HEADER GROWTH FACTOR 13-JUL-93 1AFC
TITLE STRUCTURAL STUDIES OF THE BINDING OF THE ANTI-ULCER DRUG SUCROSE
TITLE 2 OCTASULFATE TO ACIDIC FIBROBLAST GROWTH FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACIDIC FIBROBLAST GROWTH FACTOR;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GROWTH FACTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR X.ZHU,B.T.HSU,D.C.REES
REVDAT 4 07-FEB-24 1AFC 1 HETSYN
REVDAT 3 29-JUL-20 1AFC 1 COMPND REMARK SEQADV HET
REVDAT 3 2 1 HETNAM FORMUL LINK SITE
REVDAT 3 3 1 ATOM
REVDAT 2 24-FEB-09 1AFC 1 VERSN
REVDAT 1 31-OCT-93 1AFC 0
JRNL AUTH X.ZHU,B.T.HSU,D.C.REES
JRNL TITL STRUCTURAL STUDIES OF THE BINDING OF THE ANTI-ULCER DRUG
JRNL TITL 2 SUCROSE OCTASULFATE TO ACIDIC FIBROBLAST GROWTH FACTOR.
JRNL REF STRUCTURE V. 1 27 1993
JRNL REFN ISSN 0969-2126
JRNL PMID 7520817
JRNL DOI 10.1016/0969-2126(93)90006-3
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. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.204
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 : 7864
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 440
REMARK 3 SOLVENT ATOMS : 0
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) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 2.700
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 1AFC 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_1000170746.
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) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 114.80000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 57.40000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 57.40000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 114.80000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8
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, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, J
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, K
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, L
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, M
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, N
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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, O
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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, P
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 PHE A 1
REMARK 465 ASN A 2
REMARK 465 LEU A 3
REMARK 465 PRO A 4
REMARK 465 LEU A 5
REMARK 465 GLY A 6
REMARK 465 ASN A 7
REMARK 465 TYR A 8
REMARK 465 LYS A 9
REMARK 465 VAL A 137
REMARK 465 SER A 138
REMARK 465 SER A 139
REMARK 465 ASP A 140
REMARK 465 PHE B 1
REMARK 465 ASN B 2
REMARK 465 LEU B 3
REMARK 465 PRO B 4
REMARK 465 LEU B 5
REMARK 465 GLY B 6
REMARK 465 ASN B 7
REMARK 465 TYR B 8
REMARK 465 LYS B 9
REMARK 465 VAL B 137
REMARK 465 SER B 138
REMARK 465 SER B 139
REMARK 465 ASP B 140
REMARK 465 PHE C 1
REMARK 465 ASN C 2
REMARK 465 LEU C 3
REMARK 465 PRO C 4
REMARK 465 LEU C 5
REMARK 465 GLY C 6
REMARK 465 ASN C 7
REMARK 465 TYR C 8
REMARK 465 LYS C 9
REMARK 465 VAL C 137
REMARK 465 SER C 138
REMARK 465 SER C 139
REMARK 465 ASP C 140
REMARK 465 PHE D 1
REMARK 465 ASN D 2
REMARK 465 LEU D 3
REMARK 465 PRO D 4
REMARK 465 LEU D 5
REMARK 465 GLY D 6
REMARK 465 ASN D 7
REMARK 465 TYR D 8
REMARK 465 LYS D 9
REMARK 465 VAL D 137
REMARK 465 SER D 138
REMARK 465 SER D 139
REMARK 465 ASP D 140
REMARK 465 PHE E 1
REMARK 465 ASN E 2
REMARK 465 LEU E 3
REMARK 465 PRO E 4
