HEADER HORMONE 14-DEC-08 3FJ9
TITLE CRYSTAL STRUCTURE OF F85W MUTANT OF HUMAN ACIDIC FIBROBLAST GROWTH
TITLE 2 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, BETA-
COMPND 5 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 PROTEIN,
KEYWDS 2 DIFFERENTIATION, GROWTH FACTOR, HEPARIN-BINDING, MITOGEN,
KEYWDS 3 POLYMORPHISM, HORMONE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BLABER,J.LEE
REVDAT 4 06-SEP-23 3FJ9 1 REMARK
REVDAT 3 20-OCT-21 3FJ9 1 REMARK SEQADV
REVDAT 2 13-OCT-09 3FJ9 1 JRNL
REVDAT 1 06-OCT-09 3FJ9 0
JRNL AUTH J.LEE,M.BLABER
JRNL TITL THE INTERACTION BETWEEN THERMODYNAMIC STABILITY AND BURIED
JRNL TITL 2 FREE CYSTEINES IN REGULATING THE FUNCTIONAL HALF-LIFE OF
JRNL TITL 3 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 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 316647.350
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.3
REMARK 3 NUMBER OF REFLECTIONS : 27769
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) : 0.188
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1390
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3300
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE : 0.2470
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 199
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 : 2278
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 238
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.09000
REMARK 3 B22 (A**2) : 3.60000
REMARK 3 B33 (A**2) : -3.70000
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) : 0.20
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) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.10
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.820
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 : 0.39
REMARK 3 BSOL : 42.97
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 : FORMATE.PARAM
REMARK 3 PARAMETER FILE 6 : 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 : FORMATE.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3FJ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-08.
REMARK 100 THE DEPOSITION ID IS D_1000050656.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-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) : 1.5481
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 : 27769
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 25.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.3
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.07900
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) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.37900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.640
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 (%): 57.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3M NA-FORMATE, PH 7.5, VAPOR
REMARK 280 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 54.78350
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 54.78350
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 37.11600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.88550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 37.11600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.88550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 54.78350
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 37.11600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.88550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 54.78350
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 37.11600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 47.88550
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 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 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 A 214 O HOH B 222 8556 2.15
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 ASP A 32 -163.42 -164.38
REMARK 500 HIS A 93 -51.88 -155.66
REMARK 500 GLU B 49 -98.37 -112.35
REMARK 500 HIS B 93 -51.70 -157.26
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 FMT A 141
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 141
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 142
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 WITH
REMARK 900 AMINO TERMINAL HIS TAG
REMARK 900 RELATED ID: 3FGM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF L44F/C83T/C117V/F132W MUTANT OF HUMAN ACIDIC
REMARK 900 FIBROBLAST GROWTH FACTOR
REMARK 900 RELATED ID: 3FJ8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF C117I MUTANT OF HUMAN ACIDIC FIBROBLAST GROWTH
REMARK 900 FACTOR
REMARK 900 RELATED ID: 3FJA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF F132W MUTANT OF HUMAN ACIDIC FIBROBLAST GROWTH
REMARK 900 FACTOR
REMARK 900 RELATED ID: 3FJB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF V31I MUTANT OF HUMAN ACIDIC FIBROBLAST GROWTH
REMARK 900 FACTOR
REMARK 900 RELATED ID: 3FJC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF L44W MUTANT OF HHUMAN ACIDIC FIBROBLAST GROWTH
REMARK 900 FACTOR
REMARK 900 RELATED ID: 3FJD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF L44F/F132W MUTANT OF HUMAN ACIDIC FIBROBLAST
REMARK 900 GROWTH FACTOR
REMARK 900 RELATED ID: 3FJE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF C83S MUTANT OF HUMAN ACIDIC FIBROBLAST GROWTH
REMARK 900 FACTOR
REMARK 900 RELATED ID: 3FJF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF C83T MUTANT OF HHUMAN ACIDIC FIBROBLAST GROWTH
REMARK 900 FACTOR
REMARK 900 RELATED ID: 3FJH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF C83A MUTANT OF HUMAN ACIDIC FIBROBLAST GROWTH
REMARK 900 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 GROWTH
REMARK 900 FACTOR
REMARK 900 RELATED ID: 3FJK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A66C MUTANT OF HUMAN ACIDIC FIBROBLAST GROWTH
REMARK 900 FACTOR
DBREF 3FJ9 A 1G 140 UNP P05230 FGF1_HUMAN 16 155
DBREF 3FJ9 B 1G 140 UNP P05230 FGF1_HUMAN 16 155
SEQADV 3FJ9 HIS A 1A UNP P05230 EXPRESSION TAG
SEQADV 3FJ9 HIS A 1B UNP P05230 EXPRESSION TAG
SEQADV 3FJ9 HIS A 1C UNP P05230 EXPRESSION TAG
SEQADV 3FJ9 HIS A 1D UNP P05230 EXPRESSION TAG
SEQADV 3FJ9 HIS A 1E UNP P05230 EXPRESSION TAG
SEQADV 3FJ9 HIS A 1F UNP P05230 EXPRESSION TAG
SEQADV 3FJ9 TRP A 85 UNP P05230 PHE 100 ENGINEERED MUTATION
SEQADV 3FJ9 HIS B 1A UNP P05230 EXPRESSION TAG
SEQADV 3FJ9 HIS B 1B UNP P05230 EXPRESSION TAG
SEQADV 3FJ9 HIS B 1C UNP P05230 EXPRESSION TAG
SEQADV 3FJ9 HIS B 1D UNP P05230 EXPRESSION TAG
SEQADV 3FJ9 HIS B 1E UNP P05230 EXPRESSION TAG
SEQADV 3FJ9 HIS B 1F UNP P05230 EXPRESSION TAG
SEQADV 3FJ9 TRP B 85 UNP P05230 PHE 100 ENGINEERED MUTATION
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 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 TRP
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 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 TRP
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 FMT A 141 3
HET FMT A 142 3
HET FMT B 1 3
HET FMT B 141 3
HET FMT B 142 3
HETNAM FMT FORMIC ACID
FORMUL 3 FMT 5(C H2 O2)
FORMUL 8 HOH *238(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 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 TRP A 85 GLU A 90 -1 O TRP 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 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 TRP B 85 GLU B 90 -1 O TRP 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 HIS A 1C HIS A 1D HIS A 1E LEU A 86
SITE 2 AC1 7 HOH A 173 HOH A 214 HOH A 226
SITE 1 AC2 4 ASN A 18 LYS A 112 LYS A 113 LYS A 118
SITE 1 AC3 4 GLN B 127 LYS B 128 ALA B 129 HOH B 253
SITE 1 AC4 6 HIS B 1C HIS B 1D HIS B 1E LEU B 86
SITE 2 AC4 6 HOH B 166 HOH B 234
SITE 1 AC5 4 TYR A 15 ARG A 37 PHE B 22 ARG B 37
CRYST1 74.232 95.771 109.567 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 0.013471 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010442 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009127 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
