  
ATOM    831  CA  PHE A 103      53.371  16.477  25.263  1.00 37.54           C  
ATOM    832  C   PHE A 103      53.998  17.531  26.149  1.00 38.74           C  
ATOM    833  O   PHE A 103      53.657  17.627  27.330  1.00 37.83           O  
ATOM    834  CB  PHE A 103      52.026  16.024  25.842  1.00 36.76           C  
ATOM    835  CG  PHE A 103      51.060  15.533  24.802  1.00 35.98           C  
ATOM    836  CD1 PHE A 103      50.374  16.442  23.993  1.00 35.36           C  
ATOM    837  CD2 PHE A 103      50.857  14.173  24.605  1.00 34.32           C  
ATOM    838  CE1 PHE A 103      49.503  16.006  23.004  1.00 35.48           C  
ATOM    839  CE2 PHE A 103      49.986  13.727  23.615  1.00 34.80           C  
ATOM    840  CZ  PHE A 103      49.306  14.647  22.811  1.00 34.98           C  
ATOM    841  N   VAL A 104      54.902  18.327  25.574  1.00 40.36           N  
ATOM    842  CA  VAL A 104      55.553  19.389  26.327  1.00 42.10           C  
ATOM    843  C   VAL A 104      54.480  20.264  26.988  1.00 43.06           C  
ATOM    844  O   VAL A 104      54.658  20.670  28.133  1.00 45.33           O  
ATOM    845  CB  VAL A 104      56.470  20.304  25.432  1.00 41.63           C  
ATOM    846  CG1 VAL A 104      57.146  19.494  24.361  1.00 40.15           C  
ATOM    847  CG2 VAL A 104      55.665  21.437  24.836  1.00 43.06           C  
ATOM    848  N   PHE A 105      53.376  20.545  26.305  1.00 43.33           N  
ATOM    849  CA  PHE A 105      52.344  21.374  26.921  1.00 44.10           C  
ATOM    850  C   PHE A 105      51.540  20.607  27.942  1.00 43.72           C  
ATOM    851  O   PHE A 105      50.456  21.071  28.353  1.00 45.16           O  
ATOM    852  CB  PHE A 105      51.406  21.926  25.864  1.00 46.27           C  
ATOM    853  CG  PHE A 105      52.092  22.773  24.862  1.00 48.77           C  
ATOM    854  CD1 PHE A 105      52.948  23.801  25.278  1.00 49.74           C  
ATOM    855  CD2 PHE A 105      51.902  22.548  23.499  1.00 50.04           C  
ATOM    856  CE1 PHE A 105      53.617  24.598  24.357  1.00 50.85           C  
ATOM    857  CE2 PHE A 105      52.563  23.338  22.560  1.00 51.31           C  
ATOM    858  CZ  PHE A 105      53.428  24.371  22.992  1.00 51.75           C  
ATOM    859  N   GLY A 106      52.032  19.446  28.352  1.00 41.67           N  
ATOM    860  CA  GLY A 106      51.300  18.677  29.336  1.00 41.15           C  
ATOM    861  C   GLY A 106      49.846  18.389  28.984  1.00 41.16           C  
ATOM    862  O   GLY A 106      49.443  18.460  27.829  1.00 41.26           O  
ATOM    863  N   PRO A 107      49.031  18.045  29.982  1.00 41.64           N  
ATOM    864  CA  PRO A 107      47.624  17.746  29.726  1.00 42.52           C  
ATOM    865  C   PRO A 107      46.874  18.753  28.901  1.00 42.86           C  
ATOM    866  O   PRO A 107      45.934  18.369  28.208  1.00 43.94           O  
ATOM    867  CB  PRO A 107      47.040  17.563  31.135  1.00 42.07           C  
ATOM    868  CG  PRO A 107      48.051  18.183  32.042  1.00 41.05           C  
ATOM    869  CD  PRO A 107      49.349  17.841  31.401  1.00 41.61           C  
ATOM    870  N   THR A 108      47.268  20.020  28.942  1.00 43.19           N  
ATOM    871  CA  THR A 108      46.554  21.010  28.143  1.00 44.14           C  
ATOM    872  C   THR A 108      46.731  20.679  26.672  1.00 44.15           C  
ATOM    873  O   THR A 108      45.743  20.634  25.929  1.00 44.45           O  
ATOM    874  CB  THR A 108      47.053  22.434  28.418  1.00 44.53           C  
ATOM    875  OG1 THR A 108      46.988  22.695  29.824  1.00 45.33           O  
ATOM    876  CG2 THR A 108      46.168  23.443  27.709  1.00 44.16           C  
ATOM    877  N   GLY A 109      47.972  20.435  26.255  1.00 43.20           N  
ATOM    878  CA  GLY A 109      48.221  20.085  24.871  1.00 42.64           C  
ATOM    879  C   GLY A 109      47.509  18.805  24.476  1.00 42.68           C  
ATOM    880  O   GLY A 109      47.106  18.649  23.342  1.00 43.48           O  
ATOM    881  N   CYS A 110      47.342  17.902  25.436  1.00 42.09           N  
ATOM    882  CA  CYS A 110      46.710  16.607  25.237  1.00 41.45           C  
ATOM    883  C   CYS A 110      45.250  16.801  25.048  1.00 41.11           C  
ATOM    884  O   CYS A 110      44.613  16.051  24.304  1.00 40.05           O  
ATOM    885  CB  CYS A 110      46.947  15.741  26.454  1.00 41.83           C  
ATOM    886  SG  CYS A 110      46.245  14.064  26.418  1.00 41.91           S  
ATOM    887  N   ASN A 111      44.706  17.802  25.730  1.00 41.16           N  
ATOM    888  CA  ASN A 111      43.285  18.090  25.621  1.00 41.22           C  
ATOM    889  C   ASN A 111      42.993  18.725  24.281  1.00 40.97           C  
ATOM    890  O   ASN A 111      41.990  18.393  23.666  1.00 41.03           O  
ATOM    891  CB  ASN A 111      42.832  19.007  26.756  1.00 40.94           C  
ATOM    892  CG  ASN A 111      42.793  18.299  28.096  1.00 42.04           C  
ATOM    893  OD1 ASN A 111      42.142  17.268  28.263  1.00 42.29           O  
ATOM    894  ND2 ASN A 111      43.488  18.859  29.058  1.00 42.93           N  
ATOM    895  N   LEU A 112      43.860  19.625  23.823  1.00 40.50           N  
ATOM    896  CA  LEU A 112      43.666  20.273  22.525  1.00 40.12           C  
ATOM    897  C   LEU A 112      43.704  19.217  21.470  1.00 40.57           C  
ATOM    898  O   LEU A 112      42.803  19.126  20.645  1.00 40.73           O  
ATOM    899  CB  LEU A 112      44.782  21.287  22.260  1.00 39.53           C  
ATOM    900  CG  LEU A 112      44.800  22.515  23.176  1.00 39.11           C  
ATOM    901  CD1 LEU A 112      46.073  23.298  22.920  1.00 37.80           C  
ATOM    902  CD2 LEU A 112      43.538  23.372  22.953  1.00 36.74           C  
ATOM    903  N   GLU A 113      44.770  18.424  21.521  1.00 41.07           N  
ATOM    904  CA  GLU A 113      45.010  17.316  20.608  1.00 41.48           C  
ATOM    905  C   GLU A 113      43.772  16.389  20.579  1.00 41.42           C  
ATOM    906  O   GLU A 113      43.213  16.160  19.505  1.00 42.37           O  
ATOM    907  CB  GLU A 113      46.260  16.552  21.076  1.00 42.27           C  
ATOM    908  CG  GLU A 113      47.174  16.079  19.972  1.00 45.67           C  
ATOM    909  CD  GLU A 113      46.474  15.165  19.002  1.00 47.69           C  
ATOM    910  OE1 GLU A 113      45.823  14.211  19.480  1.00 48.20           O  
ATOM    911  OE2 GLU A 113      46.574  15.394  17.771  1.00 49.25           O  
ATOM    912  N   GLY A 114      43.335  15.890  21.739  1.00 41.23           N  
ATOM    913  CA  GLY A 114      42.184  15.004  21.789  1.00 39.36           C  
ATOM    914  C   GLY A 114      40.857  15.626  21.392  1.00 39.01           C  
ATOM    915  O   GLY A 114      40.156  15.093  20.544  1.00 38.37           O  
ATOM    916  N   PHE A 115      40.525  16.764  21.996  1.00 38.68           N  
ATOM    917  CA  PHE A 115      39.258  17.466  21.746  1.00 38.81           C  
ATOM    918  C   PHE A 115      39.011  17.775  20.281  1.00 39.37           C  
ATOM    919  O   PHE A 115      37.971  17.416  19.743  1.00 40.13           O  
ATOM    920  CB  PHE A 115      39.188  18.784  22.546  1.00 37.75           C  
ATOM    921  CG  PHE A 115      37.928  19.574  22.305  1.00 36.88           C  
ATOM    922  CD1 PHE A 115      36.707  19.137  22.816  1.00 36.83           C  
ATOM    923  CD2 PHE A 115      37.950  20.726  21.523  1.00 36.77           C  
ATOM    924  CE1 PHE A 115      35.521  19.832  22.551  1.00 36.61           C  
ATOM    925  CE2 PHE A 115      36.768  21.431  21.248  1.00 35.98           C  
ATOM    926  CZ  PHE A 115      35.553  20.978  21.765  1.00 36.03           C  
ATOM    927  N   PHE A 116      39.945  18.432  19.625  1.00 39.61           N  
ATOM    928  CA  PHE A 116      39.698  18.795  18.247  1.00 40.28           C  
ATOM    929  C   PHE A 116      39.623  17.645  17.300  1.00 40.43           C  
ATOM    930  O   PHE A 116      38.901  17.749  16.318  1.00 40.70           O  
ATOM    931  CB  PHE A 116      40.714  19.825  17.796  1.00 40.85           C  
ATOM    932  CG  PHE A 116      40.407  21.179  18.311  1.00 41.37           C  
ATOM    933  CD1 PHE A 116      39.189  21.785  17.992  1.00 40.54           C  
ATOM    934  CD2 PHE A 116      41.287  21.828  19.171  1.00 41.56           C  
ATOM    935  CE1 PHE A 116      38.850  23.025  18.529  1.00 41.46           C  
ATOM    936  CE2 PHE A 116      40.955  23.067  19.711  1.00 41.12           C  
ATOM    937  CZ  PHE A 116      39.734  23.668  19.392  1.00 40.94           C  
ATOM    938  N   ALA A 117      40.340  16.560  17.555  1.00 40.14           N  
ATOM    939  CA  ALA A 117      40.268  15.418  16.653  1.00 40.83           C  
ATOM    940  C   ALA A 117      38.926  14.719  16.852  1.00 41.75           C  
ATOM    941  O   ALA A 117      38.318  14.207  15.906  1.00 42.04           O  
ATOM    942  CB  ALA A 117      41.385  14.475  16.941  1.00 41.29           C  
ATOM    943  N   THR A 118      38.467  14.714  18.098  1.00 42.61           N  
ATOM    944  CA  THR A 118      37.192  14.105  18.457  1.00 43.21           C  
ATOM    945  C   THR A 118      36.070  14.962  17.890  1.00 43.20           C  
ATOM    946  O   THR A 118      35.169  14.443  17.193  1.00 43.36           O  
ATOM    947  CB  THR A 118      37.059  14.017  19.990  1.00 44.20           C  
ATOM    948  OG1 THR A 118      38.126  13.214  20.508  1.00 45.44           O  
ATOM    949  CG2 THR A 118      35.741  13.391  20.385  1.00 44.67           C  
ATOM    950  N   LEU A 119      36.125  16.260  18.183  1.00 43.50           N  
ATOM    951  CA  LEU A 119      35.141  17.216  17.691  1.00 42.96           C  
ATOM    952  C   LEU A 119      35.006  17.043  16.174  1.00 42.17           C  
ATOM    953  O   LEU A 119      33.899  16.961  15.643  1.00 41.06           O  
ATOM    954  CB  LEU A 119      35.613  18.639  18.016  1.00 43.26           C  
ATOM    955  CG  LEU A 119      34.595  19.613  18.594  1.00 43.08           C  
ATOM    956  CD1 LEU A 119      35.031  21.034  18.280  1.00 42.86           C  
ATOM    957  CD2 LEU A 119      33.234  19.327  17.985  1.00 43.05           C  
ATOM    958  N   GLY A 120      36.149  16.965  15.499  1.00 42.23           N  
ATOM    959  CA  GLY A 120      36.167  16.817  14.053  1.00 42.59           C  
ATOM    960  C   GLY A 120      35.584  15.526  13.515  1.00 42.77           C  
ATOM    961  O   GLY A 120      34.774  15.540  12.590  1.00 43.26           O  
ATOM    962  N   GLY A 121      36.000  14.401  14.074  1.00 42.64           N  
ATOM    963  CA  GLY A 121      35.471  13.138  13.606  1.00 42.59           C  
ATOM    964  C   GLY A 121      33.979  13.019  13.880  1.00 43.13           C  
ATOM    965  O   GLY A 121      33.221  12.536  13.017  1.00 42.32           O  
ATOM    966  N   GLU A 122      33.560  13.469  15.072  1.00 42.73           N  
ATOM    967  CA  GLU A 122      32.159  13.396  15.494  1.00 42.73           C  
ATOM    968  C   GLU A 122      31.259  14.366  14.732  1.00 42.91           C  
ATOM    969  O   GLU A 122      30.062  14.091  14.566  1.00 42.83           O  
ATOM    970  CB  GLU A 122      32.039  13.619  17.007  1.00 42.39           C  
ATOM    971  CG  GLU A 122      32.225  12.355  17.839  1.00 43.26           C  
ATOM    972  CD  GLU A 122      31.240  11.244  17.481  1.00 44.45           C  
ATOM    973  OE1 GLU A 122      30.049  11.544  17.254  1.00 45.15           O  
ATOM    974  OE2 GLU A 122      31.649  10.062  17.443  1.00 44.09           O  
ATOM    975  N   ILE A 123      31.784  15.502  14.272  1.00 43.39           N  
ATOM    976  CA  ILE A 123      30.955  16.425  13.494  1.00 43.21           C  
ATOM    977  C   ILE A 123      30.746  15.817  12.111  1.00 43.62           C  
ATOM    978  O   ILE A 123      29.715  16.048  11.460  1.00 43.93           O  
ATOM    979  CB  ILE A 123      31.607  17.816  13.370  1.00 42.86           C  
ATOM    980  CG1 ILE A 123      31.367  18.607  14.655  1.00 43.09           C  
ATOM    981  CG2 ILE A 123      31.021  18.569  12.173  1.00 42.74           C  
ATOM    982  CD1 ILE A 123      32.145  19.891  14.721  1.00 43.91           C  
ATOM    983  N   ALA A 124      31.730  15.039  11.666  1.00 43.18           N  
ATOM    984  CA  ALA A 124      31.636  14.352  10.391  1.00 42.72           C  
ATOM    985  C   ALA A 124      30.582  13.267  10.528  1.00 42.65           C  
ATOM    986  O   ALA A 124      29.701  13.171   9.693  1.00 42.91           O  
ATOM    987  CB  ALA A 124      32.968  13.739  10.031  1.00 42.53           C  
ATOM    988  N   LEU A 125      30.665  12.463  11.589  1.00 42.90           N  
ATOM    989  CA  LEU A 125      29.704  11.375  11.834  1.00 43.43           C  
ATOM    990  C   LEU A 125      28.282  11.895  11.884  1.00 44.01           C  
ATOM    991  O   LEU A 125      27.410  11.354  11.224  1.00 43.89           O  
ATOM    992  CB  LEU A 125      30.019  10.654  13.155  1.00 42.76           C  
ATOM    993  CG  LEU A 125      29.030   9.604  13.678  1.00 42.89           C  
ATOM    994  CD1 LEU A 125      28.914   8.466  12.670  1.00 41.68           C  
ATOM    995  CD2 LEU A 125      29.477   9.092  15.057  1.00 42.53           C  
ATOM    996  N   TRP A 126      28.041  12.940  12.660  1.00 44.80           N  
ATOM    997  CA  TRP A 126      26.703  13.453  12.753  1.00 45.81           C  
ATOM    998  C   TRP A 126      26.290  14.130  11.481  1.00 46.70           C  
ATOM    999  O   TRP A 126      25.110  14.088  11.143  1.00 47.31           O  
ATOM   1000  CB  TRP A 126      26.592  14.387  13.941  1.00 46.55           C  
ATOM   1001  CG  TRP A 126      26.599  13.630  15.210  1.00 47.46           C  
ATOM   1002  CD1 TRP A 126      27.573  13.622  16.159  1.00 48.65           C  
ATOM   1003  CD2 TRP A 126      25.596  12.721  15.658  1.00 48.52           C  
ATOM   1004  NE1 TRP A 126      27.244  12.762  17.176  1.00 48.83           N  
ATOM   1005  CE2 TRP A 126      26.032  12.194  16.892  1.00 48.85           C  
ATOM   1006  CE3 TRP A 126      24.370  12.297  15.135  1.00 48.91           C  
ATOM   1007  CZ2 TRP A 126      25.285  11.263  17.613  1.00 48.99           C  
ATOM   1008  CZ3 TRP A 126      23.628  11.375  15.850  1.00 49.22           C  
ATOM   1009  CH2 TRP A 126      24.089  10.867  17.078  1.00 49.45           C  
ATOM   1010  N   SER A 127      27.223  14.749  10.767  1.00 47.12           N  
ATOM   1011  CA  SER A 127      26.855  15.402   9.517  1.00 47.34           C  
ATOM   1012  C   SER A 127      26.419  14.344   8.515  1.00 48.12           C  
ATOM   1013  O   SER A 127      25.696  14.666   7.577  1.00 49.19           O  
ATOM   1014  CB  SER A 127      28.020  16.218   8.954  1.00 47.10           C  
ATOM   1015  OG  SER A 127      28.178  17.438   9.655  1.00 48.59           O  
ATOM   1016  N   LEU A 128      26.842  13.095   8.717  1.00 48.32           N  
ATOM   1017  CA  LEU A 128      26.466  11.988   7.825  1.00 49.32           C  
ATOM   1018  C   LEU A 128      25.049  11.524   8.102  1.00 50.35           C  
ATOM   1019  O   LEU A 128      24.365  11.079   7.187  1.00 51.17           O  
ATOM   1020  CB  LEU A 128      27.412  10.803   7.991  1.00 48.11           C  
ATOM   1021  CG  LEU A 128      28.738  10.996   7.270  1.00 48.21           C  
ATOM   1022  CD1 LEU A 128      29.651   9.812   7.537  1.00 48.03           C  
ATOM   1023  CD2 LEU A 128      28.465  11.159   5.775  1.00 48.66           C  
ATOM   1024  N   VAL A 129      24.618  11.600   9.359  1.00 51.25           N  
ATOM   1025  CA  VAL A 129      23.264  11.197   9.709  1.00 51.63           C  
ATOM   1026  C   VAL A 129      22.305  12.220   9.100  1.00 52.12           C  
ATOM   1027  O   VAL A 129      21.247  11.831   8.564  1.00 52.57           O  
ATOM   1028  CB  VAL A 129      23.074  11.126  11.249  1.00 51.51           C  
ATOM   1029  CG1 VAL A 129      21.662  10.683  11.568  1.00 51.58           C  
ATOM   1030  CG2 VAL A 129      24.064  10.153  11.860  1.00 50.68           C  
ATOM   1031  N   VAL A 130      22.679  13.504   9.166  1.00 51.71           N  
ATOM   1032  CA  VAL A 130      21.869  14.585   8.602  1.00 51.70           C  
ATOM   1033  C   VAL A 130      21.708  14.342   7.099  1.00 52.97           C  
ATOM   1034  O   VAL A 130      20.589  14.379   6.573  1.00 54.22           O  
ATOM   1035  CB  VAL A 130      22.531  15.967   8.850  1.00 50.24           C  
ATOM   1036  CG1 VAL A 130      21.680  17.080   8.282  1.00 49.12           C  
ATOM   1037  CG2 VAL A 130      22.725  16.172  10.335  1.00 49.81           C  
ATOM   1038  N   LEU A 131      22.815  14.076   6.413  1.00 53.22           N  
ATOM   1039  CA  LEU A 131      22.770  13.806   4.983  1.00 53.52           C  
ATOM   1040  C   LEU A 131      21.883  12.582   4.723  1.00 54.15           C  
ATOM   1041  O   LEU A 131      21.042  12.617   3.826  1.00 54.96           O  
ATOM   1042  CB  LEU A 131      24.200  13.588   4.455  1.00 52.76           C  
ATOM   1043  CG  LEU A 131      25.024  14.818   4.033  1.00 51.84           C  
ATOM   1044  CD1 LEU A 131      24.694  16.021   4.877  1.00 51.68           C  
ATOM   1045  CD2 LEU A 131      26.496  14.493   4.142  1.00 51.30           C  
ATOM   1046  N   ALA A 132      22.059  11.518   5.505  1.00 54.47           N  
ATOM   1047  CA  ALA A 132      21.253  10.309   5.345  1.00 54.88           C  
ATOM   1048  C   ALA A 132      19.795  10.701   5.339  1.00 55.06           C  
ATOM   1049  O   ALA A 132      19.041  10.240   4.499  1.00 54.84           O  
ATOM   1050  CB  ALA A 132      21.530   9.334   6.487  1.00 54.87           C  
ATOM   1051  N   ILE A 133      19.405  11.555   6.274  1.00 55.24           N  
ATOM   1052  CA  ILE A 133      18.033  12.012   6.355  1.00 55.79           C  
ATOM   1053  C   ILE A 133      17.693  12.818   5.133  1.00 56.60           C  
ATOM   1054  O   ILE A 133      16.884  12.388   4.324  1.00 56.57           O  
ATOM   1055  CB  ILE A 133      17.824  12.883   7.585  1.00 56.14           C  
ATOM   1056  CG1 ILE A 133      18.160  12.072   8.835  1.00 57.05           C  
ATOM   1057  CG2 ILE A 133      16.412  13.426   7.609  1.00 54.70           C  
ATOM   1058  CD1 ILE A 133      17.660  10.630   8.792  1.00 57.28           C  
ATOM   1059  N   GLU A 134      18.304  13.987   4.999  1.00 57.41           N  
ATOM   1060  CA  GLU A 134      18.049  14.837   3.853  1.00 58.66           C  
ATOM   1061  C   GLU A 134      18.027  13.981   2.618  1.00 59.20           C  
ATOM   1062  O   GLU A 134      17.140  14.106   1.787  1.00 59.53           O  
ATOM   1063  CB  GLU A 134      19.144  15.895   3.730  1.00 59.30           C  
ATOM   1064  CG  GLU A 134      18.834  16.994   2.714  1.00 62.04           C  
ATOM   1065  CD  GLU A 134      19.454  16.766   1.331  1.00 63.45           C  
ATOM   1066  OE1 GLU A 134      19.438  15.613   0.837  1.00 63.77           O  
ATOM   1067  OE2 GLU A 134      19.943  17.762   0.736  1.00 64.67           O  
ATOM   1068  N   ARG A 135      18.999  13.092   2.504  1.00 59.85           N  
ATOM   1069  CA  ARG A 135      19.080  12.224   1.347  1.00 60.99           C  
ATOM   1070  C   ARG A 135      17.793  11.452   1.208  1.00 62.72           C  
ATOM   1071  O   ARG A 135      17.230  11.334   0.125  1.00 63.13           O  
ATOM   1072  CB  ARG A 135      20.240  11.255   1.501  1.00 58.99           C  
ATOM   1073  CG  ARG A 135      20.580  10.566   0.220  1.00 58.39           C  
ATOM   1074  CD  ARG A 135      21.352  11.498  -0.715  1.00 57.44           C  
ATOM   1075  NE  ARG A 135      20.828  12.865  -0.770  1.00 55.17           N  
ATOM   1076  CZ  ARG A 135      20.351  13.447  -1.869  1.00 53.72           C  
ATOM   1077  NH1 ARG A 135      20.314  12.786  -3.023  1.00 52.34           N  
ATOM   1078  NH2 ARG A 135      19.929  14.701  -1.819  1.00 52.27           N  
ATOM   1079  N   TYR A 136      17.327  10.926   2.326  1.00 64.96           N  
ATOM   1080  CA  TYR A 136      16.115  10.147   2.359  1.00 66.71           C  
ATOM   1081  C   TYR A 136      14.938  11.005   1.993  1.00 68.26           C  
ATOM   1082  O   TYR A 136      14.220  10.699   1.059  1.00 69.18           O  
ATOM   1083  CB  TYR A 136      15.909   9.599   3.752  1.00 66.83           C  
ATOM   1084  CG  TYR A 136      14.685   8.763   3.837  1.00 68.42           C  
ATOM   1085  CD1 TYR A 136      14.676   7.473   3.309  1.00 69.21           C  
ATOM   1086  CD2 TYR A 136      13.512   9.268   4.393  1.00 68.82           C  
ATOM   1087  CE1 TYR A 136      13.532   6.702   3.327  1.00 69.37           C  
ATOM   1088  CE2 TYR A 136      12.357   8.512   4.415  1.00 69.00           C  
ATOM   1089  CZ  TYR A 136      12.377   7.225   3.878  1.00 69.81           C  
ATOM   1090  OH  TYR A 136      11.250   6.447   3.875  1.00 70.95           O  
ATOM   1091  N   VAL A 137      14.740  12.083   2.737  1.00 69.45           N  
ATOM   1092  CA  VAL A 137      13.622  12.979   2.503  1.00 70.90           C  
ATOM   1093  C   VAL A 137      13.493  13.369   1.049  1.00 73.16           C  
ATOM   1094  O   VAL A 137      12.384  13.562   0.586  1.00 74.16           O  
ATOM   1095  CB  VAL A 137      13.742  14.250   3.363  1.00 69.96           C  
ATOM   1096  CG1 VAL A 137      12.711  15.271   2.956  1.00 69.37           C  
ATOM   1097  CG2 VAL A 137      13.538  13.896   4.799  1.00 69.73           C  
ATOM   1098  N   VAL A 138      14.588  13.490   0.312  1.00 75.27           N  
ATOM   1099  CA  VAL A 138      14.447  13.889  -1.083  1.00 77.20           C  
ATOM   1100  C   VAL A 138      14.168  12.695  -1.956  1.00 79.20           C  
ATOM   1101  O   VAL A 138      13.284  12.769  -2.800  1.00 79.37           O  
ATOM   1102  CB  VAL A 138      15.698  14.610  -1.604  1.00 77.01           C  
ATOM   1103  CG1 VAL A 138      15.964  15.854  -0.772  1.00 76.74           C  
ATOM   1104  CG2 VAL A 138      16.888  13.673  -1.561  1.00 77.70           C  
ATOM   1105  N   VAL A 139      14.898  11.600  -1.757  1.00 81.49           N  
ATOM   1106  CA  VAL A 139      14.707  10.400  -2.568  1.00 84.18           C  
ATOM   1107  C   VAL A 139      13.369   9.757  -2.271  1.00 86.47           C  
ATOM   1108  O   VAL A 139      12.459   9.863  -3.085  1.00 87.02           O  
ATOM   1109  CB  VAL A 139      15.839   9.378  -2.339  1.00 83.83           C  
ATOM   1110  CG1 VAL A 139      15.461   8.036  -2.925  1.00 83.60           C  
ATOM   1111  CG2 VAL A 139      17.112   9.882  -2.990  1.00 84.02           C  
ATOM   1112  N   CYS A 140      13.233   9.102  -1.123  1.00 88.94           N  
ATOM   1113  CA  CYS A 140      11.970   8.459  -0.776  1.00 91.40           C  
ATOM   1114  C   CYS A 140      10.884   9.504  -0.448  1.00 93.23           C  
ATOM   1115  O   CYS A 140       9.773   9.141  -0.060  1.00 93.73           O  
ATOM   1116  CB  CYS A 140      12.198   7.492   0.391  1.00 90.82           C  
ATOM   1117  SG  CYS A 140      13.338   6.132  -0.026  1.00 91.94           S  
ATOM   1118  N   LYS A 141      11.217  10.783  -0.639  1.00 95.25           N  
ATOM   1119  CA  LYS A 141      10.338  11.948  -0.408  1.00 96.99           C  
ATOM   1120  C   LYS A 141       9.090  11.656   0.453  1.00 98.08           C  
ATOM   1121  O   LYS A 141       8.046  11.291  -0.096  1.00 98.17           O  
ATOM   1122  CB  LYS A 141       9.917  12.551  -1.760  1.00 96.84           C  
ATOM   1123  CG  LYS A 141       9.454  13.998  -1.680  1.00 97.21           C  
ATOM   1124  CD  LYS A 141       9.399  14.627  -3.055  1.00 97.48           C  
ATOM   1125  CE  LYS A 141       9.160  16.122  -2.961  1.00 97.51           C  
ATOM   1126  NZ  LYS A 141       9.227  16.777  -4.300  1.00 96.91           N  
ATOM   1127  N   PRO A 142       9.183  11.838   1.798  1.00 99.12           N  
ATOM   1128  CA  PRO A 142       8.106  11.619   2.785  1.00 99.61           C  
ATOM   1129  C   PRO A 142       6.910  12.563   2.672  1.00 99.88           C  
ATOM   1130  O   PRO A 142       5.779  12.140   2.923  1.00 99.96           O  
