HEADER    GROWTH FACTOR                           16-OCT-97   1AXM              
TITLE     HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST GROWTH FACTOR  
CAVEAT     1AXM    IDS I 5 HAS WRONG CHIRALITY AT ATOM C1                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACIDIC FIBROBLAST GROWTH FACTOR;                           
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: FGF-1;                                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: FOR EACH OF THE DECASACCHARIDE CHAINS IN THE          
COMPND   7 ASYMMETRIC UNIT, FIVE MONOSACCHARIDE UNITS ARE DISORDERED            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: JM109 DE3;                                                
SOURCE   6 ORGAN: BRAIN STEM;                                                   
SOURCE   7 TISSUE: NERVE;                                                       
SOURCE   8 CELL: ENDOTHELIAL;                                                   
SOURCE   9 CELLULAR_LOCATION: EXTRACELLULAR MATRIX;                             
SOURCE  10 GENE: ECGF;                                                          
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE  14 EXPRESSION_SYSTEM_CELL_LINE: JM109 DE3;                              
SOURCE  15 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;                      
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL;                            
SOURCE  17 EXPRESSION_SYSTEM_VECTOR: ESCHERICHIA COLI;                          
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET-3A                                    
KEYWDS    HUMAN ACIDIC FIBROBLAST GROWTH FACTOR,                                
KEYWDS   2 HEPARIN DECASACCHARID FACTOR                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.D.DIGABRIELE,I.LAX,D.I.CHEN,C.M.SVAHN,M.JAYE,J.SCHLESSINGER,        
AUTHOR   2 W.A.HENDRICKSON                                                      
REVDAT   7   23-OCT-24 1AXM    1       REMARK                                   
REVDAT   6 2 02-AUG-23 1AXM    1       HETSYN                                   
REVDAT   5 3 29-JUL-20 1AXM    1       CAVEAT COMPND REMARK SEQADV              
REVDAT   5 4   -  X-0          1       HETNAM LINK   SITE   ATOM                
REVDAT   4 5 13-JUL-11 1AXM    1       VERSN                                    
REVDAT   3 6 24-FEB-09 1AXM    1       VERSN                                    
REVDAT   2 7 21-JUN-05 1AXM    1       AUTHOR JRNL                              
REVDAT   1 8 22-APR-98 1AXM    0                                                
JRNL        AUTH   A.D.DIGABRIELE,I.LAX,D.I.CHEN,C.M.SVAHN,M.JAYE,              
JRNL        AUTH 2 J.SCHLESSINGER,W.A.HENDRICKSON                               
JRNL        TITL   STRUCTURE OF A HEPARIN-LINKED BIOLOGICALLY ACTIVE DIMER OF   
JRNL        TITL 2 FIBROBLAST GROWTH FACTOR.                                    
JRNL        REF    NATURE                        V. 393   812 1998              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   9655399                                                      
JRNL        DOI    10.1038/31741                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.BLABER,J.DISALVO,K.A.THOMAS                                
REMARK   1  TITL   X-RAY CRYSTAL STRUCTURE OF HUMAN ACIDIC FIBROBLAST GROWTH    
REMARK   1  TITL 2 FACTOR.                                                      
REMARK   1  REF    BIOCHEMISTRY                  V.  35  2086 1996              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   8652550                                                      
REMARK   1  DOI    10.1021/BI9521755                                            
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   S.FAHAM,R.E.HILEMAN,J.R.FROMM,R.J.LINHARDT,D.C.REES          
REMARK   1  TITL   HEPARIN STRUCTURE AND INTERACTIONS WITH BASIC FIBROBLAST     
REMARK   1  TITL 2 GROWTH FACTOR                                                
REMARK   1  REF    SCIENCE                       V. 271  1116 1996              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   X.ZHU,B.T.HSU,D.C.REES                                       
REMARK   1  TITL   STRUCTURAL STUDIES OF THE BINDING OF THE ANTI-ULCER DRUG     
REMARK   1  TITL 2 SUCROSE OCTASULFATE TO ACIDIC FIBROBLAST GROWTH FACTOR       
REMARK   1  REF    STRUCTURE                     V.   1    27 1993              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 1.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 23540                          
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) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.304                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2077                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2449                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2950                       
REMARK   3   BIN FREE R VALUE                    : 0.3840                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 313                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.022                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6125                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 267                                     
REMARK   3   SOLVENT ATOMS            : 71                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.600                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.400                           
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) : 1.500 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.000 ; 1.500                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.000 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.500 ; 2.000                
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINTS                                              
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : 0.27  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : 1.56  ; 2.0                  
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  2  : PARAMCSDX_MOD.PRO                              
REMARK   3  PARAMETER FILE  3  : HEP96.PAR                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  2   : TOPHCSDX_MOD.PRO                               
REMARK   3  TOPOLOGY FILE  3   : TOPH19.PEP                                     
REMARK   3  TOPOLOGY FILE  4   : HEP96.TOP                                      
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AXM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000171380.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-FEB-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98789                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : BENT MIRROR                        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : FUJI                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (AGROVATA, ROTAVATA           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25115                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : 0.09500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.33700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: MADSYS                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1AFC, 1HPN                               
REMARK 200                                                                      
REMARK 200 REMARK: BOTH MOLECULAR REPLACEMENT AND MAD WERE USED FOR PHASE       
REMARK 200  DETERMINATION AND COMBINATION                                       
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN/HEPARIN COMPLEX WAS              
REMARK 280  CRYSTALLIZED FROM 25% PEG 8000, 200 MM MGSO4, 100 MM HEPES, PH      
REMARK 280  7.0; CRYSTAL WAS SOAKED IN 22% XYLITOL PRIOR TO DATA COLLECTION.    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       95.29000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       95.29000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       43.84500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       79.02500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.84500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       79.02500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       95.29000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.84500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       79.02500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       95.29000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.84500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       79.02500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G                               
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F, I                               
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, E, H                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     TYR A     8                                                      
REMARK 465     SER A   139                                                      
REMARK 465     ASP A   140                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     TYR B     8                                                      
REMARK 465     LYS B     9                                                      
REMARK 465     LYS B    10                                                      
REMARK 465     SER B   138                                                      
REMARK 465     SER B   139                                                      
REMARK 465     ASP B   140                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     ASN C     7                                                      
REMARK 465     TYR C     8                                                      
REMARK 465     LYS C     9                                                      
REMARK 465     SER C   138                                                      
REMARK 465     SER C   139                                                      
REMARK 465     ASP C   140                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     ASN D     7                                                      
REMARK 465     TYR D     8                                                      
REMARK 465     LYS D     9                                                      
REMARK 465     LYS D    10                                                      
REMARK 465     SER D   138                                                      
REMARK 465     SER D   139                                                      
REMARK 465     ASP D   140                                                      
REMARK 465     GLY E     6                                                      
REMARK 465     ASN E     7                                                      
REMARK 465     TYR E     8                                                      
REMARK 465     LYS E     9                                                      
REMARK 465     SER E   139                                                      
REMARK 465     ASP E   140                                                      
REMARK 465     GLY F     6                                                      
REMARK 465     ASN F     7                                                      
REMARK 465     TYR F     8                                                      
REMARK 465     LYS F     9                                                      
REMARK 465     SER F   139                                                      
REMARK 465     ASP F   140                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   9    CG   CD   CE   NZ                                   
REMARK 470     LYS A  10    CG   CD   CE   NZ                                   
REMARK 470     PRO B  11    CG   CD                                             
REMARK 470     LYS C  10    CG   CD   CE   NZ                                   
REMARK 470     PRO D  11    CG   CD                                             
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  11   N   -  CA  -  CB  ANGL. DEV. =   7.5 DEGREES          
REMARK 500    PRO D  11   N   -  CA  -  CB  ANGL. DEV. =   7.5 DEGREES          
REMARK 500    CYS F 117   CA  -  CB  -  SG  ANGL. DEV. =   7.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  12     -168.71   -119.97                                   
REMARK 500    ASP A  32     -154.10   -160.45                                   
REMARK 500    GLN A  40       22.04    -76.32                                   
REMARK 500    SER A  50     -149.18   -161.20                                   
REMARK 500    HIS A 102       30.90    -87.94                                   
REMARK 500    PRO A 134       94.10    -66.75                                   
REMARK 500    ASN B  18       97.56    -61.06                                   
REMARK 500    ASP B  32     -155.02   -157.53                                   
REMARK 500    ASP B  36       94.23    -54.59                                   
REMARK 500    ASN B  92       31.16    -78.32                                   
REMARK 500    ASN B 106       43.63     72.03                                   
REMARK 500    PRO B 121       -6.95    -55.98                                   
REMARK 500    ASP C  32     -143.44   -153.97                                   
REMARK 500    GLU C  49      -70.63   -131.78                                   
REMARK 500    SER C  50     -162.09   -120.58                                   
REMARK 500    VAL C  51       17.30    -66.17                                   
REMARK 500    ASP C  68     -167.19    -63.90                                   
REMARK 500    PRO C  79       89.60    -66.19                                   
REMARK 500    ASN C  80     -167.16   -105.47                                   
REMARK 500    GLU C  90      -79.89    -88.55                                   
REMARK 500    ASN C  92       -4.55    -40.80                                   
REMARK 500    ASN D  18       87.99    -68.58                                   
REMARK 500    ASP D  28       30.16    -89.38                                   
REMARK 500    ASP D  32     -147.73   -160.58                                   
REMARK 500    ASP D  36       88.84    -56.33                                   
REMARK 500    ASP D  68     -167.40    -63.82                                   
REMARK 500    ASN D  80     -160.99   -112.49                                   
REMARK 500    PRO D 134       85.30    -69.29                                   
REMARK 500    ASP E  32     -153.34   -169.69                                   
REMARK 500    ASP E  36       96.46    -54.66                                   
REMARK 500    ASN E  80     -169.85   -112.69                                   
REMARK 500    GLU E  90      -86.04    -55.77                                   
REMARK 500    GLU E  91     -157.61    -80.93                                   
REMARK 500    HIS E  93      -42.51   -146.88                                   
REMARK 500    SER E  99      105.13    -56.32                                   
REMARK 500    VAL E 137       29.03   -146.93                                   
REMARK 500    ASN F  18       89.44    -65.61                                   
REMARK 500    ASP F  32     -148.35   -164.98                                   
REMARK 500    GLN F  40       27.75    -77.91                                   
REMARK 500    SER F  50      172.02    162.06                                   
REMARK 500    PRO F  79       90.25    -69.79                                   
REMARK 500    ASN F  80     -169.88   -104.07                                   
REMARK 500    HIS F  93       36.59     73.74                                   
REMARK 500    ASN F 106       43.86     71.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: HPA                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: HEPARIN BINDING LOOP.                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HPB                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: HEPARIN BINDING LOOP.                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HPC                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: HEPARIN BINDING LOOP.                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HPD                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: HEPARIN BINDING LOOP.                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HPE                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: HEPARIN BINDING LOOP.                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HPF                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: HEPARIN BINDING LOOP.                              
DBREF  1AXM A    6   140  UNP    P05230   FGF1_HUMAN      21    155             
SEQADV 1AXM MSE A   67  UNP  P05230    MET    82 MODIFIED RESIDUE               
SEQRES   1 A  135  GLY ASN TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN          
