HEADER GROWTH FACTOR 16-OCT-97 1AXM
TITLE HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST GROWTH FACTOR
CAVEAT 1AXM IDS I 5 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACIDIC FIBROBLAST GROWTH FACTOR;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: FGF-1;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: FOR EACH OF THE DECASACCHARIDE CHAINS IN THE
COMPND 7 ASYMMETRIC UNIT, FIVE MONOSACCHARIDE UNITS ARE DISORDERED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: JM109 DE3;
SOURCE 6 ORGAN: BRAIN STEM;
SOURCE 7 TISSUE: NERVE;
SOURCE 8 CELL: ENDOTHELIAL;
SOURCE 9 CELLULAR_LOCATION: EXTRACELLULAR MATRIX;
SOURCE 10 GENE: ECGF;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: JM109 DE3;
SOURCE 15 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET-3A
KEYWDS HUMAN ACIDIC FIBROBLAST GROWTH FACTOR, HEPARIN DECASACCHARIDE, GROWTH
KEYWDS 2 FACTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR A.D.DIGABRIELE,I.LAX,D.I.CHEN,C.M.SVAHN,M.JAYE,J.SCHLESSINGER,
AUTHOR 2 W.A.HENDRICKSON
REVDAT 6 02-AUG-23 1AXM 1 HETSYN
REVDAT 5 29-JUL-20 1AXM 1 CAVEAT COMPND REMARK SEQADV
REVDAT 5 2 1 HETNAM LINK SITE ATOM
REVDAT 4 13-JUL-11 1AXM 1 VERSN
REVDAT 3 24-FEB-09 1AXM 1 VERSN
REVDAT 2 21-JUN-05 1AXM 1 AUTHOR JRNL
REVDAT 1 22-APR-98 1AXM 0
JRNL AUTH A.D.DIGABRIELE,I.LAX,D.I.CHEN,C.M.SVAHN,M.JAYE,
JRNL AUTH 2 J.SCHLESSINGER,W.A.HENDRICKSON
JRNL TITL STRUCTURE OF A HEPARIN-LINKED BIOLOGICALLY ACTIVE DIMER OF
JRNL TITL 2 FIBROBLAST GROWTH FACTOR.
JRNL REF NATURE V. 393 812 1998
JRNL REFN ISSN 0028-0836
JRNL PMID 9655399
JRNL DOI 10.1038/31741
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.BLABER,J.DISALVO,K.A.THOMAS
REMARK 1 TITL X-RAY CRYSTAL STRUCTURE OF HUMAN ACIDIC FIBROBLAST GROWTH
REMARK 1 TITL 2 FACTOR.
REMARK 1 REF BIOCHEMISTRY V. 35 2086 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 8652550
REMARK 1 DOI 10.1021/BI9521755
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.FAHAM,R.E.HILEMAN,J.R.FROMM,R.J.LINHARDT,D.C.REES
REMARK 1 TITL HEPARIN STRUCTURE AND INTERACTIONS WITH BASIC FIBROBLAST
REMARK 1 TITL 2 GROWTH FACTOR
REMARK 1 REF SCIENCE V. 271 1116 1996
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 3
REMARK 1 AUTH X.ZHU,B.T.HSU,D.C.REES
REMARK 1 TITL STRUCTURAL STUDIES OF THE BINDING OF THE ANTI-ULCER DRUG
REMARK 1 TITL 2 SUCROSE OCTASULFATE TO ACIDIC FIBROBLAST GROWTH FACTOR
REMARK 1 REF STRUCTURE V. 1 27 1993
REMARK 1 REFN ISSN 0969-2126
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 1.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.6
REMARK 3 NUMBER OF REFLECTIONS : 23540
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) : 0.217
REMARK 3 FREE R VALUE : 0.304
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2077
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2449
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE : 0.3840
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 313