ATOM   1131  CB  PRO A 142       8.826  11.778   4.127  1.00 99.56           C  
ATOM   1132  CG  PRO A 142      10.216  11.326   3.823  1.00 99.42           C  
ATOM   1133  CD  PRO A 142      10.473  12.010   2.495  1.00 99.46           C  
ATOM   1134  N   MET A 143       7.156  13.827   2.331  1.00100.05           N  
ATOM   1135  CA  MET A 143       6.079  14.805   2.170  1.00100.41           C  
ATOM   1136  C   MET A 143       5.697  14.887   0.718  1.00100.84           C  
ATOM   1137  O   MET A 143       6.450  14.442  -0.150  1.00101.42           O  
ATOM   1138  CB  MET A 143       6.510  16.196   2.636  1.00100.50           C  
ATOM   1139  CG  MET A 143       6.479  16.399   4.132  1.00100.69           C  
ATOM   1140  SD  MET A 143       7.517  15.222   4.983  1.00101.42           S  
ATOM   1141  CE  MET A 143       6.259  14.100   5.656  1.00101.89           C  
ATOM   1142  N   SER A 144       4.534  15.462   0.447  1.00100.97           N  
ATOM   1143  CA  SER A 144       4.069  15.587  -0.922  1.00101.22           C  
ATOM   1144  C   SER A 144       4.270  17.008  -1.397  1.00101.04           C  
ATOM   1145  O   SER A 144       3.679  17.408  -2.405  1.00101.49           O  
ATOM   1146  CB  SER A 144       2.591  15.190  -1.013  1.00101.40           C  
ATOM   1147  OG  SER A 144       2.413  13.816  -0.689  1.00101.49           O  
ATOM   1148  N   ASN A 145       5.112  17.761  -0.693  1.00100.70           N  
ATOM   1149  CA  ASN A 145       5.369  19.151  -1.060  1.00100.38           C  
ATOM   1150  C   ASN A 145       6.400  19.775  -0.136  1.00 99.21           C  
ATOM   1151  O   ASN A 145       6.288  20.967   0.175  1.00 99.38           O  
ATOM   1152  CB  ASN A 145       4.062  19.954  -0.981  1.00101.29           C  
ATOM   1153  CG  ASN A 145       3.403  19.856   0.390  1.00102.01           C  
ATOM   1154  OD1 ASN A 145       3.073  18.758   0.861  1.00102.48           O  
ATOM   1155  ND2 ASN A 145       3.213  21.003   1.040  1.00102.69           N  
ATOM   1156  N   PHE A 146       7.404  19.004   0.288  1.00 97.81           N  
ATOM   1157  CA  PHE A 146       8.420  19.536   1.197  1.00 96.14           C  
ATOM   1158  C   PHE A 146       9.783  19.747   0.532  1.00 94.78           C  
ATOM   1159  O   PHE A 146      10.156  19.021  -0.401  1.00 94.72           O  
ATOM   1160  CB  PHE A 146       8.599  18.618   2.404  1.00 95.57           C  
ATOM   1161  CG  PHE A 146       9.640  19.102   3.374  1.00 95.18           C  
ATOM   1162  CD1 PHE A 146       9.388  20.199   4.197  1.00 94.82           C  
ATOM   1163  CD2 PHE A 146      10.892  18.488   3.437  1.00 94.73           C  
ATOM   1164  CE1 PHE A 146      10.369  20.676   5.069  1.00 94.61           C  
ATOM   1165  CE2 PHE A 146      11.879  18.958   4.302  1.00 94.46           C  
ATOM   1166  CZ  PHE A 146      11.616  20.053   5.120  1.00 94.59           C  
ATOM   1167  N   ARG A 147      10.523  20.733   1.054  1.00 93.40           N  
ATOM   1168  CA  ARG A 147      11.858  21.103   0.570  1.00 91.65           C  
ATOM   1169  C   ARG A 147      12.668  21.744   1.705  1.00 89.75           C  
ATOM   1170  O   ARG A 147      12.159  22.633   2.415  1.00 89.82           O  
ATOM   1171  CB  ARG A 147      11.741  22.102  -0.585  1.00 92.44           C  
ATOM   1172  CG  ARG A 147      13.067  22.497  -1.224  1.00 93.48           C  
ATOM   1173  CD  ARG A 147      12.894  23.730  -2.112  1.00 94.08           C  
ATOM   1174  NE  ARG A 147      12.633  24.944  -1.335  1.00 94.29           N  
ATOM   1175  CZ  ARG A 147      12.365  26.144  -1.858  1.00 94.74           C  
ATOM   1176  NH1 ARG A 147      12.314  26.312  -3.177  1.00 95.15           N  
ATOM   1177  NH2 ARG A 147      12.157  27.188  -1.059  1.00 95.10           N  
ATOM   1178  N   PHE A 148      13.918  21.305   1.859  1.00 87.00           N  
ATOM   1179  CA  PHE A 148      14.805  21.820   2.896  1.00 84.02           C  
ATOM   1180  C   PHE A 148      15.227  23.241   2.602  1.00 82.72           C  
ATOM   1181  O   PHE A 148      15.880  23.485   1.595  1.00 82.75           O  
ATOM   1182  CB  PHE A 148      16.050  20.945   3.000  1.00 82.66           C  
ATOM   1183  CG  PHE A 148      15.789  19.603   3.589  1.00 81.45           C  
ATOM   1184  CD1 PHE A 148      15.522  19.472   4.941  1.00 80.94           C  
ATOM   1185  CD2 PHE A 148      15.786  18.468   2.793  1.00 81.08           C  
ATOM   1186  CE1 PHE A 148      15.252  18.229   5.491  1.00 80.55           C  
ATOM   1187  CE2 PHE A 148      15.517  17.218   3.338  1.00 80.54           C  
ATOM   1188  CZ  PHE A 148      15.249  17.100   4.686  1.00 80.39           C  
ATOM   1189  N   GLY A 149      14.850  24.177   3.466  1.00 81.06           N  
ATOM   1190  CA  GLY A 149      15.264  25.550   3.266  1.00 79.46           C  
ATOM   1191  C   GLY A 149      16.660  25.675   3.851  1.00 78.41           C  
ATOM   1192  O   GLY A 149      17.214  24.699   4.361  1.00 78.17           O  
ATOM   1193  N   GLU A 150      17.245  26.863   3.777  1.00 77.39           N  
ATOM   1194  CA  GLU A 150      18.574  27.074   4.328  1.00 76.58           C  
ATOM   1195  C   GLU A 150      18.506  26.996   5.828  1.00 76.22           C  
ATOM   1196  O   GLU A 150      19.483  26.681   6.503  1.00 75.79           O  
ATOM   1197  CB  GLU A 150      19.101  28.426   3.878  1.00 76.16           C  
ATOM   1198  CG  GLU A 150      19.810  28.329   2.553  1.00 77.26           C  
ATOM   1199  CD  GLU A 150      19.896  29.647   1.844  1.00 77.98           C  
ATOM   1200  OE1 GLU A 150      20.184  30.670   2.500  1.00 78.02           O  
ATOM   1201  OE2 GLU A 150      19.680  29.652   0.616  1.00 78.87           O  
ATOM   1202  N   ASN A 151      17.328  27.283   6.347  1.00 75.89           N  
ATOM   1203  CA  ASN A 151      17.094  27.227   7.770  1.00 75.16           C  
ATOM   1204  C   ASN A 151      17.369  25.808   8.240  1.00 74.38           C  
ATOM   1205  O   ASN A 151      18.169  25.611   9.156  1.00 74.46           O  
ATOM   1206  CB  ASN A 151      15.647  27.658   8.050  1.00 75.35           C  
ATOM   1207  CG  ASN A 151      14.642  27.002   7.103  1.00 76.63           C  
ATOM   1208  OD1 ASN A 151      14.849  26.943   5.886  1.00 76.88           O  
ATOM   1209  ND2 ASN A 151      13.535  26.521   7.663  1.00 77.13           N  
ATOM   1210  N   HIS A 152      16.736  24.831   7.595  1.00 73.12           N  
ATOM   1211  CA  HIS A 152      16.915  23.420   7.940  1.00 71.68           C  
ATOM   1212  C   HIS A 152      18.384  23.089   7.922  1.00 70.22           C  
ATOM   1213  O   HIS A 152      18.886  22.516   8.875  1.00 70.27           O  
ATOM   1214  CB  HIS A 152      16.183  22.521   6.936  1.00 72.39           C  
ATOM   1215  CG  HIS A 152      14.735  22.867   6.753  1.00 73.57           C  
ATOM   1216  ND1 HIS A 152      13.981  22.392   5.699  1.00 74.39           N  
ATOM   1217  CD2 HIS A 152      13.908  23.661   7.477  1.00 73.66           C  
ATOM   1218  CE1 HIS A 152      12.755  22.883   5.779  1.00 74.26           C  
ATOM   1219  NE2 HIS A 152      12.685  23.656   6.849  1.00 73.63           N  
ATOM   1220  N   ALA A 153      19.069  23.452   6.843  1.00 67.95           N  
ATOM   1221  CA  ALA A 153      20.493  23.187   6.718  1.00 65.40           C  
ATOM   1222  C   ALA A 153      21.223  23.716   7.934  1.00 63.87           C  
ATOM   1223  O   ALA A 153      22.113  23.061   8.474  1.00 63.31           O  
ATOM   1224  CB  ALA A 153      21.022  23.839   5.462  1.00 65.67           C  
ATOM   1225  N   ILE A 154      20.842  24.902   8.368  1.00 62.32           N  
ATOM   1226  CA  ILE A 154      21.464  25.505   9.521  1.00 61.08           C  
ATOM   1227  C   ILE A 154      21.033  24.755  10.761  1.00 61.03           C  
ATOM   1228  O   ILE A 154      21.677  24.812  11.791  1.00 60.59           O  
ATOM   1229  CB  ILE A 154      21.075  26.969   9.586  1.00 60.18           C  
ATOM   1230  CG1 ILE A 154      21.396  27.614   8.242  1.00 59.07           C  
ATOM   1231  CG2 ILE A 154      21.847  27.661  10.670  1.00 59.33           C  
ATOM   1232  CD1 ILE A 154      20.961  29.022   8.114  1.00 58.93           C  
ATOM   1233  N   MET A 155      19.935  24.032  10.652  1.00 61.38           N  
ATOM   1234  CA  MET A 155      19.456  23.248  11.771  1.00 62.15           C  
ATOM   1235  C   MET A 155      20.309  22.042  11.889  1.00 60.64           C  
ATOM   1236  O   MET A 155      20.801  21.744  12.961  1.00 60.98           O  
ATOM   1237  CB  MET A 155      18.011  22.818  11.546  1.00 65.38           C  
ATOM   1238  CG  MET A 155      17.064  23.980  11.540  1.00 70.33           C  
ATOM   1239  SD  MET A 155      17.322  24.921  13.062  1.00 77.54           S  
ATOM   1240  CE  MET A 155      18.672  26.152  12.569  1.00 75.92           C  
ATOM   1241  N   GLY A 156      20.474  21.343  10.776  1.00 58.70           N  
ATOM   1242  CA  GLY A 156      21.287  20.154  10.771  1.00 56.37           C  
ATOM   1243  C   GLY A 156      22.675  20.530  11.221  1.00 55.30           C  
ATOM   1244  O   GLY A 156      23.258  19.860  12.065  1.00 55.43           O  
ATOM   1245  N   VAL A 157      23.202  21.621  10.682  1.00 53.65           N  
ATOM   1246  CA  VAL A 157      24.540  22.029  11.061  1.00 51.87           C  
ATOM   1247  C   VAL A 157      24.626  22.297  12.537  1.00 51.60           C  
ATOM   1248  O   VAL A 157      25.591  21.899  13.165  1.00 51.75           O  
ATOM   1249  CB  VAL A 157      24.988  23.262  10.291  1.00 51.25           C  
ATOM   1250  CG1 VAL A 157      26.203  23.881  10.962  1.00 49.29           C  
ATOM   1251  CG2 VAL A 157      25.320  22.861   8.867  1.00 50.26           C  
ATOM   1252  N   ALA A 158      23.628  22.962  13.096  1.00 51.63           N  
ATOM   1253  CA  ALA A 158      23.628  23.267  14.526  1.00 51.00           C  
ATOM   1254  C   ALA A 158      23.559  21.974  15.325  1.00 50.68           C  
ATOM   1255  O   ALA A 158      24.129  21.864  16.406  1.00 50.15           O  
ATOM   1256  CB  ALA A 158      22.431  24.150  14.858  1.00 50.64           C  
ATOM   1257  N   PHE A 159      22.855  21.000  14.772  1.00 50.67           N  
ATOM   1258  CA  PHE A 159      22.656  19.711  15.406  1.00 51.09           C  
ATOM   1259  C   PHE A 159      23.954  18.937  15.488  1.00 51.73           C  
ATOM   1260  O   PHE A 159      24.227  18.290  16.505  1.00 52.69           O  
ATOM   1261  CB  PHE A 159      21.611  18.930  14.602  1.00 50.41           C  
ATOM   1262  CG  PHE A 159      21.635  17.445  14.832  1.00 49.87           C  
ATOM   1263  CD1 PHE A 159      21.179  16.898  16.018  1.00 50.33           C  
ATOM   1264  CD2 PHE A 159      22.106  16.588  13.846  1.00 50.31           C  
ATOM   1265  CE1 PHE A 159      21.189  15.515  16.218  1.00 50.73           C  
ATOM   1266  CE2 PHE A 159      22.119  15.206  14.038  1.00 49.91           C  
ATOM   1267  CZ  PHE A 159      21.659  14.672  15.226  1.00 50.32           C  
ATOM   1268  N   THR A 160      24.752  18.990  14.430  1.00 51.95           N  
ATOM   1269  CA  THR A 160      26.001  18.252  14.420  1.00 51.81           C  
ATOM   1270  C   THR A 160      26.926  18.764  15.504  1.00 51.94           C  
ATOM   1271  O   THR A 160      27.655  17.963  16.086  1.00 52.70           O  
ATOM   1272  CB  THR A 160      26.708  18.343  13.052  1.00 52.08           C  
ATOM   1273  OG1 THR A 160      27.057  19.704  12.777  1.00 52.82           O  
ATOM   1274  CG2 THR A 160      25.810  17.821  11.955  1.00 51.87           C  
ATOM   1275  N   TRP A 161      26.898  20.068  15.790  1.00 51.07           N  
ATOM   1276  CA  TRP A 161      27.763  20.645  16.824  1.00 49.93           C  
ATOM   1277  C   TRP A 161      27.278  20.353  18.221  1.00 50.63           C  
ATOM   1278  O   TRP A 161      28.080  20.335  19.149  1.00 51.33           O  
ATOM   1279  CB  TRP A 161      27.866  22.144  16.679  1.00 47.98           C  
ATOM   1280  CG  TRP A 161      28.771  22.538  15.627  1.00 46.06           C  
ATOM   1281  CD1 TRP A 161      28.479  22.671  14.301  1.00 45.75           C  
ATOM   1282  CD2 TRP A 161      30.154  22.860  15.778  1.00 45.35           C  
ATOM   1283  NE1 TRP A 161      29.602  23.066  13.613  1.00 45.76           N  
ATOM   1284  CE2 TRP A 161      30.647  23.189  14.495  1.00 45.47           C  
ATOM   1285  CE3 TRP A 161      31.029  22.902  16.872  1.00 44.44           C  
ATOM   1286  CZ2 TRP A 161      31.988  23.563  14.274  1.00 44.87           C  
ATOM   1287  CZ3 TRP A 161      32.364  23.275  16.654  1.00 44.19           C  
ATOM   1288  CH2 TRP A 161      32.827  23.601  15.360  1.00 44.21           C  
ATOM   1289  N   VAL A 162      25.979  20.166  18.402  1.00 50.34           N  
ATOM   1290  CA  VAL A 162      25.492  19.853  19.726  1.00 49.67           C  
ATOM   1291  C   VAL A 162      25.884  18.429  20.015  1.00 50.07           C  
ATOM   1292  O   VAL A 162      26.432  18.137  21.073  1.00 49.94           O  
ATOM   1293  CB  VAL A 162      23.982  19.988  19.786  1.00 49.30           C  
ATOM   1294  CG1 VAL A 162      23.489  19.628  21.155  1.00 48.29           C  
ATOM   1295  CG2 VAL A 162      23.592  21.404  19.422  1.00 49.06           C  
ATOM   1296  N   MET A 163      25.637  17.551  19.049  1.00 49.90           N  
ATOM   1297  CA  MET A 163      25.950  16.138  19.205  1.00 50.69           C  
ATOM   1298  C   MET A 163      27.428  15.904  19.382  1.00 50.67           C  
ATOM   1299  O   MET A 163      27.811  15.115  20.232  1.00 51.31           O  
ATOM   1300  CB  MET A 163      25.460  15.351  17.995  1.00 51.15           C  
ATOM   1301  CG  MET A 163      23.969  15.433  17.789  1.00 53.03           C  
ATOM   1302  SD  MET A 163      23.114  15.106  19.346  1.00 54.85           S  
ATOM   1303  CE  MET A 163      23.521  13.367  19.596  1.00 54.03           C  
ATOM   1304  N   ALA A 164      28.248  16.583  18.587  1.00 50.10           N  
ATOM   1305  CA  ALA A 164      29.692  16.415  18.646  1.00 49.70           C  
ATOM   1306  C   ALA A 164      30.241  16.946  19.940  1.00 49.68           C  
ATOM   1307  O   ALA A 164      31.168  16.350  20.496  1.00 49.84           O  
ATOM   1308  CB  ALA A 164      30.339  17.122  17.478  1.00 49.80           C  
ATOM   1309  N   LEU A 165      29.694  18.064  20.412  1.00 49.26           N  
ATOM   1310  CA  LEU A 165      30.136  18.676  21.668  1.00 48.67           C  
ATOM   1311  C   LEU A 165      29.749  17.765  22.823  1.00 48.90           C  
ATOM   1312  O   LEU A 165      30.493  17.645  23.806  1.00 49.30           O  
ATOM   1313  CB  LEU A 165      29.475  20.054  21.867  1.00 48.34           C  
ATOM   1314  CG  LEU A 165      30.150  21.363  21.437  1.00 46.62           C  
ATOM   1315  CD1 LEU A 165      31.448  21.542  22.180  1.00 47.34           C  
ATOM   1316  CD2 LEU A 165      30.410  21.358  19.975  1.00 47.54           C  
ATOM   1317  N   ALA A 166      28.587  17.131  22.696  1.00 48.39           N  
ATOM   1318  CA  ALA A 166      28.072  16.231  23.716  1.00 48.49           C  
ATOM   1319  C   ALA A 166      29.048  15.103  23.951  1.00 48.71           C  
ATOM   1320  O   ALA A 166      29.078  14.491  25.009  1.00 49.40           O  
ATOM   1321  CB  ALA A 166      26.734  15.670  23.267  1.00 48.51           C  
ATOM   1322  N   CYS A 167      29.869  14.832  22.961  1.00 48.58           N  
ATOM   1323  CA  CYS A 167      30.798  13.745  23.079  1.00 48.67           C  
ATOM   1324  C   CYS A 167      32.197  14.249  23.365  1.00 47.54           C  
ATOM   1325  O   CYS A 167      32.901  13.674  24.187  1.00 48.01           O  
ATOM   1326  CB  CYS A 167      30.758  12.958  21.773  1.00 50.36           C  
ATOM   1327  SG  CYS A 167      31.891  11.577  21.692  1.00 57.46           S  
ATOM   1328  N   ALA A 168      32.589  15.341  22.728  1.00 45.83           N  
ATOM   1329  CA  ALA A 168      33.949  15.838  22.878  1.00 44.72           C  
ATOM   1330  C   ALA A 168      34.193  16.692  24.106  1.00 43.65           C  
ATOM   1331  O   ALA A 168      35.280  16.618  24.685  1.00 42.95           O  
ATOM   1332  CB  ALA A 168      34.348  16.603  21.612  1.00 44.62           C  
ATOM   1333  N   ALA A 169      33.218  17.488  24.515  1.00 42.87           N  
ATOM   1334  CA  ALA A 169      33.419  18.382  25.646  1.00 42.10           C  
ATOM   1335  C   ALA A 169      33.424  17.693  27.039  1.00 41.82           C  
ATOM   1336  O   ALA A 169      34.183  18.121  27.931  1.00 41.90           O  
ATOM   1337  CB  ALA A 169      32.379  19.490  25.591  1.00 42.54           C  
ATOM   1338  N   PRO A 170      32.608  16.640  27.251  1.00 41.12           N  
ATOM   1339  CA  PRO A 170      32.605  15.991  28.569  1.00 39.82           C  
ATOM   1340  C   PRO A 170      33.964  15.691  29.159  1.00 40.31           C  
ATOM   1341  O   PRO A 170      34.200  15.999  30.303  1.00 41.21           O  
ATOM   1342  CB  PRO A 170      31.797  14.721  28.336  1.00 40.50           C  
ATOM   1343  CG  PRO A 170      30.870  15.102  27.234  1.00 40.56           C  
ATOM   1344  CD  PRO A 170      31.735  15.921  26.307  1.00 41.38           C  
ATOM   1345  N   PRO A 171      34.875  15.077  28.393  1.00 40.95           N  
ATOM   1346  CA  PRO A 171      36.227  14.744  28.884  1.00 41.03           C  
ATOM   1347  C   PRO A 171      37.085  15.909  29.411  1.00 41.77           C  
ATOM   1348  O   PRO A 171      38.118  15.684  30.074  1.00 41.77           O  
ATOM   1349  CB  PRO A 171      36.868  14.056  27.676  1.00 41.01           C  
ATOM   1350  CG  PRO A 171      35.684  13.389  26.997  1.00 40.91           C  
ATOM   1351  CD  PRO A 171      34.636  14.475  27.065  1.00 40.85           C  
ATOM   1352  N   LEU A 172      36.662  17.136  29.119  1.00 41.95           N  
ATOM   1353  CA  LEU A 172      37.382  18.342  29.549  1.00 41.73           C  
ATOM   1354  C   LEU A 172      36.850  18.819  30.889  1.00 42.15           C  
ATOM   1355  O   LEU A 172      37.453  19.715  31.512  1.00 42.03           O  
ATOM   1356  CB  LEU A 172      37.164  19.470  28.543  1.00 39.83           C  
ATOM   1357  CG  LEU A 172      37.552  19.222  27.102  1.00 38.70           C  
ATOM   1358  CD1 LEU A 172      37.045  20.367  26.264  1.00 37.69           C  
ATOM   1359  CD2 LEU A 172      39.041  19.077  26.993  1.00 36.98           C  
ATOM   1360  N   VAL A 173      35.746  18.219  31.337  1.00 42.45           N  
ATOM   1361  CA  VAL A 173      35.089  18.649  32.573  1.00 42.52           C  
ATOM   1362  C   VAL A 173      34.743  17.517  33.555  1.00 43.16           C  
ATOM   1363  O   VAL A 173      33.668  17.567  34.176  1.00 43.48           O  
ATOM   1364  CB  VAL A 173      33.807  19.434  32.211  1.00 41.55           C  
ATOM   1365  CG1 VAL A 173      34.182  20.614  31.359  1.00 39.95           C  
ATOM   1366  CG2 VAL A 173      32.823  18.536  31.452  1.00 39.88           C  
ATOM   1367  N   GLY A 174      35.602  16.508  33.693  1.00 43.12           N  
ATOM   1368  CA  GLY A 174      35.317  15.464  34.661  1.00 42.21           C  
ATOM   1369  C   GLY A 174      34.663  14.163  34.257  1.00 42.40           C  
ATOM   1370  O   GLY A 174      34.508  13.280  35.113  1.00 43.45           O  
ATOM   1371  N   TRP A 175      34.237  14.023  33.008  1.00 41.81           N  
ATOM   1372  CA  TRP A 175      33.659  12.754  32.604  1.00 41.74           C  
ATOM   1373  C   TRP A 175      34.600  12.145  31.618  1.00 42.81           C  
ATOM   1374  O   TRP A 175      34.651  12.595  30.477  1.00 44.24           O  
ATOM   1375  CB  TRP A 175      32.287  12.910  31.975  1.00 40.47           C  
ATOM   1376  CG  TRP A 175      31.582  11.586  31.932  1.00 39.79           C  
ATOM   1377  CD1 TRP A 175      31.874  10.486  32.688  1.00 40.04           C  
ATOM   1378  CD2 TRP A 175      30.448  11.232  31.132  1.00 39.24           C  
ATOM   1379  NE1 TRP A 175      30.993   9.471  32.410  1.00 39.56           N  
ATOM   1380  CE2 TRP A 175      30.107   9.902  31.460  1.00 39.50           C  
ATOM   1381  CE3 TRP A 175      29.689  11.909  30.171  1.00 38.45           C  
ATOM   1382  CZ2 TRP A 175      29.037   9.235  30.862  1.00 39.21           C  
ATOM   1383  CZ3 TRP A 175      28.632  11.248  29.577  1.00 39.17           C  
ATOM   1384  CH2 TRP A 175      28.313   9.922  29.925  1.00 38.83           C  
ATOM   1385  N   SER A 176      35.311  11.100  32.053  1.00 42.67           N  
ATOM   1386  CA  SER A 176      36.347  10.465  31.255  1.00 41.40           C  
ATOM   1387  C   SER A 176      37.414  11.519  31.147  1.00 41.23           C  
ATOM   1388  O   SER A 176      37.366  12.483  31.914  1.00 41.58           O  
ATOM   1389  CB  SER A 176      35.859  10.079  29.863  1.00 41.73           C  
ATOM   1390  OG  SER A 176      36.951   9.609  29.076  1.00 40.77           O  
ATOM   1391  N   ARG A 177      38.350  11.384  30.216  1.00 40.19           N  
ATOM   1392  CA  ARG A 177      39.414  12.381  30.079  1.00 39.67           C  
ATOM   1393  C   ARG A 177      40.251  12.049  28.864  1.00 39.46           C  
ATOM   1394  O   ARG A 177      40.140  10.938  28.349  1.00 40.15           O  
ATOM   1395  CB  ARG A 177      40.310  12.381  31.329  1.00 38.73           C  
ATOM   1396  CG  ARG A 177      40.951  11.026  31.600  1.00 39.05           C  
ATOM   1397  CD  ARG A 177      41.836  10.996  32.834  1.00 40.05           C  
ATOM   1398  NE  ARG A 177      42.356   9.645  33.055  1.00 40.95           N  
ATOM   1399  CZ  ARG A 177      43.162   9.286  34.057  1.00 42.57           C  
ATOM   1400  NH1 ARG A 177      43.560  10.179  34.963  1.00 43.16           N  
ATOM   1401  NH2 ARG A 177      43.580   8.022  34.154  1.00 41.61           N  
ATOM   1402  N   TYR A 178      41.059  13.002  28.393  1.00 38.66           N  
ATOM   1403  CA  TYR A 178      41.936  12.759  27.251  1.00 37.45           C  
ATOM   1404  C   TYR A 178      43.287  12.313  27.807  1.00 37.58           C  
ATOM   1405  O   TYR A 178      43.781  12.855  28.804  1.00 36.71           O  
ATOM   1406  CB  TYR A 178      42.065  14.015  26.366  1.00 37.70           C  
ATOM   1407  CG  TYR A 178      40.809  14.338  25.570  1.00 36.91           C  
ATOM   1408  CD1 TYR A 178      40.375  13.501  24.541  1.00 36.51           C  
ATOM   1409  CD2 TYR A 178      40.020  15.446  25.894  1.00 37.15           C  
ATOM   1410  CE1 TYR A 178      39.187  13.751  23.859  1.00 36.72           C  
ATOM   1411  CE2 TYR A 178      38.819  15.710  25.215  1.00 36.95           C  
ATOM   1412  CZ  TYR A 178      38.410  14.855  24.202  1.00 36.97           C  
ATOM   1413  OH  TYR A 178      37.214  15.094  23.557  1.00 37.15           O  
ATOM   1414  N   ILE A 179      43.876  11.322  27.155  1.00 37.51           N  
ATOM   1415  CA  ILE A 179      45.117  10.728  27.610  1.00 36.95           C  
ATOM   1416  C   ILE A 179      45.941  10.359  26.375  1.00 37.42           C  
ATOM   1417  O   ILE A 179      45.396   9.942  25.361  1.00 37.79           O  
ATOM   1418  CB  ILE A 179      44.756   9.481  28.483  1.00 36.62           C  
ATOM   1419  CG1 ILE A 179      45.918   9.041  29.356  1.00 37.83           C  
ATOM   1420  CG2 ILE A 179      44.303   8.329  27.600  1.00 36.72           C  
ATOM   1421  CD1 ILE A 179      45.514   7.891  30.327  1.00 38.26           C  
ATOM   1422  N   PRO A 180      47.263  10.535  26.433  1.00 38.16           N  
ATOM   1423  CA  PRO A 180      48.078  10.194  25.260  1.00 38.06           C  
ATOM   1424  C   PRO A 180      48.011   8.711  24.827  1.00 38.53           C  
ATOM   1425  O   PRO A 180      47.844   7.862  25.669  1.00 38.73           O  
ATOM   1426  CB  PRO A 180      49.465  10.674  25.680  1.00 37.57           C  
ATOM   1427  CG  PRO A 180      49.392  10.686  27.212  1.00 37.02           C  
ATOM   1428  CD  PRO A 180      48.056  11.187  27.490  1.00 36.72           C  
ATOM   1429  N   GLU A 181      48.138   8.417  23.528  1.00 39.65           N  