SEQRES   2 A  135  GLY GLY HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL          
SEQRES   3 A  135  ASP GLY THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU          
SEQRES   4 A  135  GLN LEU SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS          
SEQRES   5 A  135  SER THR GLU THR GLY GLN TYR LEU ALA MSE ASP THR ASP          
SEQRES   6 A  135  GLY LEU LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS          
SEQRES   7 A  135  LEU PHE LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR          
SEQRES   8 A  135  TYR ILE SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL          
SEQRES   9 A  135  GLY LEU LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG          
SEQRES  10 A  135  THR HIS TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU          
SEQRES  11 A  135  PRO VAL SER SER ASP                                          
MODRES 1AXM MSE A   67  MET  SELENOMETHIONINE                                   
HET    MSE  A  67       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SGN 2-DEOXY-6-O-SULFO-2-(SULFOAMINO)-ALPHA-D-GLUCOPYRANOS            
HETNAM     IDS 2-O-SULFO-ALPHA-L-IDOPYRANURONIC ACID                            
HETSYN     SGN N,O6-DISULFO-GLUCOSAMINE;                                        
HETSYN   2 SGN 6-O-SULFO-N-SULFO-ALPHA-D- GLUCOSAMINE;                          
HETSYN   3 SGN 2-DEOXY-6-O-SULFO-2-(SULFOAMINO)-ALPHA-D- GLUCOSE;               
HETSYN   4 SGN 2-DEOXY-6-O-SULFO-2-(SULFOAMINO)-D-GLUCOSE;                      
HETSYN   5 SGN 2-DEOXY-6-O-SULFO-2-(SULFOAMINO)-GLUCOSE                         
HETSYN     IDS O2-SULFO-GLUCURONIC ACID;                                        
HETSYN   2 IDS 2-O-SULFO-ALPHA-L-IDURONIC ACID;                                 
HETSYN   3 IDS 2-O-SULFO-L-IDURONIC ACID; 2-O-SULFO-IDURONIC ACID               
FORMUL   1  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   7  SGN    8(C6 H13 N O11 S2)                                           
FORMUL   7  IDS    7(C6 H10 O10 S)                                              
FORMUL   0  HOH   *71(H2 O)                                                     
LINK         C   ALA A  66                 N   MSE A  67     1555   1555        
LINK         C   MSE A  67                 N   ASP A  68     1555   1555        
LINK         C   ALA B  66                 N   MSE B  67     1555   1555        
LINK         C   MSE B  67                 N   ASP B  68     1555   1555        
LINK         C   ALA C  66                 N   MSE C  67     1555   1555        
LINK         C   MSE C  67                 N   ASP C  68     1555   1555        
LINK         C   ALA D  66                 N   MSE D  67     1555   1555        
LINK         C   MSE D  67                 N   ASP D  68     1555   1555        
LINK         C   ALA E  66                 N   MSE E  67     1555   1555        
LINK         C   MSE E  67                 N   ASP E  68     1555   1555        
LINK         C   ALA F  66                 N   MSE F  67     1555   1555        
LINK         C   MSE F  67                 N   ASP F  68     1555   1555        
LINK         O4  SGN G   1                 C1  IDS G   2     1555   1555        
LINK         O4  IDS G   2                 C1  SGN G   3     1555   1555        
LINK         O4  SGN G   3                 C1  IDS G   4     1555   1555        
LINK         O4  IDS G   4                 C1  SGN G   5     1555   1555        
LINK         O4  SGN H   1                 C1  IDS H   2     1555   1555        
LINK         O4  IDS H   2                 C1  SGN H   3     1555   1555        
LINK         O4  SGN H   3                 C1  IDS H   4     1555   1555        
LINK         O4  IDS H   4                 C1  SGN H   5     1555   1555        
LINK         O4  IDS I   1                 C1  SGN I   2     1555   1555        
LINK         O4  SGN I   2                 C1  IDS I   3     1555   1555        
LINK         O4  IDS I   3                 C1  SGN I   4     1555   1555        
LINK         O4  SGN I   4                 C1  IDS I   5     1555   1555        
SITE     1 HPA 18 ASN A  18  LYS A 112  LYS A 113  ASN A 114                    
SITE     2 HPA 18 GLY A 115  SER A 116  CYS A 117  LYS A 118                    
SITE     3 HPA 18 ARG A 119  GLY A 120  PRO A 121  ARG A 122                    
SITE     4 HPA 18 THR A 123  HIS A 124  TYR A 125  GLY A 126                    
SITE     5 HPA 18 GLN A 127  LYS A 128                                          
SITE     1 HPB 18 ASN B  18  LYS B 112  LYS B 113  ASN B 114                    
SITE     2 HPB 18 GLY B 115  SER B 116  CYS B 117  LYS B 118                    
SITE     3 HPB 18 ARG B 119  GLY B 120  PRO B 121  ARG B 122                    
SITE     4 HPB 18 THR B 123  HIS B 124  TYR B 125  GLY B 126                    
SITE     5 HPB 18 GLN B 127  LYS B 128                                          
SITE     1 HPC 18 ASN C  18  LYS C 112  LYS C 113  ASN C 114                    
SITE     2 HPC 18 GLY C 115  SER C 116  CYS C 117  LYS C 118                    
SITE     3 HPC 18 ARG C 119  GLY C 120  PRO C 121  ARG C 122                    
SITE     4 HPC 18 THR C 123  HIS C 124  TYR C 125  GLY C 126                    
SITE     5 HPC 18 GLN C 127  LYS C 128                                          
SITE     1 HPD 18 ASN D  18  LYS D 112  LYS D 113  ASN D 114                    
SITE     2 HPD 18 GLY D 115  SER D 116  CYS D 117  LYS D 118                    
SITE     3 HPD 18 ARG D 119  GLY D 120  PRO D 121  ARG D 122                    
SITE     4 HPD 18 THR D 123  HIS D 124  TYR D 125  GLY D 126                    
SITE     5 HPD 18 GLN D 127  LYS D 128                                          
SITE     1 HPE 18 ASN E  18  LYS E 112  LYS E 113  ASN E 114                    
SITE     2 HPE 18 GLY E 115  SER E 116  CYS E 117  LYS E 118                    
SITE     3 HPE 18 ARG E 119  GLY E 120  PRO E 121  ARG E 122                    
SITE     4 HPE 18 THR E 123  HIS E 124  TYR E 125  GLY E 126                    
SITE     5 HPE 18 GLN E 127  LYS E 128                                          
SITE     1 HPF 18 ASN F  18  LYS F 112  LYS F 113  ASN F 114                    
SITE     2 HPF 18 GLY F 115  SER F 116  CYS F 117  LYS F 118                    
SITE     3 HPF 18 ARG F 119  GLY F 120  PRO F 121  ARG F 122                    
SITE     4 HPF 18 THR F 123  HIS F 124  TYR F 125  GLY F 126                    
SITE     5 HPF 18 GLN F 127  LYS F 128                                          
CRYST1   87.690  158.050  190.580  90.00  90.00  90.00 C 2 2 21     48          
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      0.011404  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006327  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005247        0.00000                         
MTRIX1   1  0.959510  0.063610  0.274410      -11.02670    1                    
MTRIX2   1 -0.010650 -0.965280  0.261020        2.80977    1                    
MTRIX3   1  0.281490 -0.253370 -0.925510       94.12106    1                    
MTRIX1   2 -0.588820  0.727080 -0.353050       28.19709    1                    
MTRIX2   2  0.759210  0.647390  0.067010       27.14610    1                    
MTRIX3   2  0.277290 -0.228580 -0.933200      157.20302    1                    
MTRIX1   3 -0.620770  0.783940  0.008980      -24.62529    1                    
MTRIX2   3 -0.783690 -0.620810  0.020340       37.83826    1                    
MTRIX3   3  0.021520  0.005590  0.999750      127.53954    1                    
MTRIX1   4 -0.399700 -0.910330  0.107390       24.34238    1                    
MTRIX2   4  0.916060 -0.400890  0.011150       39.48433    1                    
MTRIX3   4  0.032900  0.102830  0.994150       63.02549    1                    
MTRIX1   5 -0.405730 -0.913670 -0.024300      -16.08838    1                    
MTRIX2   5 -0.888050  0.400360 -0.226020       44.64824    1                    
MTRIX3   5  0.216240 -0.070130 -0.973820      221.62483    1                    
MTRIX1   6 -0.634160 -0.772970 -0.018720       25.02280    1                    
MTRIX2   6  0.773200 -0.633920 -0.017710       39.55009    1                    
MTRIX3   6  0.001820 -0.025710  0.999670       63.28213    1                    
MTRIX1   7 -0.440420  0.829730  0.342890      -46.21931    1                    
MTRIX2   7 -0.897510 -0.416540 -0.144840       49.49619    1                    
MTRIX3   7  0.022650 -0.371530  0.928140      134.70387    1                    
ATOM      1  N   LYS A   9       8.854  20.417  -0.775  1.00 44.93              
ATOM      2  CA  LYS A   9       7.893  21.206  -1.591  1.00 40.20              
ATOM      3  C   LYS A   9       7.785  20.693  -3.051  1.00 38.69              
ATOM      4  O   LYS A   9       8.782  20.507  -3.751  1.00 37.12              
ATOM      5  CB  LYS A   9       8.262  22.705  -1.548  1.00 36.05              
ATOM      6  N   LYS A  10       6.550  20.374  -3.433  1.00 38.33              
ATOM      7  CA  LYS A  10       6.119  19.912  -4.760  1.00 34.82              
ATOM      8  C   LYS A  10       4.705  20.500  -4.735  1.00 34.16              
ATOM      9  O   LYS A  10       4.055  20.499  -3.680  1.00 35.39              
ATOM     10  CB  LYS A  10       6.056  18.394  -4.814  1.00 33.69              
ATOM     11  N   PRO A  11       4.199  21.005  -5.870  1.00 33.73              
ATOM     12  CA  PRO A  11       2.848  21.579  -5.809  1.00 34.71              
ATOM     13  C   PRO A  11       1.821  20.747  -5.032  1.00 37.03              
ATOM     14  O   PRO A  11       1.826  19.498  -5.092  1.00 39.74              
ATOM     15  CB  PRO A  11       2.478  21.770  -7.276  1.00 32.36              
ATOM     16  CG  PRO A  11       3.237  20.722  -7.957  1.00 33.39              
ATOM     17  CD  PRO A  11       4.593  20.766  -7.261  1.00 33.39              
ATOM     18  N   LYS A  12       1.039  21.451  -4.209  1.00 35.92              
ATOM     19  CA  LYS A  12      -0.009  20.856  -3.405  1.00 36.83              
ATOM     20  C   LYS A  12      -1.384  21.415  -3.715  1.00 34.62              
ATOM     21  O   LYS A  12      -1.595  22.053  -4.751  1.00 36.61              
ATOM     22  CB  LYS A  12       0.316  21.003  -1.930  1.00 39.99              
ATOM     23  CG  LYS A  12       1.319  19.945  -1.491  1.00 46.81              
ATOM     24  CD  LYS A  12       1.624  20.036  -0.016  1.00 51.58              
ATOM     25  CE  LYS A  12       2.632  18.954   0.381  1.00 54.73              
ATOM     26  NZ  LYS A  12       3.118  19.159   1.788  1.00 58.44              
ATOM     27  N   LEU A  13      -2.336  21.079  -2.854  1.00 30.72              
ATOM     28  CA  LEU A  13      -3.725  21.534  -2.945  1.00 25.23              
ATOM     29  C   LEU A  13      -4.080  21.935  -1.528  1.00 23.28              
ATOM     30  O   LEU A  13      -3.644  21.318  -0.557  1.00 24.02              
ATOM     31  CB  LEU A  13      -4.637  20.405  -3.393  1.00 23.31              
ATOM     32  CG  LEU A  13      -4.346  19.694  -4.710  1.00 21.74              
ATOM     33  CD1 LEU A  13      -4.693  18.237  -4.577  1.00 21.85              
ATOM     34  CD2 LEU A  13      -5.157  20.321  -5.815  1.00 22.68              
ATOM     35  N   LEU A  14      -4.754  23.050  -1.395  1.00 22.71              
ATOM     36  CA  LEU A  14      -5.161  23.496  -0.084  1.00 23.93              
ATOM     37  C   LEU A  14      -6.650  23.207   0.002  1.00 24.43              
ATOM     38  O   LEU A  14      -7.469  23.915  -0.554  1.00 25.58              
ATOM     39  CB  LEU A  14      -4.854  24.982   0.112  1.00 19.23              
ATOM     40  CG  LEU A  14      -3.374  25.275   0.290  1.00 15.95              
ATOM     41  CD1 LEU A  14      -3.199  26.764   0.168  1.00 18.44              
ATOM     42  CD2 LEU A  14      -2.824  24.759   1.642  1.00 11.95              
ATOM     43  N   TYR A  15      -6.976  22.074   0.585  1.00 23.89              
ATOM     44  CA  TYR A  15      -8.347  21.675   0.734  1.00 23.63              
ATOM     45  C   TYR A  15      -8.837  22.200   2.102  1.00 27.64              
ATOM     46  O   TYR A  15      -8.216  21.937   3.150  1.00 27.87              
ATOM     47  CB  TYR A  15      -8.433  20.168   0.633  1.00 19.22              
ATOM     48  CG  TYR A  15      -9.674  19.582   1.210  1.00 16.92              
ATOM     49  CD1 TYR A  15     -10.851  19.557   0.487  1.00 11.91              
ATOM     50  CD2 TYR A  15      -9.663  19.024   2.506  1.00 17.27              
ATOM     51  CE1 TYR A  15     -11.989  19.005   1.017  1.00 12.64              
ATOM     52  CE2 TYR A  15     -10.816  18.460   3.066  1.00 13.64              
ATOM     53  CZ  TYR A  15     -11.974  18.456   2.308  1.00 14.43              
ATOM     54  OH  TYR A  15     -13.123  17.901   2.845  1.00 15.25              
ATOM     55  N   CYS A  16      -9.924  22.983   2.060  1.00 28.93              
ATOM     56  CA  CYS A  16     -10.559  23.579   3.238  1.00 26.54              
ATOM     57  C   CYS A  16     -11.703  22.728   3.820  1.00 26.44              
ATOM     58  O   CYS A  16     -12.718  22.489   3.166  1.00 25.73              
ATOM     59  CB  CYS A  16     -11.080  24.954   2.863  1.00 25.98              
ATOM     60  SG  CYS A  16     -11.557  25.974   4.246  1.00 28.33              
ATOM     61  N   SER A  17     -11.534  22.301   5.064  1.00 26.42              
ATOM     62  CA  SER A  17     -12.520  21.481   5.758  1.00 28.24              
ATOM     63  C   SER A  17     -13.918  22.029   5.624  1.00 28.91              
ATOM     64  O   SER A  17     -14.848  21.302   5.264  1.00 27.05              
ATOM     65  CB  SER A  17     -12.181  21.397   7.234  1.00 28.23              
ATOM     66  OG  SER A  17     -12.082  22.708   7.766  1.00 25.54              
ATOM     67  N   ASN A  18     -14.068  23.308   5.953  1.00 31.88              
ATOM     68  CA  ASN A  18     -15.367  23.990   5.862  1.00 33.29              
ATOM     69  C   ASN A  18     -15.852  24.061   4.409  1.00 34.03              
ATOM     70  O   ASN A  18     -15.328  24.794   3.588  1.00 34.69              
ATOM     71  CB  ASN A  18     -15.269  25.405   6.442  1.00 32.29              
ATOM     72  CG  ASN A  18     -16.582  26.114   6.428  1.00 30.73              
ATOM     73  OD1 ASN A  18     -17.623  25.479   6.369  1.00 30.63              
ATOM     74  ND2 ASN A  18     -16.553  27.422   6.457  1.00 30.89              
ATOM     75  N   GLY A  19     -16.823  23.246   4.066  1.00 35.78              
ATOM     76  CA  GLY A  19     -17.318  23.264   2.706  1.00 35.82              
ATOM     77  C   GLY A  19     -16.642  22.246   1.812  1.00 36.29              
ATOM     78  O   GLY A  19     -17.245  21.825   0.827  1.00 38.38              
ATOM     79  N   GLY A  20     -15.403  21.859   2.130  1.00 34.54              
ATOM     80  CA  GLY A  20     -14.700  20.881   1.312  1.00 30.58              
ATOM     81  C   GLY A  20     -14.381  21.351  -0.085  1.00 30.90              
ATOM     82  O   GLY A  20     -14.766  20.709  -1.055  1.00 31.96              
ATOM     83  N   HIS A  21     -13.689  22.487  -0.184  1.00 31.14              
ATOM     84  CA  HIS A  21     -13.311  23.091  -1.473  1.00 27.87              
ATOM     85  C   HIS A  21     -11.799  23.179  -1.519  1.00 25.82              
ATOM     86  O   HIS A  21     -11.134  23.159  -0.470  1.00 23.42              
ATOM     87  CB  HIS A  21     -13.843  24.529  -1.632  1.00 27.27              
ATOM     88  CG  HIS A  21     -15.335  24.648  -1.590  1.00 27.12              
ATOM     89  ND1 HIS A  21     -16.030  25.011  -0.453  1.00 27.31              
ATOM     90  CD2 HIS A  21     -16.257  24.521  -2.571  1.00 25.46              
ATOM     91  CE1 HIS A  21     -17.314  25.107  -0.737  1.00 26.26              
ATOM     92  NE2 HIS A  21     -17.479  24.815  -2.015  1.00 24.00              
ATOM     93  N   PHE A  22     -11.276  23.400  -2.721  1.00 23.07              
ATOM     94  CA  PHE A  22      -9.850  23.514  -2.933  1.00 22.92              
ATOM     95  C   PHE A  22      -9.581  24.977  -3.235  1.00 23.06              
ATOM     96  O   PHE A  22     -10.332  25.577  -4.003  1.00 23.17              
ATOM     97  CB  PHE A  22      -9.425  22.645  -4.105  1.00 23.47              
ATOM     98  CG  PHE A  22      -9.610  21.188  -3.868  1.00 25.00              
ATOM     99  CD1 PHE A  22      -9.084  20.589  -2.720  1.00 27.84              
ATOM    100  CD2 PHE A  22     -10.321  20.411  -4.777  1.00 24.71              
ATOM    101  CE1 PHE A  22      -9.270  19.226  -2.479  1.00 29.15              
ATOM    102  CE2 PHE A  22     -10.518  19.048  -4.558  1.00 25.40              
ATOM    103  CZ  PHE A  22      -9.995  18.452  -3.409  1.00 27.69              
ATOM    104  N   LEU A  23      -8.547  25.545  -2.601  1.00 21.88              
ATOM    105  CA  LEU A  23      -8.187  26.941  -2.782  1.00 20.57              
ATOM    106  C   LEU A  23      -7.893  27.169  -4.263  1.00 23.35              
ATOM    107  O   LEU A  23      -7.279  26.347  -4.925  1.00 24.49              