REMARK 465 LEU E 5
REMARK 465 GLY E 6
REMARK 465 ASN E 7
REMARK 465 TYR E 8
REMARK 465 LYS E 9
REMARK 465 VAL E 137
REMARK 465 SER E 138
REMARK 465 SER E 139
REMARK 465 ASP E 140
REMARK 465 PHE F 1
REMARK 465 ASN F 2
REMARK 465 LEU F 3
REMARK 465 PRO F 4
REMARK 465 LEU F 5
REMARK 465 GLY F 6
REMARK 465 ASN F 7
REMARK 465 TYR F 8
REMARK 465 LYS F 9
REMARK 465 VAL F 137
REMARK 465 SER F 138
REMARK 465 SER F 139
REMARK 465 ASP F 140
REMARK 465 PHE G 1
REMARK 465 ASN G 2
REMARK 465 LEU G 3
REMARK 465 PRO G 4
REMARK 465 LEU G 5
REMARK 465 GLY G 6
REMARK 465 ASN G 7
REMARK 465 TYR G 8
REMARK 465 LYS G 9
REMARK 465 VAL G 137
REMARK 465 SER G 138
REMARK 465 SER G 139
REMARK 465 ASP G 140
REMARK 465 PHE H 1
REMARK 465 ASN H 2
REMARK 465 LEU H 3
REMARK 465 PRO H 4
REMARK 465 LEU H 5
REMARK 465 GLY H 6
REMARK 465 ASN H 7
REMARK 465 TYR H 8
REMARK 465 LYS H 9
REMARK 465 VAL H 137
REMARK 465 SER H 138
REMARK 465 SER H 139
REMARK 465 ASP H 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 10 CG CD CE NZ
REMARK 470 GLN A 40 CG CD OE1 NE2
REMARK 470 GLN A 45 CG CD OE1 NE2
REMARK 470 SER A 50 OG
REMARK 470 ILE A 51 CG1 CG2 CD1
REMARK 470 GLU A 81 CG CD OE1 OE2
REMARK 470 ARG A 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 91 CG CD OE1 OE2
REMARK 470 LYS A 113 CG CD CE NZ
REMARK 470 LYS B 10 CG CD CE NZ
REMARK 470 GLN B 40 CG CD OE1 NE2
REMARK 470 GLN B 45 CG CD OE1 NE2
REMARK 470 SER B 50 OG
REMARK 470 ILE B 51 CG1 CG2 CD1
REMARK 470 GLU B 81 CG CD OE1 OE2
REMARK 470 ARG B 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 91 CG CD OE1 OE2
REMARK 470 LYS B 113 CG CD CE NZ
REMARK 470 LYS C 10 CG CD CE NZ
REMARK 470 GLN C 40 CG CD OE1 NE2
REMARK 470 GLN C 45 CG CD OE1 NE2
REMARK 470 SER C 50 OG
REMARK 470 ILE C 51 CG1 CG2 CD1
REMARK 470 GLU C 81 CG CD OE1 OE2
REMARK 470 ARG C 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 91 CG CD OE1 OE2
REMARK 470 LYS C 113 CG CD CE NZ
REMARK 470 LYS D 10 CG CD CE NZ
REMARK 470 GLN D 40 CG CD OE1 NE2
REMARK 470 GLN D 45 CG CD OE1 NE2
REMARK 470 SER D 50 OG
REMARK 470 ILE D 51 CG1 CG2 CD1
REMARK 470 GLU D 81 CG CD OE1 OE2
REMARK 470 ARG D 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 91 CG CD OE1 OE2
REMARK 470 LYS D 113 CG CD CE NZ
REMARK 470 LYS E 10 CG CD CE NZ
REMARK 470 GLN E 40 CG CD OE1 NE2
REMARK 470 GLN E 45 CG CD OE1 NE2
REMARK 470 SER E 50 OG
REMARK 470 ILE E 51 CG1 CG2 CD1
REMARK 470 GLU E 81 CG CD OE1 OE2
REMARK 470 ARG E 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 91 CG CD OE1 OE2
REMARK 470 LYS E 113 CG CD CE NZ
REMARK 470 LYS F 10 CG CD CE NZ
REMARK 470 GLN F 40 CG CD OE1 NE2
REMARK 470 GLN F 45 CG CD OE1 NE2
REMARK 470 SER F 50 OG
REMARK 470 ILE F 51 CG1 CG2 CD1
REMARK 470 GLU F 81 CG CD OE1 OE2
REMARK 470 ARG F 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 91 CG CD OE1 OE2
REMARK 470 LYS F 113 CG CD CE NZ
REMARK 470 LYS G 10 CG CD CE NZ
REMARK 470 GLN G 40 CG CD OE1 NE2
REMARK 470 GLN G 45 CG CD OE1 NE2
REMARK 470 SER G 50 OG
REMARK 470 ILE G 51 CG1 CG2 CD1
REMARK 470 GLU G 81 CG CD OE1 OE2
REMARK 470 ARG G 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 91 CG CD OE1 OE2
REMARK 470 LYS G 113 CG CD CE NZ
REMARK 470 LYS H 10 CG CD CE NZ
REMARK 470 GLN H 40 CG CD OE1 NE2
REMARK 470 GLN H 45 CG CD OE1 NE2
REMARK 470 SER H 50 OG
REMARK 470 ILE H 51 CG1 CG2 CD1
REMARK 470 GLU H 81 CG CD OE1 OE2
REMARK 470 ARG H 88 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 91 CG CD OE1 OE2