ATOM   1430  CA  GLU A 181      48.053   7.029  23.009  1.00 40.66           C  
ATOM   1431  C   GLU A 181      49.204   6.657  22.044  1.00 40.48           C  
ATOM   1432  O   GLU A 181      49.820   7.538  21.435  1.00 40.85           O  
ATOM   1433  CB  GLU A 181      46.744   6.806  22.239  1.00 42.11           C  
ATOM   1434  CG  GLU A 181      45.458   7.265  22.882  1.00 45.12           C  
ATOM   1435  CD  GLU A 181      44.271   6.967  21.995  1.00 47.26           C  
ATOM   1436  OE1 GLU A 181      43.873   5.794  21.903  1.00 47.86           O  
ATOM   1437  OE2 GLU A 181      43.746   7.899  21.363  1.00 48.43           O  
ATOM   1438  N   GLY A 182      49.441   5.350  21.874  1.00 39.75           N  
ATOM   1439  CA  GLY A 182      50.482   4.889  20.977  1.00 39.66           C  
ATOM   1440  C   GLY A 182      51.850   5.364  21.407  1.00 40.26           C  
ATOM   1441  O   GLY A 182      52.271   5.087  22.520  1.00 40.55           O  
ATOM   1442  N   MET A 183      52.549   6.084  20.533  1.00 40.32           N  
ATOM   1443  CA  MET A 183      53.877   6.600  20.884  1.00 41.48           C  
ATOM   1444  C   MET A 183      53.762   7.802  21.808  1.00 41.05           C  
ATOM   1445  O   MET A 183      54.766   8.469  22.090  1.00 41.23           O  
ATOM   1446  CB  MET A 183      54.665   6.961  19.625  1.00 41.95           C  
ATOM   1447  CG  MET A 183      55.354   5.747  19.014  1.00 42.24           C  
ATOM   1448  SD  MET A 183      55.964   6.014  17.365  1.00 43.88           S  
ATOM   1449  CE  MET A 183      54.817   5.069  16.464  1.00 42.17           C  
ATOM   1450  N   GLN A 184      52.531   8.064  22.252  1.00 40.09           N  
ATOM   1451  CA  GLN A 184      52.197   9.141  23.179  1.00 39.51           C  
ATOM   1452  C   GLN A 184      52.287  10.527  22.557  1.00 39.04           C  
ATOM   1453  O   GLN A 184      52.568  11.477  23.273  1.00 38.97           O  
ATOM   1454  CB  GLN A 184      53.107   9.042  24.407  1.00 39.27           C  
ATOM   1455  CG  GLN A 184      53.196   7.626  25.021  1.00 37.25           C  
ATOM   1456  CD  GLN A 184      51.930   7.198  25.732  1.00 36.81           C  
ATOM   1457  OE1 GLN A 184      51.589   7.724  26.789  1.00 36.30           O  
ATOM   1458  NE2 GLN A 184      51.226   6.239  25.151  1.00 35.29           N  
ATOM   1459  N   CYS A 185      52.028  10.654  21.256  1.00 38.61           N  
ATOM   1460  CA  CYS A 185      52.097  11.948  20.595  1.00 38.03           C  
ATOM   1461  C   CYS A 185      50.740  12.400  20.162  1.00 37.83           C  
ATOM   1462  O   CYS A 185      50.600  13.481  19.574  1.00 36.34           O  
ATOM   1463  CB  CYS A 185      53.061  11.874  19.429  1.00 39.82           C  
ATOM   1464  SG  CYS A 185      54.756  11.764  20.042  1.00 44.32           S  
ATOM   1465  N   SER A 186      49.739  11.569  20.459  1.00 38.12           N  
ATOM   1466  CA  SER A 186      48.334  11.856  20.169  1.00 38.51           C  
ATOM   1467  C   SER A 186      47.545  11.636  21.453  1.00 39.02           C  
ATOM   1468  O   SER A 186      48.055  11.015  22.393  1.00 38.21           O  
ATOM   1469  CB  SER A 186      47.786  10.961  19.033  1.00 38.94           C  
ATOM   1470  OG  SER A 186      47.746   9.581  19.361  1.00 40.47           O  
ATOM   1471  N   CYS A 187      46.323  12.153  21.511  1.00 39.54           N  
ATOM   1472  CA  CYS A 187      45.500  11.992  22.704  1.00 40.74           C  
ATOM   1473  C   CYS A 187      44.072  11.598  22.366  1.00 41.86           C  
ATOM   1474  O   CYS A 187      43.460  12.189  21.477  1.00 42.52           O  
ATOM   1475  CB  CYS A 187      45.531  13.284  23.537  1.00 40.72           C  
ATOM   1476  SG  CYS A 187      46.922  13.230  24.703  1.00 42.97           S  
ATOM   1477  N   GLY A 188      43.555  10.598  23.075  1.00 41.88           N  
ATOM   1478  CA  GLY A 188      42.189  10.145  22.862  1.00 42.02           C  
ATOM   1479  C   GLY A 188      41.430   9.980  24.172  1.00 42.54           C  
ATOM   1480  O   GLY A 188      41.866  10.475  25.207  1.00 43.28           O  
ATOM   1481  N   ILE A 189      40.278   9.305  24.135  1.00 42.41           N  
ATOM   1482  CA  ILE A 189      39.457   9.085  25.338  1.00 42.29           C  
ATOM   1483  C   ILE A 189      40.150   8.038  26.214  1.00 43.31           C  
ATOM   1484  O   ILE A 189      41.098   7.422  25.742  1.00 44.00           O  
ATOM   1485  CB  ILE A 189      38.010   8.626  24.941  1.00 41.27           C  
ATOM   1486  CG1 ILE A 189      37.301   9.745  24.155  1.00 40.78           C  
ATOM   1487  CG2 ILE A 189      37.210   8.244  26.174  1.00 40.68           C  
ATOM   1488  CD1 ILE A 189      37.221  11.092  24.870  1.00 39.65           C  
ATOM   1489  N   ASP A 190      39.713   7.813  27.454  1.00 43.60           N  
ATOM   1490  CA  ASP A 190      40.406   6.828  28.296  1.00 44.53           C  
ATOM   1491  C   ASP A 190      39.777   5.414  28.272  1.00 44.73           C  
ATOM   1492  O   ASP A 190      38.776   5.170  28.976  1.00 45.25           O  
ATOM   1493  CB  ASP A 190      40.478   7.325  29.736  1.00 46.44           C  
ATOM   1494  CG  ASP A 190      41.617   6.687  30.506  1.00 48.41           C  
ATOM   1495  OD1 ASP A 190      42.024   5.567  30.122  1.00 50.18           O  
ATOM   1496  OD2 ASP A 190      42.098   7.293  31.492  1.00 49.77           O  
ATOM   1497  N   TYR A 191      40.381   4.502  27.494  1.00 44.95           N  
ATOM   1498  CA  TYR A 191      39.927   3.104  27.357  1.00 45.17           C  
ATOM   1499  C   TYR A 191      40.880   2.226  28.105  1.00 45.39           C  
ATOM   1500  O   TYR A 191      40.668   1.017  28.187  1.00 45.56           O  
ATOM   1501  CB  TYR A 191      39.995   2.617  25.901  1.00 45.74           C  
ATOM   1502  CG  TYR A 191      39.814   3.675  24.829  1.00 46.33           C  
ATOM   1503  CD1 TYR A 191      38.550   4.220  24.560  1.00 45.84           C  
ATOM   1504  CD2 TYR A 191      40.907   4.144  24.094  1.00 45.69           C  
ATOM   1505  CE1 TYR A 191      38.378   5.206  23.590  1.00 46.41           C  
ATOM   1506  CE2 TYR A 191      40.746   5.132  23.123  1.00 46.72           C  
ATOM   1507  CZ  TYR A 191      39.478   5.664  22.875  1.00 46.92           C  
ATOM   1508  OH  TYR A 191      39.306   6.668  21.938  1.00 47.50           O  
ATOM   1509  N   TYR A 192      41.926   2.845  28.642  1.00 45.80           N  
ATOM   1510  CA  TYR A 192      43.004   2.137  29.321  1.00 46.96           C  
ATOM   1511  C   TYR A 192      42.786   1.853  30.794  1.00 47.86           C  
ATOM   1512  O   TYR A 192      43.030   0.723  31.202  1.00 48.32           O  
ATOM   1513  CB  TYR A 192      44.321   2.911  29.139  1.00 46.68           C  
ATOM   1514  CG  TYR A 192      44.643   3.205  27.686  1.00 46.72           C  
ATOM   1515  CD1 TYR A 192      44.065   4.297  27.030  1.00 47.08           C  
ATOM   1516  CD2 TYR A 192      45.464   2.348  26.940  1.00 46.14           C  
ATOM   1517  CE1 TYR A 192      44.290   4.527  25.670  1.00 47.12           C  
ATOM   1518  CE2 TYR A 192      45.695   2.569  25.579  1.00 46.18           C  
ATOM   1519  CZ  TYR A 192      45.102   3.658  24.954  1.00 47.28           C  
ATOM   1520  OH  TYR A 192      45.287   3.873  23.606  1.00 48.57           O  
ATOM   1521  N   THR A 193      42.357   2.840  31.585  1.00 48.40           N  
ATOM   1522  CA  THR A 193      42.177   2.654  33.028  1.00 48.38           C  
ATOM   1523  C   THR A 193      40.724   2.801  33.439  1.00 49.38           C  
ATOM   1524  O   THR A 193      39.944   3.474  32.757  1.00 49.86           O  
ATOM   1525  CB  THR A 193      43.035   3.683  33.807  1.00 48.37           C  
ATOM   1526  OG1 THR A 193      42.482   5.000  33.656  1.00 48.00           O  
ATOM   1527  CG2 THR A 193      44.460   3.696  33.256  1.00 48.07           C  
ATOM   1528  N   PRO A 194      40.324   2.158  34.546  1.00 50.07           N  
ATOM   1529  CA  PRO A 194      38.913   2.344  34.891  1.00 50.54           C  
ATOM   1530  C   PRO A 194      38.674   3.672  35.645  1.00 50.55           C  
ATOM   1531  O   PRO A 194      37.515   4.037  35.851  1.00 51.07           O  
ATOM   1532  CB  PRO A 194      38.588   1.098  35.732  1.00 50.48           C  
ATOM   1533  CG  PRO A 194      39.611   0.088  35.293  1.00 50.92           C  
ATOM   1534  CD  PRO A 194      40.857   0.947  35.188  1.00 50.64           C  
ATOM   1535  N   HIS A 195      39.757   4.372  36.021  1.00 50.04           N  
ATOM   1536  CA  HIS A 195      39.734   5.670  36.756  1.00 49.91           C  
ATOM   1537  C   HIS A 195      38.309   6.085  37.150  1.00 50.30           C  
ATOM   1538  O   HIS A 195      37.689   6.919  36.467  1.00 50.57           O  
ATOM   1539  CB  HIS A 195      40.390   6.798  35.912  1.00 49.23           C  
ATOM   1540  CG  HIS A 195      40.839   8.004  36.702  1.00 47.75           C  
ATOM   1541  ND1 HIS A 195      40.555   9.297  36.311  1.00 48.65           N  
ATOM   1542  CD2 HIS A 195      41.623   8.115  37.801  1.00 47.60           C  
ATOM   1543  CE1 HIS A 195      41.146  10.149  37.131  1.00 48.45           C  
ATOM   1544  NE2 HIS A 195      41.802   9.457  38.044  1.00 48.13           N  
ATOM   1545  N   GLU A 196      37.812   5.511  38.246  1.00 50.26           N  
ATOM   1546  CA  GLU A 196      36.479   5.793  38.761  1.00 50.10           C  
ATOM   1547  C   GLU A 196      36.321   7.271  39.080  1.00 50.43           C  
ATOM   1548  O   GLU A 196      35.254   7.826  38.854  1.00 50.79           O  
ATOM   1549  CB  GLU A 196      36.238   4.967  40.026  1.00 50.18           C  
ATOM   1550  CG  GLU A 196      36.216   3.464  39.810  1.00 51.64           C  
ATOM   1551  CD  GLU A 196      36.165   2.672  41.118  1.00 53.79           C  
ATOM   1552  OE1 GLU A 196      35.492   3.119  42.088  1.00 54.20           O  
ATOM   1553  OE2 GLU A 196      36.794   1.587  41.169  1.00 53.74           O  
ATOM   1554  N   GLU A 197      37.381   7.892  39.597  1.00 50.64           N  
ATOM   1555  CA  GLU A 197      37.417   9.309  39.999  1.00 51.50           C  
ATOM   1556  C   GLU A 197      36.842  10.245  38.938  1.00 50.78           C  
ATOM   1557  O   GLU A 197      36.362  11.314  39.261  1.00 50.14           O  
ATOM   1558  CB  GLU A 197      38.874   9.698  40.289  1.00 54.11           C  
ATOM   1559  CG  GLU A 197      39.094  11.064  40.943  1.00 60.24           C  
ATOM   1560  CD  GLU A 197      40.575  11.525  40.882  1.00 64.68           C  
ATOM   1561  OE1 GLU A 197      41.498  10.688  41.086  1.00 67.43           O  
ATOM   1562  OE2 GLU A 197      40.815  12.735  40.636  1.00 66.42           O  
ATOM   1563  N   THR A 198      36.884   9.833  37.682  1.00 50.45           N  
ATOM   1564  CA  THR A 198      36.420  10.661  36.590  1.00 48.93           C  
ATOM   1565  C   THR A 198      35.379   9.904  35.749  1.00 49.43           C  
ATOM   1566  O   THR A 198      34.978  10.381  34.698  1.00 49.54           O  
ATOM   1567  CB  THR A 198      37.661  11.113  35.759  1.00 48.31           C  
ATOM   1568  OG1 THR A 198      37.384  12.351  35.102  1.00 48.14           O  
ATOM   1569  CG2 THR A 198      38.051  10.060  34.745  1.00 45.82           C  
ATOM   1570  N   ASN A 199      34.960   8.730  36.228  1.00 49.78           N  
ATOM   1571  CA  ASN A 199      33.922   7.881  35.607  1.00 49.69           C  
ATOM   1572  C   ASN A 199      34.178   7.517  34.175  1.00 49.37           C  
ATOM   1573  O   ASN A 199      33.310   7.763  33.342  1.00 49.34           O  
ATOM   1574  CB  ASN A 199      32.576   8.576  35.684  1.00 50.45           C  
ATOM   1575  CG  ASN A 199      32.150   8.825  37.098  1.00 52.01           C  
ATOM   1576  OD1 ASN A 199      32.522   9.827  37.728  1.00 53.96           O  
ATOM   1577  ND2 ASN A 199      31.382   7.898  37.628  1.00 53.86           N  
ATOM   1578  N   ASN A 200      35.312   6.872  33.904  1.00 48.73           N  
ATOM   1579  CA  ASN A 200      35.735   6.499  32.548  1.00 47.17           C  
ATOM   1580  C   ASN A 200      34.948   5.383  31.908  1.00 46.82           C  
ATOM   1581  O   ASN A 200      34.502   5.540  30.786  1.00 47.46           O  
ATOM   1582  CB  ASN A 200      37.214   6.098  32.545  1.00 46.08           C  
ATOM   1583  CG  ASN A 200      38.139   7.276  32.710  1.00 44.59           C  
ATOM   1584  OD1 ASN A 200      37.707   8.406  32.911  1.00 42.98           O  
ATOM   1585  ND2 ASN A 200      39.432   7.011  32.628  1.00 43.85           N  
ATOM   1586  N   GLU A 201      34.793   4.254  32.579  1.00 46.34           N  
ATOM   1587  CA  GLU A 201      34.104   3.142  31.940  1.00 46.63           C  
ATOM   1588  C   GLU A 201      32.696   3.514  31.392  1.00 46.67           C  
ATOM   1589  O   GLU A 201      32.325   3.064  30.296  1.00 47.23           O  
ATOM   1590  CB  GLU A 201      34.053   1.953  32.902  1.00 46.27           C  
ATOM   1591  CG  GLU A 201      35.426   1.505  33.407  1.00 45.66           C  
ATOM   1592  CD  GLU A 201      35.955   0.240  32.737  1.00 45.65           C  
ATOM   1593  OE1 GLU A 201      35.150  -0.665  32.426  1.00 46.06           O  
ATOM   1594  OE2 GLU A 201      37.189   0.141  32.553  1.00 45.97           O  
ATOM   1595  N   SER A 202      31.932   4.336  32.107  1.00 46.62           N  
ATOM   1596  CA  SER A 202      30.587   4.706  31.651  1.00 45.67           C  
ATOM   1597  C   SER A 202      30.618   5.603  30.425  1.00 45.51           C  
ATOM   1598  O   SER A 202      29.815   5.408  29.523  1.00 45.99           O  
ATOM   1599  CB  SER A 202      29.827   5.401  32.772  1.00 44.60           C  
ATOM   1600  OG  SER A 202      30.610   6.442  33.320  1.00 47.30           O  
ATOM   1601  N   PHE A 203      31.516   6.581  30.390  1.00 45.30           N  
ATOM   1602  CA  PHE A 203      31.605   7.472  29.244  1.00 45.00           C  
ATOM   1603  C   PHE A 203      31.922   6.688  27.984  1.00 45.16           C  
ATOM   1604  O   PHE A 203      31.333   6.952  26.947  1.00 45.42           O  
ATOM   1605  CB  PHE A 203      32.691   8.525  29.459  1.00 45.24           C  
ATOM   1606  CG  PHE A 203      32.809   9.496  28.322  1.00 45.31           C  
ATOM   1607  CD1 PHE A 203      32.065  10.670  28.314  1.00 44.90           C  
ATOM   1608  CD2 PHE A 203      33.616   9.207  27.230  1.00 44.67           C  
ATOM   1609  CE1 PHE A 203      32.117  11.545  27.234  1.00 44.53           C  
ATOM   1610  CE2 PHE A 203      33.676  10.073  26.148  1.00 44.43           C  
ATOM   1611  CZ  PHE A 203      32.924  11.246  26.149  1.00 44.69           C  
ATOM   1612  N   VAL A 204      32.848   5.732  28.071  1.00 45.43           N  
ATOM   1613  CA  VAL A 204      33.254   4.917  26.914  1.00 45.73           C  
ATOM   1614  C   VAL A 204      32.061   4.168  26.311  1.00 46.38           C  
ATOM   1615  O   VAL A 204      31.962   4.031  25.093  1.00 46.73           O  
ATOM   1616  CB  VAL A 204      34.389   3.900  27.301  1.00 45.53           C  
ATOM   1617  CG1 VAL A 204      34.646   2.931  26.162  1.00 45.13           C  
ATOM   1618  CG2 VAL A 204      35.685   4.648  27.632  1.00 44.29           C  
ATOM   1619  N   ILE A 205      31.156   3.683  27.146  1.00 47.40           N  
ATOM   1620  CA  ILE A 205      29.992   2.978  26.634  1.00 48.58           C  
ATOM   1621  C   ILE A 205      29.020   4.003  26.098  1.00 49.07           C  
ATOM   1622  O   ILE A 205      28.325   3.739  25.116  1.00 48.24           O  
ATOM   1623  CB  ILE A 205      29.350   2.132  27.751  1.00 49.24           C  
ATOM   1624  CG1 ILE A 205      30.329   1.029  28.156  1.00 49.42           C  
ATOM   1625  CG2 ILE A 205      28.041   1.533  27.279  1.00 48.97           C  
ATOM   1626  CD1 ILE A 205      30.070   0.434  29.498  1.00 51.00           C  
ATOM   1627  N   TYR A 206      29.002   5.178  26.728  1.00 50.30           N  
ATOM   1628  CA  TYR A 206      28.121   6.259  26.308  1.00 52.22           C  
ATOM   1629  C   TYR A 206      28.539   6.743  24.926  1.00 53.48           C  
ATOM   1630  O   TYR A 206      27.691   7.131  24.123  1.00 55.09           O  
ATOM   1631  CB  TYR A 206      28.197   7.423  27.305  1.00 51.93           C  
ATOM   1632  CG  TYR A 206      27.952   8.798  26.694  1.00 52.72           C  
ATOM   1633  CD1 TYR A 206      26.670   9.201  26.287  1.00 52.60           C  
ATOM   1634  CD2 TYR A 206      29.009   9.702  26.529  1.00 53.16           C  
ATOM   1635  CE1 TYR A 206      26.455  10.465  25.742  1.00 52.06           C  
ATOM   1636  CE2 TYR A 206      28.806  10.963  25.985  1.00 52.88           C  
ATOM   1637  CZ  TYR A 206      27.531  11.333  25.598  1.00 52.25           C  
ATOM   1638  OH  TYR A 206      27.342  12.582  25.071  1.00 51.99           O  
ATOM   1639  N   MET A 207      29.834   6.706  24.642  1.00 53.51           N  
ATOM   1640  CA  MET A 207      30.335   7.171  23.358  1.00 53.61           C  
ATOM   1641  C   MET A 207      30.164   6.136  22.239  1.00 52.68           C  
ATOM   1642  O   MET A 207      29.827   6.500  21.107  1.00 52.69           O  
ATOM   1643  CB  MET A 207      31.802   7.544  23.502  1.00 55.09           C  
ATOM   1644  CG  MET A 207      32.461   7.907  22.190  1.00 57.54           C  
ATOM   1645  SD  MET A 207      34.246   8.086  22.339  1.00 61.37           S  
ATOM   1646  CE  MET A 207      34.757   6.330  22.437  1.00 60.41           C  
ATOM   1647  N   PHE A 208      30.401   4.866  22.540  1.00 51.97           N  
ATOM   1648  CA  PHE A 208      30.286   3.817  21.540  1.00 50.74           C  
ATOM   1649  C   PHE A 208      28.861   3.534  21.193  1.00 50.76           C  
ATOM   1650  O   PHE A 208      28.625   2.954  20.158  1.00 50.91           O  
ATOM   1651  CB  PHE A 208      30.932   2.539  22.038  1.00 50.94           C  
ATOM   1652  CG  PHE A 208      32.398   2.446  21.752  1.00 52.60           C  
ATOM   1653  CD1 PHE A 208      32.857   2.349  20.446  1.00 52.88           C  
ATOM   1654  CD2 PHE A 208      33.329   2.430  22.789  1.00 53.37           C  
ATOM   1655  CE1 PHE A 208      34.221   2.237  20.174  1.00 53.22           C  
ATOM   1656  CE2 PHE A 208      34.696   2.317  22.526  1.00 53.05           C  
ATOM   1657  CZ  PHE A 208      35.141   2.221  21.218  1.00 52.74           C  
ATOM   1658  N   VAL A 209      27.908   3.920  22.039  1.00 50.75           N  
ATOM   1659  CA  VAL A 209      26.496   3.653  21.733  1.00 50.80           C  
ATOM   1660  C   VAL A 209      25.829   4.883  21.156  1.00 50.29           C  
ATOM   1661  O   VAL A 209      25.279   4.812  20.052  1.00 51.20           O  
ATOM   1662  CB  VAL A 209      25.684   3.184  22.990  1.00 50.82           C  
ATOM   1663  CG1 VAL A 209      24.236   2.891  22.584  1.00 50.37           C  
ATOM   1664  CG2 VAL A 209      26.323   1.917  23.615  1.00 49.46           C  
ATOM   1665  N   VAL A 210      25.881   5.997  21.880  1.00 49.77           N  
ATOM   1666  CA  VAL A 210      25.269   7.244  21.430  1.00 49.56           C  
ATOM   1667  C   VAL A 210      26.011   7.849  20.265  1.00 49.80           C  
ATOM   1668  O   VAL A 210      25.382   8.391  19.354  1.00 50.58           O  
ATOM   1669  CB  VAL A 210      25.247   8.311  22.546  1.00 49.01           C  
ATOM   1670  CG1 VAL A 210      24.818   9.674  21.980  1.00 47.69           C  
ATOM   1671  CG2 VAL A 210      24.322   7.864  23.662  1.00 48.35           C  
ATOM   1672  N   HIS A 211      27.333   7.767  20.277  1.00 49.00           N  
ATOM   1673  CA  HIS A 211      28.098   8.383  19.214  1.00 47.74           C  
ATOM   1674  C   HIS A 211      28.841   7.391  18.373  1.00 47.31           C  
ATOM   1675  O   HIS A 211      30.042   7.532  18.186  1.00 47.03           O  
ATOM   1676  CB  HIS A 211      29.045   9.388  19.831  1.00 47.36           C  
ATOM   1677  CG  HIS A 211      28.353  10.363  20.719  1.00 47.80           C  
ATOM   1678  ND1 HIS A 211      27.520  11.341  20.231  1.00 48.32           N  
ATOM   1679  CD2 HIS A 211      28.311  10.467  22.067  1.00 48.76           C  
ATOM   1680  CE1 HIS A 211      26.990  12.009  21.239  1.00 49.29           C  
ATOM   1681  NE2 HIS A 211      27.454  11.497  22.366  1.00 49.62           N  
ATOM   1682  N   PHE A 212      28.134   6.391  17.856  1.00 46.74           N  
ATOM   1683  CA  PHE A 212      28.755   5.393  16.992  1.00 46.24           C  
ATOM   1684  C   PHE A 212      27.747   4.343  16.527  1.00 46.45           C  
ATOM   1685  O   PHE A 212      27.249   4.425  15.416  1.00 46.26           O  
ATOM   1686  CB  PHE A 212      29.939   4.721  17.700  1.00 45.19           C  
ATOM   1687  CG  PHE A 212      30.666   3.724  16.843  1.00 44.12           C  
ATOM   1688  CD1 PHE A 212      31.090   4.064  15.572  1.00 43.92           C  
ATOM   1689  CD2 PHE A 212      30.948   2.454  17.316  1.00 43.85           C  
ATOM   1690  CE1 PHE A 212      31.791   3.149  14.786  1.00 44.20           C  
ATOM   1691  CE2 PHE A 212      31.646   1.533  16.537  1.00 43.68           C  
ATOM   1692  CZ  PHE A 212      32.069   1.881  15.273  1.00 42.90           C  
ATOM   1693  N   ILE A 213      27.498   3.337  17.355  1.00 46.90           N  
ATOM   1694  CA  ILE A 213      26.576   2.285  16.971  1.00 47.47           C  
ATOM   1695  C   ILE A 213      25.302   2.886  16.458  1.00 47.54           C  
ATOM   1696  O   ILE A 213      24.852   2.532  15.378  1.00 47.74           O  
ATOM   1697  CB  ILE A 213      26.225   1.369  18.149  1.00 47.75           C  
ATOM   1698  CG1 ILE A 213      27.460   0.619  18.620  1.00 46.79           C  
ATOM   1699  CG2 ILE A 213      25.183   0.368  17.716  1.00 47.36           C  
ATOM   1700  CD1 ILE A 213      27.193  -0.213  19.838  1.00 47.73           C  
ATOM   1701  N   ILE A 214      24.742   3.811  17.219  1.00 47.42           N  
ATOM   1702  CA  ILE A 214      23.486   4.432  16.852  1.00 47.24           C  
ATOM   1703  C   ILE A 214      23.522   5.226  15.559  1.00 48.02           C  
ATOM   1704  O   ILE A 214      22.766   4.904  14.644  1.00 48.41           O  
ATOM   1705  CB  ILE A 214      22.982   5.295  18.004  1.00 46.78           C  
ATOM   1706  CG1 ILE A 214      22.393   4.372  19.069  1.00 45.85           C  
ATOM   1707  CG2 ILE A 214      21.979   6.324  17.506  1.00 47.49           C  
ATOM   1708  CD1 ILE A 214      21.787   5.096  20.218  1.00 45.49           C  
ATOM   1709  N   PRO A 215      24.361   6.269  15.454  1.00 48.63           N  
ATOM   1710  CA  PRO A 215      24.366   7.013  14.188  1.00 48.97           C  
ATOM   1711  C   PRO A 215      24.608   6.115  12.980  1.00 49.94           C  
ATOM   1712  O   PRO A 215      24.114   6.410  11.897  1.00 50.24           O  
ATOM   1713  CB  PRO A 215      25.479   8.031  14.391  1.00 48.54           C  
ATOM   1714  CG  PRO A 215      25.452   8.260  15.857  1.00 48.96           C  
ATOM   1715  CD  PRO A 215      25.292   6.873  16.418  1.00 48.81           C  
ATOM   1716  N   LEU A 216      25.365   5.034  13.171  1.00 51.10           N  
ATOM   1717  CA  LEU A 216      25.657   4.072  12.102  1.00 52.27           C  
ATOM   1718  C   LEU A 216      24.375   3.383  11.650  1.00 53.97           C  
ATOM   1719  O   LEU A 216      24.111   3.259  10.452  1.00 55.27           O  
ATOM   1720  CB  LEU A 216      26.641   2.992  12.584  1.00 51.00           C  
ATOM   1721  CG  LEU A 216      28.120   3.210  12.310  1.00 49.96           C  
ATOM   1722  CD1 LEU A 216      28.291   3.808  10.949  1.00 50.68           C  
ATOM   1723  CD2 LEU A 216      28.680   4.136  13.305  1.00 51.66           C  
ATOM   1724  N   ILE A 217      23.588   2.919  12.612  1.00 54.91           N  
ATOM   1725  CA  ILE A 217      22.334   2.239  12.332  1.00 54.99           C  
ATOM   1726  C   ILE A 217      21.417   3.107  11.472  1.00 54.92           C  
ATOM   1727  O   ILE A 217      20.907   2.632  10.453  1.00 55.20           O  
ATOM   1728  CB  ILE A 217      21.643   1.910  13.636  1.00 54.63           C  
ATOM   1729  CG1 ILE A 217      22.513   0.945  14.431  1.00 53.84           C  