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6125
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 267
REMARK 3 SOLVENT ATOMS : 71
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.400
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.500 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.000 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.000 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.500 ; 2.000
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : 0.27 ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : 1.56 ; 2.0
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARAM19.SOL
REMARK 3 PARAMETER FILE 2 : PARAMCSDX_MOD.PRO
REMARK 3 PARAMETER FILE 3 : HEP96.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 2 : TOPHCSDX_MOD.PRO
REMARK 3 TOPOLOGY FILE 3 : TOPH19.PEP
REMARK 3 TOPOLOGY FILE 4 : HEP96.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AXM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171380.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-95
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98789
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : BENT MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25115
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : 0.09500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.33700
REMARK 200 R SYM FOR SHELL (I) : 0.33700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: MADSYS
REMARK 200 STARTING MODEL: PDB ENTRIES 1AFC, 1HPN
REMARK 200
REMARK 200 REMARK: BOTH MOLECULAR REPLACEMENT AND MAD WERE USED FOR PHASE
REMARK 200 DETERMINATION AND COMBINATION
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN/HEPARIN COMPLEX WAS
REMARK 280 CRYSTALLIZED FROM 25% PEG 8000, 200 MM MGSO4, 100 MM HEPES, PH
REMARK 280 7.0; CRYSTAL WAS SOAKED IN 22% XYLITOL PRIOR TO DATA COLLECTION.
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 95.29000
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 95.29000
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 43.84500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 79.02500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 43.84500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 79.02500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 95.29000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.84500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 79.02500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 95.29000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 43.84500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 79.02500
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, 3
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F, I
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, E, H
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 GLY A 6
REMARK 465 ASN A 7
REMARK 465 TYR A 8
REMARK 465 SER A 139
