GenomeNet

Database: PDB
Entry: 3FJB
LinkDB: 3FJB
Original site: 3FJB 
HEADER    HORMONE                                 14-DEC-08   3FJB              
TITLE     CRYSTAL STRUCTURE OF V31I MUTANT OF HUMAN ACIDIC FIBROBLAST           
TITLE    2 GROWTH FACTOR                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEPARIN-BINDING GROWTH FACTOR 1;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HBGF-1, ACIDIC FIBROBLAST GROWTH FACTOR, AFGF,              
COMPND   5 BETA-ENDOTHELIAL CELL GROWTH FACTOR, ECGF-BETA;                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FGF1, FGFA;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21A(+)                             
KEYWDS    BETA-TREFOIL, ACETYLATION, ANGIOGENESIS, DEVELOPMENTAL                
KEYWDS   2 PROTEIN, DIFFERENTIATION, GROWTH FACTOR, HEPARIN-BINDING,            
KEYWDS   3 MITOGEN, POLYMORPHISM, HORMONE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.BLABER,J.LEE                                                        
REVDAT   2   13-OCT-09 3FJB    1       JRNL                                     
REVDAT   1   06-OCT-09 3FJB    0                                                
JRNL        AUTH   J.LEE,M.BLABER                                               
JRNL        TITL   THE INTERACTION BETWEEN THERMODYNAMIC STABILITY AND          
JRNL        TITL 2 BURIED FREE CYSTEINES IN REGULATING THE FUNCTIONAL           
JRNL        TITL 3 HALF-LIFE OF FIBROBLAST GROWTH FACTOR-1.                     
JRNL        REF    J.MOL.BIOL.                   V. 393   113 2009              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   19695265                                                     
JRNL        DOI    10.1016/J.JMB.2009.08.026                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 422001.970                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 23789                          
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) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1135                            
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           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3143                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1980                       
REMARK   3   BIN FREE R VALUE                    : 0.2300                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 164                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2254                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 186                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.18000                                             
REMARK   3    B22 (A**2) : 6.00000                                              
REMARK   3    B33 (A**2) : -5.82000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.08                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.27                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.10                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.87                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 48.09                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3FJB COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050658.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 103                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC MIRROR                       
REMARK 200  OPTICS                         : OSMIC BLUE CONFOCAL MIRROR         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23789                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.890                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.740                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 1JQZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5M NA FORMATE, 0.7M (NH4)2SO4, PH      
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
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       54.41250            
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       54.41250            
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       36.96550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       48.71300            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       36.96550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       48.71300            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       54.41250            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       36.96550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       48.71300            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       54.41250            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       36.96550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       48.71300            
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                                                    
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 300 REMARK: MONOMER                                                      
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A     1A                                                     
REMARK 465     HIS A     1B                                                     
REMARK 465     HIS A     1C                                                     