ATOM   1730  CG2 ILE A 217      20.279   1.337  13.357  1.00 55.13           C  
ATOM   1731  CD1 ILE A 217      22.163   0.908  15.880  1.00 54.54           C  
ATOM   1732  N   VAL A 218      21.202   4.352  11.902  1.00 54.52           N  
ATOM   1733  CA  VAL A 218      20.373   5.329  11.190  1.00 54.08           C  
ATOM   1734  C   VAL A 218      20.819   5.400   9.760  1.00 55.54           C  
ATOM   1735  O   VAL A 218      20.052   5.147   8.832  1.00 56.20           O  
ATOM   1736  CB  VAL A 218      20.552   6.742  11.776  1.00 52.79           C  
ATOM   1737  CG1 VAL A 218      19.976   7.781  10.828  1.00 52.31           C  
ATOM   1738  CG2 VAL A 218      19.912   6.820  13.136  1.00 51.67           C  
ATOM   1739  N   ILE A 219      22.081   5.761   9.601  1.00 56.77           N  
ATOM   1740  CA  ILE A 219      22.713   5.911   8.306  1.00 57.73           C  
ATOM   1741  C   ILE A 219      22.573   4.662   7.457  1.00 59.19           C  
ATOM   1742  O   ILE A 219      22.239   4.764   6.281  1.00 59.93           O  
ATOM   1743  CB  ILE A 219      24.188   6.249   8.495  1.00 56.72           C  
ATOM   1744  CG1 ILE A 219      24.304   7.614   9.173  1.00 56.87           C  
ATOM   1745  CG2 ILE A 219      24.888   6.237   7.174  1.00 56.13           C  
ATOM   1746  CD1 ILE A 219      25.712   8.055   9.465  1.00 57.61           C  
ATOM   1747  N   PHE A 220      22.827   3.494   8.033  1.00 60.43           N  
ATOM   1748  CA  PHE A 220      22.726   2.251   7.288  1.00 61.76           C  
ATOM   1749  C   PHE A 220      21.321   1.915   6.957  1.00 63.08           C  
ATOM   1750  O   PHE A 220      21.013   1.600   5.807  1.00 63.43           O  
ATOM   1751  CB  PHE A 220      23.336   1.126   8.082  1.00 61.95           C  
ATOM   1752  CG  PHE A 220      24.786   1.071   7.942  1.00 62.41           C  
ATOM   1753  CD1 PHE A 220      25.340   0.905   6.686  1.00 62.91           C  
ATOM   1754  CD2 PHE A 220      25.609   1.262   9.029  1.00 62.69           C  
ATOM   1755  CE1 PHE A 220      26.692   0.938   6.509  1.00 63.31           C  
ATOM   1756  CE2 PHE A 220      26.970   1.299   8.867  1.00 63.24           C  
ATOM   1757  CZ  PHE A 220      27.516   1.136   7.603  1.00 63.70           C  
ATOM   1758  N   PHE A 221      20.459   1.945   7.958  1.00 64.43           N  
ATOM   1759  CA  PHE A 221      19.082   1.649   7.692  1.00 65.68           C  
ATOM   1760  C   PHE A 221      18.609   2.559   6.591  1.00 66.17           C  
ATOM   1761  O   PHE A 221      18.157   2.082   5.559  1.00 66.54           O  
ATOM   1762  CB  PHE A 221      18.241   1.866   8.926  1.00 66.38           C  
ATOM   1763  CG  PHE A 221      16.798   1.634   8.679  1.00 68.18           C  
ATOM   1764  CD1 PHE A 221      15.909   2.706   8.614  1.00 68.99           C  
ATOM   1765  CD2 PHE A 221      16.328   0.341   8.431  1.00 68.71           C  
ATOM   1766  CE1 PHE A 221      14.565   2.499   8.301  1.00 68.91           C  
ATOM   1767  CE2 PHE A 221      14.990   0.118   8.118  1.00 69.07           C  
ATOM   1768  CZ  PHE A 221      14.104   1.203   8.052  1.00 69.66           C  
ATOM   1769  N   CYS A 222      18.733   3.864   6.797  1.00 67.33           N  
ATOM   1770  CA  CYS A 222      18.316   4.839   5.802  1.00 68.83           C  
ATOM   1771  C   CYS A 222      18.779   4.437   4.409  1.00 70.09           C  
ATOM   1772  O   CYS A 222      18.085   4.699   3.442  1.00 70.62           O  
ATOM   1773  CB  CYS A 222      18.876   6.211   6.145  1.00 68.19           C  
ATOM   1774  SG  CYS A 222      18.607   7.402   4.833  1.00 69.11           S  
ATOM   1775  N   TYR A 223      19.944   3.811   4.304  1.00 71.59           N  
ATOM   1776  CA  TYR A 223      20.467   3.393   3.010  1.00 73.16           C  
ATOM   1777  C   TYR A 223      19.632   2.278   2.478  1.00 74.69           C  
ATOM   1778  O   TYR A 223      19.282   2.269   1.304  1.00 74.55           O  
ATOM   1779  CB  TYR A 223      21.897   2.913   3.162  1.00 73.08           C  
ATOM   1780  CG  TYR A 223      22.459   2.230   1.938  1.00 73.29           C  
ATOM   1781  CD1 TYR A 223      22.733   2.943   0.778  1.00 73.36           C  
ATOM   1782  CD2 TYR A 223      22.779   0.875   1.962  1.00 73.88           C  
ATOM   1783  CE1 TYR A 223      23.330   2.319  -0.332  1.00 73.67           C  
ATOM   1784  CE2 TYR A 223      23.375   0.244   0.860  1.00 73.46           C  
ATOM   1785  CZ  TYR A 223      23.652   0.970  -0.281  1.00 73.30           C  
ATOM   1786  OH  TYR A 223      24.284   0.358  -1.345  1.00 73.22           O  
ATOM   1787  N   GLY A 224      19.328   1.322   3.344  1.00 76.62           N  
ATOM   1788  CA  GLY A 224      18.512   0.200   2.939  1.00 79.43           C  
ATOM   1789  C   GLY A 224      17.194   0.687   2.378  1.00 81.28           C  
ATOM   1790  O   GLY A 224      16.397  -0.112   1.913  1.00 81.14           O  
ATOM   1791  N   GLN A 225      16.965   2.000   2.441  1.00 83.58           N  
ATOM   1792  CA  GLN A 225      15.742   2.622   1.918  1.00 86.00           C  
ATOM   1793  C   GLN A 225      16.018   3.072   0.515  1.00 87.80           C  
ATOM   1794  O   GLN A 225      15.278   2.743  -0.412  1.00 87.84           O  
ATOM   1795  CB  GLN A 225      15.341   3.838   2.764  1.00 85.44           C  
ATOM   1796  CG  GLN A 225      15.199   3.504   4.219  1.00 84.97           C  
ATOM   1797  CD  GLN A 225      14.365   2.257   4.417  1.00 85.26           C  
ATOM   1798  OE1 GLN A 225      13.145   2.325   4.513  1.00 85.57           O  
ATOM   1799  NE2 GLN A 225      15.026   1.099   4.453  1.00 85.24           N  
ATOM   1800  N   LEU A 226      17.090   3.838   0.370  1.00 90.01           N  
ATOM   1801  CA  LEU A 226      17.502   4.320  -0.927  1.00 92.42           C  
ATOM   1802  C   LEU A 226      18.210   3.184  -1.638  1.00 94.29           C  
ATOM   1803  O   LEU A 226      19.252   3.358  -2.269  1.00 94.45           O  
ATOM   1804  CB  LEU A 226      18.406   5.547  -0.770  1.00 92.22           C  
ATOM   1805  CG  LEU A 226      17.656   6.856  -0.476  1.00 92.21           C  
ATOM   1806  CD1 LEU A 226      16.820   6.726   0.789  1.00 91.94           C  
ATOM   1807  CD2 LEU A 226      18.656   7.990  -0.354  1.00 92.02           C  
ATOM   1808  N   VAL A 227      17.633   1.999  -1.491  1.00 96.23           N  
ATOM   1809  CA  VAL A 227      18.137   0.800  -2.138  1.00 98.36           C  
ATOM   1810  C   VAL A 227      17.169   0.493  -3.276  1.00 99.65           C  
ATOM   1811  O   VAL A 227      17.599   0.392  -4.434  1.00 99.96           O  
ATOM   1812  CB  VAL A 227      18.217  -0.412  -1.138  1.00 98.41           C  
ATOM   1813  CG1 VAL A 227      16.816  -0.865  -0.708  1.00 98.24           C  
ATOM   1814  CG2 VAL A 227      18.975  -1.568  -1.781  1.00 98.33           C  
ATOM   1815  N   PHE A 228      15.874   0.384  -2.947  1.00101.03           N  
ATOM   1816  CA  PHE A 228      14.825   0.113  -3.937  1.00102.04           C  
ATOM   1817  C   PHE A 228      14.583   1.378  -4.744  1.00102.50           C  
ATOM   1818  O   PHE A 228      14.289   1.309  -5.943  1.00102.70           O  
ATOM   1819  CB  PHE A 228      13.515  -0.332  -3.257  1.00101.81           C  
ATOM   1820  CG  PHE A 228      12.424  -0.726  -4.236  1.00101.87           C  
ATOM   1821  CD1 PHE A 228      12.637  -1.745  -5.169  1.00101.78           C  
ATOM   1822  CD2 PHE A 228      11.188  -0.078  -4.227  1.00101.77           C  
ATOM   1823  CE1 PHE A 228      11.636  -2.114  -6.080  1.00101.77           C  
ATOM   1824  CE2 PHE A 228      10.181  -0.438  -5.133  1.00101.55           C  
ATOM   1825  CZ  PHE A 228      10.407  -1.459  -6.060  1.00101.68           C  
ATOM   1826  N   THR A 229      14.704   2.528  -4.088  1.00102.91           N  
ATOM   1827  CA  THR A 229      14.520   3.802  -4.769  1.00103.32           C  
ATOM   1828  C   THR A 229      15.838   4.142  -5.498  1.00103.84           C  
ATOM   1829  O   THR A 229      16.423   3.238  -6.118  1.00103.79           O  
ATOM   1830  CB  THR A 229      14.116   4.927  -3.757  1.00102.96           C  
ATOM   1831  OG1 THR A 229      13.153   4.416  -2.819  1.00102.53           O  
ATOM   1832  CG2 THR A 229      13.482   6.103  -4.500  1.00102.53           C  
ATOM   1833  N   VAL A 230      16.305   5.395  -5.422  1.00104.19           N  
ATOM   1834  CA  VAL A 230      17.543   5.824  -6.102  1.00104.42           C  
ATOM   1835  C   VAL A 230      18.678   4.810  -5.868  1.00104.57           C  
ATOM   1836  O   VAL A 230      18.959   4.437  -4.723  1.00104.45           O  
ATOM   1837  CB  VAL A 230      17.976   7.273  -5.636  1.00104.11           C  
ATOM   1838  CG1 VAL A 230      18.647   7.223  -4.275  1.00103.95           C  
ATOM   1839  CG2 VAL A 230      18.891   7.919  -6.667  1.00103.64           C  
ATOM   1840  N   LYS A 231      19.304   4.354  -6.954  1.00104.94           N  
ATOM   1841  CA  LYS A 231      20.392   3.378  -6.865  1.00105.28           C  
ATOM   1842  C   LYS A 231      21.684   3.954  -7.409  1.00105.74           C  
ATOM   1843  O   LYS A 231      21.674   4.990  -8.075  1.00105.55           O  
ATOM   1844  CB  LYS A 231      20.054   2.103  -7.644  1.00104.54           C  
ATOM   1845  CG  LYS A 231      18.844   1.346  -7.136  1.00103.78           C  
ATOM   1846  CD  LYS A 231      18.660   0.029  -7.886  1.00103.66           C  
ATOM   1847  CE  LYS A 231      18.519   0.227  -9.399  1.00102.84           C  
ATOM   1848  NZ  LYS A 231      19.793   0.623 -10.064  1.00102.19           N  
ATOM   1849  N   GLU A 232      22.788   3.264  -7.122  1.00106.32           N  
ATOM   1850  CA  GLU A 232      24.122   3.667  -7.567  1.00106.79           C  
ATOM   1851  C   GLU A 232      24.144   3.698  -9.076  1.00107.24           C  
ATOM   1852  O   GLU A 232      24.943   4.438  -9.672  1.00107.18           O  
ATOM   1853  CB  GLU A 232      25.165   2.675  -7.051  1.00105.96           C  
ATOM   1854  CG  GLU A 232      25.017   2.370  -5.578  1.00104.85           C  
ATOM   1855  CD  GLU A 232      26.004   1.335  -5.103  1.00104.32           C  
ATOM   1856  OE1 GLU A 232      26.041   0.228  -5.688  1.00103.46           O  
ATOM   1857  OE2 GLU A 232      26.738   1.632  -4.141  1.00103.45           O  
ATOM   1858  N   ALA A 233      23.281   2.886  -9.688  1.00107.79           N  
ATOM   1859  CA  ALA A 233      23.167   2.836 -11.140  1.00107.95           C  
ATOM   1860  C   ALA A 233      22.716   4.213 -11.601  1.00108.13           C  
ATOM   1861  O   ALA A 233      21.512   4.505 -11.600  1.00108.09           O  
ATOM   1862  CB  ALA A 233      22.146   1.762 -11.559  1.00107.71           C  
ATOM   1863  N   ALA A 234      23.683   5.057 -11.964  1.00108.00           N  
ATOM   1864  CA  ALA A 234      23.414   6.424 -12.417  1.00108.02           C  
ATOM   1865  C   ALA A 234      23.704   6.536 -13.907  1.00108.10           C  
ATOM   1866  O   ALA A 234      24.844   6.275 -14.324  1.00108.15           O  
ATOM   1867  CB  ALA A 234      24.283   7.416 -11.629  1.00108.19           C  
ATOM   1868  N   ALA A 235      22.690   6.925 -14.691  1.00107.89           N  
ATOM   1869  CA  ALA A 235      22.820   7.067 -16.150  1.00107.65           C  
ATOM   1870  C   ALA A 235      23.172   8.503 -16.548  1.00107.72           C  
ATOM   1871  O   ALA A 235      23.796   9.232 -15.763  1.00107.41           O  
ATOM   1872  CB  ALA A 235      21.518   6.613 -16.865  1.00107.16           C  
ATOM   1873  N   GLN A 236      22.746   8.899 -17.748  1.00107.63           N  
ATOM   1874  CA  GLN A 236      23.044  10.219 -18.330  1.00107.40           C  
ATOM   1875  C   GLN A 236      21.950  11.300 -18.100  1.00107.35           C  
ATOM   1876  O   GLN A 236      21.074  11.139 -17.240  1.00107.39           O  
ATOM   1877  CB  GLN A 236      23.315  10.018 -19.833  1.00106.95           C  
ATOM   1878  CG  GLN A 236      22.308   9.070 -20.511  1.00106.50           C  
ATOM   1879  CD  GLN A 236      22.922   8.229 -21.625  1.00106.28           C  
ATOM   1880  OE1 GLN A 236      23.418   8.760 -22.619  1.00105.81           O  
ATOM   1881  NE2 GLN A 236      22.885   6.908 -21.458  1.00105.62           N  
ATOM   1882  N   GLN A 237      22.033  12.392 -18.872  1.00107.12           N  
ATOM   1883  CA  GLN A 237      21.107  13.538 -18.799  1.00106.24           C  
ATOM   1884  C   GLN A 237      19.673  13.062 -18.704  1.00105.99           C  
ATOM   1885  O   GLN A 237      19.188  12.335 -19.586  1.00105.88           O  
ATOM   1886  CB  GLN A 237      21.268  14.453 -20.030  1.00105.27           C  
ATOM   1887  CG  GLN A 237      22.711  14.624 -20.507  1.00103.67           C  
ATOM   1888  CD  GLN A 237      23.219  13.405 -21.278  1.00102.98           C  
ATOM   1889  OE1 GLN A 237      24.423  13.152 -21.341  1.00102.27           O  
ATOM   1890  NE2 GLN A 237      22.294  12.652 -21.878  1.00102.57           N  
ATOM   1891  N   GLN A 238      18.996  13.499 -17.647  1.00105.45           N  
ATOM   1892  CA  GLN A 238      17.625  13.095 -17.384  1.00105.04           C  
ATOM   1893  C   GLN A 238      17.631  11.635 -17.008  1.00104.92           C  
ATOM   1894  O   GLN A 238      18.169  10.798 -17.749  1.00105.01           O  
ATOM   1895  CB  GLN A 238      16.723  13.272 -18.610  1.00104.39           C  
ATOM   1896  CG  GLN A 238      15.318  12.696 -18.393  1.00103.69           C  
ATOM   1897  CD  GLN A 238      14.597  12.340 -19.683  1.00103.52           C  
ATOM   1898  OE1 GLN A 238      14.406  13.185 -20.553  1.00102.94           O  
ATOM   1899  NE2 GLN A 238      14.186  11.077 -19.804  1.00102.64           N  
ATOM   1900  N   GLU A 239      17.045  11.328 -15.859  1.00104.09           N  
ATOM   1901  CA  GLU A 239      16.951   9.956 -15.383  1.00103.28           C  
ATOM   1902  C   GLU A 239      15.468   9.658 -15.287  1.00102.82           C  
ATOM   1903  O   GLU A 239      15.045   8.506 -15.148  1.00102.97           O  
ATOM   1904  CB  GLU A 239      17.608   9.856 -14.014  1.00102.55           C  
ATOM   1905  CG  GLU A 239      18.041   8.467 -13.621  1.00102.01           C  
ATOM   1906  CD  GLU A 239      19.420   8.142 -14.141  1.00101.58           C  
ATOM   1907  OE1 GLU A 239      19.642   8.305 -15.362  1.00101.34           O  
ATOM   1908  OE2 GLU A 239      20.278   7.729 -13.329  1.00100.76           O  
ATOM   1909  N   SER A 240      14.710  10.750 -15.388  1.00102.33           N  
ATOM   1910  CA  SER A 240      13.243  10.859 -15.343  1.00101.48           C  
ATOM   1911  C   SER A 240      13.026  12.351 -15.193  1.00100.55           C  
ATOM   1912  O   SER A 240      11.962  12.834 -14.810  1.00100.13           O  
ATOM   1913  CB  SER A 240      12.644  10.112 -14.133  1.00101.44           C  
ATOM   1914  OG  SER A 240      12.506   8.710 -14.367  1.00101.18           O  
ATOM   1915  N   ALA A 241      14.107  13.051 -15.512  1.00 99.53           N  
ATOM   1916  CA  ALA A 241      14.248  14.490 -15.447  1.00 98.48           C  
ATOM   1917  C   ALA A 241      15.715  14.702 -15.127  1.00 97.83           C  
ATOM   1918  O   ALA A 241      16.228  14.011 -14.246  1.00 97.66           O  
ATOM   1919  CB  ALA A 241      13.368  15.069 -14.327  1.00 97.66           C  
ATOM   1920  N   THR A 242      16.409  15.587 -15.839  1.00 97.16           N  
ATOM   1921  CA  THR A 242      17.814  15.827 -15.518  1.00 96.28           C  
ATOM   1922  C   THR A 242      17.878  16.199 -14.050  1.00 95.48           C  
ATOM   1923  O   THR A 242      18.935  16.136 -13.434  1.00 95.50           O  
ATOM   1924  CB  THR A 242      18.420  16.959 -16.383  1.00 96.42           C  
ATOM   1925  OG1 THR A 242      18.558  16.498 -17.733  1.00 96.48           O  
ATOM   1926  CG2 THR A 242      19.796  17.375 -15.857  1.00 96.13           C  
ATOM   1927  N   THR A 243      16.727  16.590 -13.510  1.00 94.70           N  
ATOM   1928  CA  THR A 243      16.588  16.931 -12.100  1.00 93.76           C  
ATOM   1929  C   THR A 243      16.856  15.666 -11.342  1.00 93.00           C  
ATOM   1930  O   THR A 243      17.847  15.567 -10.627  1.00 93.59           O  
ATOM   1931  CB  THR A 243      15.146  17.396 -11.774  1.00 93.72           C  
ATOM   1932  OG1 THR A 243      14.954  18.728 -12.260  1.00 93.96           O  
ATOM   1933  CG2 THR A 243      14.882  17.354 -10.272  1.00 93.83           C  
ATOM   1934  N   GLN A 244      15.963  14.698 -11.521  1.00 91.68           N  
ATOM   1935  CA  GLN A 244      16.076  13.396 -10.883  1.00 89.72           C  
ATOM   1936  C   GLN A 244      17.473  12.833 -11.134  1.00 88.17           C  
ATOM   1937  O   GLN A 244      18.087  12.270 -10.228  1.00 87.80           O  
ATOM   1938  CB  GLN A 244      14.993  12.474 -11.450  1.00 89.98           C  
ATOM   1939  CG  GLN A 244      15.002  11.063 -10.906  1.00 90.48           C  
ATOM   1940  CD  GLN A 244      16.045  10.177 -11.571  1.00 91.00           C  
ATOM   1941  OE1 GLN A 244      17.241  10.445 -11.507  1.00 91.56           O  
ATOM   1942  NE2 GLN A 244      15.586   9.110 -12.215  1.00 91.09           N  
ATOM   1943  N   LYS A 245      17.968  12.981 -12.357  1.00 86.46           N  
ATOM   1944  CA  LYS A 245      19.294  12.496 -12.714  1.00 84.66           C  
ATOM   1945  C   LYS A 245      20.333  12.971 -11.715  1.00 83.05           C  
ATOM   1946  O   LYS A 245      20.908  12.167 -11.005  1.00 82.92           O  
ATOM   1947  CB  LYS A 245      19.665  12.985 -14.113  1.00 84.86           C  
ATOM   1948  CG  LYS A 245      21.148  12.952 -14.430  1.00 85.39           C  
ATOM   1949  CD  LYS A 245      21.696  11.536 -14.591  1.00 86.89           C  
ATOM   1950  CE  LYS A 245      22.051  10.854 -13.273  1.00 87.58           C  
ATOM   1951  NZ  LYS A 245      20.868  10.310 -12.547  1.00 88.64           N  
ATOM   1952  N   ALA A 246      20.566  14.274 -11.663  1.00 81.49           N  
ATOM   1953  CA  ALA A 246      21.553  14.857 -10.764  1.00 79.91           C  
ATOM   1954  C   ALA A 246      21.252  14.574  -9.299  1.00 78.99           C  
ATOM   1955  O   ALA A 246      22.036  14.957  -8.433  1.00 78.72           O  
ATOM   1956  CB  ALA A 246      21.619  16.340 -10.993  1.00 80.45           C  
ATOM   1957  N   GLU A 247      20.133  13.921  -9.013  1.00 77.69           N  
ATOM   1958  CA  GLU A 247      19.770  13.603  -7.634  1.00 76.37           C  
ATOM   1959  C   GLU A 247      20.489  12.357  -7.241  1.00 75.03           C  
ATOM   1960  O   GLU A 247      20.845  12.136  -6.082  1.00 73.76           O  
ATOM   1961  CB  GLU A 247      18.269  13.361  -7.526  1.00 77.42           C  
ATOM   1962  CG  GLU A 247      17.768  13.590  -6.144  1.00 79.57           C  
ATOM   1963  CD  GLU A 247      18.501  14.749  -5.515  1.00 81.18           C  
ATOM   1964  OE1 GLU A 247      19.624  14.529  -5.002  1.00 81.73           O  
ATOM   1965  OE2 GLU A 247      17.975  15.884  -5.560  1.00 82.54           O  
ATOM   1966  N   LYS A 248      20.673  11.531  -8.254  1.00 74.02           N  
ATOM   1967  CA  LYS A 248      21.349  10.265  -8.142  1.00 72.94           C  
ATOM   1968  C   LYS A 248      22.811  10.537  -7.836  1.00 71.30           C  
ATOM   1969  O   LYS A 248      23.459   9.717  -7.189  1.00 71.65           O  
ATOM   1970  CB  LYS A 248      21.197   9.528  -9.477  1.00 74.17           C  
ATOM   1971  CG  LYS A 248      21.346   8.018  -9.426  1.00 76.20           C  
ATOM   1972  CD  LYS A 248      20.378   7.363 -10.420  1.00 77.28           C  
ATOM   1973  CE  LYS A 248      18.921   7.787 -10.134  1.00 78.17           C  
ATOM   1974  NZ  LYS A 248      17.912   7.168 -11.051  1.00 77.56           N  
ATOM   1975  N   GLU A 249      23.322  11.689  -8.277  1.00 68.75           N  
ATOM   1976  CA  GLU A 249      24.726  12.027  -8.064  1.00 65.79           C  
ATOM   1977  C   GLU A 249      25.015  12.366  -6.624  1.00 63.19           C  
ATOM   1978  O   GLU A 249      25.952  11.825  -6.045  1.00 62.82           O  
ATOM   1979  CB  GLU A 249      25.152  13.200  -8.945  1.00 66.61           C  
ATOM   1980  CG  GLU A 249      26.585  13.654  -8.644  1.00 68.69           C  
ATOM   1981  CD  GLU A 249      26.919  15.029  -9.221  1.00 70.22           C  
ATOM   1982  OE1 GLU A 249      26.012  15.899  -9.232  1.00 71.11           O  
ATOM   1983  OE2 GLU A 249      28.085  15.246  -9.646  1.00 70.27           O  
ATOM   1984  N   VAL A 250      24.241  13.266  -6.042  1.00 60.14           N  
ATOM   1985  CA  VAL A 250      24.485  13.631  -4.664  1.00 57.74           C  
ATOM   1986  C   VAL A 250      24.453  12.405  -3.781  1.00 56.96           C  
ATOM   1987  O   VAL A 250      25.286  12.280  -2.891  1.00 57.08           O  
ATOM   1988  CB  VAL A 250      23.448  14.631  -4.162  1.00 57.20           C  
ATOM   1989  CG1 VAL A 250      23.550  14.763  -2.658  1.00 57.09           C  
ATOM   1990  CG2 VAL A 250      23.673  15.977  -4.810  1.00 56.90           C  
ATOM   1991  N   THR A 251      23.500  11.506  -4.021  1.00 56.12           N  
ATOM   1992  CA  THR A 251      23.377  10.288  -3.221  1.00 55.17           C  
ATOM   1993  C   THR A 251      24.639   9.411  -3.402  1.00 54.93           C  
ATOM   1994  O   THR A 251      25.140   8.882  -2.409  1.00 55.01           O  
ATOM   1995  CB  THR A 251      22.069   9.485  -3.599  1.00 55.19           C  
ATOM   1996  OG1 THR A 251      20.951  10.382  -3.683  1.00 55.33           O  
ATOM   1997  CG2 THR A 251      21.747   8.434  -2.537  1.00 54.84           C  
ATOM   1998  N   ARG A 252      25.155   9.282  -4.632  1.00 54.18           N  
ATOM   1999  CA  ARG A 252      26.351   8.470  -4.901  1.00 53.41           C  
ATOM   2000  C   ARG A 252      27.477   8.991  -4.057  1.00 51.56           C  
ATOM   2001  O   ARG A 252      28.271   8.228  -3.538  1.00 51.81           O  
ATOM   2002  CB  ARG A 252      26.774   8.573  -6.372  1.00 56.08           C  
ATOM   2003  CG  ARG A 252      27.077   7.244  -7.130  1.00 61.27           C  
ATOM   2004  CD  ARG A 252      27.960   6.228  -6.350  1.00 65.21           C  
ATOM   2005  NE  ARG A 252      28.824   5.410  -7.225  1.00 68.49           N  
ATOM   2006  CZ  ARG A 252      29.215   4.159  -6.959  1.00 69.23           C  
ATOM   2007  NH1 ARG A 252      28.804   3.566  -5.841  1.00 69.28           N  
ATOM   2008  NH2 ARG A 252      30.040   3.513  -7.790  1.00 67.51           N  
ATOM   2009  N   MET A 253      27.546  10.303  -3.918  1.00 48.94           N  
ATOM   2010  CA  MET A 253      28.601  10.916  -3.136  1.00 47.00           C  
ATOM   2011  C   MET A 253      28.377  10.739  -1.645  1.00 45.85           C  
ATOM   2012  O   MET A 253      29.317  10.385  -0.927  1.00 45.97           O  
ATOM   2013  CB  MET A 253      28.690  12.395  -3.457  1.00 46.87           C  
ATOM   2014  CG  MET A 253      29.587  13.135  -2.518  1.00 46.66           C  
ATOM   2015  SD  MET A 253      29.852  14.776  -3.131  1.00 48.27           S  
ATOM   2016  CE  MET A 253      29.009  15.766  -1.952  1.00 46.98           C  
ATOM   2017  N   VAL A 254      27.160  11.004  -1.175  1.00 44.24           N  
ATOM   2018  CA  VAL A 254      26.858  10.859   0.240  1.00 42.60           C  
ATOM   2019  C   VAL A 254      27.175   9.449   0.655  1.00 43.02           C  
ATOM   2020  O   VAL A 254      27.499   9.203   1.815  1.00 43.97           O  
ATOM   2021  CB  VAL A 254      25.382  11.180   0.535  1.00 40.89           C  
ATOM   2022  CG1 VAL A 254      25.018  10.767   1.930  1.00 40.43           C  
ATOM   2023  CG2 VAL A 254      25.162  12.662   0.410  1.00 40.42           C  
ATOM   2024  N   ILE A 255      27.109   8.524  -0.294  1.00 43.25           N  
ATOM   2025  CA  ILE A 255      27.405   7.130  -0.006  1.00 44.14           C  
ATOM   2026  C   ILE A 255      28.926   6.932   0.025  1.00 44.77           C  
ATOM   2027  O   ILE A 255      29.426   6.217   0.888  1.00 45.81           O  
ATOM   2028  CB  ILE A 255      26.727   6.193  -1.058  1.00 45.21           C  