REMARK 470 LYS H 113 CG CD CE NZ
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 O6 GU4 N 1 O1S6 YYJ N 2 2.02
REMARK 500 O11 GU4 K 1 O1S1 YYJ K 2 2.04
REMARK 500 O23 GU4 N 1 O2S6 YYJ N 2 2.05
REMARK 500 O11 GU4 M 1 O1S3 YYJ M 2 2.13
REMARK 500 OG1 THR G 61 NE2 GLN G 63 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 HIS A 93 NE2 HIS A 93 CD2 -0.067
REMARK 500 HIS B 41 NE2 HIS B 41 CD2 -0.074
REMARK 500 HIS B 106 NE2 HIS B 106 CD2 -0.073
REMARK 500 HIS D 106 NE2 HIS D 106 CD2 -0.074
REMARK 500 HIS E 102 NE2 HIS E 102 CD2 -0.070
REMARK 500 HIS E 106 NE2 HIS E 106 CD2 -0.078
REMARK 500 HIS F 106 NE2 HIS F 106 CD2 -0.075
REMARK 500 HIS G 106 NE2 HIS G 106 CD2 -0.070
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 TYR A 21 O - C - N ANGL. DEV. = -11.8 DEGREES
REMARK 500 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 TRP A 107 CD1 - CG - CD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 TRP A 107 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 PHE A 125 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 TRP B 107 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP B 107 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG B 122 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 GLY C 19 C - N - CA ANGL. DEV. = -13.5 DEGREES
REMARK 500 ARG C 24 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP C 32 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP C 107 CD1 - CG - CD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 TRP C 107 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG D 24 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG D 37 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ASP D 39 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP D 107 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP D 107 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG D 116 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG D 122 CD - NE - CZ ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG E 24 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG E 24 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG E 37 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 TRP E 107 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP E 107 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 PRO E 136 C - N - CD ANGL. DEV. = -14.4 DEGREES
REMARK 500 ARG F 24 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 TRP F 107 CD1 - CG - CD2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 TRP F 107 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 TRP F 107 CE2 - CD2 - CG ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG F 122 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 TYR G 55 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 TRP G 107 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP G 107 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 TRP H 107 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP H 107 CE2 - CD2 - CG ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG H 122 NE - CZ - NH1 ANGL. DEV. = -4.3 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 18 -93.65 -28.17
REMARK 500 ASP A 36 73.65 -114.31
REMARK 500 ARG A 37 -29.25 -37.59
REMARK 500 SER A 38 38.70 -87.39
REMARK 500 THR A 69 20.46 -75.01
REMARK 500 GLU A 81 -36.32 -23.15
REMARK 500 GLU A 82 34.75 -87.56
REMARK 500 ARG A 88 102.82 -161.64