REMARK 465 ASP A 140
REMARK 465 GLY B 6
REMARK 465 ASN B 7
REMARK 465 TYR B 8
REMARK 465 LYS B 9
REMARK 465 LYS B 10
REMARK 465 SER B 138
REMARK 465 SER B 139
REMARK 465 ASP B 140
REMARK 465 GLY C 6
REMARK 465 ASN C 7
REMARK 465 TYR C 8
REMARK 465 LYS C 9
REMARK 465 SER C 138
REMARK 465 SER C 139
REMARK 465 ASP C 140
REMARK 465 GLY D 6
REMARK 465 ASN D 7
REMARK 465 TYR D 8
REMARK 465 LYS D 9
REMARK 465 LYS D 10
REMARK 465 SER D 138
REMARK 465 SER D 139
REMARK 465 ASP D 140
REMARK 465 GLY E 6
REMARK 465 ASN E 7
REMARK 465 TYR E 8
REMARK 465 LYS E 9
REMARK 465 SER E 139
REMARK 465 ASP E 140
REMARK 465 GLY F 6
REMARK 465 ASN F 7
REMARK 465 TYR F 8
REMARK 465 LYS F 9
REMARK 465 SER F 139
REMARK 465 ASP F 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 LYS A 10 CG CD CE NZ
REMARK 470 PRO B 11 CG CD
REMARK 470 LYS C 10 CG CD CE NZ
REMARK 470 PRO D 11 CG CD
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 PRO B 11 N - CA - CB ANGL. DEV. = 7.5 DEGREES
REMARK 500 PRO D 11 N - CA - CB ANGL. DEV. = 7.5 DEGREES
REMARK 500 CYS F 117 CA - CB - SG ANGL. DEV. = 7.5 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 LYS A 12 -168.71 -119.97
REMARK 500 ASP A 32 -154.10 -160.45
REMARK 500 GLN A 40 22.04 -76.32
REMARK 500 SER A 50 -149.18 -161.20
REMARK 500 HIS A 102 30.90 -87.94
REMARK 500 PRO A 134 94.10 -66.75
REMARK 500 ASN B 18 97.56 -61.06
REMARK 500 ASP B 32 -155.02 -157.53
REMARK 500 ASP B 36 94.23 -54.59
REMARK 500 ASN B 92 31.16 -78.32
REMARK 500 ASN B 106 43.63 72.03
REMARK 500 PRO B 121 -6.95 -55.98
REMARK 500 ASP C 32 -143.44 -153.97
REMARK 500 GLU C 49 -70.63 -131.78
REMARK 500 SER C 50 -162.09 -120.58
REMARK 500 VAL C 51 17.30 -66.17
REMARK 500 ASP C 68 -167.19 -63.90
REMARK 500 PRO C 79 89.60 -66.19
REMARK 500 ASN C 80 -167.16 -105.47
REMARK 500 GLU C 90 -79.89 -88.55
REMARK 500 ASN C 92 -4.55 -40.80
REMARK 500 ASN D 18 87.99 -68.58
REMARK 500 ASP D 28 30.16 -89.38
REMARK 500 ASP D 32 -147.73 -160.58
REMARK 500 ASP D 36 88.84 -56.33
REMARK 500 ASP D 68 -167.40 -63.82
REMARK 500 ASN D 80 -160.99 -112.49
REMARK 500 PRO D 134 85.30 -69.29
REMARK 500 ASP E 32 -153.34 -169.69
REMARK 500 ASP E 36 96.46 -54.66
REMARK 500 ASN E 80 -169.85 -112.69
REMARK 500 GLU E 90 -86.04 -55.77
REMARK 500 GLU E 91 -157.61 -80.93
REMARK 500 HIS E 93 -42.51 -146.88
REMARK 500 SER E 99 105.13 -56.32
REMARK 500 VAL E 137 29.03 -146.93
REMARK 500 ASN F 18 89.44 -65.61
REMARK 500 ASP F 32 -148.35 -164.98
REMARK 500 GLN F 40 27.75 -77.91
REMARK 500 SER F 50 172.02 162.06
REMARK 500 PRO F 79 90.25 -69.79
REMARK 500 ASN F 80 -169.88 -104.07
REMARK 500 HIS F 93 36.59 73.74
REMARK 500 ASN F 106 43.86 71.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: HPA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HEPARIN BINDING LOOP.
REMARK 800
REMARK 800 SITE_IDENTIFIER: HPB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HEPARIN BINDING LOOP.
REMARK 800