ATOM   2029  CG1 ILE A 255      25.199   6.362  -1.004  1.00 45.84           C  
ATOM   2030  CG2 ILE A 255      27.072   4.731  -0.785  1.00 44.71           C  
ATOM   2031  CD1 ILE A 255      24.448   5.578  -2.093  1.00 46.69           C  
ATOM   2032  N   ILE A 256      29.661   7.565  -0.888  1.00 44.43           N  
ATOM   2033  CA  ILE A 256      31.115   7.444  -0.880  1.00 43.60           C  
ATOM   2034  C   ILE A 256      31.652   8.047   0.398  1.00 42.79           C  
ATOM   2035  O   ILE A 256      32.559   7.495   0.996  1.00 42.65           O  
ATOM   2036  CB  ILE A 256      31.740   8.179  -2.066  1.00 43.75           C  
ATOM   2037  CG1 ILE A 256      31.471   7.388  -3.335  1.00 42.66           C  
ATOM   2038  CG2 ILE A 256      33.246   8.358  -1.844  1.00 44.53           C  
ATOM   2039  CD1 ILE A 256      32.159   6.070  -3.337  1.00 41.65           C  
ATOM   2040  N   MET A 257      31.075   9.174   0.804  1.00 42.42           N  
ATOM   2041  CA  MET A 257      31.468   9.884   2.018  1.00 42.19           C  
ATOM   2042  C   MET A 257      31.347   8.999   3.227  1.00 42.81           C  
ATOM   2043  O   MET A 257      32.082   9.187   4.207  1.00 43.63           O  
ATOM   2044  CB  MET A 257      30.577  11.102   2.235  1.00 41.19           C  
ATOM   2045  CG  MET A 257      30.908  12.306   1.401  1.00 39.27           C  
ATOM   2046  SD  MET A 257      29.728  13.579   1.841  1.00 39.18           S  
ATOM   2047  CE  MET A 257      30.372  14.233   3.378  1.00 37.64           C  
ATOM   2048  N   VAL A 258      30.409   8.061   3.179  1.00 43.16           N  
ATOM   2049  CA  VAL A 258      30.193   7.135   4.286  1.00 43.38           C  
ATOM   2050  C   VAL A 258      31.281   6.062   4.293  1.00 43.98           C  
ATOM   2051  O   VAL A 258      31.797   5.710   5.354  1.00 44.33           O  
ATOM   2052  CB  VAL A 258      28.814   6.467   4.174  1.00 43.33           C  
ATOM   2053  CG1 VAL A 258      28.648   5.449   5.281  1.00 43.91           C  
ATOM   2054  CG2 VAL A 258      27.718   7.529   4.235  1.00 42.59           C  
ATOM   2055  N   ILE A 259      31.630   5.546   3.119  1.00 44.13           N  
ATOM   2056  CA  ILE A 259      32.672   4.529   3.016  1.00 45.06           C  
ATOM   2057  C   ILE A 259      33.989   5.115   3.486  1.00 45.69           C  
ATOM   2058  O   ILE A 259      34.750   4.442   4.181  1.00 46.83           O  
ATOM   2059  CB  ILE A 259      32.835   4.056   1.541  1.00 45.80           C  
ATOM   2060  CG1 ILE A 259      31.572   3.331   1.086  1.00 46.47           C  
ATOM   2061  CG2 ILE A 259      34.010   3.123   1.399  1.00 44.22           C  
ATOM   2062  CD1 ILE A 259      31.193   2.204   2.003  1.00 46.71           C  
ATOM   2063  N   ALA A 260      34.255   6.365   3.108  1.00 45.07           N  
ATOM   2064  CA  ALA A 260      35.497   7.036   3.476  1.00 44.89           C  
ATOM   2065  C   ALA A 260      35.573   7.196   4.972  1.00 44.97           C  
ATOM   2066  O   ALA A 260      36.650   7.069   5.539  1.00 45.90           O  
ATOM   2067  CB  ALA A 260      35.600   8.407   2.781  1.00 43.92           C  
ATOM   2068  N   PHE A 261      34.443   7.463   5.615  1.00 44.53           N  
ATOM   2069  CA  PHE A 261      34.422   7.635   7.063  1.00 44.07           C  
ATOM   2070  C   PHE A 261      34.803   6.338   7.774  1.00 43.80           C  
ATOM   2071  O   PHE A 261      35.666   6.346   8.654  1.00 44.56           O  
ATOM   2072  CB  PHE A 261      33.028   8.069   7.530  1.00 44.15           C  
ATOM   2073  CG  PHE A 261      32.941   8.332   9.012  1.00 44.17           C  
ATOM   2074  CD1 PHE A 261      33.192   9.604   9.520  1.00 44.40           C  
ATOM   2075  CD2 PHE A 261      32.651   7.297   9.905  1.00 44.48           C  
ATOM   2076  CE1 PHE A 261      33.157   9.840  10.898  1.00 44.74           C  
ATOM   2077  CE2 PHE A 261      32.615   7.518  11.284  1.00 44.33           C  
ATOM   2078  CZ  PHE A 261      32.867   8.786  11.784  1.00 45.11           C  
ATOM   2079  N   LEU A 262      34.158   5.240   7.401  1.00 43.01           N  
ATOM   2080  CA  LEU A 262      34.404   3.942   8.027  1.00 42.82           C  
ATOM   2081  C   LEU A 262      35.836   3.495   7.867  1.00 42.93           C  
ATOM   2082  O   LEU A 262      36.436   3.010   8.836  1.00 43.71           O  
ATOM   2083  CB  LEU A 262      33.462   2.923   7.424  1.00 43.19           C  
ATOM   2084  CG  LEU A 262      32.027   3.393   7.628  1.00 42.97           C  
ATOM   2085  CD1 LEU A 262      31.158   2.787   6.571  1.00 43.65           C  
ATOM   2086  CD2 LEU A 262      31.553   3.040   9.022  1.00 42.36           C  
ATOM   2087  N   ILE A 263      36.375   3.633   6.656  1.00 42.66           N  
ATOM   2088  CA  ILE A 263      37.760   3.269   6.375  1.00 41.22           C  
ATOM   2089  C   ILE A 263      38.659   4.009   7.361  1.00 41.96           C  
ATOM   2090  O   ILE A 263      39.573   3.448   7.963  1.00 42.34           O  
ATOM   2091  CB  ILE A 263      38.136   3.701   4.956  1.00 39.00           C  
ATOM   2092  CG1 ILE A 263      37.361   2.877   3.952  1.00 37.98           C  
ATOM   2093  CG2 ILE A 263      39.611   3.555   4.734  1.00 37.48           C  
ATOM   2094  CD1 ILE A 263      37.689   3.236   2.544  1.00 38.11           C  
ATOM   2095  N   CYS A 264      38.345   5.279   7.535  1.00 42.37           N  
ATOM   2096  CA  CYS A 264      39.088   6.173   8.382  1.00 42.51           C  
ATOM   2097  C   CYS A 264      38.882   5.909   9.844  1.00 42.47           C  
ATOM   2098  O   CYS A 264      39.824   6.081  10.595  1.00 43.11           O  
ATOM   2099  CB  CYS A 264      38.651   7.590   8.067  1.00 43.80           C  
ATOM   2100  SG  CYS A 264      39.838   8.849   8.435  1.00 48.58           S  
ATOM   2101  N   TRP A 265      37.697   5.480  10.272  1.00 41.32           N  
ATOM   2102  CA  TRP A 265      37.491   5.322  11.714  1.00 39.88           C  
ATOM   2103  C   TRP A 265      37.334   3.916  12.252  1.00 39.83           C  
ATOM   2104  O   TRP A 265      37.499   3.734  13.472  1.00 40.40           O  
ATOM   2105  CB  TRP A 265      36.302   6.178  12.158  1.00 39.25           C  
ATOM   2106  CG  TRP A 265      36.600   7.618  12.005  1.00 39.65           C  
ATOM   2107  CD1 TRP A 265      36.220   8.441  10.980  1.00 39.45           C  
ATOM   2108  CD2 TRP A 265      37.411   8.406  12.875  1.00 39.47           C  
ATOM   2109  NE1 TRP A 265      36.745   9.701  11.159  1.00 38.24           N  
ATOM   2110  CE2 TRP A 265      37.480   9.709  12.314  1.00 39.12           C  
ATOM   2111  CE3 TRP A 265      38.093   8.142  14.074  1.00 37.66           C  
ATOM   2112  CZ2 TRP A 265      38.201  10.743  12.920  1.00 38.36           C  
ATOM   2113  CZ3 TRP A 265      38.805   9.159  14.664  1.00 38.25           C  
ATOM   2114  CH2 TRP A 265      38.855  10.449  14.089  1.00 38.43           C  
ATOM   2115  N   LEU A 266      37.030   2.935  11.413  1.00 39.42           N  
ATOM   2116  CA  LEU A 266      36.858   1.588  11.929  1.00 39.21           C  
ATOM   2117  C   LEU A 266      38.126   1.071  12.571  1.00 39.24           C  
ATOM   2118  O   LEU A 266      38.090   0.541  13.670  1.00 38.45           O  
ATOM   2119  CB  LEU A 266      36.379   0.655  10.820  1.00 39.10           C  
ATOM   2120  CG  LEU A 266      34.875   0.324  10.837  1.00 38.25           C  
ATOM   2121  CD1 LEU A 266      34.118   1.234  11.783  1.00 39.64           C  
ATOM   2122  CD2 LEU A 266      34.332   0.443   9.443  1.00 37.96           C  
ATOM   2123  N   PRO A 267      39.272   1.228  11.912  1.00 39.49           N  
ATOM   2124  CA  PRO A 267      40.477   0.716  12.563  1.00 40.11           C  
ATOM   2125  C   PRO A 267      40.749   1.331  13.940  1.00 41.36           C  
ATOM   2126  O   PRO A 267      41.090   0.617  14.901  1.00 42.76           O  
ATOM   2127  CB  PRO A 267      41.570   0.993  11.530  1.00 39.26           C  
ATOM   2128  CG  PRO A 267      40.977   2.066  10.639  1.00 40.20           C  
ATOM   2129  CD  PRO A 267      39.549   1.698  10.546  1.00 39.36           C  
ATOM   2130  N   TYR A 268      40.593   2.642  14.050  1.00 42.00           N  
ATOM   2131  CA  TYR A 268      40.812   3.318  15.320  1.00 41.67           C  
ATOM   2132  C   TYR A 268      39.838   2.784  16.331  1.00 42.42           C  
ATOM   2133  O   TYR A 268      40.241   2.234  17.354  1.00 43.35           O  
ATOM   2134  CB  TYR A 268      40.571   4.818  15.178  1.00 40.92           C  
ATOM   2135  CG  TYR A 268      40.671   5.531  16.501  1.00 39.54           C  
ATOM   2136  CD1 TYR A 268      41.894   5.629  17.154  1.00 38.40           C  
ATOM   2137  CD2 TYR A 268      39.533   6.045  17.137  1.00 38.80           C  
ATOM   2138  CE1 TYR A 268      41.990   6.206  18.388  1.00 37.50           C  
ATOM   2139  CE2 TYR A 268      39.622   6.621  18.376  1.00 37.29           C  
ATOM   2140  CZ  TYR A 268      40.858   6.698  18.994  1.00 38.68           C  
ATOM   2141  OH  TYR A 268      40.988   7.267  20.233  1.00 40.78           O  
ATOM   2142  N   ALA A 269      38.554   2.972  16.040  1.00 42.70           N  
ATOM   2143  CA  ALA A 269      37.483   2.528  16.911  1.00 42.74           C  
ATOM   2144  C   ALA A 269      37.695   1.078  17.281  1.00 42.80           C  
ATOM   2145  O   ALA A 269      37.456   0.697  18.424  1.00 42.60           O  
ATOM   2146  CB  ALA A 269      36.140   2.712  16.214  1.00 41.88           C  
ATOM   2147  N   GLY A 270      38.147   0.274  16.327  1.00 43.14           N  
ATOM   2148  CA  GLY A 270      38.382  -1.136  16.605  1.00 43.35           C  
ATOM   2149  C   GLY A 270      39.465  -1.386  17.648  1.00 43.39           C  
ATOM   2150  O   GLY A 270      39.268  -2.126  18.610  1.00 44.19           O  
ATOM   2151  N   VAL A 271      40.623  -0.760  17.453  1.00 42.36           N  
ATOM   2152  CA  VAL A 271      41.699  -0.911  18.404  1.00 40.60           C  
ATOM   2153  C   VAL A 271      41.219  -0.377  19.725  1.00 41.41           C  
ATOM   2154  O   VAL A 271      41.452  -1.011  20.730  1.00 42.69           O  
ATOM   2155  CB  VAL A 271      42.942  -0.139  17.974  1.00 39.21           C  
ATOM   2156  CG1 VAL A 271      43.997  -0.177  19.079  1.00 38.17           C  
ATOM   2157  CG2 VAL A 271      43.483  -0.744  16.705  1.00 38.95           C  
ATOM   2158  N   ALA A 272      40.524   0.760  19.710  1.00 41.11           N  
ATOM   2159  CA  ALA A 272      40.018   1.405  20.924  1.00 40.53           C  
ATOM   2160  C   ALA A 272      39.068   0.497  21.697  1.00 40.69           C  
ATOM   2161  O   ALA A 272      39.143   0.418  22.933  1.00 40.45           O  
ATOM   2162  CB  ALA A 272      39.322   2.699  20.564  1.00 38.67           C  
ATOM   2163  N   PHE A 273      38.176  -0.189  21.000  1.00 40.87           N  
ATOM   2164  CA  PHE A 273      37.256  -1.052  21.710  1.00 42.13           C  
ATOM   2165  C   PHE A 273      38.005  -2.212  22.323  1.00 42.38           C  
ATOM   2166  O   PHE A 273      37.740  -2.602  23.468  1.00 42.82           O  
ATOM   2167  CB  PHE A 273      36.190  -1.596  20.778  1.00 43.26           C  
ATOM   2168  CG  PHE A 273      35.111  -2.324  21.500  1.00 44.26           C  
ATOM   2169  CD1 PHE A 273      34.190  -1.621  22.280  1.00 44.29           C  
ATOM   2170  CD2 PHE A 273      35.062  -3.712  21.478  1.00 44.41           C  
ATOM   2171  CE1 PHE A 273      33.236  -2.288  23.034  1.00 44.36           C  
ATOM   2172  CE2 PHE A 273      34.116  -4.394  22.224  1.00 44.22           C  
ATOM   2173  CZ  PHE A 273      33.199  -3.680  23.009  1.00 44.78           C  
ATOM   2174  N   TYR A 274      38.932  -2.769  21.553  1.00 42.58           N  
ATOM   2175  CA  TYR A 274      39.743  -3.895  22.002  1.00 42.30           C  
ATOM   2176  C   TYR A 274      40.352  -3.572  23.340  1.00 42.26           C  
ATOM   2177  O   TYR A 274      40.076  -4.232  24.333  1.00 43.54           O  
ATOM   2178  CB  TYR A 274      40.861  -4.156  21.005  1.00 42.30           C  
ATOM   2179  CG  TYR A 274      41.764  -5.270  21.434  1.00 44.18           C  
ATOM   2180  CD1 TYR A 274      41.470  -6.583  21.111  1.00 45.76           C  
ATOM   2181  CD2 TYR A 274      42.898  -5.018  22.195  1.00 45.63           C  
ATOM   2182  CE1 TYR A 274      42.285  -7.634  21.534  1.00 47.47           C  
ATOM   2183  CE2 TYR A 274      43.725  -6.057  22.626  1.00 46.88           C  
ATOM   2184  CZ  TYR A 274      43.412  -7.368  22.290  1.00 48.39           C  
ATOM   2185  OH  TYR A 274      44.231  -8.412  22.690  1.00 50.20           O  
ATOM   2186  N   ILE A 275      41.194  -2.548  23.342  1.00 41.35           N  
ATOM   2187  CA  ILE A 275      41.889  -2.074  24.528  1.00 40.94           C  
ATOM   2188  C   ILE A 275      40.926  -1.914  25.670  1.00 41.10           C  
ATOM   2189  O   ILE A 275      41.246  -2.288  26.793  1.00 40.37           O  
ATOM   2190  CB  ILE A 275      42.585  -0.709  24.245  1.00 40.44           C  
ATOM   2191  CG1 ILE A 275      43.772  -0.925  23.301  1.00 40.17           C  
ATOM   2192  CG2 ILE A 275      43.014  -0.048  25.556  1.00 39.62           C  
ATOM   2193  CD1 ILE A 275      44.196   0.310  22.557  1.00 40.42           C  
ATOM   2194  N   PHE A 276      39.752  -1.356  25.396  1.00 41.67           N  
ATOM   2195  CA  PHE A 276      38.779  -1.147  26.457  1.00 42.21           C  
ATOM   2196  C   PHE A 276      38.413  -2.486  27.029  1.00 42.27           C  
ATOM   2197  O   PHE A 276      38.315  -2.659  28.247  1.00 42.68           O  
ATOM   2198  CB  PHE A 276      37.529  -0.446  25.914  1.00 40.99           C  
ATOM   2199  CG  PHE A 276      36.482  -0.186  26.962  1.00 38.90           C  
ATOM   2200  CD1 PHE A 276      36.734   0.687  28.015  1.00 38.05           C  
ATOM   2201  CD2 PHE A 276      35.245  -0.818  26.902  1.00 37.02           C  
ATOM   2202  CE1 PHE A 276      35.765   0.927  28.989  1.00 36.37           C  
ATOM   2203  CE2 PHE A 276      34.282  -0.577  27.873  1.00 35.04           C  
ATOM   2204  CZ  PHE A 276      34.544   0.296  28.915  1.00 34.91           C  
ATOM   2205  N   THR A 277      38.251  -3.448  26.142  1.00 42.46           N  
ATOM   2206  CA  THR A 277      37.876  -4.775  26.556  1.00 43.62           C  
ATOM   2207  C   THR A 277      39.092  -5.609  26.926  1.00 44.75           C  
ATOM   2208  O   THR A 277      38.947  -6.764  27.273  1.00 45.69           O  
ATOM   2209  CB  THR A 277      37.071  -5.447  25.451  1.00 43.11           C  
ATOM   2210  OG1 THR A 277      37.854  -5.508  24.255  1.00 43.75           O  
ATOM   2211  CG2 THR A 277      35.812  -4.641  25.181  1.00 42.27           C  
ATOM   2212  N   HIS A 278      40.289  -5.044  26.861  1.00 45.24           N  
ATOM   2213  CA  HIS A 278      41.483  -5.804  27.235  1.00 45.15           C  
ATOM   2214  C   HIS A 278      42.454  -4.871  27.939  1.00 45.51           C  
ATOM   2215  O   HIS A 278      43.643  -4.848  27.626  1.00 45.87           O  
ATOM   2216  CB  HIS A 278      42.148  -6.413  25.998  1.00 45.98           C  
ATOM   2217  CG  HIS A 278      41.332  -7.472  25.326  1.00 47.26           C  
ATOM   2218  ND1 HIS A 278      40.135  -7.206  24.696  1.00 47.71           N  
ATOM   2219  CD2 HIS A 278      41.537  -8.806  25.193  1.00 47.73           C  
ATOM   2220  CE1 HIS A 278      39.639  -8.330  24.205  1.00 48.83           C  
ATOM   2221  NE2 HIS A 278      40.470  -9.316  24.493  1.00 48.11           N  
ATOM   2222  N   GLN A 279      41.941  -4.105  28.890  1.00 44.65           N  
ATOM   2223  CA  GLN A 279      42.743  -3.146  29.618  1.00 44.79           C  
ATOM   2224  C   GLN A 279      43.864  -3.871  30.345  1.00 44.79           C  
ATOM   2225  O   GLN A 279      43.640  -4.936  30.873  1.00 45.93           O  
ATOM   2226  CB  GLN A 279      41.822  -2.400  30.587  1.00 44.85           C  
ATOM   2227  CG  GLN A 279      40.492  -2.055  29.930  1.00 46.41           C  
ATOM   2228  CD  GLN A 279      39.481  -1.432  30.868  1.00 47.55           C  
ATOM   2229  OE1 GLN A 279      39.399  -0.207  30.997  1.00 49.15           O  
ATOM   2230  NE2 GLN A 279      38.701  -2.275  31.531  1.00 46.51           N  
ATOM   2231  N   GLY A 280      45.075  -3.323  30.338  1.00 44.86           N  
ATOM   2232  CA  GLY A 280      46.174  -3.959  31.053  1.00 44.15           C  
ATOM   2233  C   GLY A 280      46.905  -5.103  30.371  1.00 44.62           C  
ATOM   2234  O   GLY A 280      47.923  -5.588  30.880  1.00 45.40           O  
ATOM   2235  N   SER A 281      46.386  -5.540  29.229  1.00 44.32           N  
ATOM   2236  CA  SER A 281      47.003  -6.617  28.476  1.00 44.32           C  
ATOM   2237  C   SER A 281      48.261  -6.115  27.827  1.00 44.28           C  
ATOM   2238  O   SER A 281      48.593  -4.935  27.948  1.00 43.43           O  
ATOM   2239  CB  SER A 281      46.048  -7.154  27.418  1.00 45.59           C  
ATOM   2240  OG  SER A 281      45.542  -6.112  26.606  1.00 46.94           O  
ATOM   2241  N   ASP A 282      48.934  -6.994  27.097  1.00 44.44           N  
ATOM   2242  CA  ASP A 282      50.206  -6.643  26.508  1.00 45.21           C  
ATOM   2243  C   ASP A 282      50.185  -6.109  25.075  1.00 45.22           C  
ATOM   2244  O   ASP A 282      50.551  -6.832  24.154  1.00 46.38           O  
ATOM   2245  CB  ASP A 282      51.134  -7.851  26.592  1.00 47.94           C  
ATOM   2246  CG  ASP A 282      52.594  -7.489  26.337  1.00 51.12           C  
ATOM   2247  OD1 ASP A 282      52.899  -6.273  26.283  1.00 53.22           O  
ATOM   2248  OD2 ASP A 282      53.436  -8.419  26.208  1.00 53.02           O  
ATOM   2249  N   PHE A 283      49.777  -4.861  24.871  1.00 43.61           N  
ATOM   2250  CA  PHE A 283      49.839  -4.277  23.535  1.00 41.92           C  
ATOM   2251  C   PHE A 283      50.973  -3.270  23.555  1.00 41.71           C  
ATOM   2252  O   PHE A 283      51.353  -2.827  24.633  1.00 41.81           O  
ATOM   2253  CB  PHE A 283      48.512  -3.604  23.130  1.00 41.74           C  
ATOM   2254  CG  PHE A 283      47.867  -2.805  24.211  1.00 40.74           C  
ATOM   2255  CD1 PHE A 283      46.885  -3.368  25.008  1.00 40.95           C  
ATOM   2256  CD2 PHE A 283      48.247  -1.489  24.442  1.00 41.36           C  
ATOM   2257  CE1 PHE A 283      46.285  -2.635  26.028  1.00 40.95           C  
ATOM   2258  CE2 PHE A 283      47.656  -0.743  25.459  1.00 41.42           C  
ATOM   2259  CZ  PHE A 283      46.671  -1.319  26.257  1.00 40.99           C  
ATOM   2260  N   GLY A 284      51.525  -2.911  22.398  1.00 42.13           N  
ATOM   2261  CA  GLY A 284      52.632  -1.960  22.386  1.00 41.42           C  
ATOM   2262  C   GLY A 284      52.278  -0.583  21.869  1.00 41.15           C  
ATOM   2263  O   GLY A 284      51.132  -0.349  21.492  1.00 41.21           O  
ATOM   2264  N   PRO A 285      53.249   0.348  21.821  1.00 40.27           N  
ATOM   2265  CA  PRO A 285      53.005   1.717  21.338  1.00 40.52           C  
ATOM   2266  C   PRO A 285      52.540   1.859  19.889  1.00 41.14           C  
ATOM   2267  O   PRO A 285      51.765   2.756  19.576  1.00 42.79           O  
ATOM   2268  CB  PRO A 285      54.348   2.423  21.593  1.00 39.31           C  
ATOM   2269  CG  PRO A 285      55.334   1.332  21.465  1.00 39.28           C  
ATOM   2270  CD  PRO A 285      54.661   0.177  22.201  1.00 39.35           C  
ATOM   2271  N   ILE A 286      52.996   0.976  19.010  1.00 41.31           N  
ATOM   2272  CA  ILE A 286      52.630   1.068  17.598  1.00 40.83           C  
ATOM   2273  C   ILE A 286      51.182   0.675  17.402  1.00 40.23           C  
ATOM   2274  O   ILE A 286      50.502   1.235  16.543  1.00 40.30           O  
ATOM   2275  CB  ILE A 286      53.541   0.156  16.725  1.00 41.27           C  
ATOM   2276  CG1 ILE A 286      55.026   0.364  17.092  1.00 41.51           C  
ATOM   2277  CG2 ILE A 286      53.308   0.454  15.256  1.00 41.59           C  
ATOM   2278  CD1 ILE A 286      55.574   1.772  16.896  1.00 41.86           C  
ATOM   2279  N   PHE A 287      50.723  -0.275  18.208  1.00 39.88           N  
ATOM   2280  CA  PHE A 287      49.361  -0.774  18.140  1.00 38.89           C  
ATOM   2281  C   PHE A 287      48.375   0.329  17.787  1.00 39.45           C  
ATOM   2282  O   PHE A 287      47.716   0.250  16.741  1.00 40.57           O  
ATOM   2283  CB  PHE A 287      48.985  -1.418  19.481  1.00 38.14           C  
ATOM   2284  CG  PHE A 287      47.660  -2.146  19.470  1.00 36.53           C  
ATOM   2285  CD1 PHE A 287      47.263  -2.900  18.367  1.00 36.38           C  
ATOM   2286  CD2 PHE A 287      46.846  -2.148  20.600  1.00 36.07           C  
ATOM   2287  CE1 PHE A 287      46.081  -3.647  18.397  1.00 34.98           C  
ATOM   2288  CE2 PHE A 287      45.665  -2.891  20.644  1.00 34.56           C  
ATOM   2289  CZ  PHE A 287      45.286  -3.638  19.544  1.00 35.29           C  
ATOM   2290  N   MET A 288      48.287   1.369  18.611  1.00 39.45           N  
ATOM   2291  CA  MET A 288      47.308   2.441  18.378  1.00 38.54           C  
ATOM   2292  C   MET A 288      47.852   3.639  17.604  1.00 37.07           C  
ATOM   2293  O   MET A 288      47.081   4.466  17.122  1.00 36.39           O  
ATOM   2294  CB  MET A 288      46.718   2.892  19.721  1.00 39.66           C  
ATOM   2295  CG  MET A 288      45.702   4.014  19.623  1.00 40.12           C  
ATOM   2296  SD  MET A 288      44.301   3.691  18.533  1.00 42.85           S  
ATOM   2297  CE  MET A 288      42.959   3.521  19.732  1.00 41.67           C  
ATOM   2298  N   THR A 289      49.156   3.747  17.456  1.00 35.49           N  
ATOM   2299  CA  THR A 289      49.665   4.885  16.726  1.00 34.85           C  
ATOM   2300  C   THR A 289      49.176   4.855  15.280  1.00 35.92           C  
ATOM   2301  O   THR A 289      48.738   5.880  14.749  1.00 36.62           O  
ATOM   2302  CB  THR A 289      51.198   4.906  16.759  1.00 33.72           C  
ATOM   2303  OG1 THR A 289      51.637   5.052  18.113  1.00 34.25           O  
ATOM   2304  CG2 THR A 289      51.732   6.051  15.941  1.00 32.04           C  
ATOM   2305  N   ILE A 290      49.220   3.689  14.650  1.00 35.96           N  
ATOM   2306  CA  ILE A 290      48.832   3.593  13.252  1.00 35.16           C  
ATOM   2307  C   ILE A 290      47.394   4.019  12.952  1.00 35.52           C  
ATOM   2308  O   ILE A 290      47.197   4.883  12.112  1.00 36.96           O  
ATOM   2309  CB  ILE A 290      49.043   2.176  12.703  1.00 35.47           C  
ATOM   2310  CG1 ILE A 290      50.435   1.656  13.076  1.00 34.59           C  
ATOM   2311  CG2 ILE A 290      48.853   2.206  11.187  1.00 34.87           C  
ATOM   2312  CD1 ILE A 290      51.532   2.352  12.374  1.00 34.48           C  
ATOM   2313  N   PRO A 291      46.379   3.430  13.607  1.00 34.86           N  
ATOM   2314  CA  PRO A 291      45.019   3.869  13.270  1.00 34.25           C  
ATOM   2315  C   PRO A 291      44.718   5.255  13.787  1.00 35.04           C  
ATOM   2316  O   PRO A 291      43.953   5.975  13.170  1.00 36.09           O  
ATOM   2317  CB  PRO A 291      44.139   2.802  13.915  1.00 33.39           C  
ATOM   2318  CG  PRO A 291      44.890   2.438  15.107  1.00 34.45           C  
ATOM   2319  CD  PRO A 291      46.334   2.348  14.606  1.00 34.66           C  
ATOM   2320  N   ALA A 292      45.324   5.625  14.912  1.00 35.81           N  
ATOM   2321  CA  ALA A 292      45.124   6.937  15.514  1.00 36.76           C  
ATOM   2322  C   ALA A 292      45.592   8.020  14.564  1.00 37.75           C  
ATOM   2323  O   ALA A 292      44.862   8.992  14.332  1.00 38.27           O  
ATOM   2324  CB  ALA A 292      45.887   7.029  16.820  1.00 36.63           C  
ATOM   2325  N   PHE A 293      46.797   7.870  14.013  1.00 38.23           N  
ATOM   2326  CA  PHE A 293      47.332   8.878  13.092  1.00 38.11           C  
ATOM   2327  C   PHE A 293      46.714   8.764  11.696  1.00 38.26           C  
ATOM   2328  O   PHE A 293      46.587   9.786  11.031  1.00 39.16           O  