ATOM    108  CB  LEU A  23      -7.007  27.297  -1.903  1.00 15.38              
ATOM    109  CG  LEU A  23      -6.615  28.776  -1.873  1.00 10.88              
ATOM    110  CD1 LEU A  23      -7.844  29.602  -1.844  1.00  7.36              
ATOM    111  CD2 LEU A  23      -5.668  29.061  -0.689  1.00  9.82              
ATOM    112  N   ARG A  24      -8.334  28.293  -4.791  1.00 25.37              
ATOM    113  CA  ARG A  24      -8.167  28.553  -6.195  1.00 26.02              
ATOM    114  C   ARG A  24      -7.828  29.987  -6.477  1.00 29.84              
ATOM    115  O   ARG A  24      -8.335  30.902  -5.816  1.00 34.78              
ATOM    116  CB  ARG A  24      -9.452  28.208  -6.887  1.00 24.71              
ATOM    117  CG  ARG A  24      -9.459  28.525  -8.321  1.00 23.71              
ATOM    118  CD  ARG A  24     -10.534  27.727  -9.016  1.00 22.40              
ATOM    119  NE  ARG A  24     -11.837  28.301  -8.811  1.00 23.33              
ATOM    120  CZ  ARG A  24     -12.804  28.229  -9.715  1.00 26.95              
ATOM    121  NH1 ARG A  24     -12.591  27.592 -10.867  1.00 28.31              
ATOM    122  NH2 ARG A  24     -13.967  28.844  -9.507  1.00 27.93              
ATOM    123  N   ILE A  25      -6.932  30.183  -7.439  1.00 29.16              
ATOM    124  CA  ILE A  25      -6.495  31.523  -7.836  1.00 26.33              
ATOM    125  C   ILE A  25      -6.825  31.676  -9.317  1.00 28.03              
ATOM    126  O   ILE A  25      -6.050  31.272 -10.184  1.00 28.48              
ATOM    127  CB  ILE A  25      -4.984  31.724  -7.612  1.00 20.93              
ATOM    128  CG1 ILE A  25      -4.597  31.361  -6.183  1.00 17.27              
ATOM    129  CG2 ILE A  25      -4.648  33.124  -7.839  1.00 20.02              
ATOM    130  CD1 ILE A  25      -3.145  31.389  -5.896  1.00 15.39              
ATOM    131  N   LEU A  26      -8.017  32.190  -9.597  1.00 29.09              
ATOM    132  CA  LEU A  26      -8.478  32.415 -10.958  1.00 30.69              
ATOM    133  C   LEU A  26      -7.498  33.336 -11.707  1.00 35.97              
ATOM    134  O   LEU A  26      -6.961  34.288 -11.115  1.00 37.73              
ATOM    135  CB  LEU A  26      -9.855  33.052 -10.921  1.00 26.95              
ATOM    136  CG  LEU A  26     -10.911  32.214 -10.229  1.00 24.27              
ATOM    137  CD1 LEU A  26     -12.233  32.941 -10.216  1.00 24.93              
ATOM    138  CD2 LEU A  26     -11.053  30.911 -10.957  1.00 21.34              
ATOM    139  N   PRO A  27      -7.327  33.139 -13.041  1.00 37.41              
ATOM    140  CA  PRO A  27      -6.409  33.955 -13.849  1.00 37.51              
ATOM    141  C   PRO A  27      -6.586  35.465 -13.667  1.00 40.49              
ATOM    142  O   PRO A  27      -5.623  36.228 -13.793  1.00 44.64              
ATOM    143  CB  PRO A  27      -6.728  33.519 -15.267  1.00 33.93              
ATOM    144  CG  PRO A  27      -8.166  33.213 -15.181  1.00 34.34              
ATOM    145  CD  PRO A  27      -8.233  32.396 -13.925  1.00 35.09              
ATOM    146  N   ASP A  28      -7.788  35.875 -13.282  1.00 39.55              
ATOM    147  CA  ASP A  28      -8.122  37.273 -13.097  1.00 39.32              
ATOM    148  C   ASP A  28      -7.870  37.813 -11.713  1.00 37.71              
ATOM    149  O   ASP A  28      -8.519  38.756 -11.293  1.00 37.09              
ATOM    150  CB  ASP A  28      -9.575  37.459 -13.463  1.00 42.25              
ATOM    151  CG  ASP A  28     -10.421  36.304 -12.997  1.00 44.30              
ATOM    152  OD1 ASP A  28     -10.505  36.142 -11.765  1.00 44.79              
ATOM    153  OD2 ASP A  28     -10.924  35.510 -13.847  1.00 45.29              
ATOM    154  N   GLY A  29      -6.960  37.185 -10.983  1.00 38.85              
ATOM    155  CA  GLY A  29      -6.612  37.636  -9.634  1.00 38.56              
ATOM    156  C   GLY A  29      -7.642  37.391  -8.547  1.00 36.98              
ATOM    157  O   GLY A  29      -7.494  37.846  -7.411  1.00 36.39              
ATOM    158  N   THR A  30      -8.679  36.652  -8.906  1.00 36.26              
ATOM    159  CA  THR A  30      -9.755  36.318  -8.004  1.00 34.82              
ATOM    160  C   THR A  30      -9.520  35.039  -7.228  1.00 36.03              
ATOM    161  O   THR A  30      -9.373  33.976  -7.839  1.00 39.15              
ATOM    162  CB  THR A  30     -11.013  36.166  -8.777  1.00 32.93              
ATOM    163  OG1 THR A  30     -11.350  37.447  -9.272  1.00 32.90              
ATOM    164  CG2 THR A  30     -12.122  35.639  -7.930  1.00 34.51              
ATOM    165  N   VAL A  31      -9.548  35.135  -5.895  1.00 35.10              
ATOM    166  CA  VAL A  31      -9.350  33.969  -5.027  1.00 35.98              
ATOM    167  C   VAL A  31     -10.667  33.380  -4.499  1.00 34.32              
ATOM    168  O   VAL A  31     -11.535  34.099  -4.029  1.00 34.48              
ATOM    169  CB  VAL A  31      -8.474  34.305  -3.832  1.00 36.10              
ATOM    170  CG1 VAL A  31      -8.267  33.062  -2.976  1.00 35.93              
ATOM    171  CG2 VAL A  31      -7.168  34.873  -4.304  1.00 37.12              
ATOM    172  N   ASP A  32     -10.788  32.068  -4.548  1.00 33.55              
ATOM    173  CA  ASP A  32     -11.987  31.408  -4.086  1.00 35.10              
ATOM    174  C   ASP A  32     -11.707  29.945  -3.800  1.00 35.54              
ATOM    175  O   ASP A  32     -10.569  29.587  -3.488  1.00 39.47              
ATOM    176  CB  ASP A  32     -13.124  31.556  -5.108  1.00 34.55              
ATOM    177  CG  ASP A  32     -12.840  30.881  -6.429  1.00 32.42              
ATOM    178  OD1 ASP A  32     -11.656  30.623  -6.737  1.00 31.44              
ATOM    179  OD2 ASP A  32     -13.822  30.618  -7.164  1.00 32.26              
ATOM    180  N   GLY A  33     -12.734  29.111  -3.886  1.00 31.67              
ATOM    181  CA  GLY A  33     -12.545  27.702  -3.631  1.00 28.73              
ATOM    182  C   GLY A  33     -13.366  26.942  -4.620  1.00 26.39              
ATOM    183  O   GLY A  33     -14.251  27.509  -5.212  1.00 28.45              
ATOM    184  N   THR A  34     -13.048  25.684  -4.845  1.00 25.82              
ATOM    185  CA  THR A  34     -13.821  24.892  -5.781  1.00 26.08              
ATOM    186  C   THR A  34     -13.749  23.448  -5.372  1.00 29.89              
ATOM    187  O   THR A  34     -12.795  23.043  -4.703  1.00 32.15              
ATOM    188  CB  THR A  34     -13.319  25.003  -7.228  1.00 22.90              
ATOM    189  OG1 THR A  34     -14.130  24.172  -8.055  1.00 24.07              
ATOM    190  CG2 THR A  34     -11.907  24.561  -7.359  1.00 19.49              
ATOM    191  N   ARG A  35     -14.778  22.689  -5.727  1.00 31.46              
ATOM    192  CA  ARG A  35     -14.802  21.281  -5.391  1.00 35.38              
ATOM    193  C   ARG A  35     -14.343  20.448  -6.584  1.00 38.18              
ATOM    194  O   ARG A  35     -14.122  19.246  -6.463  1.00 41.05              
ATOM    195  CB  ARG A  35     -16.194  20.880  -4.913  1.00 37.67              
ATOM    196  CG  ARG A  35     -16.558  21.465  -3.566  1.00 39.97              
ATOM    197  CD  ARG A  35     -18.033  21.293  -3.265  1.00 43.52              
ATOM    198  NE  ARG A  35     -18.280  20.385  -2.140  1.00 47.39              
ATOM    199  CZ  ARG A  35     -18.911  20.728  -1.017  1.00 48.42              
ATOM    200  NH1 ARG A  35     -19.359  21.972  -0.851  1.00 48.03              
ATOM    201  NH2 ARG A  35     -19.087  19.831  -0.051  1.00 49.03              
ATOM    202  N   ASP A  36     -14.189  21.099  -7.736  1.00 39.42              
ATOM    203  CA  ASP A  36     -13.725  20.442  -8.956  1.00 40.99              
ATOM    204  C   ASP A  36     -12.221  20.194  -8.859  1.00 39.31              
ATOM    205  O   ASP A  36     -11.413  21.110  -8.981  1.00 36.16              
ATOM    206  CB  ASP A  36     -14.040  21.314 -10.187  1.00 46.74              
ATOM    207  CG  ASP A  36     -13.463  20.740 -11.495  1.00 51.45              
ATOM    208  OD1 ASP A  36     -13.231  19.503 -11.560  1.00 53.62              
ATOM    209  OD2 ASP A  36     -13.242  21.524 -12.465  1.00 51.73              
ATOM    210  N   ARG A  37     -11.864  18.941  -8.629  1.00 40.70              
ATOM    211  CA  ARG A  37     -10.473  18.524  -8.502  1.00 40.71              
ATOM    212  C   ARG A  37      -9.747  18.686  -9.818  1.00 41.34              
ATOM    213  O   ARG A  37      -8.551  18.943  -9.858  1.00 39.68              
ATOM    214  CB  ARG A  37     -10.431  17.066  -8.062  1.00 40.58              
ATOM    215  CG  ARG A  37      -9.117  16.364  -8.321  1.00 37.27              
ATOM    216  CD  ARG A  37      -8.033  16.860  -7.421  1.00 33.35              
ATOM    217  NE  ARG A  37      -6.766  16.792  -8.116  1.00 30.02              
ATOM    218  CZ  ARG A  37      -5.641  16.316  -7.592  1.00 30.93              
ATOM    219  NH1 ARG A  37      -5.601  15.845  -6.335  1.00 30.24              
ATOM    220  NH2 ARG A  37      -4.544  16.287  -8.351  1.00 32.03              
ATOM    221  N   SER A  38     -10.499  18.550 -10.900  1.00 44.80              
ATOM    222  CA  SER A  38      -9.954  18.680 -12.243  1.00 49.15              
ATOM    223  C   SER A  38      -9.835  20.133 -12.690  1.00 49.23              
ATOM    224  O   SER A  38      -9.662  20.423 -13.880  1.00 48.95              
ATOM    225  CB  SER A  38     -10.823  17.900 -13.215  1.00 52.10              
ATOM    226  OG  SER A  38     -11.069  16.607 -12.680  1.00 56.22              
ATOM    227  N   ASP A  39      -9.955  21.040 -11.730  1.00 48.54              
ATOM    228  CA  ASP A  39      -9.843  22.455 -12.001  1.00 47.14              
ATOM    229  C   ASP A  39      -8.345  22.741 -12.134  1.00 48.91              
ATOM    230  O   ASP A  39      -7.540  22.413 -11.250  1.00 45.20              
ATOM    231  CB  ASP A  39     -10.464  23.247 -10.850  1.00 43.94              
ATOM    232  CG  ASP A  39     -10.446  24.727 -11.087  1.00 43.09              
ATOM    233  OD1 ASP A  39     -11.260  25.205 -11.908  1.00 43.68              
ATOM    234  OD2 ASP A  39      -9.598  25.409 -10.466  1.00 41.53              
ATOM    235  N   GLN A  40      -7.976  23.346 -13.257  1.00 52.37              
ATOM    236  CA  GLN A  40      -6.573  23.682 -13.534  1.00 53.23              
ATOM    237  C   GLN A  40      -5.998  24.897 -12.796  1.00 50.74              
ATOM    238  O   GLN A  40      -5.044  25.481 -13.266  1.00 51.63              
ATOM    239  CB  GLN A  40      -6.369  23.855 -15.045  1.00 56.08              
ATOM    240  CG  GLN A  40      -6.481  22.547 -15.863  1.00 60.45              
ATOM    241  CD  GLN A  40      -5.202  21.679 -15.861  1.00 63.43              
ATOM    242  OE1 GLN A  40      -4.328  21.821 -14.998  1.00 67.21              
ATOM    243  NE2 GLN A  40      -5.092  20.783 -16.842  1.00 62.53              
ATOM    244  N   HIS A  41      -6.586  25.297 -11.668  1.00 48.46              
ATOM    245  CA  HIS A  41      -6.076  26.447 -10.916  1.00 45.34              
ATOM    246  C   HIS A  41      -6.054  26.193  -9.417  1.00 43.07              
ATOM    247  O   HIS A  41      -6.116  27.138  -8.641  1.00 46.63              
ATOM    248  CB  HIS A  41      -6.903  27.705 -11.148  1.00 46.98              
ATOM    249  CG  HIS A  41      -6.882  28.224 -12.551  1.00 47.46              
ATOM    250  ND1 HIS A  41      -7.520  27.583 -13.598  1.00 47.93              
ATOM    251  CD2 HIS A  41      -6.381  29.375 -13.061  1.00 47.96              
ATOM    252  CE1 HIS A  41      -7.411  28.316 -14.690  1.00 48.99              
ATOM    253  NE2 HIS A  41      -6.726  29.407 -14.394  1.00 49.67              
ATOM    254  N   ILE A  42      -6.015  24.931  -9.001  1.00 37.13              
ATOM    255  CA  ILE A  42      -5.952  24.603  -7.584  1.00 30.45              
ATOM    256  C   ILE A  42      -4.607  24.033  -7.161  1.00 31.80              
ATOM    257  O   ILE A  42      -4.430  23.683  -5.996  1.00 31.69              
ATOM    258  CB  ILE A  42      -7.038  23.654  -7.197  1.00 25.49              
ATOM    259  CG1 ILE A  42      -6.885  22.340  -7.945  1.00 23.15              
ATOM    260  CG2 ILE A  42      -8.331  24.294  -7.470  1.00 26.71              
ATOM    261  CD1 ILE A  42      -7.979  21.342  -7.728  1.00 20.28              
ATOM    262  N   GLN A  43      -3.678  23.903  -8.114  1.00 32.74              
ATOM    263  CA  GLN A  43      -2.330  23.395  -7.835  1.00 30.57              
ATOM    264  C   GLN A  43      -1.489  24.572  -7.333  1.00 29.47              
ATOM    265  O   GLN A  43      -1.243  25.528  -8.069  1.00 29.08              
ATOM    266  CB  GLN A  43      -1.680  22.802  -9.077  1.00 28.91              
ATOM    267  CG  GLN A  43      -2.320  21.563  -9.586  1.00 30.20              
ATOM    268  CD  GLN A  43      -3.541  21.848 -10.455  1.00 35.64              
ATOM    269  OE1 GLN A  43      -4.523  21.114 -10.407  1.00 39.79              
ATOM    270  NE2 GLN A  43      -3.478  22.903 -11.274  1.00 36.33              
ATOM    271  N   LEU A  44      -1.030  24.486  -6.095  1.00 26.50              
ATOM    272  CA  LEU A  44      -0.277  25.567  -5.541  1.00 29.20              
ATOM    273  C   LEU A  44       1.068  25.117  -5.033  1.00 32.03              
ATOM    274  O   LEU A  44       1.179  24.082  -4.431  1.00 34.01              
ATOM    275  CB  LEU A  44      -1.073  26.234  -4.399  1.00 29.58              
ATOM    276  CG  LEU A  44      -2.523  26.652  -4.695  1.00 28.34              
ATOM    277  CD1 LEU A  44      -3.155  27.219  -3.466  1.00 25.85              
ATOM    278  CD2 LEU A  44      -2.598  27.646  -5.833  1.00 29.57              
ATOM    279  N   GLN A  45       2.091  25.916  -5.287  1.00 35.27              
ATOM    280  CA  GLN A  45       3.423  25.617  -4.825  1.00 37.57              
ATOM    281  C   GLN A  45       3.742  26.513  -3.614  1.00 35.41              
ATOM    282  O   GLN A  45       3.679  27.763  -3.705  1.00 34.62              
ATOM    283  CB  GLN A  45       4.417  25.835  -5.970  1.00 43.26              
ATOM    284  CG  GLN A  45       5.905  25.654  -5.566  1.00 50.66              
ATOM    285  CD  GLN A  45       6.231  24.250  -5.051  1.00 53.53              
ATOM    286  OE1 GLN A  45       6.428  24.037  -3.827  1.00 54.29              
ATOM    287  NE2 GLN A  45       6.288  23.281  -5.979  1.00 53.44              
ATOM    288  N   LEU A  46       4.029  25.878  -2.478  1.00 30.64              
ATOM    289  CA  LEU A  46       4.315  26.631  -1.275  1.00 30.03              
ATOM    290  C   LEU A  46       5.811  26.828  -1.091  1.00 31.96              
ATOM    291  O   LEU A  46       6.556  25.890  -0.928  1.00 33.85              
ATOM    292  CB  LEU A  46       3.665  25.968  -0.052  1.00 28.23              
ATOM    293  CG  LEU A  46       2.159  26.096   0.263  1.00 24.88              
ATOM    294  CD1 LEU A  46       1.249  25.677  -0.904  1.00 23.80              
ATOM    295  CD2 LEU A  46       1.838  25.259   1.490  1.00 24.98              
ATOM    296  N   SER A  47       6.230  28.078  -1.087  1.00 35.86              
ATOM    297  CA  SER A  47       7.624  28.489  -0.967  1.00 38.18              
ATOM    298  C   SER A  47       7.967  29.033   0.440  1.00 39.93              
ATOM    299  O   SER A  47       7.475  30.088   0.866  1.00 41.97              
ATOM    300  CB  SER A  47       7.880  29.548  -2.079  1.00 37.65              
ATOM    301  OG  SER A  47       9.103  30.239  -1.921  1.00 37.58              
ATOM    302  N   ALA A  48       8.820  28.334   1.173  1.00 42.35              
ATOM    303  CA  ALA A  48       9.183  28.789   2.525  1.00 45.32              
ATOM    304  C   ALA A  48      10.265  29.852   2.520  1.00 48.70              
ATOM    305  O   ALA A  48      11.408  29.572   2.163  1.00 51.01              
ATOM    306  CB  ALA A  48       9.618  27.620   3.374  1.00 43.97              
ATOM    307  N   GLU A  49       9.928  31.077   2.903  1.00 52.50              
ATOM    308  CA  GLU A  49      10.951  32.126   2.918  1.00 57.71              
ATOM    309  C   GLU A  49      11.751  32.202   4.221  1.00 60.42              
ATOM    310  O   GLU A  49      12.763  32.894   4.308  1.00 61.87              
ATOM    311  CB  GLU A  49      10.384  33.513   2.590  1.00 58.05              
ATOM    312  CG  GLU A  49      11.490  34.432   2.033  1.00 59.48              
ATOM    313  CD  GLU A  49      11.126  35.898   1.956  1.00 60.35              
ATOM    314  OE1 GLU A  49       9.957  36.264   2.227  1.00 60.63              
ATOM    315  OE2 GLU A  49      12.038  36.695   1.634  1.00 60.53              
ATOM    316  N   SER A  50      11.301  31.485   5.236  1.00 61.84              
ATOM    317  CA  SER A  50      11.982  31.492   6.516  1.00 62.23              
ATOM    318  C   SER A  50      11.522  30.261   7.274  1.00 63.23              
ATOM    319  O   SER A  50      11.207  29.230   6.658  1.00 65.52              
ATOM    320  CB  SER A  50      11.655  32.769   7.304  1.00 62.85              
