HEADER PROTEIN BINDING 11-MAR-15 4YOL
TITLE HUMAN FIBROBLAST GROWTH FACTOR-1 C16S/A66C/C117A/P134A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBROBLAST GROWTH FACTOR 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 16-155;
COMPND 5 SYNONYM: FGF-1, ACIDIC FIBROBLAST GROWTH FACTOR, AFGF, ENDOTHELIAL
COMPND 6 CELL GROWTH FACTOR, ECGF, HEPARIN-BINDING GROWTH FACTOR 1, HBGF-1;
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, FGFA;
SOURCE 6 EXPRESSION_SYSTEM: ATLANTIBACTER HERMANNII;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: ESCHERICHIA HERMANNII;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 565
KEYWDS FIBROBLAST GROWTH FACTOR-1, CYSTEINE-FREE MUTANT, FGF-1,
KEYWDS 2 INTRAMOLECULAR DISULFIDE, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR X.XIA,M.BLABER
REVDAT 3 13-FEB-19 4YOL 1 SOURCE JRNL REMARK
REVDAT 2 13-APR-16 4YOL 1 JRNL
REVDAT 1 16-MAR-16 4YOL 0
JRNL AUTH X.XIA,O.S.KUMRU,S.I.BLABER,C.R.MIDDAUGH,L.LI,D.M.ORNITZ,
JRNL AUTH 2 M.A.SUTHERLAND,C.A.TENORIO,M.BLABER
JRNL TITL ENGINEERING A CYSTEINE-FREE FORM OF HUMAN FIBROBLAST GROWTH
JRNL TITL 2 FACTOR-1 FOR "SECOND GENERATION" THERAPEUTIC APPLICATION.
JRNL REF J.PHARM.SCI. V. 105 1444 2016
JRNL REFN ISSN 0022-3549
JRNL PMID 27019961
JRNL DOI 10.1016/J.XPHS.2016.02.010
REMARK 2
REMARK 2 RESOLUTION. 1.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 28135
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 37.8220 - 4.7246 0.93 1899 146 0.1629 0.2012
REMARK 3 2 4.7246 - 3.7512 0.96 1877 143 0.1321 0.1519
REMARK 3 3 3.7512 - 3.2773 0.97 1873 143 0.1447 0.1917
REMARK 3 4 3.2773 - 2.9778 0.97 1891 144 0.1602 0.2135
REMARK 3 5 2.9778 - 2.7644 0.98 1884 144 0.1742 0.2097
REMARK 3 6 2.7644 - 2.6015 0.98 1871 143 0.1715 0.2242
REMARK 3 7 2.6015 - 2.4712 0.98 1868 144 0.1894 0.2129
REMARK 3 8 2.4712 - 2.3637 0.98 1880 143 0.1703 0.2072
REMARK 3 9 2.3637 - 2.2727 0.99 1892 145 0.1672 0.2088
REMARK 3 10 2.2727 - 2.1943 0.99 1874 144 0.1676 0.2103
REMARK 3 11 2.1943 - 2.1257 0.99 1869 143 0.1605 0.1883
REMARK 3 12 2.1257 - 2.0649 0.99 1890 145 0.1585 0.2086
REMARK 3 13 2.0649 - 2.0105 0.99 1890 145 0.1741 0.2417
REMARK 3 14 2.0105 - 1.9615 0.89 1679 126 0.1917 0.2283
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.490
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 2475
REMARK 3 ANGLE : 1.060 3351
REMARK 3 CHIRALITY : 0.045 339
REMARK 3 PLANARITY : 0.005 446
REMARK 3 DIHEDRAL : 14.119 928
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4YOL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207840.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28191
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.970
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 9.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 39.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 9.70
REMARK 200 R MERGE FOR SHELL (I) : 0.40500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.7 M SODIUM CITRATE, 0.1 M IMIDAZOLE,
REMARK 280 PH 8.5, 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 53.95700
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 53.95700
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 37.81500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.91550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 37.81500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.91550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.95700
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 37.81500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.91550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.95700
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 37.81500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.91550
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 344 LIES ON A SPECIAL POSITION.