ATOM   2329  CB  PHE A 293      48.881   8.812  13.022  1.00 36.80           C  
ATOM   2330  CG  PHE A 293      49.585   9.672  14.071  1.00 36.11           C  
ATOM   2331  CD1 PHE A 293      49.547   9.322  15.428  1.00 35.60           C  
ATOM   2332  CD2 PHE A 293      50.225  10.870  13.706  1.00 35.54           C  
ATOM   2333  CE1 PHE A 293      50.126  10.153  16.400  1.00 35.37           C  
ATOM   2334  CE2 PHE A 293      50.804  11.707  14.669  1.00 34.82           C  
ATOM   2335  CZ  PHE A 293      50.754  11.352  16.014  1.00 35.32           C  
ATOM   2336  N   PHE A 294      46.326   7.561  11.263  1.00 38.34           N  
ATOM   2337  CA  PHE A 294      45.732   7.396   9.940  1.00 37.55           C  
ATOM   2338  C   PHE A 294      44.389   8.078   9.893  1.00 37.97           C  
ATOM   2339  O   PHE A 294      44.026   8.649   8.875  1.00 38.24           O  
ATOM   2340  CB  PHE A 294      45.538   5.922   9.598  1.00 36.40           C  
ATOM   2341  CG  PHE A 294      44.619   5.700   8.433  1.00 34.43           C  
ATOM   2342  CD1 PHE A 294      44.939   6.185   7.178  1.00 34.10           C  
ATOM   2343  CD2 PHE A 294      43.411   5.053   8.598  1.00 34.69           C  
ATOM   2344  CE1 PHE A 294      44.069   6.030   6.101  1.00 34.06           C  
ATOM   2345  CE2 PHE A 294      42.530   4.893   7.519  1.00 34.79           C  
ATOM   2346  CZ  PHE A 294      42.865   5.383   6.275  1.00 34.72           C  
ATOM   2347  N   ALA A 295      43.659   8.005  11.001  1.00 39.05           N  
ATOM   2348  CA  ALA A 295      42.330   8.596  11.118  1.00 39.24           C  
ATOM   2349  C   ALA A 295      42.377  10.104  10.979  1.00 40.30           C  
ATOM   2350  O   ALA A 295      41.348  10.698  10.651  1.00 41.34           O  
ATOM   2351  CB  ALA A 295      41.707   8.218  12.446  1.00 38.03           C  
ATOM   2352  N   LYS A 296      43.538  10.727  11.209  1.00 40.81           N  
ATOM   2353  CA  LYS A 296      43.652  12.188  11.096  1.00 40.30           C  
ATOM   2354  C   LYS A 296      43.513  12.639   9.657  1.00 40.53           C  
ATOM   2355  O   LYS A 296      43.510  13.830   9.428  1.00 41.84           O  
ATOM   2356  CB  LYS A 296      44.959  12.672  11.641  1.00 39.15           C  
ATOM   2357  CG  LYS A 296      45.045  12.291  13.101  1.00 40.26           C  
ATOM   2358  CD  LYS A 296      46.393  12.695  13.669  1.00 40.04           C  
ATOM   2359  CE  LYS A 296      46.627  12.709  15.174  1.00 39.92           C  
ATOM   2360  NZ  LYS A 296      45.589  12.484  16.204  1.00 41.03           N  
ATOM   2361  N   THR A 297      43.430  11.724   8.693  1.00 40.51           N  
ATOM   2362  CA  THR A 297      43.258  12.147   7.309  1.00 39.77           C  
ATOM   2363  C   THR A 297      41.806  12.562   7.125  1.00 39.47           C  
ATOM   2364  O   THR A 297      41.417  13.080   6.070  1.00 39.23           O  
ATOM   2365  CB  THR A 297      43.636  11.025   6.313  1.00 39.22           C  
ATOM   2366  OG1 THR A 297      42.953   9.810   6.657  1.00 39.19           O  
ATOM   2367  CG2 THR A 297      45.127  10.805   6.321  1.00 37.46           C  
ATOM   2368  N   SER A 298      41.021  12.359   8.183  1.00 39.85           N  
ATOM   2369  CA  SER A 298      39.600  12.706   8.205  1.00 40.19           C  
ATOM   2370  C   SER A 298      39.404  14.208   8.059  1.00 40.81           C  
ATOM   2371  O   SER A 298      38.282  14.663   7.779  1.00 41.84           O  
ATOM   2372  CB  SER A 298      38.982  12.264   9.525  1.00 39.91           C  
ATOM   2373  OG  SER A 298      39.522  13.012  10.599  1.00 38.78           O  
ATOM   2374  N   ALA A 299      40.474  14.971   8.263  1.00 40.27           N  
ATOM   2375  CA  ALA A 299      40.401  16.420   8.162  1.00 40.56           C  
ATOM   2376  C   ALA A 299      40.595  16.845   6.742  1.00 41.33           C  
ATOM   2377  O   ALA A 299      40.545  18.049   6.462  1.00 41.15           O  
ATOM   2378  CB  ALA A 299      41.460  17.078   9.050  1.00 39.49           C  
ATOM   2379  N   VAL A 300      40.796  15.896   5.823  1.00 41.90           N  
ATOM   2380  CA  VAL A 300      41.029  16.278   4.428  1.00 42.45           C  
ATOM   2381  C   VAL A 300      40.230  15.502   3.380  1.00 42.33           C  
ATOM   2382  O   VAL A 300      39.856  16.088   2.371  1.00 42.72           O  
ATOM   2383  CB  VAL A 300      42.515  16.138   4.073  1.00 42.68           C  
ATOM   2384  CG1 VAL A 300      43.356  16.903   5.048  1.00 42.19           C  
ATOM   2385  CG2 VAL A 300      42.916  14.687   4.112  1.00 44.55           C  
ATOM   2386  N   TYR A 301      39.946  14.224   3.587  1.00 42.05           N  
ATOM   2387  CA  TYR A 301      39.275  13.498   2.521  1.00 42.24           C  
ATOM   2388  C   TYR A 301      37.918  14.034   2.166  1.00 42.58           C  
ATOM   2389  O   TYR A 301      37.562  13.923   1.014  1.00 43.44           O  
ATOM   2390  CB  TYR A 301      39.196  11.999   2.823  1.00 41.68           C  
ATOM   2391  CG  TYR A 301      38.142  11.606   3.813  1.00 41.42           C  
ATOM   2392  CD1 TYR A 301      36.794  11.573   3.459  1.00 42.24           C  
ATOM   2393  CD2 TYR A 301      38.488  11.311   5.121  1.00 41.29           C  
ATOM   2394  CE1 TYR A 301      35.813  11.265   4.402  1.00 42.59           C  
ATOM   2395  CE2 TYR A 301      37.529  10.998   6.066  1.00 42.48           C  
ATOM   2396  CZ  TYR A 301      36.192  10.982   5.713  1.00 42.81           C  
ATOM   2397  OH  TYR A 301      35.260  10.744   6.702  1.00 42.89           O  
ATOM   2398  N   ASN A 302      37.167  14.622   3.093  1.00 42.92           N  
ATOM   2399  CA  ASN A 302      35.820  15.105   2.745  1.00 43.04           C  
ATOM   2400  C   ASN A 302      35.813  16.060   1.561  1.00 43.21           C  
ATOM   2401  O   ASN A 302      35.075  15.817   0.600  1.00 43.79           O  
ATOM   2402  CB  ASN A 302      35.138  15.748   3.944  1.00 43.14           C  
ATOM   2403  CG  ASN A 302      34.535  14.720   4.876  1.00 44.68           C  
ATOM   2404  OD1 ASN A 302      34.880  14.645   6.080  1.00 45.47           O  
ATOM   2405  ND2 ASN A 302      33.630  13.905   4.332  1.00 43.72           N  
ATOM   2406  N   PRO A 303      36.606  17.153   1.604  1.00 43.10           N  
ATOM   2407  CA  PRO A 303      36.655  18.118   0.491  1.00 42.50           C  
ATOM   2408  C   PRO A 303      37.106  17.498  -0.826  1.00 41.95           C  
ATOM   2409  O   PRO A 303      36.653  17.916  -1.893  1.00 41.99           O  
ATOM   2410  CB  PRO A 303      37.646  19.170   0.987  1.00 42.71           C  
ATOM   2411  CG  PRO A 303      37.463  19.133   2.449  1.00 42.99           C  
ATOM   2412  CD  PRO A 303      37.382  17.657   2.751  1.00 42.57           C  
ATOM   2413  N   VAL A 304      37.990  16.509  -0.757  1.00 41.05           N  
ATOM   2414  CA  VAL A 304      38.475  15.873  -1.970  1.00 40.88           C  
ATOM   2415  C   VAL A 304      37.340  15.141  -2.654  1.00 40.60           C  
ATOM   2416  O   VAL A 304      37.148  15.275  -3.856  1.00 40.31           O  
ATOM   2417  CB  VAL A 304      39.641  14.893  -1.659  1.00 41.06           C  
ATOM   2418  CG1 VAL A 304      40.173  14.273  -2.937  1.00 40.35           C  
ATOM   2419  CG2 VAL A 304      40.755  15.640  -0.966  1.00 40.89           C  
ATOM   2420  N   ILE A 305      36.580  14.379  -1.884  1.00 41.11           N  
ATOM   2421  CA  ILE A 305      35.472  13.616  -2.432  1.00 42.14           C  
ATOM   2422  C   ILE A 305      34.473  14.568  -3.045  1.00 42.34           C  
ATOM   2423  O   ILE A 305      33.898  14.300  -4.097  1.00 42.73           O  
ATOM   2424  CB  ILE A 305      34.794  12.781  -1.323  1.00 42.17           C  
ATOM   2425  CG1 ILE A 305      35.799  11.781  -0.742  1.00 41.98           C  
ATOM   2426  CG2 ILE A 305      33.610  12.040  -1.884  1.00 42.40           C  
ATOM   2427  CD1 ILE A 305      35.222  10.899   0.311  1.00 42.11           C  
ATOM   2428  N   TYR A 306      34.301  15.701  -2.387  1.00 42.85           N  
ATOM   2429  CA  TYR A 306      33.358  16.733  -2.786  1.00 43.67           C  
ATOM   2430  C   TYR A 306      33.724  17.343  -4.130  1.00 44.87           C  
ATOM   2431  O   TYR A 306      32.904  17.387  -5.036  1.00 45.65           O  
ATOM   2432  CB  TYR A 306      33.357  17.786  -1.682  1.00 42.80           C  
ATOM   2433  CG  TYR A 306      32.378  18.934  -1.810  1.00 41.96           C  
ATOM   2434  CD1 TYR A 306      31.069  18.738  -2.257  1.00 41.00           C  
ATOM   2435  CD2 TYR A 306      32.743  20.210  -1.380  1.00 40.74           C  
ATOM   2436  CE1 TYR A 306      30.150  19.800  -2.264  1.00 40.31           C  
ATOM   2437  CE2 TYR A 306      31.848  21.265  -1.373  1.00 40.44           C  
ATOM   2438  CZ  TYR A 306      30.557  21.065  -1.812  1.00 41.38           C  
ATOM   2439  OH  TYR A 306      29.689  22.139  -1.767  1.00 42.20           O  
ATOM   2440  N   ILE A 307      34.954  17.811  -4.257  1.00 45.55           N  
ATOM   2441  CA  ILE A 307      35.397  18.432  -5.484  1.00 46.20           C  
ATOM   2442  C   ILE A 307      35.446  17.432  -6.633  1.00 48.27           C  
ATOM   2443  O   ILE A 307      35.173  17.803  -7.781  1.00 49.61           O  
ATOM   2444  CB  ILE A 307      36.752  19.050  -5.253  1.00 44.78           C  
ATOM   2445  CG1 ILE A 307      36.637  19.996  -4.068  1.00 44.21           C  
ATOM   2446  CG2 ILE A 307      37.219  19.781  -6.488  1.00 44.31           C  
ATOM   2447  CD1 ILE A 307      37.939  20.413  -3.501  1.00 45.27           C  
ATOM   2448  N   MET A 308      35.767  16.175  -6.348  1.00 49.48           N  
ATOM   2449  CA  MET A 308      35.831  15.174  -7.407  1.00 50.45           C  
ATOM   2450  C   MET A 308      34.445  14.653  -7.776  1.00 51.24           C  
ATOM   2451  O   MET A 308      34.238  14.200  -8.919  1.00 51.71           O  
ATOM   2452  CB  MET A 308      36.707  13.990  -6.980  1.00 51.07           C  
ATOM   2453  CG  MET A 308      38.065  14.374  -6.431  1.00 52.58           C  
ATOM   2454  SD  MET A 308      38.902  15.651  -7.396  1.00 54.18           S  
ATOM   2455  CE  MET A 308      38.880  14.902  -8.936  1.00 54.19           C  
ATOM   2456  N   MET A 309      33.499  14.708  -6.838  1.00 52.10           N  
ATOM   2457  CA  MET A 309      32.157  14.172  -7.101  1.00 52.25           C  
ATOM   2458  C   MET A 309      31.077  15.249  -7.203  1.00 51.82           C  
ATOM   2459  O   MET A 309      29.900  14.959  -6.986  1.00 51.58           O  
ATOM   2460  CB  MET A 309      31.773  13.147  -6.024  1.00 52.34           C  
ATOM   2461  CG  MET A 309      32.688  11.931  -5.963  1.00 52.54           C  
ATOM   2462  SD  MET A 309      32.050  10.663  -4.856  1.00 53.65           S  
ATOM   2463  CE  MET A 309      30.866   9.882  -5.921  1.00 53.61           C  
ATOM   2464  N   ASN A 310      31.455  16.474  -7.539  1.00 51.27           N  
ATOM   2465  CA  ASN A 310      30.458  17.511  -7.660  1.00 50.82           C  
ATOM   2466  C   ASN A 310      30.859  18.472  -8.729  1.00 51.62           C  
ATOM   2467  O   ASN A 310      31.595  19.425  -8.455  1.00 51.79           O  
ATOM   2468  CB  ASN A 310      30.307  18.224  -6.348  1.00 49.80           C  
ATOM   2469  CG  ASN A 310      28.915  18.685  -6.128  1.00 49.50           C  
ATOM   2470  OD1 ASN A 310      28.577  19.849  -6.372  1.00 48.10           O  
ATOM   2471  ND2 ASN A 310      28.067  17.764  -5.680  1.00 49.32           N  
ATOM   2472  N   LYS A 311      30.371  18.224  -9.944  1.00 51.93           N  
ATOM   2473  CA  LYS A 311      30.693  19.042 -11.105  1.00 52.55           C  
ATOM   2474  C   LYS A 311      30.421  20.504 -10.825  1.00 52.34           C  
ATOM   2475  O   LYS A 311      31.208  21.347 -11.255  1.00 53.34           O  
ATOM   2476  CB  LYS A 311      29.879  18.577 -12.320  1.00 53.76           C  
ATOM   2477  CG  LYS A 311      30.543  18.809 -13.696  1.00 56.46           C  
ATOM   2478  CD  LYS A 311      31.240  17.531 -14.257  1.00 58.75           C  
ATOM   2479  CE  LYS A 311      31.672  17.659 -15.744  1.00 59.26           C  
ATOM   2480  NZ  LYS A 311      32.651  18.760 -15.986  1.00 59.04           N  
ATOM   2481  N   GLN A 312      29.345  20.815 -10.099  1.00 51.86           N  
ATOM   2482  CA  GLN A 312      29.012  22.211  -9.821  1.00 50.97           C  
ATOM   2483  C   GLN A 312      29.961  22.877  -8.862  1.00 50.06           C  
ATOM   2484  O   GLN A 312      30.321  24.020  -9.094  1.00 50.53           O  
ATOM   2485  CB  GLN A 312      27.604  22.366  -9.265  1.00 51.93           C  
ATOM   2486  CG  GLN A 312      27.317  23.836  -8.887  1.00 54.40           C  
ATOM   2487  CD  GLN A 312      25.913  24.089  -8.310  1.00 55.80           C  
ATOM   2488  OE1 GLN A 312      25.533  23.541  -7.262  1.00 56.77           O  
ATOM   2489  NE2 GLN A 312      25.143  24.935  -8.991  1.00 56.38           N  
ATOM   2490  N   PHE A 313      30.348  22.213  -7.777  1.00 48.56           N  
ATOM   2491  CA  PHE A 313      31.258  22.840  -6.832  1.00 45.99           C  
ATOM   2492  C   PHE A 313      32.636  22.944  -7.431  1.00 45.66           C  
ATOM   2493  O   PHE A 313      33.309  23.938  -7.231  1.00 44.31           O  
ATOM   2494  CB  PHE A 313      31.322  22.043  -5.549  1.00 45.26           C  
ATOM   2495  CG  PHE A 313      32.146  22.694  -4.503  1.00 44.35           C  
ATOM   2496  CD1 PHE A 313      31.658  23.793  -3.810  1.00 43.88           C  
ATOM   2497  CD2 PHE A 313      33.438  22.242  -4.239  1.00 44.61           C  
ATOM   2498  CE1 PHE A 313      32.444  24.440  -2.866  1.00 44.09           C  
ATOM   2499  CE2 PHE A 313      34.238  22.878  -3.296  1.00 44.31           C  
ATOM   2500  CZ  PHE A 313      33.742  23.980  -2.607  1.00 44.15           C  
ATOM   2501  N   ARG A 314      33.049  21.912  -8.159  1.00 46.07           N  
ATOM   2502  CA  ARG A 314      34.356  21.887  -8.811  1.00 46.86           C  
ATOM   2503  C   ARG A 314      34.483  23.074  -9.754  1.00 47.61           C  
ATOM   2504  O   ARG A 314      35.515  23.731  -9.806  1.00 46.24           O  
ATOM   2505  CB  ARG A 314      34.513  20.582  -9.589  1.00 45.95           C  
ATOM   2506  CG  ARG A 314      35.866  20.396 -10.220  1.00 45.03           C  
ATOM   2507  CD  ARG A 314      36.034  18.952 -10.647  1.00 44.68           C  
ATOM   2508  NE  ARG A 314      35.141  18.526 -11.725  1.00 43.80           N  
ATOM   2509  CZ  ARG A 314      34.273  17.521 -11.623  1.00 44.16           C  
ATOM   2510  NH1 ARG A 314      34.155  16.845 -10.487  1.00 44.35           N  
ATOM   2511  NH2 ARG A 314      33.564  17.142 -12.676  1.00 44.67           N  
ATOM   2512  N   ASN A 315      33.414  23.330 -10.493  1.00 49.36           N  
ATOM   2513  CA  ASN A 315      33.347  24.426 -11.444  1.00 51.80           C  
ATOM   2514  C   ASN A 315      33.394  25.754 -10.746  1.00 53.62           C  
ATOM   2515  O   ASN A 315      34.075  26.657 -11.213  1.00 54.30           O  
ATOM   2516  CB  ASN A 315      32.060  24.327 -12.233  1.00 52.21           C  
ATOM   2517  CG  ASN A 315      32.256  23.663 -13.544  1.00 54.38           C  
ATOM   2518  OD1 ASN A 315      32.756  24.282 -14.477  1.00 57.05           O  
ATOM   2519  ND2 ASN A 315      31.890  22.386 -13.633  1.00 55.09           N  
ATOM   2520  N   CYS A 316      32.653  25.887  -9.650  1.00 55.48           N  
ATOM   2521  CA  CYS A 316      32.641  27.139  -8.890  1.00 57.05           C  
ATOM   2522  C   CYS A 316      34.029  27.388  -8.336  1.00 58.17           C  
ATOM   2523  O   CYS A 316      34.420  28.542  -8.148  1.00 58.87           O  
ATOM   2524  CB  CYS A 316      31.617  27.089  -7.737  1.00 56.58           C  
ATOM   2525  SG  CYS A 316      29.919  27.553  -8.199  1.00 55.84           S  
ATOM   2526  N   MET A 317      34.768  26.311  -8.084  1.00 59.05           N  
ATOM   2527  CA  MET A 317      36.122  26.409  -7.562  1.00 58.87           C  
ATOM   2528  C   MET A 317      37.060  26.823  -8.689  1.00 58.41           C  
ATOM   2529  O   MET A 317      37.882  27.718  -8.503  1.00 57.38           O  
ATOM   2530  CB  MET A 317      36.547  25.062  -6.994  1.00 59.54           C  
ATOM   2531  CG  MET A 317      37.944  25.065  -6.417  1.00 60.71           C  
ATOM   2532  SD  MET A 317      38.527  23.397  -6.188  1.00 63.89           S  
ATOM   2533  CE  MET A 317      38.980  22.924  -8.005  1.00 61.24           C  
ATOM   2534  N   VAL A 318      36.941  26.167  -9.844  1.00 58.22           N  
ATOM   2535  CA  VAL A 318      37.772  26.504 -10.988  1.00 58.23           C  
ATOM   2536  C   VAL A 318      37.479  27.929 -11.342  1.00 59.38           C  
ATOM   2537  O   VAL A 318      38.385  28.688 -11.614  1.00 59.91           O  
ATOM   2538  CB  VAL A 318      37.460  25.640 -12.195  1.00 56.78           C  
ATOM   2539  CG1 VAL A 318      38.290  26.080 -13.355  1.00 55.47           C  
ATOM   2540  CG2 VAL A 318      37.745  24.206 -11.875  1.00 57.63           C  
ATOM   2541  N   THR A 319      36.205  28.299 -11.330  1.00 60.21           N  
ATOM   2542  CA  THR A 319      35.818  29.670 -11.632  1.00 60.64           C  
ATOM   2543  C   THR A 319      36.507  30.611 -10.667  1.00 61.29           C  
ATOM   2544  O   THR A 319      37.049  31.616 -11.091  1.00 61.78           O  
ATOM   2545  CB  THR A 319      34.302  29.857 -11.513  1.00 60.39           C  
ATOM   2546  OG1 THR A 319      33.664  29.357 -12.693  1.00 61.40           O  
ATOM   2547  CG2 THR A 319      33.965  31.311 -11.330  1.00 60.66           C  
ATOM   2548  N   THR A 320      36.486  30.280  -9.377  1.00 62.25           N  
ATOM   2549  CA  THR A 320      37.111  31.102  -8.340  1.00 63.22           C  
ATOM   2550  C   THR A 320      38.619  31.138  -8.531  1.00 65.00           C  
ATOM   2551  O   THR A 320      39.179  32.218  -8.667  1.00 64.19           O  
ATOM   2552  CB  THR A 320      36.794  30.550  -6.928  1.00 62.86           C  
ATOM   2553  OG1 THR A 320      35.377  30.532  -6.729  1.00 63.11           O  
ATOM   2554  CG2 THR A 320      37.410  31.422  -5.855  1.00 61.82           C  
ATOM   2555  N   LEU A 321      39.267  29.971  -8.535  1.00 67.89           N  
ATOM   2556  CA  LEU A 321      40.718  29.891  -8.713  1.00 70.92           C  
ATOM   2557  C   LEU A 321      41.160  30.667  -9.938  1.00 74.10           C  
ATOM   2558  O   LEU A 321      42.120  31.424  -9.832  1.00 74.29           O  
ATOM   2559  CB  LEU A 321      41.178  28.435  -8.847  1.00 69.23           C  
ATOM   2560  CG  LEU A 321      41.314  27.582  -7.588  1.00 67.32           C  
ATOM   2561  CD1 LEU A 321      41.736  26.185  -7.974  1.00 66.89           C  
ATOM   2562  CD2 LEU A 321      42.334  28.181  -6.669  1.00 66.28           C  
ATOM   2563  N   CYS A 322      40.482  30.487 -11.078  1.00 78.44           N  
ATOM   2564  CA  CYS A 322      40.835  31.190 -12.319  1.00 82.99           C  
ATOM   2565  C   CYS A 322      40.571  32.661 -12.178  1.00 85.44           C  
ATOM   2566  O   CYS A 322      40.216  33.310 -13.153  1.00 85.76           O  
ATOM   2567  CB  CYS A 322      40.095  30.680 -13.558  1.00 84.00           C  
ATOM   2568  SG  CYS A 322      40.200  28.891 -13.832  1.00 88.36           S  
ATOM   2569  N   CYS A 323      40.733  33.157 -10.951  1.00 88.92           N  
ATOM   2570  CA  CYS A 323      40.564  34.565 -10.579  1.00 92.40           C  
ATOM   2571  C   CYS A 323      39.303  35.137 -11.195  1.00 93.52           C  
ATOM   2572  O   CYS A 323      38.373  35.452 -10.462  1.00 94.02           O  
ATOM   2573  CB  CYS A 323      41.787  35.378 -11.000  1.00 93.13           C  
ATOM   2574  SG  CYS A 323      43.328  34.809 -10.190  1.00 97.77           S  
ATOM   2575  N   GLY A 324      39.267  35.286 -12.512  1.00 95.26           N  
ATOM   2576  CA  GLY A 324      38.075  35.806 -13.153  1.00 97.48           C  
ATOM   2577  C   GLY A 324      36.999  34.739 -13.174  1.00 99.06           C  
ATOM   2578  O   GLY A 324      36.445  34.393 -12.142  1.00 98.88           O  
ATOM   2579  N   LYS A 325      36.701  34.215 -14.354  1.00100.80           N  
ATOM   2580  CA  LYS A 325      35.694  33.172 -14.481  1.00102.88           C  
ATOM   2581  C   LYS A 325      36.211  32.128 -15.437  1.00104.27           C  
ATOM   2582  O   LYS A 325      37.259  31.515 -15.173  1.00103.95           O  
ATOM   2583  CB  LYS A 325      34.364  33.744 -15.013  1.00103.52           C  
ATOM   2584  CG  LYS A 325      33.211  32.729 -15.015  1.00103.72           C  
ATOM   2585  CD  LYS A 325      32.142  33.025 -16.055  1.00103.15           C  
ATOM   2586  CE  LYS A 325      31.171  31.867 -16.090  1.00103.27           C  
ATOM   2587  NZ  LYS A 325      30.294  31.896 -17.263  1.00102.69           N  
ATOM   2588  N   ASN A 326      35.494  31.948 -16.548  1.00105.98           N  
ATOM   2589  CA  ASN A 326      35.859  30.966 -17.554  1.00107.38           C  
ATOM   2590  C   ASN A 326      35.984  29.629 -16.849  1.00108.23           C  
ATOM   2591  O   ASN A 326      37.095  29.134 -16.639  1.00107.85           O  
ATOM   2592  CB  ASN A 326      37.176  31.381 -18.223  1.00107.78           C  
ATOM   2593  CG  ASN A 326      37.681  30.359 -19.216  1.00108.33           C  
ATOM   2594  OD1 ASN A 326      36.927  29.836 -20.045  1.00108.48           O  
ATOM   2595  ND2 ASN A 326      38.974  30.079 -19.150  1.00108.49           N  
ATOM   2596  N   PRO A 327      34.836  29.040 -16.446  1.00109.17           N  
ATOM   2597  CA  PRO A 327      34.801  27.751 -15.748  1.00109.87           C  
ATOM   2598  C   PRO A 327      35.182  26.585 -16.647  1.00110.75           C  
ATOM   2599  O   PRO A 327      34.724  25.464 -16.401  1.00111.02           O  
ATOM   2600  CB  PRO A 327      33.354  27.667 -15.257  1.00109.46           C  
ATOM   2601  CG  PRO A 327      32.602  28.328 -16.363  1.00109.53           C  
ATOM   2602  CD  PRO A 327      33.467  29.546 -16.671  1.00109.36           C  
ATOM   2603  N   LEU A 328      36.009  26.854 -17.664  1.00111.40           N  
ATOM   2604  CA  LEU A 328      36.481  25.848 -18.630  1.00111.99           C  
ATOM   2605  C   LEU A 328      35.712  24.543 -18.524  1.00112.88           C  
ATOM   2606  O   LEU A 328      34.593  24.452 -19.045  1.00113.43           O  
ATOM   2607  CB  LEU A 328      37.974  25.556 -18.431  1.00111.04           C  
ATOM   2608  CG  LEU A 328      38.959  26.683 -18.722  1.00110.56           C  
ATOM   2609  CD1 LEU A 328      38.513  27.398 -19.998  1.00110.06           C  
ATOM   2610  CD2 LEU A 328      39.028  27.639 -17.543  1.00109.80           C  
ATOM   2611  N   GLY A 329      36.325  23.554 -17.860  1.00113.30           N  
ATOM   2612  CA  GLY A 329      35.736  22.234 -17.668  1.00113.60           C  
ATOM   2613  C   GLY A 329      34.661  21.866 -18.668  1.00114.06           C  
ATOM   2614  O   GLY A 329      34.807  22.040 -19.884  1.00114.36           O  
ATOM   2615  N   ASP A 330      33.580  21.314 -18.140  1.00114.20           N  
ATOM   2616  CA  ASP A 330      32.422  20.972 -18.943  1.00114.52           C  
ATOM   2617  C   ASP A 330      31.262  21.713 -18.301  1.00115.39           C  
ATOM   2618  O   ASP A 330      30.115  21.537 -18.711  1.00116.04           O  
ATOM   2619  CB  ASP A 330      32.160  19.458 -18.910  1.00112.70           C  
ATOM   2620  CG  ASP A 330      33.254  18.660 -19.582  1.00111.12           C  
ATOM   2621  OD1 ASP A 330      33.060  17.443 -19.786  1.00110.11           O  
ATOM   2622  OD2 ASP A 330      34.308  19.246 -19.902  1.00110.08           O  
ATOM   2623  N   ASP A 331      31.589  22.571 -17.325  1.00115.95           N  
ATOM   2624  CA  ASP A 331      30.606  23.326 -16.527  1.00116.44           C  
ATOM   2625  C   ASP A 331      29.782  22.244 -15.803  1.00116.30           C  
ATOM   2626  O   ASP A 331      30.336  21.164 -15.521  1.00116.34           O  
ATOM   2627  CB  ASP A 331      29.707  24.230 -17.425  1.00116.73           C  
ATOM   2628  CG  ASP A 331      29.906  25.761 -17.167  1.00117.42           C  