ATOM    321  OG  SER A  50      11.999  33.945   6.578  1.00 62.42              
ATOM    322  N   VAL A  51      11.482  30.365   8.601  1.00 62.63              
ATOM    323  CA  VAL A  51      11.080  29.236   9.413  1.00 60.38              
ATOM    324  C   VAL A  51       9.571  29.135   9.622  1.00 58.38              
ATOM    325  O   VAL A  51       9.043  28.026   9.719  1.00 62.12              
ATOM    326  CB  VAL A  51      11.813  29.225  10.782  1.00 60.56              
ATOM    327  CG1 VAL A  51      11.798  27.819  11.376  1.00 61.52              
ATOM    328  CG2 VAL A  51      13.238  29.695  10.630  1.00 61.31              
ATOM    329  N   GLY A  52       8.863  30.261   9.662  1.00 52.37              
ATOM    330  CA  GLY A  52       7.420  30.190   9.885  1.00 46.60              
ATOM    331  C   GLY A  52       6.546  30.824   8.808  1.00 43.47              
ATOM    332  O   GLY A  52       5.305  30.701   8.864  1.00 40.72              
ATOM    333  N   GLU A  53       7.196  31.467   7.825  1.00 40.56              
ATOM    334  CA  GLU A  53       6.522  32.170   6.734  1.00 37.24              
ATOM    335  C   GLU A  53       6.507  31.325   5.475  1.00 33.63              
ATOM    336  O   GLU A  53       7.337  30.457   5.303  1.00 34.43              
ATOM    337  CB  GLU A  53       7.253  33.484   6.444  1.00 39.52              
ATOM    338  CG  GLU A  53       7.552  34.346   7.692  1.00 41.70              
ATOM    339  CD  GLU A  53       8.665  35.393   7.472  1.00 43.11              
ATOM    340  OE1 GLU A  53       9.057  35.619   6.281  1.00 44.30              
ATOM    341  OE2 GLU A  53       9.153  35.971   8.494  1.00 39.91              
ATOM    342  N   VAL A  54       5.574  31.596   4.575  1.00 28.75              
ATOM    343  CA  VAL A  54       5.491  30.852   3.327  1.00 22.45              
ATOM    344  C   VAL A  54       4.909  31.708   2.207  1.00 21.13              
ATOM    345  O   VAL A  54       4.300  32.750   2.461  1.00 23.13              
ATOM    346  CB  VAL A  54       4.584  29.686   3.494  1.00 19.91              
ATOM    347  CG1 VAL A  54       5.096  28.811   4.602  1.00 19.38              
ATOM    348  CG2 VAL A  54       3.164  30.164   3.781  1.00 17.74              
ATOM    349  N   TYR A  55       5.109  31.279   0.972  1.00 15.68              
ATOM    350  CA  TYR A  55       4.565  31.971  -0.169  1.00 16.30              
ATOM    351  C   TYR A  55       3.645  30.957  -0.837  1.00 17.84              
ATOM    352  O   TYR A  55       4.005  29.801  -0.983  1.00 18.01              
ATOM    353  CB  TYR A  55       5.672  32.391  -1.134  1.00 17.37              
ATOM    354  CG  TYR A  55       6.332  33.745  -0.830  1.00 19.38              
ATOM    355  CD1 TYR A  55       5.760  34.943  -1.270  1.00 21.36              
ATOM    356  CD2 TYR A  55       7.507  33.827  -0.084  1.00 17.43              
ATOM    357  CE1 TYR A  55       6.334  36.164  -0.962  1.00 21.75              
ATOM    358  CE2 TYR A  55       8.075  35.025   0.205  1.00 19.19              
ATOM    359  CZ  TYR A  55       7.489  36.205  -0.220  1.00 21.93              
ATOM    360  OH  TYR A  55       8.052  37.435   0.133  1.00 23.08              
ATOM    361  N   ILE A  56       2.443  31.366  -1.199  1.00 18.38              
ATOM    362  CA  ILE A  56       1.516  30.449  -1.824  1.00 20.49              
ATOM    363  C   ILE A  56       1.340  30.913  -3.245  1.00 23.97              
ATOM    364  O   ILE A  56       0.517  31.775  -3.508  1.00 26.05              
ATOM    365  CB  ILE A  56       0.127  30.433  -1.072  1.00 18.92              
ATOM    366  CG1 ILE A  56       0.356  30.313   0.437  1.00 18.34              
ATOM    367  CG2 ILE A  56      -0.732  29.285  -1.529  1.00 15.97              
ATOM    368  CD1 ILE A  56      -0.856  29.881   1.191  1.00 20.36              
ATOM    369  N   LYS A  57       2.088  30.322  -4.171  1.00 26.78              
ATOM    370  CA  LYS A  57       2.019  30.726  -5.585  1.00 27.99              
ATOM    371  C   LYS A  57       1.496  29.657  -6.505  1.00 27.64              
ATOM    372  O   LYS A  57       2.003  28.537  -6.529  1.00 27.63              
ATOM    373  CB  LYS A  57       3.389  31.194  -6.083  1.00 30.48              
ATOM    374  CG  LYS A  57       3.531  31.189  -7.575  1.00 35.27              
ATOM    375  CD  LYS A  57       4.981  31.133  -7.960  1.00 38.36              
ATOM    376  CE  LYS A  57       5.209  30.306  -9.217  1.00 39.38              
ATOM    377  NZ  LYS A  57       6.652  29.834  -9.209  1.00 41.40              
ATOM    378  N   SER A  58       0.540  30.066  -7.332  1.00 28.08              
ATOM    379  CA  SER A  58      -0.120  29.217  -8.312  1.00 27.19              
ATOM    380  C   SER A  58       0.868  28.681  -9.307  1.00 29.50              
ATOM    381  O   SER A  58       1.726  29.405  -9.787  1.00 31.45              
ATOM    382  CB  SER A  58      -1.183  30.026  -9.028  1.00 25.57              
ATOM    383  OG  SER A  58      -1.683  29.349 -10.148  1.00 27.34              
ATOM    384  N   THR A  59       0.764  27.397  -9.608  1.00 32.30              
ATOM    385  CA  THR A  59       1.654  26.790 -10.589  1.00 36.21              
ATOM    386  C   THR A  59       1.191  27.120 -12.011  1.00 38.26              
ATOM    387  O   THR A  59       2.022  27.439 -12.859  1.00 41.36              
ATOM    388  CB  THR A  59       1.784  25.259 -10.412  1.00 37.42              
ATOM    389  OG1 THR A  59       0.486  24.671 -10.308  1.00 39.63              
ATOM    390  CG2 THR A  59       2.606  24.936  -9.152  1.00 36.81              
ATOM    391  N   GLU A  60      -0.124  27.112 -12.254  1.00 38.35              
ATOM    392  CA  GLU A  60      -0.675  27.417 -13.574  1.00 37.60              
ATOM    393  C   GLU A  60      -0.517  28.885 -14.047  1.00 37.40              
ATOM    394  O   GLU A  60      -0.160  29.131 -15.186  1.00 40.21              
ATOM    395  CB  GLU A  60      -2.111  26.969 -13.645  1.00 37.74              
ATOM    396  CG  GLU A  60      -2.973  27.695 -14.651  1.00 41.23              
ATOM    397  CD  GLU A  60      -2.665  27.330 -16.099  1.00 46.52              
ATOM    398  OE1 GLU A  60      -2.919  26.155 -16.509  1.00 47.46              
ATOM    399  OE2 GLU A  60      -2.194  28.247 -16.835  1.00 48.45              
ATOM    400  N   THR A  61      -0.777  29.871 -13.213  1.00 31.70              
ATOM    401  CA  THR A  61      -0.610  31.223 -13.702  1.00 28.54              
ATOM    402  C   THR A  61       0.560  31.949 -13.075  1.00 27.54              
ATOM    403  O   THR A  61       0.864  33.062 -13.439  1.00 26.65              
ATOM    404  CB  THR A  61      -1.907  32.084 -13.518  1.00 28.84              
ATOM    405  OG1 THR A  61      -2.091  32.457 -12.144  1.00 28.50              
ATOM    406  CG2 THR A  61      -3.109  31.339 -14.007  1.00 26.94              
ATOM    407  N   GLY A  62       1.154  31.362 -12.056  1.00 28.17              
ATOM    408  CA  GLY A  62       2.286  31.988 -11.415  1.00 27.67              
ATOM    409  C   GLY A  62       1.928  33.068 -10.433  1.00 27.80              
ATOM    410  O   GLY A  62       2.812  33.664  -9.813  1.00 28.67              
ATOM    411  N   GLN A  63       0.643  33.328 -10.243  1.00 28.51              
ATOM    412  CA  GLN A  63       0.250  34.371  -9.289  1.00 28.28              
ATOM    413  C   GLN A  63       0.454  33.989  -7.807  1.00 30.27              
ATOM    414  O   GLN A  63       0.274  32.836  -7.404  1.00 30.22              
ATOM    415  CB  GLN A  63      -1.196  34.750  -9.514  1.00 24.58              
ATOM    416  CG  GLN A  63      -1.465  35.339 -10.826  1.00 24.00              
ATOM    417  CD  GLN A  63      -2.924  35.525 -11.040  1.00 25.84              
ATOM    418  OE1 GLN A  63      -3.565  36.265 -10.311  1.00 26.77              
ATOM    419  NE2 GLN A  63      -3.477  34.834 -12.023  1.00 24.19              
ATOM    420  N   TYR A  64       0.869  34.962  -7.015  1.00 30.53              
ATOM    421  CA  TYR A  64       1.057  34.779  -5.600  1.00 32.11              
ATOM    422  C   TYR A  64      -0.221  35.195  -4.875  1.00 34.26              
ATOM    423  O   TYR A  64      -0.775  36.253  -5.150  1.00 35.97              
ATOM    424  CB  TYR A  64       2.191  35.650  -5.118  1.00 33.30              
ATOM    425  CG  TYR A  64       3.548  35.060  -5.363  1.00 36.54              
ATOM    426  CD1 TYR A  64       4.239  35.317  -6.551  1.00 37.32              
ATOM    427  CD2 TYR A  64       4.172  34.280  -4.393  1.00 36.76              
ATOM    428  CE1 TYR A  64       5.518  34.818  -6.767  1.00 37.32              
ATOM    429  CE2 TYR A  64       5.442  33.775  -4.591  1.00 37.08              
ATOM    430  CZ  TYR A  64       6.122  34.049  -5.775  1.00 38.51              
ATOM    431  OH  TYR A  64       7.429  33.597  -5.928  1.00 39.73              
ATOM    432  N   LEU A  65      -0.699  34.369  -3.955  1.00 34.82              
ATOM    433  CA  LEU A  65      -1.902  34.667  -3.187  1.00 32.40              
ATOM    434  C   LEU A  65      -1.496  35.791  -2.279  1.00 31.50              
ATOM    435  O   LEU A  65      -0.428  35.711  -1.646  1.00 30.54              
ATOM    436  CB  LEU A  65      -2.282  33.435  -2.335  1.00 32.82              
ATOM    437  CG  LEU A  65      -3.431  33.525  -1.312  1.00 31.64              
ATOM    438  CD1 LEU A  65      -4.738  33.197  -2.005  1.00 29.37              
ATOM    439  CD2 LEU A  65      -3.196  32.572  -0.133  1.00 29.74              
ATOM    440  N   ALA A  66      -2.298  36.848  -2.228  1.00 31.39              
ATOM    441  CA  ALA A  66      -1.957  37.965  -1.326  1.00 34.12              
ATOM    442  C   ALA A  66      -3.190  38.568  -0.683  1.00 34.07              
ATOM    443  O   ALA A  66      -4.320  38.276  -1.105  1.00 36.97              
ATOM    444  CB  ALA A  66      -1.180  39.040  -2.063  1.00 35.29              
HETATM  445  N   MSE A  67      -2.989  39.408   0.325  1.00 30.52              
HETATM  446  CA  MSE A  67      -4.119  40.019   0.988  1.00 32.66              
HETATM  447  C   MSE A  67      -3.943  41.502   1.197  1.00 33.37              
HETATM  448  O   MSE A  67      -3.042  41.935   1.916  1.00 32.62              
HETATM  449  CB  MSE A  67      -4.362  39.361   2.326  1.00 36.40              
HETATM  450  CG  MSE A  67      -5.574  39.911   3.063  1.00 39.23              
HETATM  451 SE   MSE A  67      -5.809  39.126   4.802  1.00 40.19          S   
HETATM  452  CE  MSE A  67      -7.270  37.981   4.269  1.00 36.46              
ATOM    453  N   ASP A  68      -4.852  42.279   0.628  1.00 33.69              
ATOM    454  CA  ASP A  68      -4.779  43.721   0.733  1.00 35.29              
ATOM    455  C   ASP A  68      -5.113  44.261   2.119  1.00 37.43              
ATOM    456  O   ASP A  68      -5.480  43.505   3.003  1.00 40.50              
ATOM    457  CB  ASP A  68      -5.684  44.364  -0.327  1.00 34.89              
ATOM    458  CG  ASP A  68      -7.148  44.016  -0.154  1.00 33.80              
ATOM    459  OD1 ASP A  68      -7.603  43.835   0.993  1.00 31.50              
ATOM    460  OD2 ASP A  68      -7.850  43.946  -1.189  1.00 36.17              
ATOM    461  N   THR A  69      -5.038  45.581   2.275  1.00 37.49              
ATOM    462  CA  THR A  69      -5.356  46.268   3.529  1.00 34.29              
ATOM    463  C   THR A  69      -6.801  46.127   3.983  1.00 33.15              
ATOM    464  O   THR A  69      -7.115  46.497   5.096  1.00 33.01              
ATOM    465  CB  THR A  69      -5.069  47.796   3.424  1.00 33.88              
ATOM    466  OG1 THR A  69      -5.574  48.298   2.176  1.00 34.84              
ATOM    467  CG2 THR A  69      -3.576  48.109   3.557  1.00 31.35              
ATOM    468  N   ASP A  70      -7.678  45.664   3.101  1.00 34.66              
ATOM    469  CA  ASP A  70      -9.098  45.497   3.421  1.00 37.84              
ATOM    470  C   ASP A  70      -9.427  44.067   3.796  1.00 37.54              
ATOM    471  O   ASP A  70     -10.591  43.711   3.919  1.00 37.01              
ATOM    472  CB  ASP A  70      -9.982  45.857   2.209  1.00 42.13              
ATOM    473  CG  ASP A  70      -9.820  47.303   1.748  1.00 45.79              
ATOM    474  OD1 ASP A  70      -8.834  47.989   2.116  1.00 44.89              
ATOM    475  OD2 ASP A  70     -10.705  47.751   0.990  1.00 49.34              
ATOM    476  N   GLY A  71      -8.408  43.227   3.863  1.00 38.07              
ATOM    477  CA  GLY A  71      -8.633  41.836   4.182  1.00 39.80              
ATOM    478  C   GLY A  71      -9.109  40.980   3.012  1.00 40.62              
ATOM    479  O   GLY A  71      -9.489  39.833   3.228  1.00 42.84              
ATOM    480  N   LEU A  72      -9.120  41.509   1.788  1.00 39.16              
ATOM    481  CA  LEU A  72      -9.538  40.708   0.629  1.00 37.35              
ATOM    482  C   LEU A  72      -8.364  39.976  -0.010  1.00 31.96              
ATOM    483  O   LEU A  72      -7.272  40.516  -0.106  1.00 28.49              
ATOM    484  CB  LEU A  72     -10.256  41.563  -0.419  1.00 43.22              
ATOM    485  CG  LEU A  72     -10.730  40.888  -1.738  1.00 48.00              
ATOM    486  CD1 LEU A  72     -11.569  39.611  -1.503  1.00 48.16              
ATOM    487  CD2 LEU A  72     -11.547  41.901  -2.552  1.00 49.20              
ATOM    488  N   LEU A  73      -8.599  38.730  -0.414  1.00 31.98              
ATOM    489  CA  LEU A  73      -7.573  37.882  -1.032  1.00 30.06              
ATOM    490  C   LEU A  73      -7.568  38.169  -2.497  1.00 30.19              
ATOM    491  O   LEU A  73      -8.642  38.399  -3.073  1.00 31.84              
ATOM    492  CB  LEU A  73      -7.915  36.407  -0.866  1.00 25.74              
ATOM    493  CG  LEU A  73      -8.256  35.865   0.519  1.00 21.39              
ATOM    494  CD1 LEU A  73      -8.615  34.402   0.385  1.00 19.21              
ATOM    495  CD2 LEU A  73      -7.087  36.090   1.457  1.00 17.86              
ATOM    496  N   TYR A  74      -6.382  38.127  -3.107  1.00 29.97              
ATOM    497  CA  TYR A  74      -6.239  38.367  -4.549  1.00 28.79              
ATOM    498  C   TYR A  74      -4.988  37.700  -5.105  1.00 28.91              
ATOM    499  O   TYR A  74      -4.081  37.279  -4.342  1.00 27.78              
ATOM    500  CB  TYR A  74      -6.232  39.875  -4.867  1.00 25.94              
ATOM    501  CG  TYR A  74      -5.013  40.612  -4.363  1.00 24.56              
ATOM    502  CD1 TYR A  74      -3.850  40.667  -5.117  1.00 22.29              
ATOM    503  CD2 TYR A  74      -5.028  41.270  -3.137  1.00 26.02              
ATOM    504  CE1 TYR A  74      -2.731  41.347  -4.674  1.00 23.50              
ATOM    505  CE2 TYR A  74      -3.904  41.969  -2.675  1.00 27.32              
ATOM    506  CZ  TYR A  74      -2.748  42.005  -3.451  1.00 25.87              
ATOM    507  OH  TYR A  74      -1.601  42.674  -2.991  1.00 25.33              
ATOM    508  N   GLY A  75      -4.951  37.606  -6.431  1.00 29.80              
ATOM    509  CA  GLY A  75      -3.817  37.024  -7.114  1.00 33.46              
ATOM    510  C   GLY A  75      -2.864  38.106  -7.590  1.00 35.31              
ATOM    511  O   GLY A  75      -3.221  38.894  -8.457  1.00 37.60              
ATOM    512  N   SER A  76      -1.677  38.177  -6.991  1.00 35.95              
ATOM    513  CA  SER A  76      -0.666  39.163  -7.346  1.00 37.74              
ATOM    514  C   SER A  76       0.389  38.551  -8.260  1.00 40.31              
ATOM    515  O   SER A  76       0.739  37.387  -8.121  1.00 43.15              
ATOM    516  CB  SER A  76       0.016  39.680  -6.083  1.00 37.22              
ATOM    517  OG  SER A  76       0.797  40.827  -6.359  1.00 37.43              
ATOM    518  N   GLN A  77       0.910  39.343  -9.183  1.00 41.30              
ATOM    519  CA  GLN A  77       1.937  38.866 -10.102  1.00 43.89              
ATOM    520  C   GLN A  77       3.332  39.115  -9.513  1.00 45.79              
ATOM    521  O   GLN A  77       4.369  38.817 -10.130  1.00 47.28              
ATOM    522  CB  GLN A  77       1.811  39.580 -11.454  1.00 45.38              
ATOM    523  CG  GLN A  77       0.552  39.245 -12.276  1.00 47.00              
ATOM    524  CD  GLN A  77       0.758  38.089 -13.271  1.00 47.59              
ATOM    525  OE1 GLN A  77       1.716  37.290 -13.164  1.00 47.12              
ATOM    526  NE2 GLN A  77      -0.140  38.007 -14.254  1.00 46.05              
ATOM    527  N   THR A  78       3.360  39.618  -8.288  1.00 44.96              
ATOM    528  CA  THR A  78       4.620  39.914  -7.650  1.00 44.25              
ATOM    529  C   THR A  78       4.639  39.573  -6.183  1.00 45.38              
ATOM    530  O   THR A  78       3.669  39.799  -5.462  1.00 46.65              
ATOM    531  CB  THR A  78       4.879  41.371  -7.733  1.00 45.26              
ATOM    532  OG1 THR A  78       4.499  41.841  -9.026  1.00 48.70              
ATOM    533  CG2 THR A  78       6.339  41.640  -7.492  1.00 46.33              
