HEADER GROWTH FACTOR 12-DEC-95 1BFB
TITLE BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN TETRAMER
TITLE 2 FRAGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BASIC FIBROBLAST GROWTH FACTOR;
COMPND 3 CHAIN: A;
COMPND 4 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS GROWTH FACTOR, MITOGEN, VASCULARIZATION, HEPARIN-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.FAHAM,D.C.REES
REVDAT 6 07-FEB-24 1BFB 1 REMARK
REVDAT 5 03-NOV-21 1BFB 1 SEQADV HETSYN
REVDAT 4 29-JUL-20 1BFB 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 13-JUL-11 1BFB 1 VERSN
REVDAT 2 24-FEB-09 1BFB 1 VERSN
REVDAT 1 03-APR-96 1BFB 0
JRNL AUTH S.FAHAM,R.E.HILEMAN,J.R.FROMM,R.J.LINHARDT,D.C.REES
JRNL TITL HEPARIN STRUCTURE AND INTERACTIONS WITH BASIC FIBROBLAST
JRNL TITL 2 GROWTH FACTOR.
JRNL REF SCIENCE V. 271 1116 1996
JRNL REFN ISSN 0036-8075
JRNL PMID 8599088
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH X.ZHU,H.KOMIYA,A.CHIRINO,S.FAHAM,G.M.FOX,T.ARAKAWA,B.T.HSU,
REMARK 1 AUTH 2 D.C.REES
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURES OF ACIDIC AND BASIC FIBROBLAST
REMARK 1 TITL 2 GROWTH FACTORS
REMARK 1 REF SCIENCE V. 251 90 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 8437
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.206
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 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 991
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 9
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 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) : 0.140
REMARK 3 BOND ANGLES (DEGREES) : 2.350
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 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 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BFB 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_1000171687.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MSC
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9084
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 29.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 16.01000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.93500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.90000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.93500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.01000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 20.90000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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, 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 LEU A 1
REMARK 465 PRO A 2
REMARK 465 ALA A 3
REMARK 465 LEU A 4
REMARK 465 PRO A 5
REMARK 465 GLU A 6
REMARK 465 ASP A 7
REMARK 465 GLY A 8
REMARK 465 GLY A 9
REMARK 465 SER A 10
REMARK 465 GLY A 11
REMARK 465 ALA A 12
REMARK 465 PHE A 13
REMARK 465 PRO A 14
REMARK 465 PRO A 15
REMARK 465 GLY A 16
REMARK 465 HIS A 17
REMARK 465 PHE A 18
REMARK 465 LYS A 19
REMARK 465 ASP A 20
REMARK 465 ALA A 145
REMARK 465 LYS A 146
REMARK 465 SER A 147
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 ARG A 61 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 79 CG CD OE1 OE2
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 ARG A 23 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 TYR A 25 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 34 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP A 38 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 40 CG - CD - NE ANGL. DEV. = -19.4 DEGREES
REMARK 500 ARG A 40 NE - CZ - NH1 ANGL. DEV. = -17.7 DEGREES
REMARK 500 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 TYR A 74 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 TYR A 107 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 108 NE - CZ - NH2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 ARG A 110 NE - CZ - NH2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 TRP A 115 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP A 115 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 60 -175.83 -172.53
REMARK 500 ASP A 91 2.61 -64.49