REMARK 800 SITE_IDENTIFIER: HPC
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HEPARIN BINDING LOOP.
REMARK 800
REMARK 800 SITE_IDENTIFIER: HPD
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HEPARIN BINDING LOOP.
REMARK 800
REMARK 800 SITE_IDENTIFIER: HPE
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HEPARIN BINDING LOOP.
REMARK 800
REMARK 800 SITE_IDENTIFIER: HPF
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HEPARIN BINDING LOOP.
DBREF 1AXM A 6 140 UNP P05230 FGF1_HUMAN 21 155
DBREF 1AXM B 6 140 UNP P05230 FGF1_HUMAN 21 155
DBREF 1AXM C 6 140 UNP P05230 FGF1_HUMAN 21 155
DBREF 1AXM D 6 140 UNP P05230 FGF1_HUMAN 21 155
DBREF 1AXM E 6 140 UNP P05230 FGF1_HUMAN 21 155
DBREF 1AXM F 6 140 UNP P05230 FGF1_HUMAN 21 155
SEQADV 1AXM MSE A 67 UNP P05230 MET 82 MODIFIED RESIDUE
SEQADV 1AXM MSE B 67 UNP P05230 MET 82 MODIFIED RESIDUE
SEQADV 1AXM MSE C 67 UNP P05230 MET 82 MODIFIED RESIDUE
SEQADV 1AXM MSE D 67 UNP P05230 MET 82 MODIFIED RESIDUE
SEQADV 1AXM MSE E 67 UNP P05230 MET 82 MODIFIED RESIDUE
SEQADV 1AXM MSE F 67 UNP P05230 MET 82 MODIFIED RESIDUE
SEQRES 1 A 135 GLY ASN TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN
SEQRES 2 A 135 GLY GLY HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL
SEQRES 3 A 135 ASP GLY THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU
SEQRES 4 A 135 GLN LEU SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS
SEQRES 5 A 135 SER THR GLU THR GLY GLN TYR LEU ALA MSE ASP THR ASP
SEQRES 6 A 135 GLY LEU LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS
SEQRES 7 A 135 LEU PHE LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR
SEQRES 8 A 135 TYR ILE SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL
SEQRES 9 A 135 GLY LEU LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG
SEQRES 10 A 135 THR HIS TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU
SEQRES 11 A 135 PRO VAL SER SER ASP
SEQRES 1 B 135 GLY ASN TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN
SEQRES 2 B 135 GLY GLY HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL
SEQRES 3 B 135 ASP GLY THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU
SEQRES 4 B 135 GLN LEU SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS
SEQRES 5 B 135 SER THR GLU THR GLY GLN TYR LEU ALA MSE ASP THR ASP
SEQRES 6 B 135 GLY LEU LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS
SEQRES 7 B 135 LEU PHE LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR
SEQRES 8 B 135 TYR ILE SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL
SEQRES 9 B 135 GLY LEU LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG
SEQRES 10 B 135 THR HIS TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU
SEQRES 11 B 135 PRO VAL SER SER ASP
SEQRES 1 C 135 GLY ASN TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN
SEQRES 2 C 135 GLY GLY HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL
SEQRES 3 C 135 ASP GLY THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU
SEQRES 4 C 135 GLN LEU SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS
SEQRES 5 C 135 SER THR GLU THR GLY GLN TYR LEU ALA MSE ASP THR ASP
SEQRES 6 C 135 GLY LEU LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS
SEQRES 7 C 135 LEU PHE LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR
SEQRES 8 C 135 TYR ILE SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL
SEQRES 9 C 135 GLY LEU LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG
SEQRES 10 C 135 THR HIS TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU
SEQRES 11 C 135 PRO VAL SER SER ASP
SEQRES 1 D 135 GLY ASN TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN
SEQRES 2 D 135 GLY GLY HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL
SEQRES 3 D 135 ASP GLY THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU
SEQRES 4 D 135 GLN LEU SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS
SEQRES 5 D 135 SER THR GLU THR GLY GLN TYR LEU ALA MSE ASP THR ASP
SEQRES 6 D 135 GLY LEU LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS
SEQRES 7 D 135 LEU PHE LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR
SEQRES 8 D 135 TYR ILE SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL
SEQRES 9 D 135 GLY LEU LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG
SEQRES 10 D 135 THR HIS TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU
SEQRES 11 D 135 PRO VAL SER SER ASP
SEQRES 1 E 135 GLY ASN TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN
SEQRES 2 E 135 GLY GLY HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL
SEQRES 3 E 135 ASP GLY THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU
SEQRES 4 E 135 GLN LEU SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS
SEQRES 5 E 135 SER THR GLU THR GLY GLN TYR LEU ALA MSE ASP THR ASP
SEQRES 6 E 135 GLY LEU LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS
SEQRES 7 E 135 LEU PHE LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR
SEQRES 8 E 135 TYR ILE SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL
SEQRES 9 E 135 GLY LEU LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG
SEQRES 10 E 135 THR HIS TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU
SEQRES 11 E 135 PRO VAL SER SER ASP
SEQRES 1 F 135 GLY ASN TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN
SEQRES 2 F 135 GLY GLY HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL
SEQRES 3 F 135 ASP GLY THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU
SEQRES 4 F 135 GLN LEU SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS
SEQRES 5 F 135 SER THR GLU THR GLY GLN TYR LEU ALA MSE ASP THR ASP
SEQRES 6 F 135 GLY LEU LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS
SEQRES 7 F 135 LEU PHE LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR
SEQRES 8 F 135 TYR ILE SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL
SEQRES 9 F 135 GLY LEU LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG
SEQRES 10 F 135 THR HIS TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU
SEQRES 11 F 135 PRO VAL SER SER ASP
MODRES 1AXM MSE A 67 MET SELENOMETHIONINE
MODRES 1AXM MSE B 67 MET SELENOMETHIONINE
MODRES 1AXM MSE C 67 MET SELENOMETHIONINE
MODRES 1AXM MSE D 67 MET SELENOMETHIONINE
MODRES 1AXM MSE E 67 MET SELENOMETHIONINE
MODRES 1AXM MSE F 67 MET SELENOMETHIONINE
HET MSE A 67 8
HET MSE B 67 8
HET MSE C 67 8
HET MSE D 67 8
HET MSE E 67 8
HET MSE F 67 8
HET SGN G 1 20
HET IDS G 2 16
HET SGN G 3 19
HET IDS G 4 16
HET SGN G 5 19
HET SGN H 1 20
HET IDS H 2 16
HET SGN H 3 19
HET IDS H 4 16
HET SGN H 5 19
HET IDS I 1 17
HET SGN I 2 19
HET IDS I 3 16
HET SGN I 4 19
HET IDS I 5 16
HETNAM MSE SELENOMETHIONINE
HETNAM SGN 2-DEOXY-6-O-SULFO-2-(SULFOAMINO)-ALPHA-D-GLUCOPYRANOSE
HETNAM IDS 2-O-SULFO-ALPHA-L-IDOPYRANURONIC ACID
HETSYN SGN N,O6-DISULFO-GLUCOSAMINE; 6-O-SULFO-N-SULFO-ALPHA-D-
HETSYN 2 SGN GLUCOSAMINE; 2-DEOXY-6-O-SULFO-2-(SULFOAMINO)-ALPHA-D-
HETSYN 3 SGN GLUCOSE; 2-DEOXY-6-O-SULFO-2-(SULFOAMINO)-D-GLUCOSE;
HETSYN 4 SGN 2-DEOXY-6-O-SULFO-2-(SULFOAMINO)-GLUCOSE
HETSYN IDS O2-SULFO-GLUCURONIC ACID; 2-O-SULFO-ALPHA-L-IDURONIC
HETSYN 2 IDS ACID; 2-O-SULFO-L-IDURONIC ACID; 2-O-SULFO-IDURONIC
HETSYN 3 IDS ACID
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 7 SGN 8(C6 H13 N O11 S2)
FORMUL 7 IDS 7(C6 H10 O10 S)
FORMUL 10 HOH *71(H2 O)
HELIX 1 1 GLU A 81 CYS A 83 5 3
HELIX 2 2 ALA A 103 LYS A 105 5 3
HELIX 3 3 GLY A 120 ARG A 122 5 3
HELIX 4 4 GLU B 81 CYS B 83 5 3
HELIX 5 5 ALA B 103 LYS B 105 5 3
HELIX 6 6 GLY B 120 ARG B 122 5 3
HELIX 7 7 LYS B 128 ILE B 130 5 3
HELIX 8 8 GLU C 81 CYS C 83 5 3
HELIX 9 9 ALA C 103 LYS C 105 5 3
HELIX 10 10 GLY C 120 ARG C 122 5 3
HELIX 11 11 LYS C 128 ILE C 130 5 3
HELIX 12 12 GLU D 81 CYS D 83 5 3
HELIX 13 13 LYS D 101 LYS D 105 5 5
HELIX 14 14 GLY D 120 ARG D 122 5 3
HELIX 15 15 LYS D 128 ILE D 130 5 3
HELIX 16 16 GLU E 81 CYS E 83 5 3
HELIX 17 17 ALA E 103 LYS E 105 5 3
HELIX 18 18 GLY E 120 ARG E 122 5 3
HELIX 19 19 LYS E 128 ILE E 130 5 3
HELIX 20 20 GLU F 81 CYS F 83 5 3
HELIX 21 21 ALA F 103 LYS F 105 5 3
HELIX 22 22 GLY F 120 ARG F 122 5 3
HELIX 23 23 LYS F 128 ILE F 130 5 3
SHEET 1 A 2 LYS A 12 CYS A 16 0
SHEET 2 A 2 PHE A 132 PRO A 136 -1 N LEU A 135 O LEU A 13
SHEET 1 B 2 PHE A 22 ILE A 25 0
SHEET 2 B 2 VAL A 31 THR A 34 -1 N THR A 34 O PHE A 22
SHEET 1 C 4 LEU A 44 SER A 47 0
SHEET 2 C 4 GLU A 53 SER A 58 -1 N LYS A 57 O GLN A 45
SHEET 3 C 4 LEU A 84 LEU A 89 -1 N PHE A 85 O VAL A 54
SHEET 4 C 4 ASN A 95 SER A 99 -1 N ILE A 98 O LEU A 86
SHEET 1 D 2 TYR A 64 ALA A 66 0
SHEET 2 D 2 TYR A 74 SER A 76 -1 N SER A 76 O TYR A 64
SHEET 1 E 2 LYS B 12 CYS B 16 0
SHEET 2 E 2 PHE B 132 PRO B 136 -1 N LEU B 135 O LEU B 13
SHEET 1 F 2 PHE B 22 ILE B 25 0
SHEET 2 F 2 VAL B 31 THR B 34 -1 N THR B 34 O PHE B 22
SHEET 1 G 2 LEU B 44 ALA B 48 0