ATOM    534  N   PRO A  79       5.731  38.982  -5.726  1.00 45.40              
ATOM    535  CA  PRO A  79       5.903  38.602  -4.327  1.00 46.77              
ATOM    536  C   PRO A  79       6.220  39.879  -3.535  1.00 48.62              
ATOM    537  O   PRO A  79       7.359  40.362  -3.550  1.00 52.34              
ATOM    538  CB  PRO A  79       7.134  37.684  -4.366  1.00 46.43              
ATOM    539  CG  PRO A  79       7.159  37.198  -5.744  1.00 45.97              
ATOM    540  CD  PRO A  79       6.782  38.395  -6.554  1.00 45.89              
ATOM    541  N   ASN A  80       5.211  40.465  -2.902  1.00 47.12              
ATOM    542  CA  ASN A  80       5.404  41.677  -2.111  1.00 44.31              
ATOM    543  C   ASN A  80       5.191  41.364  -0.638  1.00 42.24              
ATOM    544  O   ASN A  80       4.986  40.210  -0.294  1.00 39.94              
ATOM    545  CB  ASN A  80       4.421  42.738  -2.568  1.00 43.64              
ATOM    546  CG  ASN A  80       3.039  42.193  -2.765  1.00 43.98              
ATOM    547  OD1 ASN A  80       2.483  42.266  -3.865  1.00 45.74              
ATOM    548  ND2 ASN A  80       2.475  41.615  -1.715  1.00 42.36              
ATOM    549  N   GLU A  81       5.211  42.379   0.224  1.00 41.55              
ATOM    550  CA  GLU A  81       4.971  42.144   1.643  1.00 40.54              
ATOM    551  C   GLU A  81       3.543  41.599   1.858  1.00 36.92              
ATOM    552  O   GLU A  81       3.308  40.842   2.755  1.00 35.35              
ATOM    553  CB  GLU A  81       5.161  43.414   2.454  1.00 45.76              
ATOM    554  CG  GLU A  81       3.909  44.295   2.538  1.00 54.93              
ATOM    555  CD  GLU A  81       4.068  45.523   3.460  1.00 59.67              
ATOM    556  OE1 GLU A  81       4.203  45.343   4.696  1.00 60.56              
ATOM    557  OE2 GLU A  81       4.012  46.677   2.954  1.00 62.95              
ATOM    558  N   GLU A  82       2.606  41.945   0.988  1.00 36.90              
ATOM    559  CA  GLU A  82       1.242  41.464   1.115  1.00 39.25              
ATOM    560  C   GLU A  82       1.012  40.003   0.690  1.00 39.13              
ATOM    561  O   GLU A  82      -0.148  39.536   0.644  1.00 37.46              
ATOM    562  CB  GLU A  82       0.291  42.364   0.322  1.00 44.72              
ATOM    563  CG  GLU A  82       0.321  43.865   0.725  1.00 52.03              
ATOM    564  CD  GLU A  82      -0.921  44.650   0.234  1.00 55.71              
ATOM    565  OE1 GLU A  82      -1.350  44.450  -0.939  1.00 54.87              
ATOM    566  OE2 GLU A  82      -1.477  45.450   1.043  1.00 57.58              
ATOM    567  N   CYS A  83       2.098  39.280   0.385  1.00 39.41              
ATOM    568  CA  CYS A  83       2.026  37.870  -0.071  1.00 35.41              
ATOM    569  C   CYS A  83       2.599  36.863   0.879  1.00 28.26              
ATOM    570  O   CYS A  83       2.502  35.688   0.633  1.00 26.06              
ATOM    571  CB  CYS A  83       2.741  37.691  -1.408  1.00 41.11              
ATOM    572  SG  CYS A  83       1.956  38.482  -2.848  1.00 49.88              
ATOM    573  N   LEU A  84       3.228  37.334   1.942  1.00 25.13              
ATOM    574  CA  LEU A  84       3.821  36.482   2.956  1.00 25.66              
ATOM    575  C   LEU A  84       2.798  36.068   4.026  1.00 27.28              
ATOM    576  O   LEU A  84       2.032  36.905   4.518  1.00 29.16              
ATOM    577  CB  LEU A  84       4.938  37.233   3.617  1.00 27.64              
ATOM    578  CG  LEU A  84       6.083  36.434   4.204  1.00 31.88              
ATOM    579  CD1 LEU A  84       6.676  35.570   3.121  1.00 33.45              
ATOM    580  CD2 LEU A  84       7.141  37.374   4.751  1.00 32.19              
ATOM    581  N   PHE A  85       2.760  34.778   4.373  1.00 27.58              
ATOM    582  CA  PHE A  85       1.827  34.247   5.392  1.00 24.02              
ATOM    583  C   PHE A  85       2.508  33.322   6.406  1.00 22.26              
ATOM    584  O   PHE A  85       3.424  32.580   6.069  1.00 24.23              
ATOM    585  CB  PHE A  85       0.728  33.461   4.746  1.00 22.86              
ATOM    586  CG  PHE A  85      -0.122  34.238   3.812  1.00 24.22              
ATOM    587  CD1 PHE A  85      -1.182  34.984   4.282  1.00 27.82              
ATOM    588  CD2 PHE A  85       0.061  34.141   2.456  1.00 24.71              
ATOM    589  CE1 PHE A  85      -2.056  35.620   3.410  1.00 29.44              
ATOM    590  CE2 PHE A  85      -0.807  34.771   1.559  1.00 27.14              
ATOM    591  CZ  PHE A  85      -1.864  35.508   2.032  1.00 28.31              
ATOM    592  N   LEU A  86       2.081  33.395   7.657  1.00 21.87              
ATOM    593  CA  LEU A  86       2.610  32.543   8.724  1.00 21.94              
ATOM    594  C   LEU A  86       1.795  31.234   8.712  1.00 26.07              
ATOM    595  O   LEU A  86       0.551  31.249   8.771  1.00 28.25              
ATOM    596  CB  LEU A  86       2.414  33.196  10.078  1.00 16.97              
ATOM    597  CG  LEU A  86       3.054  34.526  10.291  1.00 16.59              
ATOM    598  CD1 LEU A  86       2.712  35.006  11.675  1.00 18.52              
ATOM    599  CD2 LEU A  86       4.541  34.374  10.151  1.00 18.45              
ATOM    600  N   GLU A  87       2.472  30.099   8.630  1.00 27.07              
ATOM    601  CA  GLU A  87       1.760  28.832   8.610  1.00 26.09              
ATOM    602  C   GLU A  87       1.778  28.329  10.025  1.00 25.48              
ATOM    603  O   GLU A  87       2.866  28.216  10.602  1.00 27.03              
ATOM    604  CB  GLU A  87       2.492  27.853   7.719  1.00 25.34              
ATOM    605  CG  GLU A  87       1.735  26.607   7.461  1.00 26.54              
ATOM    606  CD  GLU A  87       2.393  25.759   6.406  1.00 29.25              
ATOM    607  OE1 GLU A  87       3.636  25.580   6.515  1.00 29.65              
ATOM    608  OE2 GLU A  87       1.680  25.280   5.472  1.00 27.56              
ATOM    609  N   ARG A  88       0.604  28.086  10.612  1.00 23.53              
ATOM    610  CA  ARG A  88       0.523  27.560  11.983  1.00 21.14              
ATOM    611  C   ARG A  88      -0.296  26.271  12.068  1.00 19.61              
ATOM    612  O   ARG A  88      -0.966  25.862  11.124  1.00 20.07              
ATOM    613  CB  ARG A  88      -0.048  28.607  12.949  1.00 20.66              
ATOM    614  CG  ARG A  88       0.834  29.833  13.174  1.00 21.04              
ATOM    615  CD  ARG A  88       2.215  29.449  13.590  1.00 23.67              
ATOM    616  NE  ARG A  88       3.104  30.590  13.789  1.00 26.08              
ATOM    617  CZ  ARG A  88       4.064  30.986  12.947  1.00 27.11              
ATOM    618  NH1 ARG A  88       4.280  30.345  11.799  1.00 27.31              
ATOM    619  NH2 ARG A  88       4.852  32.004  13.282  1.00 26.37              
ATOM    620  N   LEU A  89      -0.257  25.629  13.222  1.00 19.52              
ATOM    621  CA  LEU A  89      -1.018  24.399  13.407  1.00 19.73              
ATOM    622  C   LEU A  89      -2.105  24.540  14.458  1.00 24.94              
ATOM    623  O   LEU A  89      -1.850  25.075  15.563  1.00 26.02              
ATOM    624  CB  LEU A  89      -0.093  23.259  13.804  1.00 14.86              
ATOM    625  CG  LEU A  89       0.421  22.438  12.635  1.00 12.82              
ATOM    626  CD1 LEU A  89       1.437  21.444  13.152  1.00 11.80              
ATOM    627  CD2 LEU A  89      -0.737  21.756  11.921  1.00 10.44              
ATOM    628  N   GLU A  90      -3.320  24.131  14.071  1.00 28.08              
ATOM    629  CA  GLU A  90      -4.486  24.127  14.956  1.00 33.17              
ATOM    630  C   GLU A  90      -4.257  22.870  15.843  1.00 35.78              
ATOM    631  O   GLU A  90      -3.451  22.009  15.465  1.00 36.99              
ATOM    632  CB  GLU A  90      -5.778  23.986  14.110  1.00 34.28              
ATOM    633  CG  GLU A  90      -7.097  23.733  14.904  1.00 38.82              
ATOM    634  CD  GLU A  90      -7.563  24.936  15.823  1.00 41.25              
ATOM    635  OE1 GLU A  90      -6.892  25.257  16.857  1.00 39.22              
ATOM    636  OE2 GLU A  90      -8.633  25.535  15.523  1.00 42.08              
ATOM    637  N   GLU A  91      -4.931  22.740  16.993  1.00 36.66              
ATOM    638  CA  GLU A  91      -4.729  21.541  17.797  1.00 37.77              
ATOM    639  C   GLU A  91      -5.339  20.265  17.190  1.00 34.07              
ATOM    640  O   GLU A  91      -5.150  19.158  17.691  1.00 35.05              
ATOM    641  CB  GLU A  91      -5.167  21.726  19.243  1.00 43.91              
ATOM    642  CG  GLU A  91      -4.532  20.664  20.171  1.00 50.72              
ATOM    643  CD  GLU A  91      -3.096  20.245  19.747  1.00 54.60              
ATOM    644  OE1 GLU A  91      -2.154  21.057  19.946  1.00 57.16              
ATOM    645  OE2 GLU A  91      -2.922  19.106  19.208  1.00 54.27              
ATOM    646  N   ASN A  92      -6.005  20.415  16.063  1.00 30.46              
ATOM    647  CA  ASN A  92      -6.565  19.284  15.383  1.00 29.06              
ATOM    648  C   ASN A  92      -5.767  18.945  14.150  1.00 26.22              
ATOM    649  O   ASN A  92      -6.240  18.263  13.253  1.00 24.50              
ATOM    650  CB  ASN A  92      -7.992  19.564  15.021  1.00 35.68              
ATOM    651  CG  ASN A  92      -8.911  19.248  16.132  1.00 38.94              
ATOM    652  OD1 ASN A  92      -8.467  19.022  17.262  1.00 40.63              
ATOM    653  ND2 ASN A  92     -10.205  19.215  15.839  1.00 40.47              
ATOM    654  N   HIS A  93      -4.545  19.446  14.118  1.00 24.49              
ATOM    655  CA  HIS A  93      -3.628  19.182  13.042  1.00 25.76              
ATOM    656  C   HIS A  93      -4.106  19.669  11.682  1.00 26.50              
ATOM    657  O   HIS A  93      -4.185  18.926  10.705  1.00 28.02              
ATOM    658  CB  HIS A  93      -3.314  17.703  13.018  1.00 28.24              
ATOM    659  CG  HIS A  93      -3.123  17.127  14.381  1.00 29.96              
ATOM    660  ND1 HIS A  93      -4.102  16.408  15.028  1.00 30.86              
ATOM    661  CD2 HIS A  93      -2.096  17.246  15.252  1.00 31.62              
ATOM    662  CE1 HIS A  93      -3.696  16.111  16.242  1.00 32.30              
ATOM    663  NE2 HIS A  93      -2.482  16.606  16.410  1.00 33.44              
ATOM    664  N   TYR A  94      -4.493  20.924  11.640  1.00 24.33              
ATOM    665  CA  TYR A  94      -4.886  21.523  10.401  1.00 20.80              
ATOM    666  C   TYR A  94      -3.924  22.727  10.263  1.00 19.78              
ATOM    667  O   TYR A  94      -3.391  23.247  11.277  1.00 13.54              
ATOM    668  CB  TYR A  94      -6.319  21.983  10.498  1.00 19.37              
ATOM    669  CG  TYR A  94      -7.309  21.010   9.993  1.00 18.80              
ATOM    670  CD1 TYR A  94      -7.439  20.765   8.643  1.00 21.40              
ATOM    671  CD2 TYR A  94      -8.160  20.363  10.854  1.00 20.54              
ATOM    672  CE1 TYR A  94      -8.415  19.886   8.139  1.00 21.18              
ATOM    673  CE2 TYR A  94      -9.136  19.482  10.376  1.00 21.12              
ATOM    674  CZ  TYR A  94      -9.260  19.249   9.016  1.00 22.02              
ATOM    675  OH  TYR A  94     -10.250  18.392   8.539  1.00 24.46              
ATOM    676  N   ASN A  95      -3.633  23.105   9.023  1.00 19.99              
ATOM    677  CA  ASN A  95      -2.779  24.244   8.779  1.00 19.46              
ATOM    678  C   ASN A  95      -3.612  25.505   8.629  1.00 22.64              
ATOM    679  O   ASN A  95      -4.630  25.500   7.918  1.00 27.04              
ATOM    680  CB  ASN A  95      -1.967  24.034   7.524  1.00 16.51              
ATOM    681  CG  ASN A  95      -0.694  23.313   7.790  1.00 17.19              
ATOM    682  OD1 ASN A  95      -0.042  23.494   8.821  1.00 15.52              
ATOM    683  ND2 ASN A  95      -0.333  22.455   6.869  1.00 21.28              
ATOM    684  N   THR A  96      -3.212  26.578   9.306  1.00 20.81              
ATOM    685  CA  THR A  96      -3.898  27.852   9.197  1.00 18.31              
ATOM    686  C   THR A  96      -2.888  28.897   8.775  1.00 19.15              
ATOM    687  O   THR A  96      -1.762  28.926   9.251  1.00 21.57              
ATOM    688  CB  THR A  96      -4.560  28.227  10.507  1.00 19.46              
ATOM    689  OG1 THR A  96      -3.684  27.933  11.604  1.00 21.28              
ATOM    690  CG2 THR A  96      -5.836  27.482  10.672  1.00 16.82              
ATOM    691  N   TYR A  97      -3.296  29.752   7.862  1.00 21.02              
ATOM    692  CA  TYR A  97      -2.433  30.808   7.338  1.00 23.85              
ATOM    693  C   TYR A  97      -2.876  32.225   7.690  1.00 22.57              
ATOM    694  O   TYR A  97      -3.909  32.685   7.224  1.00 25.79              
ATOM    695  CB  TYR A  97      -2.360  30.654   5.822  1.00 24.96              
ATOM    696  CG  TYR A  97      -1.928  29.270   5.394  1.00 25.52              
ATOM    697  CD1 TYR A  97      -2.835  28.239   5.303  1.00 23.75              
ATOM    698  CD2 TYR A  97      -0.600  28.995   5.126  1.00 27.24              
ATOM    699  CE1 TYR A  97      -2.438  26.986   4.970  1.00 23.61              
ATOM    700  CE2 TYR A  97      -0.192  27.723   4.788  1.00 27.39              
ATOM    701  CZ  TYR A  97      -1.119  26.729   4.719  1.00 24.88              
ATOM    702  OH  TYR A  97      -0.700  25.473   4.432  1.00 24.57              
ATOM    703  N   ILE A  98      -2.095  32.911   8.503  1.00 19.12              
ATOM    704  CA  ILE A  98      -2.422  34.274   8.878  1.00 19.11              
ATOM    705  C   ILE A  98      -1.506  35.296   8.164  1.00 20.74              
ATOM    706  O   ILE A  98      -0.289  35.118   8.095  1.00 19.57              
ATOM    707  CB  ILE A  98      -2.294  34.466  10.389  1.00 18.37              
ATOM    708  CG1 ILE A  98      -2.751  35.862  10.793  1.00 15.72              
ATOM    709  CG2 ILE A  98      -0.843  34.216  10.861  1.00 17.14              
ATOM    710  CD1 ILE A  98      -2.692  36.055  12.293  1.00 16.99              
ATOM    711  N   SER A  99      -2.107  36.362   7.637  1.00 20.82              
ATOM    712  CA  SER A  99      -1.388  37.427   6.934  1.00 18.53              
ATOM    713  C   SER A  99      -0.292  37.997   7.837  1.00 17.40              
ATOM    714  O   SER A  99      -0.559  38.558   8.881  1.00 19.80              
ATOM    715  CB  SER A  99      -2.383  38.527   6.493  1.00 18.03              
ATOM    716  OG  SER A  99      -1.749  39.789   6.299  1.00 18.28              
ATOM    717  N   LYS A 100       0.954  37.865   7.422  1.00 17.38              
ATOM    718  CA  LYS A 100       2.063  38.364   8.213  1.00 18.40              
ATOM    719  C   LYS A 100       1.976  39.851   8.407  1.00 20.69              
ATOM    720  O   LYS A 100       2.373  40.364   9.450  1.00 21.36              
ATOM    721  CB  LYS A 100       3.401  38.056   7.547  1.00 18.85              
ATOM    722  CG  LYS A 100       4.563  38.326   8.463  1.00 21.19              
ATOM    723  CD  LYS A 100       5.861  38.378   7.758  1.00 25.52              
ATOM    724  CE  LYS A 100       6.950  38.495   8.813  1.00 32.14              
ATOM    725  NZ  LYS A 100       8.344  38.673   8.275  1.00 36.60              
ATOM    726  N   LYS A 101       1.480  40.558   7.393  1.00 22.66              
ATOM    727  CA  LYS A 101       1.365  42.016   7.484  1.00 23.78              
ATOM    728  C   LYS A 101       0.337  42.367   8.534  1.00 23.69              
ATOM    729  O   LYS A 101       0.637  43.079   9.542  1.00 22.40              
ATOM    730  CB  LYS A 101       0.940  42.628   6.160  1.00 22.81              
ATOM    731  CG  LYS A 101       1.226  44.119   6.130  1.00 23.89              
ATOM    732  CD  LYS A 101       0.834  44.751   4.814  1.00 27.63              
ATOM    733  CE  LYS A 101       1.153  46.238   4.854  1.00 30.35              
ATOM    734  NZ  LYS A 101       0.927  46.846   3.502  1.00 33.07              
ATOM    735  N   HIS A 102      -0.856  41.807   8.307  1.00 21.32              
ATOM    736  CA  HIS A 102      -1.982  42.005   9.186  1.00 21.84              
ATOM    737  C   HIS A 102      -2.035  40.995  10.324  1.00 18.73              
ATOM    738  O   HIS A 102      -3.089  40.653  10.809  1.00 24.46              
ATOM    739  CB  HIS A 102      -3.232  41.941   8.350  1.00 24.54              
ATOM    740  CG  HIS A 102      -3.198  42.883   7.199  1.00 30.21              
ATOM    741  ND1 HIS A 102      -3.014  44.238   7.356  1.00 31.55              
ATOM    742  CD2 HIS A 102      -3.297  42.664   5.870  1.00 34.85              
ATOM    743  CE1 HIS A 102      -3.003  44.818   6.168  1.00 34.65              
ATOM    744  NE2 HIS A 102      -3.173  43.884   5.249  1.00 36.48              
ATOM    745  N   ALA A 103      -0.892  40.534  10.767  1.00 11.59              
ATOM    746  CA  ALA A 103      -0.840  39.580  11.813  1.00 11.21              