REMARK 500 THR A 113 -6.93 -52.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 23 0.07 SIDE CHAIN
REMARK 500 ARG A 34 0.09 SIDE CHAIN
REMARK 500 ARG A 40 0.18 SIDE CHAIN
REMARK 500 ARG A 73 0.08 SIDE CHAIN
REMARK 500 ASP A 80 0.08 SIDE CHAIN
REMARK 500 ASP A 91 0.07 SIDE CHAIN
REMARK 500 GLU A 100 0.07 SIDE CHAIN
REMARK 500 TYR A 107 0.07 SIDE CHAIN
REMARK 500 ARG A 108 0.11 SIDE CHAIN
REMARK 500 ARG A 110 0.08 SIDE CHAIN
REMARK 500 TYR A 125 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 PRO A 21 15.87
REMARK 500 LYS A 22 -12.88
REMARK 500 ARG A 23 16.83
REMARK 500 GLY A 29 13.83
REMARK 500 GLY A 30 13.91
REMARK 500 LEU A 33 -15.97
REMARK 500 ILE A 35 14.31
REMARK 500 PRO A 37 -10.09
REMARK 500 ASP A 38 15.22
REMARK 500 ARG A 40 12.18
REMARK 500 ASP A 42 10.13
REMARK 500 VAL A 44 -15.45
REMARK 500 LEU A 54 -12.48
REMARK 500 GLN A 55 15.35
REMARK 500 LEU A 56 11.40
REMARK 500 GLU A 59 22.76
REMARK 500 ARG A 61 16.09
REMARK 500 VAL A 64 11.30
REMARK 500 SER A 65 10.10
REMARK 500 GLY A 68 14.74
REMARK 500 SER A 70 11.11
REMARK 500 ALA A 71 -11.24
REMARK 500 ARG A 73 -10.58
REMARK 500 LYS A 78 -13.11
REMARK 500 ARG A 82 -13.01
REMARK 500 LEU A 84 12.95
REMARK 500 SER A 88 14.90
REMARK 500 VAL A 89 14.99
REMARK 500 ARG A 98 16.43
REMARK 500 TYR A 112 11.86
REMARK 500 GLY A 123 16.39
REMARK 500 GLN A 124 11.96
REMARK 500 TYR A 125 13.56
REMARK 500 LYS A 130 -13.27
REMARK 500 THR A 131 10.03
REMARK 500 GLY A 134 13.26
REMARK 500 ALA A 137 -12.07
REMARK 500 LEU A 141 14.79
REMARK 500 PRO A 142 13.56
REMARK 500 MET A 143 11.27
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BFB A 1 147 UNP P09038 FGF2_HUMAN 9 155
SEQADV 1BFB SER A 70 UNP P09038 CYS 78 ENGINEERED MUTATION
SEQADV 1BFB SER A 88 UNP P09038 CYS 96 ENGINEERED MUTATION
SEQRES 1 A 147 LEU PRO ALA LEU PRO GLU ASP GLY GLY SER GLY ALA PHE
SEQRES 2 A 147 PRO PRO GLY HIS PHE LYS ASP PRO LYS ARG LEU TYR CYS
SEQRES 3 A 147 LYS ASN GLY GLY PHE PHE LEU ARG ILE HIS PRO ASP GLY
SEQRES 4 A 147 ARG VAL ASP GLY VAL ARG GLU LYS SER ASP PRO HIS ILE
SEQRES 5 A 147 LYS LEU GLN LEU GLN ALA GLU GLU ARG GLY VAL VAL SER
SEQRES 6 A 147 ILE LYS GLY VAL SER ALA ASN ARG TYR LEU ALA MET LYS
SEQRES 7 A 147 GLU ASP GLY ARG LEU LEU ALA SER LYS SER VAL THR ASP
SEQRES 8 A 147 GLU CYS PHE PHE PHE GLU ARG LEU GLU SER ASN ASN TYR
SEQRES 9 A 147 ASN THR TYR ARG SER ARG LYS TYR THR SER TRP TYR VAL
SEQRES 10 A 147 ALA LEU LYS ARG THR GLY GLN TYR LYS LEU GLY SER LYS
SEQRES 11 A 147 THR GLY PRO GLY GLN LYS ALA ILE LEU PHE LEU PRO MET
SEQRES 12 A 147 SER ALA LYS SER
HET SGN B 1 20
HET IDS B 2 16
HET SGN B 3 19
HET UAP B 4 15
HETNAM SGN 2-DEOXY-6-O-SULFO-2-(SULFOAMINO)-ALPHA-D-GLUCOPYRANOSE
HETNAM IDS 2-O-SULFO-ALPHA-L-IDOPYRANURONIC ACID
HETNAM UAP 4-DEOXY-2-O-SULFO-ALPHA-L-THREO-HEX-4-ENOPYRANURONIC
HETNAM 2 UAP 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
HETSYN UAP 4-DEOXY-2-O-SULFO-ALPHA-L-THREO-HEX-4-ENURONIC ACID; 4-
HETSYN 2 UAP DEOXY-2-O-SULFO-L-THREO-HEX-4-ENURONIC ACID; 4-DEOXY-
HETSYN 3 UAP 2-O-SULFO-THREO-HEX-4-ENURONIC ACID
FORMUL 2 SGN 2(C6 H13 N O11 S2)
FORMUL 2 IDS C6 H10 O10 S
FORMUL 2 UAP C6 H8 O9 S
FORMUL 3 HOH *9(H2 O)
HELIX 1 1 PRO A 50 ILE A 52 5 3
HELIX 2 2 SER A 101 ASN A 103 5 3
HELIX 3 3 GLY A 128 LYS A 130 5 3
SHEET 1 A 2 ARG A 23 CYS A 26 0
SHEET 2 A 2 PHE A 140 MET A 143 -1 N MET A 143 O ARG A 23
SHEET 1 B 2 PHE A 32 ILE A 35 0
SHEET 2 B 2 VAL A 41 VAL A 44 -1 N VAL A 44 O PHE A 32
SHEET 1 C 2 TYR A 74 MET A 77 0
SHEET 2 C 2 LEU A 83 SER A 86 -1 N SER A 86 O TYR A 74
SHEET 1 D 2 PHE A 95 LEU A 99 0
SHEET 2 D 2 ASN A 105 SER A 109 -1 N ARG A 108 O PHE A 96
SHEET 1 E 2 LEU A 54 GLU A 60 0
SHEET 2 E 2 VAL A 63 GLY A 68 -1 N LYS A 67 O GLN A 55
LINK O4 SGN B 1 C1 IDS B 2 1555 1555 1.44
LINK O4 IDS B 2 C1 SGN B 3 1555 1555 1.40
LINK O4 SGN B 3 C1 UAP B 4 1555 1555 1.41
CRYST1 32.020 41.800 85.870 90.00 90.00 90.00 P 21 21 21 4
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 0.031230 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023923 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011646 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