ATOM   2629  OD1 ASP A 331      29.532  26.273 -16.079  1.00117.21           O  
ATOM   2630  OD2 ASP A 331      30.429  26.459 -18.072  1.00118.04           O  
ATOM   2631  N   GLU A 332      28.512  22.508 -15.489  1.00115.69           N  
ATOM   2632  CA  GLU A 332      27.659  21.497 -14.849  1.00114.34           C  
ATOM   2633  C   GLU A 332      26.561  21.132 -15.857  1.00113.79           C  
ATOM   2634  O   GLU A 332      25.743  20.238 -15.597  1.00113.40           O  
ATOM   2635  CB  GLU A 332      27.029  22.051 -13.555  1.00113.82           C  
ATOM   2636  CG  GLU A 332      26.759  21.014 -12.430  1.00113.49           C  
ATOM   2637  CD  GLU A 332      25.518  20.120 -12.639  1.00113.14           C  
ATOM   2638  OE1 GLU A 332      25.547  19.212 -13.496  1.00112.70           O  
ATOM   2639  OE2 GLU A 332      24.507  20.320 -11.931  1.00112.71           O  
ATOM   2640  N   ALA A 333      26.571  21.813 -17.011  1.00112.60           N  
ATOM   2641  CA  ALA A 333      25.571  21.617 -18.070  1.00110.91           C  
ATOM   2642  C   ALA A 333      24.268  22.148 -17.532  1.00109.43           C  
ATOM   2643  O   ALA A 333      23.406  22.622 -18.286  1.00109.54           O  
ATOM   2644  CB  ALA A 333      25.433  20.131 -18.426  1.00111.42           C  
ATOM   2645  N   SER A 334      24.155  22.058 -16.208  1.00107.01           N  
ATOM   2646  CA  SER A 334      23.014  22.531 -15.448  1.00104.33           C  
ATOM   2647  C   SER A 334      23.439  23.807 -14.700  1.00102.04           C  
ATOM   2648  O   SER A 334      24.455  24.425 -15.055  1.00101.20           O  
ATOM   2649  CB  SER A 334      22.542  21.437 -14.469  1.00104.53           C  
ATOM   2650  OG  SER A 334      22.085  20.277 -15.158  1.00104.37           O  
ATOM   2651  N   THR A 335      22.676  24.184 -13.678  1.00 99.91           N  
ATOM   2652  CA  THR A 335      22.926  25.397 -12.897  1.00 97.76           C  
ATOM   2653  C   THR A 335      24.411  25.674 -12.639  1.00 95.39           C  
ATOM   2654  O   THR A 335      25.266  24.788 -12.743  1.00 94.72           O  
ATOM   2655  CB  THR A 335      22.144  25.360 -11.526  1.00 98.45           C  
ATOM   2656  OG1 THR A 335      22.424  24.137 -10.830  1.00 98.50           O  
ATOM   2657  CG2 THR A 335      20.631  25.458 -11.757  1.00 98.39           C  
ATOM   2658  N   THR A 336      24.694  26.932 -12.321  1.00 92.53           N  
ATOM   2659  CA  THR A 336      26.035  27.407 -12.008  1.00 89.69           C  
ATOM   2660  C   THR A 336      25.882  28.333 -10.798  1.00 87.30           C  
ATOM   2661  O   THR A 336      24.785  28.379 -10.245  1.00 86.86           O  
ATOM   2662  CB  THR A 336      26.639  28.160 -13.227  1.00 90.04           C  
ATOM   2663  OG1 THR A 336      25.574  28.650 -14.057  1.00 89.89           O  
ATOM   2664  CG2 THR A 336      27.548  27.224 -14.052  1.00 90.41           C  
ATOM   2665  N   VAL A 337      26.935  29.031 -10.364  1.00 84.79           N  
ATOM   2666  CA  VAL A 337      26.817  29.941  -9.218  1.00 81.89           C  
ATOM   2667  C   VAL A 337      28.100  30.654  -8.913  1.00 79.73           C  
ATOM   2668  O   VAL A 337      29.163  30.150  -9.169  1.00 77.63           O  
ATOM   2669  CB  VAL A 337      26.356  29.219  -7.942  1.00 82.00           C  
ATOM   2670  CG1 VAL A 337      26.965  27.842  -7.856  1.00 82.25           C  
ATOM   2671  CG2 VAL A 337      26.749  30.034  -6.732  1.00 82.57           C  
ATOM   2672  N   SER A 338      27.975  31.842  -8.358  1.00 78.60           N  
ATOM   2673  CA  SER A 338      29.121  32.627  -8.015  1.00 78.74           C  
ATOM   2674  C   SER A 338      28.666  33.879  -7.334  1.00 81.68           C  
ATOM   2675  O   SER A 338      27.669  33.861  -6.603  1.00 81.17           O  
ATOM   2676  CB  SER A 338      29.886  32.983  -9.260  1.00 76.21           C  
ATOM   2677  OG  SER A 338      29.890  31.886 -10.125  1.00 73.86           O  
ATOM   2678  N   LYS A 339      29.378  34.974  -7.594  1.00 84.78           N  
ATOM   2679  CA  LYS A 339      29.087  36.275  -6.979  1.00 87.97           C  
ATOM   2680  C   LYS A 339      28.468  37.316  -7.975  1.00 89.67           C  
ATOM   2681  O   LYS A 339      27.272  37.616  -7.842  1.00 90.21           O  
ATOM   2682  CB  LYS A 339      30.382  36.821  -6.353  1.00 88.24           C  
ATOM   2683  CG  LYS A 339      30.197  37.906  -5.284  1.00 89.20           C  
ATOM   2684  CD  LYS A 339      31.536  38.579  -4.950  1.00 88.95           C  
ATOM   2685  CE  LYS A 339      32.136  39.250  -6.189  1.00 87.89           C  
ATOM   2686  NZ  LYS A 339      33.504  39.758  -5.943  1.00 86.67           N  
ATOM   2687  N   THR A 340      29.242  37.855  -8.933  1.00 90.97           N  
ATOM   2688  CA  THR A 340      28.720  38.859  -9.890  1.00 92.41           C  
ATOM   2689  C   THR A 340      28.493  38.294 -11.308  1.00 92.93           C  
ATOM   2690  O   THR A 340      27.836  38.967 -12.141  1.00 93.30           O  
ATOM   2691  CB  THR A 340      29.668  40.091 -10.015  1.00 92.51           C  
ATOM   2692  OG1 THR A 340      29.128  41.025 -10.969  1.00 92.61           O  
ATOM   2693  CG2 THR A 340      31.065  39.649 -10.468  1.00 92.75           C  
ATOM   2694  N   GLU A 341      29.021  37.095 -11.584  1.00 92.74           N  
ATOM   2695  CA  GLU A 341      28.869  36.459 -12.904  1.00 92.06           C  
ATOM   2696  C   GLU A 341      27.427  36.009 -13.134  1.00 91.23           C  
ATOM   2697  O   GLU A 341      26.484  36.834 -13.076  1.00 91.70           O  
ATOM   2698  CB  GLU A 341      29.816  35.239 -13.065  1.00 92.98           C  
ATOM   2699  CG  GLU A 341      29.454  33.984 -12.239  1.00 92.47           C  
ATOM   2700  CD  GLU A 341      29.787  32.683 -12.959  1.00 91.97           C  
ATOM   2701  OE1 GLU A 341      29.342  32.502 -14.109  1.00 91.44           O  
ATOM   2702  OE2 GLU A 341      30.488  31.836 -12.380  1.00 91.76           O  
ATOM   2703  N   THR A 342      27.261  34.708 -13.381  1.00 88.75           N  
ATOM   2704  CA  THR A 342      25.959  34.127 -13.647  1.00 85.73           C  
ATOM   2705  C   THR A 342      25.361  33.508 -12.405  1.00 83.56           C  
ATOM   2706  O   THR A 342      24.849  32.398 -12.462  1.00 82.90           O  
ATOM   2707  CB  THR A 342      26.054  33.075 -14.756  1.00 85.59           C  
ATOM   2708  OG1 THR A 342      24.733  32.751 -15.205  1.00 84.59           O  
ATOM   2709  CG2 THR A 342      26.773  31.818 -14.253  1.00 84.86           C  
ATOM   2710  N   SER A 343      25.429  34.223 -11.285  1.00 81.53           N  
ATOM   2711  CA  SER A 343      24.839  33.761 -10.030  1.00 79.24           C  
ATOM   2712  C   SER A 343      23.386  34.238 -10.067  1.00 77.10           C  
ATOM   2713  O   SER A 343      22.671  34.251  -9.054  1.00 76.69           O  
ATOM   2714  CB  SER A 343      25.590  34.366  -8.837  1.00 80.11           C  
ATOM   2715  OG  SER A 343      25.673  33.450  -7.759  1.00 82.32           O  
ATOM   2716  N   GLN A 344      22.995  34.628 -11.283  1.00 74.72           N  
ATOM   2717  CA  GLN A 344      21.674  35.126 -11.680  1.00 71.81           C  
ATOM   2718  C   GLN A 344      20.561  34.171 -11.212  1.00 72.24           C  
ATOM   2719  O   GLN A 344      20.414  33.099 -11.771  1.00 72.29           O  
ATOM   2720  CB  GLN A 344      21.679  35.317 -13.235  1.00 69.25           C  
ATOM   2721  CG  GLN A 344      22.243  34.098 -14.123  1.00 64.14           C  
ATOM   2722  CD  GLN A 344      22.818  34.489 -15.523  1.00 60.15           C  
ATOM   2723  OE1 GLN A 344      23.904  35.031 -15.620  1.00 58.82           O  
ATOM   2724  NE2 GLN A 344      22.083  34.199 -16.577  1.00 51.41           N  
ATOM   2725  N   VAL A 345      19.792  34.554 -10.192  1.00 73.19           N  
ATOM   2726  CA  VAL A 345      18.710  33.707  -9.658  1.00 74.95           C  
ATOM   2727  C   VAL A 345      17.825  33.182 -10.774  1.00 76.66           C  
ATOM   2728  O   VAL A 345      17.412  33.949 -11.632  1.00 77.14           O  
ATOM   2729  CB  VAL A 345      17.825  34.479  -8.643  1.00 74.63           C  
ATOM   2730  CG1 VAL A 345      16.766  33.556  -8.052  1.00 74.55           C  
ATOM   2731  CG2 VAL A 345      18.698  35.069  -7.534  1.00 75.35           C  
ATOM   2732  N   ALA A 346      17.514  31.888 -10.754  1.00 79.03           N  
ATOM   2733  CA  ALA A 346      16.702  31.296 -11.813  1.00 81.76           C  
ATOM   2734  C   ALA A 346      15.798  30.182 -11.306  1.00 84.51           C  
ATOM   2735  O   ALA A 346      15.931  29.045 -11.776  1.00 84.65           O  
ATOM   2736  CB  ALA A 346      17.613  30.754 -12.905  1.00 80.90           C  
ATOM   2737  N   PRO A 347      14.880  30.470 -10.353  1.00 87.34           N  
ATOM   2738  CA  PRO A 347      13.990  29.406  -9.855  1.00 89.19           C  
ATOM   2739  C   PRO A 347      12.822  29.263 -10.812  1.00 90.67           C  
ATOM   2740  O   PRO A 347      12.970  28.774 -11.939  1.00 90.07           O  
ATOM   2741  CB  PRO A 347      13.525  29.932  -8.482  1.00 89.10           C  
ATOM   2742  CG  PRO A 347      14.470  31.080  -8.159  1.00 88.70           C  
ATOM   2743  CD  PRO A 347      14.749  31.675  -9.518  1.00 88.09           C  
ATOM   2744  N   ALA A 348      11.664  29.716 -10.347  1.00 92.82           N  
ATOM   2745  CA  ALA A 348      10.436  29.683 -11.129  1.00 95.17           C  
ATOM   2746  C   ALA A 348       9.879  31.115 -11.234  1.00 96.36           C  
ATOM   2747  O   ALA A 348      10.409  32.002 -10.511  1.00 97.35           O  
ATOM   2748  CB  ALA A 348       9.412  28.746 -10.453  1.00 94.88           C  
ATOM   2749  OXT ALA A 348       8.926  31.344 -12.029  1.00 97.15           O  
TER    2750      ALA A 348                                                      
                   


HETATM 5571 ZN    ZN A 957      37.135  -1.787  32.041  0.66 35.13          ZN  
HETATM 5572 ZN    ZN A 959      34.185  19.475 -16.677  0.85 66.76          ZN  
HETATM 5573 ZN    ZN A 962      28.991  12.960  19.179  0.62 56.73          ZN  
HETATM 5574 ZN    ZN A2011      43.253  10.256  39.493  0.68 44.04          ZN  

 
HETATM 5885  O   HOH A 964      41.824   4.738  11.658  1.00 48.13           O  
HETATM 5886  O   HOH A2000      49.110   7.658  28.237  1.00 32.50           O  
HETATM 5887  O   HOH A2002      49.342  -2.814  33.463  1.00 46.30           O  
HETATM 5888  O   HOH A2004      40.768  15.488  29.883  1.00 43.44           O  
HETATM 5889  O   HOH A2007      28.580  29.852 -16.188  1.00 60.35           O  
HETATM 5890  O   HOH A2014      44.912   9.872  19.727  0.94 34.81           O  
HETATM 5891  O   HOH A2015      35.893  12.241   8.920  1.00 56.63           O  
HETATM 5892  O   HOH A2017      37.208  16.105   5.882  1.00 26.67           O  
HETATM 5893  O   HOH A2020      33.214  11.359   5.382  1.00 45.27           O  
HETATM 5894  O   HOH A2021      44.328  16.987  16.914  1.00 42.23           O  
HETATM 5895  O   HOH A2024      29.916  23.848   0.458  1.00 37.57           O  
HETATM 5896  O   HOH A2027      46.968  22.773  19.155  1.00 42.15           O  
HETATM 5897  O   HOH A2028      52.690  19.627  23.119  1.00 40.87           O  
HETATM 5898  O   HOH A2030      35.579  15.961   9.298  1.00 44.48           O  
HETATM 5899  O   HOH A2032      48.193   3.343  23.561  1.00 28.45           O  
HETATM 5900  O   HOH A2033      44.911  12.701  31.169  1.00 45.01           O  
HETATM 5901  O   HOH A2035      50.973   8.201  19.008  1.00 59.41           O  
HETATM 5902  O   HOH A2039      39.965 -11.559  23.863  1.00 32.58           O  
HETATM 5903  O   HOH A2041      52.533  -2.907  19.218  1.00 29.91           O  
HETATM 5904  O   HOH A2042      58.414  10.737  35.179  1.00 35.52           O  
HETATM 5905  O   HOH A2045      44.990  15.499  29.228  1.00 36.97           O  
HETATM 5906  O   HOH A2047      50.078  -0.478  35.016  1.00 40.53           O  
HETATM 5907  O   HOH A2048      49.387   1.275  21.525  1.00 42.25           O  
HETATM 5908  O   HOH A2049      52.069  13.027  34.780  1.00 46.18           O  
HETATM 5909  O   HOH A2051      55.564  -2.577  25.226  1.00 39.20           O  
HETATM 5910  O   HOH A2052      44.768  -0.431  29.501  1.00 45.41           O  
HETATM 5911  O   HOH A2053      27.336  19.021  -9.912  1.00 40.69           O  
HETATM 5912  O   HOH A2055      61.141  -1.783  31.346  0.98 46.50           O  
HETATM 5913  O   HOH A2057      38.335   2.452  30.394  1.00 71.53           O  
HETATM 5914  O   HOH A2058      42.132  18.219  32.056  1.00 45.59           O  
HETATM 5915  O   HOH A2059      45.613  15.970  34.061  0.99 53.71           O  
HETATM 5916  O   HOH A2061      30.369  29.006 -11.025  1.00 47.20           O  
HETATM 5917  O   HOH A2062      42.839  12.670  35.850  1.00 40.51           O  
HETATM 5918  O   HOH A2063      37.788  14.979  32.972  1.00 46.07           O  
HETATM 5919  O   HOH A2064      48.953   4.821  25.720  1.00 44.54           O  
HETATM 5920  O   HOH A2068      34.641   4.694  44.098  1.00 45.55           O  
HETATM 5921  O   HOH A2070      24.499  16.592 -12.939  1.00 49.71           O  

CONECT    1    2    3    4                                                      
CONECT    2    1                                                                
CONECT    3    1                                                                
CONECT    4    1                                                                
CONECT   19 5554                                                                
CONECT  120 5526                                                                
CONECT  886 1476                                                                
CONECT  973 5573                                                                
CONECT 1004 5573                                                                
CONECT 1299 5573                                                                
CONECT 1476  886                                                                
CONECT 1544 5574                                                                
CONECT 1561 5574                                                                
CONECT 1593 5571                                                                
CONECT 1594 5571                                                                
CONECT 1678 5573                                                                
CONECT 1774 5569                                                                
CONECT 2100 5568                                                                
CONECT 2230 5571                                                                
CONECT 2360 5589                                                                
CONECT 2366 5568                                                                
CONECT 2480 5572                                                                
CONECT 2484 5570                                                                
CONECT 2525 5570                                                                
CONECT 2568 5595                                                                
CONECT 2574 5612                                                                
CONECT 2615 5572                                                                
CONECT 2751 2752 2753 2754                                                      
CONECT 2752 2751                                                                
CONECT 2753 2751                                                                
CONECT 2754 2751                                                                
CONECT 2769 5728                                                                
CONECT 2870 5700                                                                
CONECT 3280 5744                                                                
CONECT 3636 4226                                                                
CONECT 3754 5747                                                                
CONECT 4226 3636                                                                
CONECT 4294 5745                                                                
CONECT 4311 5745                                                                
CONECT 4343 5746                                                                
CONECT 4344 5746                                                                
CONECT 4428 5747                                                                
CONECT 4850 5742                                                                
CONECT 4980 5746                                                                
CONECT 5110 5762                                                                
CONECT 5275 5744                                                                
CONECT 5318 5768                                                                
CONECT 5324 5785                                                                
CONECT 5411 5744                                                                
CONECT 5418 5744                                                                
CONECT 5501 5502 5510 5522                                                      
CONECT 5502 5501 5503 5507                                                      
CONECT 5503 5502 5504 5508                                                      
CONECT 5504 5503 5505 5509                                                      
CONECT 5505 5504 5506 5510                                                      
CONECT 5506 5505 5511                                                           
CONECT 5507 5502                                                                
CONECT 5508 5503                                                                
CONECT 5509 5504                                                                
CONECT 5510 5501 5505                                                           
CONECT 5511 5506                                                                
CONECT 5512 5513 5523 5536                                                      
CONECT 5513 5512 5514 5520                                                      
CONECT 5514 5513 5515 5521                                                      
CONECT 5515 5514 5516 5522                                                      
CONECT 5516 5515 5517 5523                                                      
CONECT 5517 5516 5524                                                           
CONECT 5518 5519 5520 5525                                                      
CONECT 5519 5518                                                                
CONECT 5520 5513 5518                                                           
CONECT 5521 5514                                                                
CONECT 5522 5501 5515                                                           
CONECT 5523 5512 5516                                                           
CONECT 5524 5517                                                                
CONECT 5525 5518                                                                
CONECT 5526  120 5527 5537                                                      
CONECT 5527 5526 5528 5534                                                      
CONECT 5528 5527 5529 5535                                                      
CONECT 5529 5528 5530 5536                                                      
CONECT 5530 5529 5531 5537                                                      
CONECT 5531 5530 5538                                                           
CONECT 5532 5533 5534 5539                                                      
CONECT 5533 5532                                                                
CONECT 5534 5527 5532                                                           
CONECT 5535 5528                                                                
CONECT 5536 5512 5529                                                           
CONECT 5537 5526 5530                                                           
CONECT 5538 5531                                                                
CONECT 5539 5532                                                                
CONECT 5540 5541 5551 5564                                                      
CONECT 5541 5540 5542 5548                                                      
CONECT 5542 5541 5543 5549                                                      
CONECT 5543 5542 5544 5550                                                      
CONECT 5544 5543 5545 5551                                                      
CONECT 5545 5544 5552                                                           
CONECT 5546 5547 5548 5553                                                      
CONECT 5547 5546                                                                
CONECT 5548 5541 5546                                                           
CONECT 5549 5542                                                                
CONECT 5550 5543                                                                
CONECT 5551 5540 5544                                                           
CONECT 5552 5545                                                                
CONECT 5553 5546                                                                
CONECT 5554   19 5555 5565                                                      
CONECT 5555 5554 5556 5562                                                      
CONECT 5556 5555 5557 5563                                                      
CONECT 5557 5556 5558 5564                                                      
CONECT 5558 5557 5559 5565                                                      
CONECT 5559 5558 5566                                                           
CONECT 5560 5561 5562 5567                                                      
CONECT 5561 5560                                                                
CONECT 5562 5555 5560                                                           
CONECT 5563 5556                                                                
CONECT 5564 5540 5557                                                           
CONECT 5565 5554 5558                                                           
CONECT 5566 5559                                                                
CONECT 5567 5560                                                                
CONECT 5568 2100 2366                                                           
CONECT 5569 1774                                                                
CONECT 5570 2484 2525 5916                                                      
CONECT 5571 1593 1594 2230                                                      
CONECT 5572 2480 2615                                                           
CONECT 5573  973 1004 1299 1678                                                 
CONECT 5574 1544 1561                                                           
CONECT 5575 5576 5580 5590 5591                                                 
CONECT 5576 5575 5577                                                           
CONECT 5577 5576 5578                                                           
CONECT 5578 5577 5579                                                           
CONECT 5579 5578 5580 5592                                                      
CONECT 5580 5575 5579 5581                                                      
CONECT 5581 5580 5582                                                           
CONECT 5582 5581 5583                                                           
CONECT 5583 5582 5584 5593                                                      
CONECT 5584 5583 5585                                                           
CONECT 5585 5584 5586                                                           
CONECT 5586 5585 5587                                                           