ATOM    747  C   ALA A 103      -1.604  40.037  13.079  1.00 15.79              
ATOM    748  O   ALA A 103      -2.505  39.368  13.542  1.00 17.79              
ATOM    749  CB  ALA A 103       0.627  39.298  12.121  1.00 12.45              
ATOM    750  N   GLU A 104      -1.296  41.221  13.588  1.00 18.26              
ATOM    751  CA  GLU A 104      -1.911  41.726  14.800  1.00 19.90              
ATOM    752  C   GLU A 104      -3.450  41.906  14.734  1.00 19.75              
ATOM    753  O   GLU A 104      -4.137  41.918  15.748  1.00 20.17              
ATOM    754  CB  GLU A 104      -1.184  42.997  15.282  1.00 23.92              
ATOM    755  CG  GLU A 104      -1.662  44.339  14.645  1.00 29.79              
ATOM    756  CD  GLU A 104      -1.097  44.651  13.261  1.00 30.45              
ATOM    757  OE1 GLU A 104      -0.327  43.835  12.708  1.00 31.26              
ATOM    758  OE2 GLU A 104      -1.432  45.731  12.718  1.00 30.55              
ATOM    759  N   LYS A 105      -4.005  42.018  13.544  1.00 20.28              
ATOM    760  CA  LYS A 105      -5.457  42.142  13.413  1.00 22.25              
ATOM    761  C   LYS A 105      -6.116  40.787  13.479  1.00 25.21              
ATOM    762  O   LYS A 105      -7.327  40.721  13.621  1.00 29.57              
ATOM    763  CB  LYS A 105      -5.837  42.768  12.069  1.00 22.39              
ATOM    764  CG  LYS A 105      -5.245  44.174  11.857  1.00 22.06              
ATOM    765  CD  LYS A 105      -5.571  44.682  10.457  1.00 22.34              
ATOM    766  CE  LYS A 105      -4.704  45.868  10.154  1.00 22.87              
ATOM    767  NZ  LYS A 105      -3.306  45.688  10.685  1.00 24.02              
ATOM    768  N   ASN A 106      -5.325  39.712  13.338  1.00 26.11              
ATOM    769  CA  ASN A 106      -5.792  38.307  13.344  1.00 23.81              
ATOM    770  C   ASN A 106      -6.661  38.017  12.126  1.00 21.34              
ATOM    771  O   ASN A 106      -7.837  37.705  12.251  1.00 18.99              
ATOM    772  CB  ASN A 106      -6.557  37.986  14.631  1.00 26.15              
ATOM    773  CG  ASN A 106      -6.486  36.508  15.004  1.00 26.57              
ATOM    774  OD1 ASN A 106      -7.502  35.790  15.066  1.00 22.93              
ATOM    775  ND2 ASN A 106      -5.275  36.049  15.269  1.00 29.49              
ATOM    776  N   TRP A 107      -6.075  38.221  10.947  1.00 22.44              
ATOM    777  CA  TRP A 107      -6.741  37.988   9.644  1.00 24.84              
ATOM    778  C   TRP A 107      -6.143  36.737   9.032  1.00 22.86              
ATOM    779  O   TRP A 107      -4.910  36.628   8.866  1.00 27.10              
ATOM    780  CB  TRP A 107      -6.445  39.129   8.682  1.00 32.00              
ATOM    781  CG  TRP A 107      -7.258  40.378   8.877  1.00 40.06              
ATOM    782  CD1 TRP A 107      -8.297  40.562   9.728  1.00 41.25              
ATOM    783  CD2 TRP A 107      -7.121  41.598   8.141  1.00 44.24              
ATOM    784  NE1 TRP A 107      -8.830  41.810   9.565  1.00 41.97              
ATOM    785  CE2 TRP A 107      -8.123  42.470   8.597  1.00 44.38              
ATOM    786  CE3 TRP A 107      -6.244  42.041   7.133  1.00 45.42              
ATOM    787  CZ2 TRP A 107      -8.277  43.755   8.082  1.00 46.04              
ATOM    788  CZ3 TRP A 107      -6.400  43.315   6.625  1.00 45.36              
ATOM    789  CH2 TRP A 107      -7.408  44.157   7.101  1.00 46.25              
ATOM    790  N   PHE A 108      -6.978  35.788   8.676  1.00 15.90              
ATOM    791  CA  PHE A 108      -6.452  34.566   8.124  1.00 14.76              
ATOM    792  C   PHE A 108      -6.940  34.394   6.712  1.00 12.46              
ATOM    793  O   PHE A 108      -7.734  35.165   6.215  1.00 11.44              
ATOM    794  CB  PHE A 108      -6.946  33.354   8.948  1.00 19.24              
ATOM    795  CG  PHE A 108      -6.337  33.219  10.324  1.00 19.63              
ATOM    796  CD1 PHE A 108      -6.911  33.843  11.414  1.00 18.47              
ATOM    797  CD2 PHE A 108      -5.187  32.479  10.515  1.00 20.21              
ATOM    798  CE1 PHE A 108      -6.342  33.747  12.689  1.00 18.26              
ATOM    799  CE2 PHE A 108      -4.620  32.377  11.774  1.00 21.22              
ATOM    800  CZ  PHE A 108      -5.202  33.023  12.873  1.00 19.24              
ATOM    801  N   VAL A 109      -6.450  33.349   6.072  1.00 10.93              
ATOM    802  CA  VAL A 109      -6.853  32.984   4.726  1.00  9.36              
ATOM    803  C   VAL A 109      -8.042  32.101   5.027  1.00  9.58              
ATOM    804  O   VAL A 109      -7.966  31.252   5.908  1.00 13.37              
ATOM    805  CB  VAL A 109      -5.728  32.160   4.066  1.00  6.88              
ATOM    806  CG1 VAL A 109      -6.097  31.678   2.672  1.00  4.78              
ATOM    807  CG2 VAL A 109      -4.450  32.970   4.067  1.00  6.90              
ATOM    808  N   GLY A 110      -9.158  32.314   4.368  1.00  7.67              
ATOM    809  CA  GLY A 110     -10.287  31.446   4.664  1.00 14.80              
ATOM    810  C   GLY A 110     -11.394  31.386   3.628  1.00 17.38              
ATOM    811  O   GLY A 110     -11.632  32.335   2.893  1.00 16.49              
ATOM    812  N   LEU A 111     -12.097  30.273   3.572  1.00 17.94              
ATOM    813  CA  LEU A 111     -13.157  30.169   2.597  1.00 20.95              
ATOM    814  C   LEU A 111     -14.513  29.947   3.259  1.00 23.35              
ATOM    815  O   LEU A 111     -14.645  29.164   4.211  1.00 23.65              
ATOM    816  CB  LEU A 111     -12.878  29.015   1.634  1.00 22.29              
ATOM    817  CG  LEU A 111     -11.560  29.051   0.877  1.00 23.24              
ATOM    818  CD1 LEU A 111     -11.350  27.752   0.140  1.00 23.83              
ATOM    819  CD2 LEU A 111     -11.591  30.218  -0.083  1.00 23.72              
ATOM    820  N   LYS A 112     -15.514  30.678   2.788  1.00 23.50              
ATOM    821  CA  LYS A 112     -16.861  30.519   3.281  1.00 22.35              
ATOM    822  C   LYS A 112     -17.265  29.098   2.951  1.00 23.07              
ATOM    823  O   LYS A 112     -16.734  28.481   2.014  1.00 20.62              
ATOM    824  CB  LYS A 112     -17.807  31.458   2.564  1.00 22.17              
ATOM    825  CG  LYS A 112     -17.649  32.915   2.930  1.00 26.06              
ATOM    826  CD  LYS A 112     -18.708  33.698   2.217  1.00 27.55              
ATOM    827  CE  LYS A 112     -18.765  35.132   2.652  1.00 32.04              
ATOM    828  NZ  LYS A 112     -19.855  35.846   1.882  1.00 36.30              
ATOM    829  N   LYS A 113     -18.230  28.590   3.705  1.00 26.83              
ATOM    830  CA  LYS A 113     -18.745  27.254   3.493  1.00 27.61              
ATOM    831  C   LYS A 113     -19.293  27.123   2.087  1.00 27.53              
ATOM    832  O   LYS A 113     -19.223  26.077   1.500  1.00 28.19              
ATOM    833  CB  LYS A 113     -19.813  26.946   4.520  1.00 31.35              
ATOM    834  CG  LYS A 113     -20.325  25.548   4.444  1.00 34.99              
ATOM    835  CD  LYS A 113     -21.175  25.230   5.635  1.00 40.01              
ATOM    836  CE  LYS A 113     -21.754  23.830   5.496  1.00 46.24              
ATOM    837  NZ  LYS A 113     -22.628  23.465   6.674  1.00 51.82              
ATOM    838  N   ASN A 114     -19.794  28.215   1.526  1.00 31.46              
ATOM    839  CA  ASN A 114     -20.353  28.223   0.156  1.00 32.85              
ATOM    840  C   ASN A 114     -19.290  28.253  -0.904  1.00 33.27              
ATOM    841  O   ASN A 114     -19.621  28.297  -2.063  1.00 34.59              
ATOM    842  CB  ASN A 114     -21.214  29.449  -0.067  1.00 36.22              
ATOM    843  CG  ASN A 114     -20.483  30.699   0.280  1.00 43.36              
ATOM    844  OD1 ASN A 114     -19.293  30.832  -0.025  1.00 44.86              
ATOM    845  ND2 ASN A 114     -21.145  31.595   1.012  1.00 47.87              
ATOM    846  N   GLY A 115     -18.027  28.347  -0.500  1.00 34.25              
ATOM    847  CA  GLY A 115     -16.947  28.381  -1.465  1.00 33.52              
ATOM    848  C   GLY A 115     -16.209  29.696  -1.613  1.00 35.46              
ATOM    849  O   GLY A 115     -15.012  29.671  -1.932  1.00 36.19              
ATOM    850  N   SER A 116     -16.896  30.829  -1.412  1.00 36.59              
ATOM    851  CA  SER A 116     -16.282  32.174  -1.546  1.00 35.98              
ATOM    852  C   SER A 116     -15.144  32.390  -0.555  1.00 33.97              
ATOM    853  O   SER A 116     -14.984  31.615   0.373  1.00 36.61              
ATOM    854  CB  SER A 116     -17.331  33.262  -1.300  1.00 35.22              
ATOM    855  OG  SER A 116     -18.434  33.151  -2.177  1.00 35.45              
ATOM    856  N   CYS A 117     -14.320  33.400  -0.772  1.00 32.57              
ATOM    857  CA  CYS A 117     -13.258  33.693   0.188  1.00 34.20              
ATOM    858  C   CYS A 117     -13.940  34.433   1.349  1.00 34.92              
ATOM    859  O   CYS A 117     -15.019  34.985   1.190  1.00 36.18              
ATOM    860  CB  CYS A 117     -12.143  34.552  -0.433  1.00 34.55              
ATOM    861  SG  CYS A 117     -12.695  35.866  -1.634  1.00 37.35              
ATOM    862  N   LYS A 118     -13.385  34.345   2.547  1.00 35.57              
ATOM    863  CA  LYS A 118     -13.964  35.021   3.715  1.00 32.11              
ATOM    864  C   LYS A 118     -13.048  36.202   3.886  1.00 29.40              
ATOM    865  O   LYS A 118     -11.833  36.082   3.754  1.00 27.47              
ATOM    866  CB  LYS A 118     -13.889  34.122   4.958  1.00 31.38              
ATOM    867  CG  LYS A 118     -15.004  34.300   5.977  1.00 29.04              
ATOM    868  CD  LYS A 118     -14.571  33.704   7.311  1.00 27.77              
ATOM    869  CE  LYS A 118     -15.702  33.610   8.332  1.00 25.43              
ATOM    870  NZ  LYS A 118     -16.670  32.542   8.044  1.00 22.13              
ATOM    871  N   ARG A 119     -13.624  37.363   4.134  1.00 31.27              
ATOM    872  CA  ARG A 119     -12.807  38.574   4.294  1.00 33.79              
ATOM    873  C   ARG A 119     -11.895  38.542   5.520  1.00 31.17              
ATOM    874  O   ARG A 119     -12.285  38.093   6.581  1.00 31.94              
ATOM    875  CB  ARG A 119     -13.697  39.834   4.304  1.00 35.40              
ATOM    876  CG  ARG A 119     -14.408  40.082   2.961  1.00 36.46              
ATOM    877  CD  ARG A 119     -14.901  41.521   2.831  1.00 38.41              
ATOM    878  NE  ARG A 119     -16.199  41.778   3.466  1.00 39.35              
ATOM    879  CZ  ARG A 119     -16.372  42.371   4.649  1.00 39.45              
ATOM    880  NH1 ARG A 119     -15.334  42.784   5.370  1.00 36.78              
ATOM    881  NH2 ARG A 119     -17.608  42.548   5.107  1.00 40.81              
ATOM    882  N   GLY A 120     -10.664  38.974   5.336  1.00 28.53              
ATOM    883  CA  GLY A 120      -9.712  39.028   6.424  1.00 31.17              
ATOM    884  C   GLY A 120     -10.388  39.407   7.727  1.00 34.72              
ATOM    885  O   GLY A 120     -10.458  38.589   8.645  1.00 37.57              
ATOM    886  N   PRO A 121     -10.951  40.618   7.830  1.00 35.35              
ATOM    887  CA  PRO A 121     -11.626  41.039   9.054  1.00 33.04              
ATOM    888  C   PRO A 121     -12.696  40.071   9.546  1.00 31.23              
ATOM    889  O   PRO A 121     -12.975  40.068  10.718  1.00 34.94              
ATOM    890  CB  PRO A 121     -12.233  42.381   8.653  1.00 34.41              
ATOM    891  CG  PRO A 121     -12.445  42.248   7.162  1.00 35.00              
ATOM    892  CD  PRO A 121     -11.130  41.633   6.782  1.00 36.37              
ATOM    893  N   ARG A 122     -13.318  39.295   8.662  1.00 29.22              
ATOM    894  CA  ARG A 122     -14.343  38.328   9.078  1.00 30.94              
ATOM    895  C   ARG A 122     -13.864  36.947   9.561  1.00 30.47              
ATOM    896  O   ARG A 122     -14.685  36.093   9.872  1.00 30.11              
ATOM    897  CB  ARG A 122     -15.429  38.130   8.013  1.00 31.38              
ATOM    898  CG  ARG A 122     -16.339  39.317   7.877  1.00 34.18              
ATOM    899  CD  ARG A 122     -16.740  39.899   9.235  1.00 37.50              
ATOM    900  NE  ARG A 122     -16.843  41.357   9.169  1.00 40.66              
ATOM    901  CZ  ARG A 122     -17.843  41.997   8.580  1.00 40.24              
ATOM    902  NH1 ARG A 122     -18.830  41.305   8.023  1.00 40.79              
ATOM    903  NH2 ARG A 122     -17.819  43.317   8.493  1.00 39.82              
ATOM    904  N   THR A 123     -12.554  36.716   9.593  1.00 30.53              
ATOM    905  CA  THR A 123     -12.031  35.441  10.044  1.00 28.26              
ATOM    906  C   THR A 123     -11.415  35.687  11.381  1.00 29.84              
ATOM    907  O   THR A 123     -11.051  36.810  11.683  1.00 31.43              
ATOM    908  CB  THR A 123     -10.917  34.940   9.165  1.00 26.56              
ATOM    909  OG1 THR A 123      -9.757  35.749   9.385  1.00 24.22              
ATOM    910  CG2 THR A 123     -11.328  34.990   7.690  1.00 26.24              
ATOM    911  N   HIS A 124     -11.251  34.631  12.167  1.00 32.90              
ATOM    912  CA  HIS A 124     -10.634  34.753  13.477  1.00 33.77              
ATOM    913  C   HIS A 124     -10.211  33.370  13.922  1.00 30.92              
ATOM    914  O   HIS A 124     -10.794  32.358  13.484  1.00 28.63              
ATOM    915  CB  HIS A 124     -11.598  35.370  14.503  1.00 40.57              
ATOM    916  CG  HIS A 124     -10.948  35.699  15.821  1.00 46.63              
ATOM    917  ND1 HIS A 124     -10.994  34.855  16.911  1.00 48.42              
ATOM    918  CD2 HIS A 124     -10.176  36.751  16.201  1.00 48.74              
ATOM    919  CE1 HIS A 124     -10.278  35.361  17.901  1.00 48.11              
ATOM    920  NE2 HIS A 124      -9.771  36.511  17.496  1.00 48.82              
ATOM    921  N   TYR A 125      -9.173  33.345  14.762  1.00 28.15              
ATOM    922  CA  TYR A 125      -8.631  32.113  15.324  1.00 24.55              
ATOM    923  C   TYR A 125      -9.699  31.210  15.828  1.00 22.51              
ATOM    924  O   TYR A 125     -10.523  31.663  16.592  1.00 22.59              
ATOM    925  CB  TYR A 125      -7.738  32.397  16.504  1.00 25.05              
ATOM    926  CG  TYR A 125      -7.033  31.158  17.017  1.00 25.32              
ATOM    927  CD1 TYR A 125      -6.596  30.171  16.143  1.00 24.30              
ATOM    928  CD2 TYR A 125      -6.745  31.010  18.373  1.00 26.35              
ATOM    929  CE1 TYR A 125      -5.895  29.103  16.589  1.00 25.73              
ATOM    930  CE2 TYR A 125      -6.044  29.929  18.829  1.00 26.87              
ATOM    931  CZ  TYR A 125      -5.615  28.984  17.927  1.00 28.52              
ATOM    932  OH  TYR A 125      -4.859  27.920  18.355  1.00 34.86              
ATOM    933  N   GLY A 126      -9.643  29.939  15.427  1.00 21.10              
ATOM    934  CA  GLY A 126     -10.611  28.961  15.857  1.00 17.14              
ATOM    935  C   GLY A 126     -11.686  28.598  14.869  1.00 16.38              
ATOM    936  O   GLY A 126     -12.295  27.569  14.997  1.00 18.63              
ATOM    937  N   GLN A 127     -11.918  29.398  13.855  1.00 17.61              
ATOM    938  CA  GLN A 127     -12.990  29.051  12.915  1.00 21.59              
ATOM    939  C   GLN A 127     -12.664  27.824  12.108  1.00 21.56              
ATOM    940  O   GLN A 127     -11.533  27.420  12.036  1.00 25.12              
ATOM    941  CB  GLN A 127     -13.278  30.209  11.945  1.00 25.34              
ATOM    942  CG  GLN A 127     -13.795  31.477  12.594  1.00 27.96              
ATOM    943  CD  GLN A 127     -14.352  32.415  11.588  1.00 29.81              
ATOM    944  OE1 GLN A 127     -13.668  32.774  10.623  1.00 31.27              
ATOM    945  NE2 GLN A 127     -15.587  32.825  11.786  1.00 30.14              
ATOM    946  N   LYS A 128     -13.658  27.287  11.431  1.00 23.75              
ATOM    947  CA  LYS A 128     -13.517  26.094  10.597  1.00 24.22              
ATOM    948  C   LYS A 128     -13.221  26.490   9.158  1.00 27.14              
ATOM    949  O   LYS A 128     -12.770  25.681   8.366  1.00 31.99              
ATOM    950  CB  LYS A 128     -14.813  25.279  10.662  1.00 21.39              
ATOM    951  CG  LYS A 128     -14.820  24.007   9.934  1.00 19.07              
ATOM    952  CD  LYS A 128     -16.191  23.371  10.024  1.00 21.52              
ATOM    953  CE  LYS A 128     -16.235  22.043   9.271  1.00 22.22              
ATOM    954  NZ  LYS A 128     -17.566  21.804   8.586  1.00 23.17              
ATOM    955  N   ALA A 129     -13.499  27.732   8.805  1.00 27.91              
ATOM    956  CA  ALA A 129     -13.236  28.218   7.439  1.00 29.25              
ATOM    957  C   ALA A 129     -11.727  28.500   7.167  1.00 26.07              
ATOM    958  O   ALA A 129     -11.291  28.665   6.005  1.00 24.91              
