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Database: PDB
Entry: 1P63
LinkDB: 1P63
Original site: 1P63 
HEADER    HORMONE/GROWTH FACTOR                   28-APR-03   1P63              
TITLE     HUMAN ACIDIC FIBROBLAST GROWTH FACTOR. 140 AMINO ACID FORM            
TITLE    2 WITH AMINO TERMINAL HIS TAG AND LEU111 REPLACED WITH ILE             
TITLE    3 (L111I)                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACIDIC FIBROBLAST GROWTH FACTOR;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: 140 AMINO ACID FORM WITH AMINO TERMINAL HIS TAG;           
COMPND   5 SYNONYM: HEPARIN-BINDING GROWTH FACTOR 1; HBGF-1; AFGF;              
COMPND   6 BETA-ENDOTHELIAL CELL GROWTH FACTOR; ECGF-BETA;                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET21A(+)                                 
KEYWDS    BETA-TREFOIL, HORMONE/GROWTH FACTOR COMPLEX                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.R.BRYCH,J.KIM,T.M.LOGAN,M.BLABER                                    
REVDAT   3   24-FEB-09 1P63    1       VERSN                                    
REVDAT   2   22-MAR-05 1P63    1       JRNL                                     
REVDAT   1   11-MAY-04 1P63    0                                                
JRNL        AUTH   S.R.BRYCH,J.KIM,T.M.LOGAN,M.BLABER                           
JRNL        TITL   ACCOMMODATION OF A HIGHLY SYMMETRIC CORE WITHIN A            
JRNL        TITL 2 SYMMETRIC PROTEIN SUPERFOLD                                  
JRNL        REF    PROTEIN SCI.                  V.  12  2704 2003              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   14627732                                                     
JRNL        DOI    10.1110/PS.03374903                                          
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 49432                          
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1462                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 51569                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2262                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 225                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : 16.700                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.009 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 1.700 ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : 16.800; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : 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  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : TRONRUD                                          
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1P63 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019053.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-APR-03                          
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                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.900                              
REMARK 200  MONOCHROMATOR                  : BENT GE(111) MONOCHROMATOR         
REMARK 200  OPTICS                         : OSMIC BLUE CONFOCAL MIRRORS        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49432                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 46.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: TNT                                                   
REMARK 200 STARTING MODEL: 1JQZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, AMMONIUM SULFATE,        
REMARK 280  PH 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       53.89500            
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       53.89500            
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       37.20500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       48.36000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       37.20500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       48.36000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       53.89500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       37.20500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       48.36000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       53.89500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       37.20500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       48.36000            
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     1                                                      
REMARK 465     SER A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     ASP A   140                                                      
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   O    HOH B  2403     O    HOH B  2419     3556     2.00            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B  82   CD    GLU B  82   OE2     0.075                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  28   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A  32   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A  36   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A  36   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ASP A  39   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP A  68   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A  68   CB  -  CG  -  OD2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ASP B  28   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP B  36   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP B  36   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP B  68   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 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    GLU A  49      -81.16    -85.09                                   
REMARK 500    HIS A  93      -49.70   -152.52                                   
REMARK 500    GLU B  49     -100.64   -102.34                                   
REMARK 500    ASN B  80     -168.61   -115.33                                   
REMARK 500    HIS B  93      -46.55   -151.53                                   
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 162                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 160                 
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.                                         
DBREF  1P63 A    1E  140  UNP    P05230   FGF1_HUMAN      16    155             
DBREF  1P63 B    1E  140  UNP    P05230   FGF1_HUMAN      16    155             
SEQADV 1P63 HIS A    1  UNP  P05230              EXPRESSION TAG                 
SEQADV 1P63 HIS A    1B UNP  P05230              EXPRESSION TAG                 
SEQADV 1P63 HIS A    1C UNP  P05230              EXPRESSION TAG                 
SEQADV 1P63 HIS A    1D UNP  P05230              EXPRESSION TAG                 
SEQADV 1P63 ILE A  111  UNP  P05230    LEU   126 ENGINEERED                     
SEQADV 1P63 HIS B    1A UNP  P05230              EXPRESSION TAG                 
SEQADV 1P63 HIS B    1B UNP  P05230              EXPRESSION TAG                 
SEQADV 1P63 HIS B    1C UNP  P05230              EXPRESSION TAG                 
SEQADV 1P63 HIS B    1D UNP  P05230              EXPRESSION TAG                 
SEQADV 1P63 ILE B  111  UNP  P05230    LEU   126 ENGINEERED                     
SEQRES   1 A  144  HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY ASN TYR LYS          
SEQRES   2 A  144  LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY HIS PHE          
SEQRES   3 A  144  LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY THR ARG          
SEQRES   4 A  144  ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU SER ALA          
SEQRES   5 A  144  GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR GLU THR          
SEQRES   6 A  144  GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU LEU TYR          
SEQRES   7 A  144  GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE LEU GLU          
SEQRES   8 A  144  ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE SER LYS          
SEQRES   9 A  144  LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY ILE LYS LYS          
SEQRES  10 A  144  ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS TYR GLY          
SEQRES  11 A  144  GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL SER SER          
SEQRES  12 A  144  ASP                                                          
SEQRES   1 B  144  HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY ASN TYR LYS          
SEQRES   2 B  144  LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY HIS PHE          
SEQRES   3 B  144  LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY THR ARG          
SEQRES   4 B  144  ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU SER ALA          
SEQRES   5 B  144  GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR GLU THR          
SEQRES   6 B  144  GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU LEU TYR          
SEQRES   7 B  144  GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE LEU GLU          
SEQRES   8 B  144  ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE SER LYS          
SEQRES   9 B  144  LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY ILE LYS LYS          
SEQRES  10 B  144  ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS TYR GLY          
SEQRES  11 B  144  GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL SER SER          
SEQRES  12 B  144  ASP                                                          
HET    SO4  A 162       5                                                       
HET    FMT  B 160       3                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     FMT FORMIC ACID                                                      
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  FMT    C H2 O2                                                      
FORMUL   5  HOH   *219(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 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 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  ALA A  48  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 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 A1270                    
SITE     2 AC1  5 HOH A1310                                                     
SITE     1 AC2  4 HIS B   1A HIS B   1B HIS B   1C HOH B2235                    
CRYST1   74.410   96.720  107.790  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      0.013439  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010339  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009277        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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