HEADER HORMONE/GROWTH FACTOR 20-AUG-01 1JTC
TITLE HUMAN ACIDIC FIBROBLAST GROWTH FACTOR. 141 AMINO ACID FORM WITH AMINO
TITLE 2 TERMINAL HIS TAG AND LEU 44 REPLACED BY PHE (L44F)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACIDIC FIBROBLAST GROWTH FACTOR;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: HEPARIN-BINDING GROWTH FACTOR 1, HBGF-1, AFGF;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA-TREFOIL, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.R.BRYCH,S.I.BLABER,T.M.LOGAN,M.BLABER
REVDAT 4 16-AUG-23 1JTC 1 REMARK
REVDAT 3 27-OCT-21 1JTC 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1JTC 1 VERSN
REVDAT 1 19-DEC-01 1JTC 0
JRNL AUTH S.R.BRYCH,S.I.BLABER,T.M.LOGAN,M.BLABER
JRNL TITL STRUCTURE AND STABILITY EFFECTS OF MUTATIONS DESIGNED TO
JRNL TITL 2 INCREASE THE PRIMARY SEQUENCE SYMMETRY WITHIN THE CORE
JRNL TITL 3 REGION OF A BETA-TREFOIL.
JRNL REF PROTEIN SCI. V. 10 2587 2001
JRNL REFN ISSN 0961-8368
JRNL PMID 11714927
JRNL DOI 10.1110/PS.PS.34701
REMARK 2
REMARK 2 RESOLUTION. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 76.4
REMARK 3 NUMBER OF REFLECTIONS : 65452
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1970
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1930
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.00
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 7195
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 85721
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4538
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 434
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 11.300
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.008 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 1.800 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : 11.200; 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 : TNT
REMARK 3 KSOL : 0.98
REMARK 3 BSOL : 248.8
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : TRONRUD
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : TRONRUD
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JTC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000014159.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-00
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : OSMIC BLUE CONFOCAL MIRRORS
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 : 85721
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 36.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.600
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 200 DATA REDUNDANCY : 1.200
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.31900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MRCHK
REMARK 200 STARTING MODEL: 1JQZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM 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 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 48.46150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.89200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 48.46150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.89200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 465 HIS C 1A
REMARK 465 HIS C 1B
REMARK 465 SER C 138
REMARK 465 SER C 139
REMARK 465 ASP C 140
REMARK 465 HIS D 1A
REMARK 465 HIS D 1B
REMARK 465 SER D 138
REMARK 465 SER D 139
REMARK 465 ASP D 140
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 9 CG CD CE NZ
REMARK 470 ARG B 37 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 9 CG CD CE NZ
REMARK 470 GLU C 49 CG CD OE1 OE2
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 104 CD GLU B 104 OE2 0.074
REMARK 500 GLU D 104 CD GLU D 104 OE2 0.074
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 - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 28 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ASP A 32 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 39 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP A 68 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 68 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 70 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 70 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP B 32 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 32 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP B 36 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP B 39 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP C 28 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP C 32 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ASP C 39 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP C 68 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP C 68 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ASP D 32 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP D 32 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP D 36 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP D 39 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP D 68 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP D 70 CB - CG - OD2 ANGL. DEV. = -5.8 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 ASN A 7 -168.93 -118.71
REMARK 500 ASP A 32 -160.33 -166.78
REMARK 500 GLU A 49 -75.42 -83.60
REMARK 500 ASN A 92 -10.17 66.70
REMARK 500 ASP B 32 -159.80 -166.24
REMARK 500 GLU B 49 -100.62 -108.77
REMARK 500 ASN B 80 -168.53 -110.25
REMARK 500 HIS B 93 -52.21 -150.82
REMARK 500 PRO C 5 -156.51 -77.60
REMARK 500 ASN C 7 -167.19 -114.92
REMARK 500 ASP C 32 -161.36 -168.45
REMARK 500 GLU C 49 -85.01 -85.97
REMARK 500 ASN C 92 -8.41 65.91
REMARK 500 ASP D 32 -162.55 -170.27
REMARK 500 GLU D 49 -97.81 -107.91
REMARK 500 HIS D 93 -52.67 -151.77
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 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 166
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 167
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JQZ RELATED DB: PDB
REMARK 900 1JQZ IS HUMAN ACIDIC FIBROBLAST GROWTH FACTOR. 141 AMINO ACID FORM
REMARK 900 WITH AMINO TERMINAL HIS TAG.