ATOM    959  CB  ALA A 129     -14.070  29.499   7.165  1.00 29.65              
ATOM    960  N   ILE A 130     -10.962  28.589   8.247  1.00 19.07              
ATOM    961  CA  ILE A 130      -9.561  28.850   8.138  1.00 17.43              
ATOM    962  C   ILE A 130      -8.734  27.560   8.300  1.00 21.94              
ATOM    963  O   ILE A 130      -7.491  27.598   8.305  1.00 24.76              
ATOM    964  CB  ILE A 130      -9.134  29.844   9.201  1.00 13.22              
ATOM    965  CG1 ILE A 130      -9.045  29.177  10.571  1.00  9.75              
ATOM    966  CG2 ILE A 130     -10.100  30.995   9.231  1.00 12.41              
ATOM    967  CD1 ILE A 130      -8.092  29.842  11.515  1.00  9.74              
ATOM    968  N   LEU A 131      -9.417  26.431   8.473  1.00 21.38              
ATOM    969  CA  LEU A 131      -8.745  25.172   8.676  1.00 21.10              
ATOM    970  C   LEU A 131      -8.476  24.526   7.330  1.00 21.83              
ATOM    971  O   LEU A 131      -9.379  23.964   6.699  1.00 21.83              
ATOM    972  CB  LEU A 131      -9.569  24.286   9.609  1.00 20.79              
ATOM    973  CG  LEU A 131      -9.560  24.795  11.068  1.00 21.49              
ATOM    974  CD1 LEU A 131     -10.522  24.027  11.986  1.00 20.79              
ATOM    975  CD2 LEU A 131      -8.161  24.751  11.654  1.00 20.98              
ATOM    976  N   PHE A 132      -7.218  24.624   6.901  1.00 20.79              
ATOM    977  CA  PHE A 132      -6.757  24.102   5.627  1.00 20.21              
ATOM    978  C   PHE A 132      -5.909  22.883   5.811  1.00 25.36              
ATOM    979  O   PHE A 132      -5.123  22.781   6.760  1.00 27.97              
ATOM    980  CB  PHE A 132      -5.944  25.163   4.885  1.00 18.22              
ATOM    981  CG  PHE A 132      -6.788  26.262   4.254  1.00 18.99              
ATOM    982  CD1 PHE A 132      -7.151  27.378   4.968  1.00 17.80              
ATOM    983  CD2 PHE A 132      -7.236  26.154   2.947  1.00 19.13              
ATOM    984  CE1 PHE A 132      -7.943  28.355   4.394  1.00 18.33              
ATOM    985  CE2 PHE A 132      -8.036  27.142   2.369  1.00 16.44              
ATOM    986  CZ  PHE A 132      -8.385  28.231   3.088  1.00 16.17              
ATOM    987  N   LEU A 133      -6.021  21.965   4.863  1.00 27.78              
ATOM    988  CA  LEU A 133      -5.255  20.717   4.892  1.00 25.93              
ATOM    989  C   LEU A 133      -4.500  20.560   3.566  1.00 24.31              
ATOM    990  O   LEU A 133      -5.097  20.573   2.488  1.00 26.79              
ATOM    991  CB  LEU A 133      -6.235  19.561   5.135  1.00 26.34              
ATOM    992  CG  LEU A 133      -5.730  18.129   5.296  1.00 28.23              
ATOM    993  CD1 LEU A 133      -4.645  18.036   6.313  1.00 27.74              
ATOM    994  CD2 LEU A 133      -6.892  17.272   5.713  1.00 31.80              
ATOM    995  N   PRO A 134      -3.172  20.563   3.617  1.00 22.27              
ATOM    996  CA  PRO A 134      -2.322  20.416   2.415  1.00 26.16              
ATOM    997  C   PRO A 134      -2.385  19.040   1.706  1.00 29.45              
ATOM    998  O   PRO A 134      -1.691  18.105   2.063  1.00 33.03              
ATOM    999  CB  PRO A 134      -0.905  20.702   2.962  1.00 22.26              
ATOM   1000  CG  PRO A 134      -1.164  21.661   4.027  1.00 19.02              
ATOM   1001  CD  PRO A 134      -2.405  21.132   4.729  1.00 20.16              
ATOM   1002  N   LEU A 135      -3.231  18.918   0.705  1.00 29.16              
ATOM   1003  CA  LEU A 135      -3.363  17.659   0.006  1.00 31.12              
ATOM   1004  C   LEU A 135      -2.362  17.521  -1.123  1.00 32.30              
ATOM   1005  O   LEU A 135      -2.087  18.463  -1.833  1.00 33.76              
ATOM   1006  CB  LEU A 135      -4.769  17.528  -0.546  1.00 32.92              
ATOM   1007  CG  LEU A 135      -5.726  16.667   0.266  1.00 32.92              
ATOM   1008  CD1 LEU A 135      -5.573  16.899   1.775  1.00 30.83              
ATOM   1009  CD2 LEU A 135      -7.143  16.959  -0.249  1.00 34.86              
ATOM   1010  N   PRO A 136      -1.789  16.332  -1.294  1.00 33.97              
ATOM   1011  CA  PRO A 136      -0.811  16.074  -2.345  1.00 35.97              
ATOM   1012  C   PRO A 136      -1.389  15.739  -3.714  1.00 32.84              
ATOM   1013  O   PRO A 136      -2.378  15.046  -3.800  1.00 31.35              
ATOM   1014  CB  PRO A 136      -0.053  14.864  -1.787  1.00 38.17              
ATOM   1015  CG  PRO A 136      -0.274  14.943  -0.285  1.00 36.89              
ATOM   1016  CD  PRO A 136      -1.713  15.279  -0.274  1.00 35.50              
ATOM   1017  N   VAL A 137      -0.766  16.253  -4.771  1.00 32.99              
ATOM   1018  CA  VAL A 137      -1.185  15.948  -6.146  1.00 34.08              
ATOM   1019  C   VAL A 137      -0.066  15.098  -6.811  1.00 39.24              
ATOM   1020  O   VAL A 137       1.111  15.225  -6.426  1.00 43.23              
ATOM   1021  CB  VAL A 137      -1.492  17.210  -6.982  1.00 28.11              
ATOM   1022  CG1 VAL A 137      -0.506  18.323  -6.669  1.00 24.20              
ATOM   1023  CG2 VAL A 137      -1.518  16.847  -8.490  1.00 22.99              
ATOM   1024  N   SER A 138      -0.435  14.198  -7.728  1.00 39.82              
ATOM   1025  CA  SER A 138       0.526  13.317  -8.388  1.00 43.89              
ATOM   1026  C   SER A 138       1.547  12.681  -7.429  1.00 43.53              
ATOM   1027  O   SER A 138       2.077  11.586  -7.758  1.00 42.38              
ATOM   1028  CB  SER A 138       1.254  14.042  -9.532  1.00 47.18              
ATOM   1029  OG  SER A 138       0.494  13.995 -10.737  1.00 48.90              
TER    1030      SER A 138                                                      
HETATM 6399  O   HOH A 601      -1.520  40.514   3.515  1.00  2.98              
HETATM 6400  O   HOH A 604      -5.602  24.223  -3.613  1.00 13.17              
HETATM 6401  O   HOH A 605      -8.140  27.900  14.608  1.00 14.53              
HETATM 6402  O   HOH A 608      -5.770  29.428   7.046  1.00  2.64              
HETATM 6403  O   HOH A 609      -5.119  14.372  -3.128  1.00  2.40              
HETATM 6404  O   HOH A 614       4.643  56.218  34.684  1.00 27.91              
HETATM 6405  O   HOH A 616       8.086  31.458  13.839  1.00 29.50              
HETATM 6406  O   HOH A 617     -15.547  44.846   7.383  1.00  4.81              
HETATM 6407  O   HOH A 620       5.666  29.852  -4.649  1.00 16.17              
HETATM 6408  O   HOH A 622     -11.055  37.122   1.122  1.00 18.42              
HETATM 6409  O   HOH A 624     -11.351  37.924  -4.591  1.00 47.86              
HETATM 6410  O   HOH A 630      -1.268  47.395  16.025  1.00 42.35              
HETATM 6411  O   HOH A 631       8.397  30.551  -6.133  1.00 17.00              
HETATM 6412  O   HOH A 637       1.751  33.835  -1.888  1.00 18.29              
HETATM 6413  O   HOH A 638      -4.018  27.972  14.217  1.00 44.45              
HETATM 6414  O   HOH A 640     -13.098  43.810   4.078  1.00 38.41              
HETATM 6415  O   HOH A 642     -18.476  22.026   5.861  1.00 63.03              
HETATM 6416  O   HOH A 646       1.362  55.694  35.633  1.00 65.82              
HETATM 6417  O   HOH A 650     -15.527  44.623   9.890  1.00 23.64              
HETATM 6418  O   HOH A 658       0.555  39.508   4.798  1.00 30.12              
HETATM 6419  O   HOH A 660      -1.510  20.043  16.781  1.00 64.15              
HETATM 6420  O   HOH A 665       5.939  56.606  37.252  1.00  9.33              
HETATM 6421  O   HOH A 666      -8.935  34.934   3.673  1.00 36.15              
HETATM 6422  O   HOH A 667     -13.628  24.048 -11.993  1.00 31.68              
HETATM 6423  O   HOH A 671      -2.437  19.736   8.338  1.00 73.33              
CONECT  442  445                                                                
CONECT  445  442  446                                                           
CONECT  446  445  447  449                                                      
CONECT  447  446  448  453                                                      
CONECT  448  447                                                                
CONECT  449  446  450                                                           
CONECT  450  449  451                                                           
CONECT  451  450  452                                                           
CONECT  452  451                                                                
CONECT  453  447                                                                
CONECT 1460 1463                                                                
CONECT 1463 1460 1464                                                           
CONECT 1464 1463 1465 1467                                                      
CONECT 1465 1464 1466 1471                                                      
CONECT 1466 1465                                                                
CONECT 1467 1464 1468                                                           
CONECT 1468 1467 1469                                                           
CONECT 1469 1468 1470                                                           
CONECT 1470 1469                                                                
CONECT 1471 1465                                                                
CONECT 2479 2482                                                                
CONECT 2482 2479 2483                                                           
CONECT 2483 2482 2484 2486                                                      
CONECT 2484 2483 2485 2490                                                      
CONECT 2485 2484                                                                
CONECT 2486 2483 2487                                                           
CONECT 2487 2486 2488                                                           
CONECT 2488 2487 2489                                                           
CONECT 2489 2488                                                                
CONECT 2490 2484                                                                
CONECT 3491 3494                                                                
CONECT 3494 3491 3495                                                           
CONECT 3495 3494 3496 3498                                                      
CONECT 3496 3495 3497 3502                                                      
CONECT 3497 3496                                                                
CONECT 3498 3495 3499                                                           
CONECT 3499 3498 3500                                                           
CONECT 3500 3499 3501                                                           
CONECT 3501 3500                                                                
CONECT 3502 3496                                                                
CONECT 4514 4517                                                                
CONECT 4517 4514 4518                                                           
CONECT 4518 4517 4519 4521                                                      
CONECT 4519 4518 4520 4525                                                      
CONECT 4520 4519                                                                
CONECT 4521 4518 4522                                                           
CONECT 4522 4521 4523                                                           
CONECT 4523 4522 4524                                                           
CONECT 4524 4523                                                                
CONECT 4525 4519                                                                
CONECT 5543 5546                                                                
CONECT 5546 5543 5547                                                           
CONECT 5547 5546 5548 5550                                                      
CONECT 5548 5547 5549 5554                                                      
CONECT 5549 5548                                                                
CONECT 5550 5547 5551                                                           
CONECT 5551 5550 5552                                                           
CONECT 5552 5551 5553                                                           
CONECT 5553 5552                                                                
CONECT 5554 5548                                                                
CONECT 6132 6133 6139 6142                                                      
CONECT 6133 6132 6134 6138                                                      
CONECT 6134 6133 6135 6140                                                      
CONECT 6135 6134 6136 6141                                                      
CONECT 6136 6135 6137 6142                                                      
CONECT 6137 6136 6143                                                           
CONECT 6138 6133 6144                                                           
CONECT 6139 6132                                                                
CONECT 6140 6134                                                                
CONECT 6141 6135 6152                                                           
CONECT 6142 6132 6136                                                           
CONECT 6143 6137 6148                                                           
CONECT 6144 6138 6145 6146 6147                                                 
CONECT 6145 6144                                                                
CONECT 6146 6144                                                                
CONECT 6147 6144                                                                
CONECT 6148 6143 6149 6150 6151                                                 
CONECT 6149 6148                                                                
CONECT 6150 6148                                                                
CONECT 6151 6148                                                                
CONECT 6152 6141 6153 6161                                                      
CONECT 6153 6152 6154 6158                                                      
CONECT 6154 6153 6155 6159                                                      
CONECT 6155 6154 6156 6160                                                      
CONECT 6156 6155 6157 6161                                                      
CONECT 6157 6156 6162 6163                                                      
CONECT 6158 6153 6164                                                           
CONECT 6159 6154                                                                
CONECT 6160 6155 6168                                                           
CONECT 6161 6152 6156                                                           
CONECT 6162 6157                                                                
CONECT 6163 6157                                                                
CONECT 6164 6158 6165 6166 6167                                                 
CONECT 6165 6164                                                                
CONECT 6166 6164                                                                
CONECT 6167 6164                                                                
CONECT 6168 6160 6169 6177                                                      
CONECT 6169 6168 6170 6174                                                      
CONECT 6170 6169 6171 6175                                                      
CONECT 6171 6170 6172 6176                                                      
CONECT 6172 6171 6173 6177                                                      
CONECT 6173 6172 6178                                                           
CONECT 6174 6169 6179                                                           
CONECT 6175 6170                                                                
CONECT 6176 6171 6187                                                           
CONECT 6177 6168 6172                                                           
CONECT 6178 6173 6183                                                           
CONECT 6179 6174 6180 6181 6182                                                 
CONECT 6180 6179                                                                
CONECT 6181 6179                                                                
CONECT 6182 6179                                                                
CONECT 6183 6178 6184 6185 6186                                                 
CONECT 6184 6183                                                                
CONECT 6185 6183                                                                
CONECT 6186 6183                                                                
CONECT 6187 6176 6188 6196                                                      