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 MET A -1
REMARK 465 HIS A 0
REMARK 465 SER A 139
REMARK 465 ASP A 140
REMARK 465 MET B -1
REMARK 465 HIS B 0
REMARK 465 SER B 139
REMARK 465 ASP B 140
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 442 O HOH B 443 1.81
REMARK 500 O HOH A 405 O HOH A 406 1.96
REMARK 500 O HOH A 428 O HOH A 429 1.97
REMARK 500 O HOH A 420 O HOH A 424 1.97
REMARK 500 O HOH B 342 O HOH B 354 2.00
REMARK 500 OE1 GLN A 43 O HOH A 375 2.01
REMARK 500 O HOH A 434 O HOH A 435 2.02
REMARK 500 O HOH B 460 O HOH B 470 2.06
REMARK 500 OG SER B 138 O HOH B 461 2.08
REMARK 500 O HOH B 434 O HOH B 443 2.08
REMARK 500 O HOH B 310 O HOH B 340 2.14
REMARK 500 O HOH A 433 O HOH A 447 2.14
REMARK 500 O HOH A 421 O HOH A 443 2.16
REMARK 500 O HOH B 305 O HOH B 336 2.16
REMARK 500 NE2 GLN B 77 O HOH B 466 2.16
REMARK 500 O THR A 78 O HOH A 301 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 323 O HOH B 335 3655 2.14
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 18 -75.22 -58.23
REMARK 500 ASP A 32 -159.82 -148.67
REMARK 500 GLU A 49 -107.05 -100.26
REMARK 500 HIS A 93 -54.70 -155.43
REMARK 500 ASN B 18 -72.92 -61.46
REMARK 500 ASP B 32 -157.65 -155.62
REMARK 500 GLU B 49 -104.90 -102.29
REMARK 500 HIS B 93 -49.88 -157.87
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 FLC A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AFG RELATED DB: PDB
REMARK 900 WILD-TYPE HUMAN FGF-1
REMARK 900 RELATED ID: 1JQZ RELATED DB: PDB
REMARK 900 WILD-TYPE HUMAN FGF-1 WITH 6*HIS TAG
REMARK 900 RELATED ID: 1RG8 RELATED DB: PDB
REMARK 900 WILD-TYPE HUMAN FGF-1
REMARK 900 RELATED ID: 4Q9G RELATED DB: PDB
REMARK 900 FGF-1 MUTANT C16S/K12V/C117V/P134V
REMARK 900 RELATED ID: 4QAL RELATED DB: PDB
REMARK 900 FGF-1 MUTANT C117A
REMARK 900 RELATED ID: 3HOM RELATED DB: PDB
REMARK 900 FGF-1 MUTANT A66C (OXIDIZED FORM)
REMARK 900 RELATED ID: 3FJK RELATED DB: PDB
REMARK 900 FGF-1 MUTANT A66C (REDUCED FORM)
DBREF 4YOL A 1G 140 UNP P05230 FGF1_HUMAN 16 155
DBREF 4YOL B 1G 140 UNP P05230 FGF1_HUMAN 16 155
SEQADV 4YOL MET A -1 UNP P05230 EXPRESSION TAG
SEQADV 4YOL HIS A 0 UNP P05230 EXPRESSION TAG
SEQADV 4YOL HIS A 1B UNP P05230 EXPRESSION TAG
SEQADV 4YOL HIS A 1C UNP P05230 EXPRESSION TAG
SEQADV 4YOL HIS A 1D UNP P05230 EXPRESSION TAG
SEQADV 4YOL HIS A 1E UNP P05230 EXPRESSION TAG
SEQADV 4YOL HIS A 1F UNP P05230 EXPRESSION TAG
SEQADV 4YOL SER A 16 UNP P05230 CYS 31 ENGINEERED MUTATION
SEQADV 4YOL CYS A 66 UNP P05230 ALA 81 ENGINEERED MUTATION
SEQADV 4YOL ALA A 117 UNP P05230 CYS 132 ENGINEERED MUTATION
SEQADV 4YOL ALA A 134 UNP P05230 PRO 149 ENGINEERED MUTATION
SEQADV 4YOL MET B -1 UNP P05230 EXPRESSION TAG
SEQADV 4YOL HIS B 0 UNP P05230 EXPRESSION TAG
SEQADV 4YOL HIS B 1B UNP P05230 EXPRESSION TAG
SEQADV 4YOL HIS B 1C UNP P05230 EXPRESSION TAG
SEQADV 4YOL HIS B 1D UNP P05230 EXPRESSION TAG
SEQADV 4YOL HIS B 1E UNP P05230 EXPRESSION TAG
SEQADV 4YOL HIS B 1F UNP P05230 EXPRESSION TAG
SEQADV 4YOL SER B 16 UNP P05230 CYS 31 ENGINEERED MUTATION
SEQADV 4YOL CYS B 66 UNP P05230 ALA 81 ENGINEERED MUTATION
SEQADV 4YOL ALA B 117 UNP P05230 CYS 132 ENGINEERED MUTATION
SEQADV 4YOL ALA B 134 UNP P05230 PRO 149 ENGINEERED MUTATION
SEQRES 1 A 147 MET HIS HIS HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY
SEQRES 2 A 147 ASN TYR LYS LYS PRO LYS LEU LEU TYR SER SER ASN GLY
SEQRES 3 A 147 GLY HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP
SEQRES 4 A 147 GLY THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN
SEQRES 5 A 147 LEU SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER
SEQRES 6 A 147 THR GLU THR GLY GLN TYR LEU CYS MET ASP THR ASP GLY
SEQRES 7 A 147 LEU LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU
SEQRES 8 A 147 PHE LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR
SEQRES 9 A 147 ILE SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY
SEQRES 10 A 147 LEU LYS LYS ASN GLY SER ALA LYS ARG GLY PRO ARG THR
SEQRES 11 A 147 HIS TYR GLY GLN LYS ALA ILE LEU PHE LEU ALA LEU PRO
SEQRES 12 A 147 VAL SER SER ASP
SEQRES 1 B 147 MET HIS HIS HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY
SEQRES 2 B 147 ASN TYR LYS LYS PRO LYS LEU LEU TYR SER SER ASN GLY
SEQRES 3 B 147 GLY HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP
SEQRES 4 B 147 GLY THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN
SEQRES 5 B 147 LEU SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER
SEQRES 6 B 147 THR GLU THR GLY GLN TYR LEU CYS MET ASP THR ASP GLY
SEQRES 7 B 147 LEU LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU
SEQRES 8 B 147 PHE LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR
SEQRES 9 B 147 ILE SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY
SEQRES 10 B 147 LEU LYS LYS ASN GLY SER ALA LYS ARG GLY PRO ARG THR
SEQRES 11 B 147 HIS TYR GLY GLN LYS ALA ILE LEU PHE LEU ALA LEU PRO
SEQRES 12 B 147 VAL SER SER ASP
HET FLC A 201 13
HET IMD A 202 5
HET FLC B 201 13
HETNAM FLC CITRATE ANION
HETNAM IMD IMIDAZOLE
FORMUL 3 FLC 2(C6 H5 O7 3-)
FORMUL 4 IMD C3 H5 N2 1+
FORMUL 6 HOH *321(H2 O)
HELIX 1 AA1 ASN A 80 CYS A 83 5 4
HELIX 2 AA2 HIS A 102 ASN A 106 5 5
HELIX 3 AA3 ARG A 119 THR A 123 5 5
HELIX 4 AA4 ASN B 80 CYS B 83 5 4
HELIX 5 AA5 HIS B 102 ASN B 106 5 5
HELIX 6 AA6 ARG B 119 THR B 123 5 5
SHEET 1 AA1 2 LYS A 12 SER A 16 0
SHEET 2 AA1 2 PHE A 132 PRO A 136 -1 O LEU A 133 N TYR A 15
SHEET 1 AA2 2 PHE A 22 ILE A 25 0
SHEET 2 AA2 2 VAL A 31 THR A 34 -1 O ASP A 32 N ARG A 24
SHEET 1 AA3 4 LEU A 44 ALA A 48 0
SHEET 2 AA3 4 GLU A 53 SER A 58 -1 O LYS A 57 N GLN A 45
SHEET 3 AA3 4 PHE A 85 GLU A 90 -1 O PHE A 85 N VAL A 54
SHEET 4 AA3 4 TYR A 94 SER A 99 -1 O ILE A 98 N LEU A 86
SHEET 1 AA4 2 TYR A 64 MET A 67 0
SHEET 2 AA4 2 LEU A 73 SER A 76 -1 O SER A 76 N TYR A 64
SHEET 1 AA5 2 LYS B 12 SER B 16 0
SHEET 2 AA5 2 PHE B 132 PRO B 136 -1 O LEU B 135 N LEU B 13
SHEET 1 AA6 2 PHE B 22 ILE B 25 0
SHEET 2 AA6 2 VAL B 31 THR B 34 -1 O ASP B 32 N ARG B 24
SHEET 1 AA7 4 LEU B 44 ALA B 48 0
SHEET 2 AA7 4 GLU B 53 SER B 58 -1 O LYS B 57 N GLN B 45
SHEET 3 AA7 4 PHE B 85 GLU B 90 -1 O PHE B 85 N VAL B 54
SHEET 4 AA7 4 TYR B 94 SER B 99 -1 O ILE B 98 N LEU B 86
SHEET 1 AA8 2 TYR B 64 MET B 67 0
SHEET 2 AA8 2 LEU B 73 SER B 76 -1 O SER B 76 N TYR B 64
SSBOND 1 CYS A 66 CYS A 83 1555 1555 2.04
SSBOND 2 CYS B 66 CYS B 83 1555 1555 2.03
SITE 1 AC1 8 ASN A 18 LYS A 112 LYS A 113 LYS A 118
SITE 2 AC1 8 GLN A 127 LYS A 128 ALA A 129 HOH A 407
SITE 1 AC2 6 TYR A 15 PHE A 22 ARG A 37 TYR B 15
SITE 2 AC2 6 ARG B 37 HOH B 387
SITE 1 AC3 13 ASP A 70 ASN B 18 LYS B 112 LYS B 113
SITE 2 AC3 13 LYS B 118 GLN B 127 LYS B 128 ALA B 129
SITE 3 AC3 13 HOH B 308 HOH B 417 HOH B 441 HOH B 469
SITE 4 AC3 13 HOH B 471
CRYST1 75.630 97.831 107.914 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 0.013222 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010222 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009267 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
