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Database: PDB
Entry: 2HWA
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Original site: 2HWA 
HEADER    HORMONE/GROWTH FACTOR                   01-AUG-06   2HWA              
TITLE     CRYSTAL STRUCTURE OF LYS12THR/CYS117VAL MUTANT OF HUMAN               
TITLE    2 ACIDIC FIBROBLAST GROWTH FACTOR AT 1.65 ANGSTROM                     
TITLE    3 RESOLUTION.                                                          
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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21A(+)                                 
KEYWDS    BETA-TREFOIL, HORMONE/GROWTH FACTOR COMPLEX                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.K.DUBEY,J.LEE,T.SOMASUNDARAM,M.BLABER                               
REVDAT   3   24-FEB-09 2HWA    1       VERSN                                    
REVDAT   2   05-FEB-08 2HWA    1       JRNL                                     
REVDAT   1   12-JUN-07 2HWA    0                                                
JRNL        AUTH   V.K.DUBEY,J.LEE,T.SOMASUNDARAM,S.BLABER,M.BLABER             
JRNL        TITL   SPACKLING THE CRACK: STABILIZING HUMAN FIBROBLAST            
JRNL        TITL 2 GROWTH FACTOR-1 BY TARGETING THE N AND C TERMINUS            
JRNL        TITL 3 BETA-STRAND INTERACTIONS.                                    
JRNL        REF    J.MOL.BIOL.                   V. 371   256 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17570396                                                     
JRNL        DOI    10.1016/J.JMB.2007.05.065                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 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 : CNS                                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.66                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 40329                          
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) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2005                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.71                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2610                       
REMARK   3   BIN FREE R VALUE                    : 0.2720                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 290                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2260                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 229                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.70                          
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) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.14                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : CNS                                       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2HWA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB038837.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUL-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 103                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : SI(111) MONOCHROMATOR              
REMARK 200  OPTICS                         : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40329                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.660                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY                : 8.900                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 37.1900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: PDB ENTRY 1JQZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM FORMATE,        
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.15K          
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       54.27500            
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       54.27500            
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       37.24500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       48.50000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       37.24500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       48.50000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       54.27500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       37.24500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       48.50000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       54.27500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       37.24500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       48.50000            
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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     SER A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     ASP A   140                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
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   OE1  GLU A    81     OE1  GLU A    81     4566     2.03            
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    HIS A  93      -46.07   -161.39                                   
REMARK 500    ASP B  32     -163.51   -163.59                                   
REMARK 500    GLU B  49      -85.41    -99.31                                   
REMARK 500    HIS B  93      -47.79   -161.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 141                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 141                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 142                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 143                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JQZ   RELATED DB: PDB                                   
REMARK 900 HUMAN ACIDIC FIBROBLAST GROWTH FACTOR, 140 AMINO ACID FORM           
REMARK 900 WITH AMINO TERMINAL HIS TAG                                          
DBREF  2HWA A    1G  140  UNP    P05230   FGF1_HUMAN      16    155             
DBREF  2HWA B    1G  140  UNP    P05230   FGF1_HUMAN      16    155             
SEQADV 2HWA HIS A    1D UNP  P05230              EXPRESSION TAG                 
SEQADV 2HWA HIS A    1D UNP  P05230              EXPRESSION TAG                 
SEQADV 2HWA HIS A    1D UNP  P05230              EXPRESSION TAG                 
SEQADV 2HWA HIS A    1D UNP  P05230              EXPRESSION TAG                 
SEQADV 2HWA HIS A    1E UNP  P05230              EXPRESSION TAG                 
SEQADV 2HWA HIS A    1F UNP  P05230              EXPRESSION TAG                 
SEQADV 2HWA THR A   12  UNP  P05230    LYS    27 ENGINEERED                     
SEQADV 2HWA VAL A  117  UNP  P05230    CYS   132 ENGINEERED                     
SEQADV 2HWA HIS B    1C UNP  P05230              EXPRESSION TAG                 
SEQADV 2HWA HIS B    1C UNP  P05230              EXPRESSION TAG                 
SEQADV 2HWA HIS B    1C UNP  P05230              EXPRESSION TAG                 
SEQADV 2HWA HIS B    1D UNP  P05230              EXPRESSION TAG                 
SEQADV 2HWA HIS B    1E UNP  P05230              EXPRESSION TAG                 
SEQADV 2HWA HIS B    1F UNP  P05230              EXPRESSION TAG                 
SEQADV 2HWA THR B   12  UNP  P05230    LYS    27 ENGINEERED                     
SEQADV 2HWA VAL B  117  UNP  P05230    CYS   132 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 THR LEU LEU TYR CYS SER ASN GLY GLY          
SEQRES   3 A  146  HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL 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 VAL 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 THR LEU LEU TYR CYS SER ASN GLY GLY          
SEQRES   3 B  146  HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL 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 VAL 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 141       5                                                       
HET    SO4  B 141       5                                                       
HET    FMT  B 142       3                                                       
HET    FMT  B 143       3                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     FMT FORMIC ACID                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  FMT    2(C H2 O2)                                                   
FORMUL   7  HOH   *223(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 GLN A  127  ILE A  130  5                                   4    
HELIX    5   5 ASN B   80  CYS B   83  5                                   4    
HELIX    6   6 HIS B  102  ASN B  106  5                                   5    
HELIX    7   7 ARG B  119  THR B  123  5                                   5    
SHEET    1   A 4 VAL 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 LEU A  13  CYS A  16 -1  N  CYS A  16   O  HIS A  21           
SHEET    4   A 4 PHE A 132  LEU A 135 -1  O  LEU A 133   N  TYR A  15           
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 VAL 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 LEU B  13  CYS B  16 -1  N  CYS B  16   O  HIS B  21           
SHEET    4   D 4 PHE B 132  LEU B 135 -1  O  LEU B 133   N  TYR B  15           
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  7 ASN A  18  LYS A 112  LYS A 113  LYS A 118                    
SITE     2 AC1  7 HOH A 154  HOH A 188  ASP B  70                               
SITE     1 AC2  6 ASN B  18  LYS B 112  LYS B 113  LYS B 118                    
SITE     2 AC2  6 FMT B 143  HOH B 198                                          
SITE     1 AC3  4 HIS B   1C HIS B   1D HIS B   1E HOH B 208                    
SITE     1 AC4  5 LYS B 118  GLN B 127  LYS B 128  ALA B 129                    
SITE     2 AC4  5 SO4 B 141                                                     
CRYST1   74.490   97.000  108.550  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      0.013425  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010309  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009212        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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