REMARK 500 HIS A 93 35.03 72.81
REMARK 500 THR A 96 108.33 -171.29
REMARK 500 HIS A 102 50.49 -114.63
REMARK 500 GLU A 104 -50.47 -26.97
REMARK 500 HIS A 106 46.53 76.43
REMARK 500 ARG A 122 10.84 -142.81
REMARK 500 LEU B 14 82.88 -69.89
REMARK 500 ASN B 18 -124.74 -48.85
REMARK 500 LEU B 23 134.54 -36.13
REMARK 500 ILE B 25 79.55 -115.23
REMARK 500 ASP B 68 -172.74 -24.59
REMARK 500 GLU B 81 -22.70 -36.59
REMARK 500 CYS B 83 32.60 -84.84
REMARK 500 HIS B 93 31.38 90.64
REMARK 500 PHE B 108 -169.46 -105.36
REMARK 500 LYS B 113 -0.63 -57.08
REMARK 500 LYS C 12 -165.21 -105.28
REMARK 500 ASN C 18 -78.99 -67.87
REMARK 500 PRO C 27 -31.42 -39.70
REMARK 500 ASP C 32 -167.53 -122.53
REMARK 500 ALA C 48 45.72 -97.67
REMARK 500 ILE C 51 72.69 -66.87
REMARK 500 GLU C 60 -71.24 -93.35
REMARK 500 ASP C 68 -176.75 -58.06
REMARK 500 GLN C 77 54.47 -93.44
REMARK 500 THR C 78 137.88 177.20
REMARK 500 GLU C 81 -18.96 -41.37
REMARK 500 HIS C 102 51.34 -109.26
REMARK 500 LYS C 113 -17.28 -49.19
REMARK 500 ASN D 18 -121.72 -50.15
REMARK 500 GLU D 49 79.07 -118.53
REMARK 500 SER D 50 -172.42 120.40
REMARK 500 GLU D 60 -52.47 -24.81
REMARK 500 PRO D 79 170.43 -53.88
REMARK 500 ASN D 80 -164.44 -166.30
REMARK 500 GLU D 87 -162.19 -78.73
REMARK 500 ARG D 88 105.54 163.68
REMARK 500 LEU D 89 173.65 -56.82
REMARK 500 HIS D 93 7.76 90.78
REMARK 500 HIS D 102 30.90 -142.16
REMARK 500 THR D 123 -168.78 -65.95
REMARK 500 HIS D 124 159.03 145.96
REMARK 500
REMARK 500 THIS ENTRY HAS 120 RAMACHANDRAN OUTLIERS.
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 TYR A 15 0.11 SIDE CHAIN
REMARK 500 ARG A 24 0.07 SIDE CHAIN
REMARK 500 ASP A 39 0.11 SIDE CHAIN
REMARK 500 TYR A 55 0.06 SIDE CHAIN
REMARK 500 TYR A 74 0.14 SIDE CHAIN
REMARK 500 TYR A 97 0.08 SIDE CHAIN
REMARK 500 PHE A 125 0.15 SIDE CHAIN
REMARK 500 ARG B 24 0.08 SIDE CHAIN
REMARK 500 ASP B 39 0.09 SIDE CHAIN
REMARK 500 TYR B 55 0.07 SIDE CHAIN
REMARK 500 ASP B 68 0.09 SIDE CHAIN
REMARK 500 ASP B 70 0.08 SIDE CHAIN
REMARK 500 TYR B 74 0.08 SIDE CHAIN
REMARK 500 PHE B 85 0.08 SIDE CHAIN
REMARK 500 GLU B 87 0.07 SIDE CHAIN
REMARK 500 HIS B 93 0.15 SIDE CHAIN
REMARK 500 ARG B 122 0.09 SIDE CHAIN
REMARK 500 TYR C 15 0.06 SIDE CHAIN
REMARK 500 TYR C 21 0.06 SIDE CHAIN
REMARK 500 ASP C 32 0.07 SIDE CHAIN
REMARK 500 ASP C 36 0.11 SIDE CHAIN
REMARK 500 ASP C 39 0.09 SIDE CHAIN
REMARK 500 ASP C 68 0.08 SIDE CHAIN
REMARK 500 TYR C 74 0.09 SIDE CHAIN
REMARK 500 PHE C 85 0.10 SIDE CHAIN
REMARK 500 TYR C 97 0.11 SIDE CHAIN
REMARK 500 PHE C 108 0.08 SIDE CHAIN
REMARK 500 ARG C 116 0.10 SIDE CHAIN
REMARK 500 ARG D 24 0.08 SIDE CHAIN
REMARK 500 ASP D 36 0.09 SIDE CHAIN
REMARK 500 ARG D 37 0.07 SIDE CHAIN
REMARK 500 GLU D 53 0.10 SIDE CHAIN
REMARK 500 PHE D 64 0.10 SIDE CHAIN
REMARK 500 ASP D 70 0.07 SIDE CHAIN
REMARK 500 GLU D 87 0.07 SIDE CHAIN
REMARK 500 TYR D 97 0.11 SIDE CHAIN
REMARK 500 ARG D 122 0.08 SIDE CHAIN
REMARK 500 HIS D 124 0.09 SIDE CHAIN
REMARK 500 ASP E 32 0.07 SIDE CHAIN
REMARK 500 ARG E 37 0.08 SIDE CHAIN
REMARK 500 PHE E 85 0.10 SIDE CHAIN
REMARK 500 GLU E 87 0.07 SIDE CHAIN
REMARK 500 HIS E 93 0.14 SIDE CHAIN
REMARK 500 TYR E 97 0.12 SIDE CHAIN
REMARK 500 GLU E 104 0.08 SIDE CHAIN
REMARK 500 TYR F 15 0.07 SIDE CHAIN
REMARK 500 PHE F 22 0.13 SIDE CHAIN
REMARK 500 ASP F 32 0.07 SIDE CHAIN
REMARK 500 TYR F 55 0.18 SIDE CHAIN
REMARK 500 ASP F 70 0.09 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 68 PLANE DEVIATIONS.