DBREF 1JTC A 1A 140 UNP P05230 FGF1_HUMAN 16 155
DBREF 1JTC B 1A 140 UNP P05230 FGF1_HUMAN 16 155
DBREF 1JTC C 1A 140 UNP P05230 FGF1_HUMAN 16 155
DBREF 1JTC D 1A 140 UNP P05230 FGF1_HUMAN 16 155
SEQADV 1JTC HIS A 1A UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS A 1B UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS A 1C UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS A 1D UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS A 1E UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS A 1F UNP P05230 EXPRESSION TAG
SEQADV 1JTC PHE A 44 UNP P05230 LEU 59 ENGINEERED MUTATION
SEQADV 1JTC HIS B 1A UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS B 1B UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS B 1C UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS B 1D UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS B 1E UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS B 1F UNP P05230 EXPRESSION TAG
SEQADV 1JTC PHE B 44 UNP P05230 LEU 59 ENGINEERED MUTATION
SEQADV 1JTC HIS C 1A UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS C 1B UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS C 1C UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS C 1D UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS C 1E UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS C 1F UNP P05230 EXPRESSION TAG
SEQADV 1JTC PHE C 44 UNP P05230 LEU 59 ENGINEERED MUTATION
SEQADV 1JTC HIS D 1A UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS D 1B UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS D 1C UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS D 1D UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS D 1E UNP P05230 EXPRESSION TAG
SEQADV 1JTC HIS D 1F UNP P05230 EXPRESSION TAG
SEQADV 1JTC PHE D 44 UNP P05230 LEU 59 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 PHE 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 VAL ASP GLY
SEQRES 4 B 146 THR ARG ASP ARG SER ASP GLN HIS ILE GLN PHE 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
SEQRES 1 C 146 HIS HIS HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY ASN
SEQRES 2 C 146 TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY
SEQRES 3 C 146 HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY
SEQRES 4 C 146 THR ARG ASP ARG SER ASP GLN HIS ILE GLN PHE GLN LEU
SEQRES 5 C 146 SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR
SEQRES 6 C 146 GLU THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU
SEQRES 7 C 146 LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE
SEQRES 8 C 146 LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE
SEQRES 9 C 146 SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU
SEQRES 10 C 146 LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS
SEQRES 11 C 146 TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL
SEQRES 12 C 146 SER SER ASP
SEQRES 1 D 146 HIS HIS HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY ASN
SEQRES 2 D 146 TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY
SEQRES 3 D 146 HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY
SEQRES 4 D 146 THR ARG ASP ARG SER ASP GLN HIS ILE GLN PHE GLN LEU
SEQRES 5 D 146 SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR
SEQRES 6 D 146 GLU THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU
SEQRES 7 D 146 LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE
SEQRES 8 D 146 LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE
SEQRES 9 D 146 SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU
SEQRES 10 D 146 LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS
SEQRES 11 D 146 TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL
SEQRES 12 D 146 SER SER ASP
HET FMT A 160 3
HET FMT A 161 3
HET FMT B 162 3
HET FMT B 163 3
HET FMT C 164 3
HET FMT C 165 3
HET FMT D 166 3
HET FMT D 167 3
HETNAM FMT FORMIC ACID
FORMUL 5 FMT 8(C H2 O2)
FORMUL 13 HOH *434(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
HELIX 7 7 ASN C 80 CYS C 83 5 4
HELIX 8 8 HIS C 102 ASN C 106 5 5
HELIX 9 9 ARG C 119 THR C 123 5 5
HELIX 10 10 ASN D 80 CYS D 83 5 4
HELIX 11 11 HIS D 102 ASN D 106 5 5
HELIX 12 12 ARG D 119 THR D 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 PHE A 22 O THR A 34
SHEET 3 A 4 LYS A 10 CYS A 16 -1 O LEU A 14 N LEU A 23
SHEET 4 A 4 PHE A 132 PRO A 134 -1 O LEU A 131 N TYR A 15
SHEET 1 B 4 PHE A 44 ALA A 48 0
SHEET 2 B 4 GLU A 53 SER A 58 -1 N TYR A 55 O SER A 47
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 N TYR A 94 O GLU A 90
SHEET 1 C 2 TYR A 64 MET A 67 0
SHEET 2 C 2 LEU A 73 SER A 76 -1 N TYR A 74 O ALA A 66
SHEET 1 D 4 PHE B 132 PRO B 134 0
SHEET 2 D 4 LYS B 10 CYS B 16 -1 O LEU B 13 N LEU B 133
SHEET 3 D 4 HIS B 21 ILE B 25 -1 O HIS B 21 N CYS B 16
SHEET 4 D 4 VAL B 31 THR B 34 -1 O ASP B 32 N ARG B 24
SHEET 1 E 2 TYR B 64 MET B 67 0
SHEET 2 E 2 LEU B 73 SER B 76 -1 N TYR B 74 O ALA B 66
SHEET 1 F 4 PHE B 44 ALA B 48 0
SHEET 2 F 4 GLU B 53 SER B 58 -1 N TYR B 55 O SER B 47
SHEET 3 F 4 PHE B 85 GLU B 90 -1 O PHE B 85 N VAL B 54
SHEET 4 F 4 TYR B 94 SER B 99 -1 N TYR B 94 O GLU B 90
SHEET 1 G 9 VAL C 31 THR C 34 0
SHEET 2 G 9 HIS C 21 ILE C 25 -1 N PHE C 22 O THR C 34
SHEET 3 G 9 LYS C 10 CYS C 16 -1 O LEU C 14 N LEU C 23
SHEET 4 G 9 PHE C 132 PRO C 134 -1 O LEU C 131 N TYR C 15
SHEET 5 G 9 TYR C 94 SER C 99 -1 N ASN C 95 O PHE C 132
SHEET 6 G 9 PHE C 85 GLU C 90 -1 N LEU C 84 O ILE C 98
SHEET 7 G 9 GLU C 53 SER C 58 -1 N VAL C 54 O PHE C 85
SHEET 8 G 9 GLN C 43 ALA C 48 -1 N GLN C 43 O LYS C 57
SHEET 9 G 9 LYS C 10 CYS C 16 -1 N LYS C 10 O PHE C 44
SHEET 1 H 2 TYR C 64 MET C 67 0
SHEET 2 H 2 LEU C 73 SER C 76 -1 N TYR C 74 O ALA C 66
SHEET 1 I 4 VAL D 31 THR D 34 0
SHEET 2 I 4 HIS D 21 ILE D 25 -1 N PHE D 22 O THR D 34
SHEET 3 I 4 LYS D 10 CYS D 16 -1 O LEU D 14 N LEU D 23
SHEET 4 I 4 PHE D 132 PRO D 134 -1 O LEU D 131 N TYR D 15
SHEET 1 J 4 PHE D 44 ALA D 48 0
SHEET 2 J 4 GLU D 53 SER D 58 -1 N TYR D 55 O SER D 47
SHEET 3 J 4 PHE D 85 GLU D 90 -1 O PHE D 85 N VAL D 54
SHEET 4 J 4 TYR D 94 SER D 99 -1 N TYR D 94 O GLU D 90
SHEET 1 K 2 TYR D 64 MET D 67 0
SHEET 2 K 2 LEU D 73 SER D 76 -1 N TYR D 74 O ALA D 66
SITE 1 AC1 4 HIS A 1C HIS A 1D HIS A 1E HOH A 235
SITE 1 AC2 3 GLN A 127 LYS A 128 ALA A 129
SITE 1 AC3 6 HIS B 1C HIS B 1D HIS B 1E LEU B 86
SITE 2 AC3 6 HOH B1235 HOH B1432
SITE 1 AC4 4 GLN B 127 LYS B 128 ALA B 129 HOH B1270
SITE 1 AC5 4 HIS C 1C HIS C 1D HIS C 1E HOH C2235
SITE 1 AC6 4 GLN C 127 LYS C 128 ALA C 129 HOH C2270
SITE 1 AC7 6 HIS D 1C HIS D 1D HIS D 1E LEU D 86
SITE 2 AC7 6 HOH D3235 HOH D3423
SITE 1 AC8 4 GLN D 127 LYS D 128 ALA D 129 HOH D3270
CRYST1 96.923 73.784 109.131 90.00 89.98 90.00 C 1 2 1 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 0.010317 0.000000 -0.000004 0.00000
SCALE2 0.000000 0.013553 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009163 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