CONECT 6188 6187 6189 6193                                                      
CONECT 6189 6188 6190 6194                                                      
CONECT 6190 6189 6191 6195                                                      
CONECT 6191 6190 6192 6196                                                      
CONECT 6192 6191 6197 6198                                                      
CONECT 6193 6188 6199                                                           
CONECT 6194 6189                                                                
CONECT 6195 6190 6203                                                           
CONECT 6196 6187 6191                                                           
CONECT 6197 6192                                                                
CONECT 6198 6192                                                                
CONECT 6199 6193 6200 6201 6202                                                 
CONECT 6200 6199                                                                
CONECT 6201 6199                                                                
CONECT 6202 6199                                                                
CONECT 6203 6195 6204 6212                                                      
CONECT 6204 6203 6205 6209                                                      
CONECT 6205 6204 6206 6210                                                      
CONECT 6206 6205 6207 6211                                                      
CONECT 6207 6206 6208 6212                                                      
CONECT 6208 6207 6213                                                           
CONECT 6209 6204 6214                                                           
CONECT 6210 6205                                                                
CONECT 6211 6206                                                                
CONECT 6212 6203 6207                                                           
CONECT 6213 6208 6218                                                           
CONECT 6214 6209 6215 6216 6217                                                 
CONECT 6215 6214                                                                
CONECT 6216 6214                                                                
CONECT 6217 6214                                                                
CONECT 6218 6213 6219 6220 6221                                                 
CONECT 6219 6218                                                                
CONECT 6220 6218                                                                
CONECT 6221 6218                                                                
CONECT 6222 6223 6229 6232                                                      
CONECT 6223 6222 6224 6228                                                      
CONECT 6224 6223 6225 6230                                                      
CONECT 6225 6224 6226 6231                                                      
CONECT 6226 6225 6227 6232                                                      
CONECT 6227 6226 6233                                                           
CONECT 6228 6223 6234                                                           
CONECT 6229 6222                                                                
CONECT 6230 6224                                                                
CONECT 6231 6225 6242                                                           
CONECT 6232 6222 6226                                                           
CONECT 6233 6227 6238                                                           
CONECT 6234 6228 6235 6236 6237                                                 
CONECT 6235 6234                                                                
CONECT 6236 6234                                                                
CONECT 6237 6234                                                                
CONECT 6238 6233 6239 6240 6241                                                 
CONECT 6239 6238                                                                
CONECT 6240 6238                                                                
CONECT 6241 6238                                                                
CONECT 6242 6231 6243 6251                                                      
CONECT 6243 6242 6244 6248                                                      
CONECT 6244 6243 6245 6249                                                      
CONECT 6245 6244 6246 6250                                                      
CONECT 6246 6245 6247 6251                                                      
CONECT 6247 6246 6252 6253                                                      
CONECT 6248 6243 6254                                                           
CONECT 6249 6244                                                                
CONECT 6250 6245 6258                                                           
CONECT 6251 6242 6246                                                           
CONECT 6252 6247                                                                
CONECT 6253 6247                                                                
CONECT 6254 6248 6255 6256 6257                                                 
CONECT 6255 6254                                                                
CONECT 6256 6254                                                                
CONECT 6257 6254                                                                
CONECT 6258 6250 6259 6267                                                      
CONECT 6259 6258 6260 6264                                                      
CONECT 6260 6259 6261 6265                                                      
CONECT 6261 6260 6262 6266                                                      
CONECT 6262 6261 6263 6267                                                      
CONECT 6263 6262 6268                                                           
CONECT 6264 6259 6269                                                           
CONECT 6265 6260                                                                
CONECT 6266 6261 6277                                                           
CONECT 6267 6258 6262                                                           
CONECT 6268 6263 6273                                                           
CONECT 6269 6264 6270 6271 6272                                                 
CONECT 6270 6269                                                                
CONECT 6271 6269                                                                
CONECT 6272 6269                                                                
CONECT 6273 6268 6274 6275 6276                                                 
CONECT 6274 6273                                                                
CONECT 6275 6273                                                                
CONECT 6276 6273                                                                
CONECT 6277 6266 6278 6286                                                      
CONECT 6278 6277 6279 6283                                                      
CONECT 6279 6278 6280 6284                                                      
CONECT 6280 6279 6281 6285                                                      
CONECT 6281 6280 6282 6286                                                      
CONECT 6282 6281 6287 6288                                                      
CONECT 6283 6278 6289                                                           
CONECT 6284 6279                                                                
CONECT 6285 6280 6293                                                           
CONECT 6286 6277 6281                                                           
CONECT 6287 6282                                                                
CONECT 6288 6282                                                                
CONECT 6289 6283 6290 6291 6292                                                 
CONECT 6290 6289                                                                
CONECT 6291 6289                                                                
CONECT 6292 6289                                                                
CONECT 6293 6285 6294 6302                                                      
CONECT 6294 6293 6295 6299                                                      
CONECT 6295 6294 6296 6300                                                      
CONECT 6296 6295 6297 6301                                                      
CONECT 6297 6296 6298 6302                                                      
CONECT 6298 6297 6303                                                           
CONECT 6299 6294 6304                                                           
CONECT 6300 6295                                                                
CONECT 6301 6296                                                                
CONECT 6302 6293 6297                                                           
CONECT 6303 6298 6308                                                           
CONECT 6304 6299 6305 6306 6307                                                 
CONECT 6305 6304                                                                
CONECT 6306 6304                                                                
CONECT 6307 6304                                                                
CONECT 6308 6303 6309 6310 6311                                                 
CONECT 6309 6308                                                                
CONECT 6310 6308                                                                
CONECT 6311 6308                                                                
CONECT 6312 6313 6318 6322                                                      
CONECT 6313 6312 6314 6319                                                      
CONECT 6314 6313 6315 6320                                                      
CONECT 6315 6314 6316 6321                                                      
CONECT 6316 6315 6317 6322                                                      
CONECT 6317 6316 6323 6324                                                      
CONECT 6318 6312                                                                
CONECT 6319 6313 6325                                                           
CONECT 6320 6314                                                                
CONECT 6321 6315 6329                                                           
CONECT 6322 6312 6316                                                           
CONECT 6323 6317                                                                
CONECT 6324 6317                                                                
CONECT 6325 6319 6326 6327 6328                                                 
CONECT 6326 6325                                                                
CONECT 6327 6325                                                                
CONECT 6328 6325                                                                
CONECT 6329 6321 6330 6338                                                      
CONECT 6330 6329 6331 6335                                                      
CONECT 6331 6330 6332 6336                                                      
CONECT 6332 6331 6333 6337                                                      
CONECT 6333 6332 6334 6338                                                      
CONECT 6334 6333 6339                                                           
CONECT 6335 6330 6340                                                           
CONECT 6336 6331                                                                
CONECT 6337 6332 6348                                                           
CONECT 6338 6329 6333                                                           
CONECT 6339 6334 6344                                                           
CONECT 6340 6335 6341 6342 6343                                                 
CONECT 6341 6340                                                                
CONECT 6342 6340                                                                
CONECT 6343 6340                                                                
CONECT 6344 6339 6345 6346 6347                                                 
CONECT 6345 6344                                                                
CONECT 6346 6344                                                                
CONECT 6347 6344                                                                
CONECT 6348 6337 6349 6357                                                      
CONECT 6349 6348 6350 6354                                                      
CONECT 6350 6349 6351 6355                                                      
CONECT 6351 6350 6352 6356                                                      
CONECT 6352 6351 6353 6357                                                      
CONECT 6353 6352 6358 6359                                                      
CONECT 6354 6349 6360                                                           
CONECT 6355 6350                                                                
CONECT 6356 6351 6364                                                           
CONECT 6357 6348 6352                                                           
CONECT 6358 6353                                                                
CONECT 6359 6353                                                                
CONECT 6360 6354 6361 6362 6363                                                 
CONECT 6361 6360                                                                
CONECT 6362 6360                                                                
CONECT 6363 6360                                                                
CONECT 6364 6356 6365 6373                                                      
CONECT 6365 6364 6366 6370                                                      
CONECT 6366 6365 6367 6371                                                      
CONECT 6367 6366 6368 6372                                                      
CONECT 6368 6367 6369 6373                                                      
CONECT 6369 6368 6374                                                           
CONECT 6370 6365 6375                                                           
CONECT 6371 6366                                                                
CONECT 6372 6367 6383                                                           
CONECT 6373 6364 6368                                                           
CONECT 6374 6369 6379                                                           
CONECT 6375 6370 6376 6377 6378                                                 
CONECT 6376 6375                                                                
CONECT 6377 6375                                                                
CONECT 6378 6375                                                                
CONECT 6379 6374 6380 6381 6382                                                 
CONECT 6380 6379                                                                
CONECT 6381 6379                                                                
CONECT 6382 6379                                                                
CONECT 6383 6372 6384 6392                                                      
CONECT 6384 6383 6385 6389                                                      
CONECT 6385 6384 6386 6390                                                      
CONECT 6386 6385 6387 6391                                                      
CONECT 6387 6386 6388 6392                                                      
CONECT 6388 6387 6393 6394                                                      
CONECT 6389 6384 6395                                                           
CONECT 6390 6385                                                                
CONECT 6391 6386                                                                
CONECT 6392 6383 6387                                                           
CONECT 6393 6388                                                                
CONECT 6394 6388                                                                
CONECT 6395 6389 6396 6397 6398                                                 
CONECT 6396 6395                                                                
CONECT 6397 6395                                                                
CONECT 6398 6395                                                                
MASTER      425    0   21   23   60    0   30   27 6463    6  327   66          
END                                                                             