CONECT 5587 5586 5588 5594                                                      
CONECT 5588 5587 5589                                                           
CONECT 5589 2360 5588                                                           
CONECT 5590 5575                                                                
CONECT 5591 5575                                                                
CONECT 5592 5579                                                                
CONECT 5593 5583                                                                
CONECT 5594 5587                                                                
CONECT 5595 2568 5596 5597                                                      
CONECT 5596 5595                                                                
CONECT 5597 5595 5598                                                           
CONECT 5598 5597 5599                                                           
CONECT 5599 5598 5600                                                           
CONECT 5600 5599 5601                                                           
CONECT 5601 5600 5602                                                           
CONECT 5602 5601 5603                                                           
CONECT 5603 5602 5604                                                           
CONECT 5604 5603 5605                                                           
CONECT 5605 5604 5606                                                           
CONECT 5606 5605 5607                                                           
CONECT 5607 5606 5608                                                           
CONECT 5608 5607 5609                                                           
CONECT 5609 5608 5610                                                           
CONECT 5610 5609 5611                                                           
CONECT 5611 5610                                                                
CONECT 5612 2574 5613 5614                                                      
CONECT 5613 5612                                                                
CONECT 5614 5612 5615                                                           
CONECT 5615 5614 5616                                                           
CONECT 5616 5615 5617                                                           
CONECT 5617 5616 5618                                                           
CONECT 5618 5617 5619                                                           
CONECT 5619 5618 5620                                                           
CONECT 5620 5619 5621                                                           
CONECT 5621 5620 5622                                                           
CONECT 5622 5621 5623                                                           
CONECT 5623 5622 5624                                                           
CONECT 5624 5623 5625                                                           
CONECT 5625 5624 5626                                                           
CONECT 5626 5625 5627                                                           
CONECT 5627 5626 5628                                                           
CONECT 5628 5627                                                                
CONECT 5629 5630                                                                
CONECT 5630 5629 5631                                                           
CONECT 5631 5630 5632                                                           
CONECT 5632 5631 5633                                                           
CONECT 5633 5632 5634                                                           
CONECT 5634 5633 5635                                                           
CONECT 5635 5634 5636                                                           
CONECT 5636 5635 5637                                                           
CONECT 5637 5636 5638                                                           
CONECT 5638 5637 5639                                                           
CONECT 5639 5638 5640                                                           
CONECT 5640 5639 5641                                                           
CONECT 5641 5640 5642                                                           
CONECT 5642 5641 5643                                                           
CONECT 5643 5642 5644                                                           
CONECT 5644 5643                                                                
CONECT 5645 5646 5647 5654                                                      
CONECT 5646 5645 5657                                                           
CONECT 5647 5645 5648 5649                                                      
CONECT 5648 5647                                                                
CONECT 5649 5647 5650 5651                                                      
CONECT 5650 5649                                                                
CONECT 5651 5649 5652 5653                                                      
CONECT 5652 5651                                                                
CONECT 5653 5651 5654 5655                                                      
CONECT 5654 5645 5653                                                           
CONECT 5655 5653 5656                                                           
CONECT 5656 5655                                                                
CONECT 5657 5646 5658                                                           
CONECT 5658 5657 5659                                                           
CONECT 5659 5658 5660                                                           
CONECT 5660 5659 5661                                                           
CONECT 5661 5660 5662                                                           
CONECT 5662 5661 5663                                                           
CONECT 5663 5662                                                                
CONECT 5664 5665 5673 5682                                                      
CONECT 5665 5664 5666 5670                                                      
CONECT 5666 5665 5667 5671                                                      
CONECT 5667 5666 5668 5672                                                      
CONECT 5668 5667 5669 5673                                                      
CONECT 5669 5668 5674                                                           
CONECT 5670 5665                                                                
CONECT 5671 5666                                                                
CONECT 5672 5667                                                                
CONECT 5673 5664 5668                                                           
CONECT 5674 5669                                                                
CONECT 5675 5676 5684 5696                                                      
CONECT 5676 5675 5677 5681                                                      
CONECT 5677 5676 5678 5682                                                      
CONECT 5678 5677 5679 5683                                                      
CONECT 5679 5678 5680 5684                                                      
CONECT 5680 5679 5685                                                           
CONECT 5681 5676                                                                
CONECT 5682 5664 5677                                                           
CONECT 5683 5678                                                                
CONECT 5684 5675 5679                                                           
CONECT 5685 5680                                                                
CONECT 5686 5687 5697 5710                                                      
CONECT 5687 5686 5688 5694                                                      
CONECT 5688 5687 5689 5695                                                      
CONECT 5689 5688 5690 5696                                                      
CONECT 5690 5689 5691 5697                                                      
CONECT 5691 5690 5698                                                           
CONECT 5692 5693 5694 5699                                                      
CONECT 5693 5692                                                                
CONECT 5694 5687 5692                                                           
CONECT 5695 5688                                                                
CONECT 5696 5675 5689                                                           
CONECT 5697 5686 5690                                                           
CONECT 5698 5691                                                                
CONECT 5699 5692                                                                
CONECT 5700 2870 5701 5711                                                      
CONECT 5701 5700 5702 5708                                                      
CONECT 5702 5701 5703 5709                                                      
CONECT 5703 5702 5704 5710                                                      
CONECT 5704 5703 5705 5711                                                      
CONECT 5705 5704 5712                                                           
CONECT 5706 5707 5708 5713                                                      
CONECT 5707 5706                                                                
CONECT 5708 5701 5706                                                           
CONECT 5709 5702                                                                
CONECT 5710 5686 5703                                                           
CONECT 5711 5700 5704                                                           
CONECT 5712 5705                                                                
CONECT 5713 5706                                                                
CONECT 5714 5715 5725 5738                                                      
CONECT 5715 5714 5716 5722                                                      
CONECT 5716 5715 5717 5723                                                      
CONECT 5717 5716 5718 5724                                                      
CONECT 5718 5717 5719 5725                                                      
CONECT 5719 5718 5726                                                           
CONECT 5720 5721 5722 5727                                                      
CONECT 5721 5720                                                                
CONECT 5722 5715 5720                                                           
CONECT 5723 5716                                                                
CONECT 5724 5717                                                                
CONECT 5725 5714 5718                                                           
CONECT 5726 5719                                                                
CONECT 5727 5720                                                                
CONECT 5728 2769 5729 5739                                                      
CONECT 5729 5728 5730 5736                                                      
CONECT 5730 5729 5731 5737                                                      
CONECT 5731 5730 5732 5738                                                      
CONECT 5732 5731 5733 5739                                                      
CONECT 5733 5732 5740                                                           
CONECT 5734 5735 5736 5741                                                      
CONECT 5735 5734                                                                
CONECT 5736 5729 5734                                                           
CONECT 5737 5730                                                                
CONECT 5738 5714 5731                                                           
CONECT 5739 5728 5732                                                           
CONECT 5740 5733                                                                
CONECT 5741 5734                                                                
CONECT 5742 4850                                                                
CONECT 5744 3280 5275 5411 5418                                                 
CONECT 5745 4294 4311                                                           
CONECT 5746 4343 4344 4980                                                      
CONECT 5747 3754 4428                                                           
CONECT 5748 5749 5753 5763 5764                                                 
CONECT 5749 5748 5750                                                           
CONECT 5750 5749 5751                                                           
CONECT 5751 5750 5752                                                           
CONECT 5752 5751 5753 5765                                                      
CONECT 5753 5748 5752 5754                                                      
CONECT 5754 5753 5755                                                           
CONECT 5755 5754 5756                                                           
CONECT 5756 5755 5757 5766                                                      
CONECT 5757 5756 5758                                                           
CONECT 5758 5757 5759                                                           
CONECT 5759 5758 5760                                                           
CONECT 5760 5759 5761 5767                                                      
CONECT 5761 5760 5762                                                           
CONECT 5762 5110 5761                                                           
CONECT 5763 5748                                                                
CONECT 5764 5748                                                                
CONECT 5765 5752                                                                
CONECT 5766 5756                                                                
CONECT 5767 5760                                                                
CONECT 5768 5318 5769 5770                                                      
CONECT 5769 5768                                                                
CONECT 5770 5768 5771                                                           
CONECT 5771 5770 5772                                                           
CONECT 5772 5771 5773                                                           
CONECT 5773 5772 5774                                                           
CONECT 5774 5773 5775                                                           
CONECT 5775 5774 5776                                                           
CONECT 5776 5775 5777                                                           
CONECT 5777 5776 5778                                                           
CONECT 5778 5777 5779                                                           
CONECT 5779 5778 5780                                                           
CONECT 5780 5779 5781                                                           
CONECT 5781 5780 5782                                                           
CONECT 5782 5781 5783                                                           
CONECT 5783 5782 5784                                                           
CONECT 5784 5783                                                                
CONECT 5785 5324 5786 5787                                                      
CONECT 5786 5785                                                                
CONECT 5787 5785 5788                                                           
CONECT 5788 5787 5789                                                           
CONECT 5789 5788 5790                                                           
CONECT 5790 5789 5791                                                           
CONECT 5791 5790 5792                                                           
CONECT 5792 5791 5793                                                           
CONECT 5793 5792 5794                                                           
CONECT 5794 5793 5795                                                           
CONECT 5795 5794 5796                                                           
CONECT 5796 5795 5797                                                           
CONECT 5797 5796 5798                                                           
CONECT 5798 5797 5799                                                           
CONECT 5799 5798 5800                                                           
CONECT 5800 5799 5801                                                           
CONECT 5801 5800                                                                
CONECT 5802 5803 5804                                                           
CONECT 5803 5802                                                                
CONECT 5804 5802 5805 5806                                                      
CONECT 5805 5804                                                                
CONECT 5806 5804 5807 5808                                                      
CONECT 5807 5806                                                                
CONECT 5808 5806 5809                                                           
CONECT 5809 5808 5810                                                           
CONECT 5810 5809 5811                                                           
CONECT 5811 5810                                                                
CONECT 5812 5813                                                                
CONECT 5813 5812 5814                                                           
CONECT 5814 5813 5815                                                           
CONECT 5815 5814 5816                                                           
CONECT 5816 5815 5817                                                           
CONECT 5817 5816 5818                                                           
CONECT 5818 5817 5819                                                           
CONECT 5819 5818 5820                                                           
CONECT 5820 5819 5821                                                           
CONECT 5821 5820 5822                                                           
CONECT 5822 5821 5823                                                           
CONECT 5823 5822 5824                                                           
CONECT 5824 5823 5825                                                           
CONECT 5825 5824 5826                                                           
CONECT 5826 5825 5827                                                           
CONECT 5827 5826                                                                
CONECT 5828 5829 5830 5837                                                      
CONECT 5829 5828 5840                                                           
CONECT 5830 5828 5831 5832                                                      
CONECT 5831 5830                                                                
CONECT 5832 5830 5833 5834                                                      
CONECT 5833 5832                                                                
CONECT 5834 5832 5835 5836                                                      
CONECT 5835 5834                                                                
CONECT 5836 5834 5837 5838                                                      
CONECT 5837 5828 5836                                                           
CONECT 5838 5836 5839                                                           
CONECT 5839 5838                                                                
CONECT 5840 5829 5841                                                           
CONECT 5841 5840 5842                                                           
CONECT 5842 5841 5843                                                           
CONECT 5843 5842 5844                                                           
CONECT 5844 5843 5845                                                           
CONECT 5845 5844 5846                                                           
CONECT 5846 5845                                                                
CONECT 5847 5848 5849 5856                                                      
CONECT 5848 5847 5859                                                           
CONECT 5849 5847 5850 5851                                                      
CONECT 5850 5849                                                                
CONECT 5851 5849 5852 5853                                                      
CONECT 5852 5851                                                                
CONECT 5853 5851 5854 5855                                                      
CONECT 5854 5853                                                                
CONECT 5855 5853 5856 5857                                                      
CONECT 5856 5847 5855                                                           
CONECT 5857 5855 5858                                                           
CONECT 5858 5857                                                                
CONECT 5859 5848 5860                                                           
CONECT 5860 5859 5861                                                           
CONECT 5861 5860 5862                                                           
CONECT 5862 5861 5863                                                           
CONECT 5863 5862 5864                                                           
CONECT 5864 5863 5865                                                           
CONECT 5865 5864                                                                
CONECT 5866 5867 5868 5875                                                      
CONECT 5867 5866 5878                                                           
CONECT 5868 5866 5869 5870                                                      
CONECT 5869 5868                                                                
CONECT 5870 5868 5871 5872                                                      
CONECT 5871 5870                                                                
CONECT 5872 5870 5873 5874                                                      
CONECT 5873 5872                                                                
CONECT 5874 5872 5875 5876                                                      
CONECT 5875 5866 5874                                                           
CONECT 5876 5874 5877                                                           
CONECT 5877 5876                                                                
CONECT 5878 5867 5879                                                           
CONECT 5879 5878 5880                                                           
CONECT 5880 5879 5881                                                           
CONECT 5881 5880 5882                                                           
CONECT 5882 5881 5883                                                           
CONECT 5883 5882 5884                                                           
CONECT 5884 5883                                                                
CONECT 5916 5570                                                                
MASTER      575    0   39   29    8    0   57    6 5948    2  434   54          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.