SHEET 2 G 2 VAL B 54 SER B 58 -1 N LYS B 57 O GLN B 45
SHEET 1 H 2 TYR B 64 ALA B 66 0
SHEET 2 H 2 TYR B 74 SER B 76 -1 N SER B 76 O TYR B 64
SHEET 1 I 2 PHE B 85 GLU B 90 0
SHEET 2 I 2 TYR B 94 SER B 99 -1 N ILE B 98 O LEU B 86
SHEET 1 J 2 LYS C 12 CYS C 16 0
SHEET 2 J 2 PHE C 132 PRO C 136 -1 N LEU C 135 O LEU C 13
SHEET 1 K 2 PHE C 22 ILE C 25 0
SHEET 2 K 2 VAL C 31 THR C 34 -1 N THR C 34 O PHE C 22
SHEET 1 L 2 LEU C 44 ALA C 48 0
SHEET 2 L 2 VAL C 54 SER C 58 -1 N LYS C 57 O GLN C 45
SHEET 1 M 2 TYR C 64 ALA C 66 0
SHEET 2 M 2 TYR C 74 SER C 76 -1 N SER C 76 O TYR C 64
SHEET 1 N 2 PHE C 85 LEU C 89 0
SHEET 2 N 2 ASN C 95 SER C 99 -1 N ILE C 98 O LEU C 86
SHEET 1 O 2 LYS D 12 CYS D 16 0
SHEET 2 O 2 PHE D 132 PRO D 136 -1 N LEU D 135 O LEU D 13
SHEET 1 P 2 PHE D 22 ILE D 25 0
SHEET 2 P 2 VAL D 31 THR D 34 -1 N THR D 34 O PHE D 22
SHEET 1 Q 2 TYR D 64 ALA D 66 0
SHEET 2 Q 2 TYR D 74 SER D 76 -1 N SER D 76 O TYR D 64
SHEET 1 R 2 PHE D 85 LEU D 89 0
SHEET 2 R 2 ASN D 95 SER D 99 -1 N ILE D 98 O LEU D 86
SHEET 1 S 2 LEU D 44 SER D 50 0
SHEET 2 S 2 GLU D 53 SER D 58 -1 N LYS D 57 O GLN D 45
SHEET 1 T 2 LYS E 12 CYS E 16 0
SHEET 2 T 2 PHE E 132 PRO E 136 -1 N LEU E 135 O LEU E 13
SHEET 1 U 2 PHE E 22 ILE E 25 0
SHEET 2 U 2 VAL E 31 THR E 34 -1 N THR E 34 O PHE E 22
SHEET 1 V 2 LEU E 44 SER E 47 0
SHEET 2 V 2 TYR E 55 SER E 58 -1 N LYS E 57 O GLN E 45
SHEET 1 W 2 TYR E 64 ALA E 66 0
SHEET 2 W 2 TYR E 74 SER E 76 -1 N SER E 76 O TYR E 64
SHEET 1 X 2 PHE E 85 LEU E 89 0
SHEET 2 X 2 ASN E 95 SER E 99 -1 N ILE E 98 O LEU E 86
SHEET 1 Y 2 LYS F 12 CYS F 16 0
SHEET 2 Y 2 PHE F 132 PRO F 136 -1 N LEU F 135 O LEU F 13
SHEET 1 Z 2 PHE F 22 ILE F 25 0
SHEET 2 Z 2 VAL F 31 THR F 34 -1 N THR F 34 O PHE F 22
SHEET 1 AA 2 LEU F 44 SER F 47 0
SHEET 2 AA 2 TYR F 55 SER F 58 -1 N LYS F 57 O GLN F 45
SHEET 1 AB 2 TYR F 64 ALA F 66 0
SHEET 2 AB 2 TYR F 74 SER F 76 -1 N SER F 76 O TYR F 64
SHEET 1 AC 2 PHE F 85 LEU F 89 0
SHEET 2 AC 2 ASN F 95 SER F 99 -1 N ILE F 98 O LEU F 86
LINK C ALA A 66 N MSE A 67 1555 1555 1.33
LINK C MSE A 67 N ASP A 68 1555 1555 1.32
LINK C ALA B 66 N MSE B 67 1555 1555 1.33
LINK C MSE B 67 N ASP B 68 1555 1555 1.33
LINK C ALA C 66 N MSE C 67 1555 1555 1.34
LINK C MSE C 67 N ASP C 68 1555 1555 1.34
LINK C ALA D 66 N MSE D 67 1555 1555 1.33
LINK C MSE D 67 N ASP D 68 1555 1555 1.34
LINK C ALA E 66 N MSE E 67 1555 1555 1.33
LINK C MSE E 67 N ASP E 68 1555 1555 1.34
LINK C ALA F 66 N MSE F 67 1555 1555 1.33
LINK C MSE F 67 N ASP F 68 1555 1555 1.33
LINK O4 SGN G 1 C1 IDS G 2 1555 1555 1.40
LINK O4 IDS G 2 C1 SGN G 3 1555 1555 1.41
LINK O4 SGN G 3 C1 IDS G 4 1555 1555 1.41
LINK O4 IDS G 4 C1 SGN G 5 1555 1555 1.41
LINK O4 SGN H 1 C1 IDS H 2 1555 1555 1.41
LINK O4 IDS H 2 C1 SGN H 3 1555 1555 1.40
LINK O4 SGN H 3 C1 IDS H 4 1555 1555 1.41
LINK O4 IDS H 4 C1 SGN H 5 1555 1555 1.40
LINK O4 IDS I 1 C1 SGN I 2 1555 1555 1.40
LINK O4 SGN I 2 C1 IDS I 3 1555 1555 1.40