REMARK 465     SER A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     ASP A   140                                                      
REMARK 465     HIS B     1A                                                     
REMARK 465     HIS B     1B                                                     
REMARK 465     HIS B     1C                                                     
REMARK 465     SER B   138                                                      
REMARK 465     SER B   139                                                      
REMARK 465     ASP B   140                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU A    81     OE2  GLU A    81     4566     2.06            
REMARK 500   CD   GLU A    81     CD   GLU A    81     4566     2.19            
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    PRO A   5     -165.27    -79.03                                   
REMARK 500    ASN A   7     -162.13   -128.78                                   
REMARK 500    ASN A  18      -73.60    -45.42                                   
REMARK 500    HIS A  93      -49.72   -152.24                                   
REMARK 500    ASN B  18      -89.36    -44.30                                   
REMARK 500    ASP B  32     -162.83   -161.38                                   
REMARK 500    GLU B  49      -86.26    -81.85                                   
REMARK 500    HIS B  93      -49.45   -156.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 169        DISTANCE =  5.51 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1                   
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 141                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JQZ   RELATED DB: PDB                                   
REMARK 900 HUMAN ACIDIC FIBROBLAST GROWTH FACTOR. 141 AMINO ACID FORM           
REMARK 900 WITH AMINO TERMINAL HIS TAG                                          
REMARK 900 RELATED ID: 3FGM   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF L44F/C83T/C117V/F132W MUTANT OF HUMAN           
REMARK 900 ACIDIC FIBROBLAST GROWTH FACTOR                                      
REMARK 900 RELATED ID: 3FJ8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF C117I MUTANT OF HUMAN ACIDIC                    
REMARK 900 FIBROBLAST GROWTH FACTOR                                             
REMARK 900 RELATED ID: 3FJ9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF F85W MUTANT OF HUMAN ACIDIC FIBROBLAST          
REMARK 900 GROWTH FACTOR                                                        
REMARK 900 RELATED ID: 3FJA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF F132W MUTANT OF HUMAN ACIDIC                    
REMARK 900 FIBROBLAST GROWTH FACTOR                                             
REMARK 900 RELATED ID: 3FJC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF L44W MUTANT OF HHUMAN ACIDIC                    
REMARK 900 FIBROBLAST GROWTH FACTOR                                             
REMARK 900 RELATED ID: 3FJD   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF L44F/F132W MUTANT OF HUMAN ACIDIC               
REMARK 900 FIBROBLAST GROWTH FACTOR                                             
REMARK 900 RELATED ID: 3FJE   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF C83S MUTANT OF HUMAN ACIDIC FIBROBLAST          
REMARK 900 GROWTH FACTOR                                                        
REMARK 900 RELATED ID: 3FJF   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF C83T MUTANT OF HHUMAN ACIDIC                    
REMARK 900 FIBROBLAST GROWTH FACTOR                                             
REMARK 900 RELATED ID: 3FJH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF C83A MUTANT OF HUMAN ACIDIC FIBROBLAST          
REMARK 900 GROWTH FACTOR                                                        
REMARK 900 RELATED ID: 3FJI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF K12V/C83I/C117V MUTANT OF HUMAN ACIDIC          
REMARK 900 FIBROBLAST GROWTH FACTOR                                             
REMARK 900 RELATED ID: 3FJJ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF C83V MUTANT OF HUMAN ACIDIC FIBROBLAST          
REMARK 900 GROWTH FACTOR                                                        
REMARK 900 RELATED ID: 3FJK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A66C MUTANT OF HUMAN ACIDIC FIBROBLAST          
REMARK 900 GROWTH FACTOR                                                        
DBREF  3FJB A    1G  140  UNP    P05230   FGF1_HUMAN      16    155             
DBREF  3FJB B    1G  140  UNP    P05230   FGF1_HUMAN      16    155             
SEQADV 3FJB HIS A    1A UNP  P05230              EXPRESSION TAG                 
SEQADV 3FJB HIS A    1B UNP  P05230              EXPRESSION TAG                 
SEQADV 3FJB HIS A    1C UNP  P05230              EXPRESSION TAG                 
SEQADV 3FJB HIS A    1D UNP  P05230              EXPRESSION TAG                 
SEQADV 3FJB HIS A    1E UNP  P05230              EXPRESSION TAG                 
SEQADV 3FJB HIS A    1F UNP  P05230              EXPRESSION TAG                 
SEQADV 3FJB ILE A   31  UNP  P05230    VAL    46 ENGINEERED                     
SEQADV 3FJB HIS B    1A UNP  P05230              EXPRESSION TAG                 
SEQADV 3FJB HIS B    1B UNP  P05230              EXPRESSION TAG                 
SEQADV 3FJB HIS B    1C UNP  P05230              EXPRESSION TAG                 