LINK O4 IDS I 3 C1 SGN I 4 1555 1555 1.40
LINK O4 SGN I 4 C1 IDS I 5 1555 1555 1.39
SITE 1 HPA 18 ASN A 18 LYS A 112 LYS A 113 ASN A 114
SITE 2 HPA 18 GLY A 115 SER A 116 CYS A 117 LYS A 118
SITE 3 HPA 18 ARG A 119 GLY A 120 PRO A 121 ARG A 122
SITE 4 HPA 18 THR A 123 HIS A 124 TYR A 125 GLY A 126
SITE 5 HPA 18 GLN A 127 LYS A 128
SITE 1 HPB 18 ASN B 18 LYS B 112 LYS B 113 ASN B 114
SITE 2 HPB 18 GLY B 115 SER B 116 CYS B 117 LYS B 118
SITE 3 HPB 18 ARG B 119 GLY B 120 PRO B 121 ARG B 122
SITE 4 HPB 18 THR B 123 HIS B 124 TYR B 125 GLY B 126
SITE 5 HPB 18 GLN B 127 LYS B 128
SITE 1 HPC 18 ASN C 18 LYS C 112 LYS C 113 ASN C 114
SITE 2 HPC 18 GLY C 115 SER C 116 CYS C 117 LYS C 118
SITE 3 HPC 18 ARG C 119 GLY C 120 PRO C 121 ARG C 122
SITE 4 HPC 18 THR C 123 HIS C 124 TYR C 125 GLY C 126
SITE 5 HPC 18 GLN C 127 LYS C 128
SITE 1 HPD 18 ASN D 18 LYS D 112 LYS D 113 ASN D 114
SITE 2 HPD 18 GLY D 115 SER D 116 CYS D 117 LYS D 118
SITE 3 HPD 18 ARG D 119 GLY D 120 PRO D 121 ARG D 122
SITE 4 HPD 18 THR D 123 HIS D 124 TYR D 125 GLY D 126
SITE 5 HPD 18 GLN D 127 LYS D 128
SITE 1 HPE 18 ASN E 18 LYS E 112 LYS E 113 ASN E 114
SITE 2 HPE 18 GLY E 115 SER E 116 CYS E 117 LYS E 118
SITE 3 HPE 18 ARG E 119 GLY E 120 PRO E 121 ARG E 122
SITE 4 HPE 18 THR E 123 HIS E 124 TYR E 125 GLY E 126
SITE 5 HPE 18 GLN E 127 LYS E 128
SITE 1 HPF 18 ASN F 18 LYS F 112 LYS F 113 ASN F 114
SITE 2 HPF 18 GLY F 115 SER F 116 CYS F 117 LYS F 118
SITE 3 HPF 18 ARG F 119 GLY F 120 PRO F 121 ARG F 122
SITE 4 HPF 18 THR F 123 HIS F 124 TYR F 125 GLY F 126
SITE 5 HPF 18 GLN F 127 LYS F 128
CRYST1 87.690 158.050 190.580 90.00 90.00 90.00 C 2 2 21 48
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 0.011404 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006327 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005247 0.00000
MTRIX1 1 0.959510 0.063610 0.274410 -11.02670 1
MTRIX2 1 -0.010650 -0.965280 0.261020 2.80977 1
MTRIX3 1 0.281490 -0.253370 -0.925510 94.12106 1
MTRIX1 2 -0.588820 0.727080 -0.353050 28.19709 1
MTRIX2 2 0.759210 0.647390 0.067010 27.14610 1
MTRIX3 2 0.277290 -0.228580 -0.933200 157.20302 1
MTRIX1 3 -0.620770 0.783940 0.008980 -24.62529 1
MTRIX2 3 -0.783690 -0.620810 0.020340 37.83826 1
MTRIX3 3 0.021520 0.005590 0.999750 127.53954 1
MTRIX1 4 -0.399700 -0.910330 0.107390 24.34238 1
MTRIX2 4 0.916060 -0.400890 0.011150 39.48433 1
MTRIX3 4 0.032900 0.102830 0.994150 63.02549 1
MTRIX1 5 -0.405730 -0.913670 -0.024300 -16.08838 1
MTRIX2 5 -0.888050 0.400360 -0.226020 44.64824 1
MTRIX3 5 0.216240 -0.070130 -0.973820 221.62483 1
MTRIX1 6 -0.634160 -0.772970 -0.018720 25.02280 1
MTRIX2 6 0.773200 -0.633920 -0.017710 39.55009 1
MTRIX3 6 0.001820 -0.025710 0.999670 63.28213 1
MTRIX1 7 -0.440420 0.829730 0.342890 -46.21931 1
MTRIX2 7 -0.897510 -0.416540 -0.144840 49.49619 1
MTRIX3 7 0.022650 -0.371530 0.928140 134.70387 1
(ATOM LINES ARE NOT SHOWN.)
END