SEQADV 3FJB HIS B    1D UNP  P05230              EXPRESSION TAG                 
SEQADV 3FJB HIS B    1E UNP  P05230              EXPRESSION TAG                 
SEQADV 3FJB HIS B    1F UNP  P05230              EXPRESSION TAG                 
SEQADV 3FJB ILE B   31  UNP  P05230    VAL    46 ENGINEERED                     
SEQRES   1 A  146  HIS HIS HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY ASN          
SEQRES   2 A  146  TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY          
SEQRES   3 A  146  HIS PHE LEU ARG ILE LEU PRO ASP GLY THR ILE ASP GLY          
SEQRES   4 A  146  THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU          
SEQRES   5 A  146  SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR          
SEQRES   6 A  146  GLU THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU          
SEQRES   7 A  146  LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE          
SEQRES   8 A  146  LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE          
SEQRES   9 A  146  SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU          
SEQRES  10 A  146  LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS          
SEQRES  11 A  146  TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL          
SEQRES  12 A  146  SER SER ASP                                                  
SEQRES   1 B  146  HIS HIS HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY ASN          
SEQRES   2 B  146  TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY          
SEQRES   3 B  146  HIS PHE LEU ARG ILE LEU PRO ASP GLY THR ILE ASP GLY          
SEQRES   4 B  146  THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU          
SEQRES   5 B  146  SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR          
SEQRES   6 B  146  GLU THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU          
SEQRES   7 B  146  LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE          
SEQRES   8 B  146  LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE          
SEQRES   9 B  146  SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU          
SEQRES  10 B  146  LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS          
SEQRES  11 B  146  TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL          
SEQRES  12 B  146  SER SER ASP                                                  
HET    SO4  A   1       5                                                       
HET    SO4  A 141       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *186(H2 O)                                                    
HELIX    1   1 ASN A   80  CYS A   83  5                                   4    
HELIX    2   2 HIS A  102  ASN A  106  5                                   5    
HELIX    3   3 ARG A  119  THR A  123  5                                   5    
HELIX    4   4 ASN B   80  CYS B   83  5                                   4    
HELIX    5   5 HIS B  102  ASN B  106  5                                   5    
HELIX    6   6 ARG B  119  THR B  123  5                                   5    
SHEET    1   A 4 ILE A  31  THR A  34  0                                        
SHEET    2   A 4 HIS A  21  ILE A  25 -1  N  ARG A  24   O  ASP A  32           
SHEET    3   A 4 LYS A  12  CYS A  16 -1  N  CYS A  16   O  HIS A  21           
SHEET    4   A 4 PHE A 132  PRO A 136 -1  O  LEU A 135   N  LEU A  13           
SHEET    1   B 4 LEU A  44  SER A  50  0                                        
SHEET    2   B 4 GLU A  53  SER A  58 -1  O  LYS A  57   N  GLN A  45           
SHEET    3   B 4 PHE A  85  GLU A  90 -1  O  PHE A  85   N  VAL A  54           
SHEET    4   B 4 TYR A  94  SER A  99 -1  O  ILE A  98   N  LEU A  86           
SHEET    1   C 2 TYR A  64  MET A  67  0                                        
SHEET    2   C 2 LEU A  73  SER A  76 -1  O  SER A  76   N  TYR A  64           
SHEET    1   D 4 ILE B  31  THR B  34  0                                        
SHEET    2   D 4 HIS B  21  ILE B  25 -1  N  ARG B  24   O  ASP B  32           
SHEET    3   D 4 LYS B  12  CYS B  16 -1  N  CYS B  16   O  HIS B  21           
SHEET    4   D 4 PHE B 132  PRO B 136 -1  O  LEU B 135   N  LEU B  13           
SHEET    1   E 4 LEU B  44  ALA B  48  0                                        
SHEET    2   E 4 GLU B  53  SER B  58 -1  O  LYS B  57   N  GLN B  45           
SHEET    3   E 4 PHE B  85  GLU B  90 -1  O  PHE B  85   N  VAL B  54           
SHEET    4   E 4 TYR B  94  SER B  99 -1  O  ILE B  98   N  LEU B  86           
SHEET    1   F 2 TYR B  64  MET B  67  0                                        
SHEET    2   F 2 LEU B  73  SER B  76 -1  O  SER B  76   N  TYR B  64           
SITE     1 AC1  5 ASN A  18  LYS A 112  LYS A 113  HOH A 189                    
SITE     2 AC1  5 ASP B  70                                                     
SITE     1 AC2  6 HIS A   1E HIS A   1F TYR A 125  HIS B   1E                   
SITE     2 AC2  6 HIS B   1F TYR B 125                                          
CRYST1   73.931   97.426  108.825  90.00  90.00  90.00 C 2 2 21     16          
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      0.013526  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010264  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009189        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system