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 LYS A 10 11.76
REMARK 500 PRO A 11 -15.58
REMARK 500 LYS A 12 18.83
REMARK 500 LEU A 14 -13.26
REMARK 500 CYS A 16 -10.78
REMARK 500 ASN A 18 13.70
REMARK 500 GLY A 20 -14.20
REMARK 500 TYR A 21 -24.77
REMARK 500 PHE A 22 12.65
REMARK 500 ARG A 24 10.44
REMARK 500 ASP A 28 16.82
REMARK 500 THR A 30 17.84
REMARK 500 VAL A 31 -11.33
REMARK 500 GLY A 33 10.10
REMARK 500 LYS A 35 -13.86
REMARK 500 ASP A 36 19.13
REMARK 500 SER A 38 10.12
REMARK 500 ASP A 39 18.35
REMARK 500 HIS A 41 15.16
REMARK 500 ILE A 42 -13.46
REMARK 500 GLN A 43 -15.08
REMARK 500 GLN A 45 12.72
REMARK 500 LEU A 46 -10.62
REMARK 500 ALA A 47 -11.93
REMARK 500 ALA A 48 13.35
REMARK 500 GLU A 49 10.66
REMARK 500 SER A 50 14.17
REMARK 500 ILE A 51 -11.27
REMARK 500 GLU A 53 -21.86
REMARK 500 VAL A 54 -11.17
REMARK 500 TYR A 55 15.09
REMARK 500 ILE A 56 -10.11
REMARK 500 SER A 58 11.27
REMARK 500 THR A 59 -18.18
REMARK 500 GLU A 60 10.50
REMARK 500 THR A 61 11.87
REMARK 500 GLN A 63 -13.54
REMARK 500 PHE A 64 -14.64
REMARK 500 LEU A 65 10.28
REMARK 500 ALA A 66 15.66
REMARK 500 MET A 67 14.61
REMARK 500 THR A 69 -10.68
REMARK 500 ASP A 70 -13.35
REMARK 500 GLY A 71 -15.08
REMARK 500 LEU A 73 21.49
REMARK 500 TYR A 74 14.19
REMARK 500 SER A 76 -14.67
REMARK 500 GLN A 77 16.98
REMARK 500 PRO A 79 21.15
REMARK 500 ASN A 80 14.82
REMARK 500
REMARK 500 THIS ENTRY HAS 552 MAIN CHAIN PLANARITY DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AFC A 1 140 UNP P03968 FGF1_BOVIN 16 155
DBREF 1AFC B 1 140 UNP P03968 FGF1_BOVIN 16 155
DBREF 1AFC C 1 140 UNP P03968 FGF1_BOVIN 16 155
DBREF 1AFC D 1 140 UNP P03968 FGF1_BOVIN 16 155
DBREF 1AFC E 1 140 UNP P03968 FGF1_BOVIN 16 155
DBREF 1AFC F 1 140 UNP P03968 FGF1_BOVIN 16 155
DBREF 1AFC G 1 140 UNP P03968 FGF1_BOVIN 16 155
DBREF 1AFC H 1 140 UNP P03968 FGF1_BOVIN 16 155
SEQADV 1AFC ALA A 47 UNP P03968 CYS 62 CONFLICT
SEQADV 1AFC ALA B 47 UNP P03968 CYS 62 CONFLICT
SEQADV 1AFC ALA C 47 UNP P03968 CYS 62 CONFLICT
SEQADV 1AFC ALA D 47 UNP P03968 CYS 62 CONFLICT
SEQADV 1AFC ALA E 47 UNP P03968 CYS 62 CONFLICT
SEQADV 1AFC ALA F 47 UNP P03968 CYS 62 CONFLICT
SEQADV 1AFC ALA G 47 UNP P03968 CYS 62 CONFLICT
SEQADV 1AFC ALA H 47 UNP P03968 CYS 62 CONFLICT
SEQRES 1 A 140 PHE ASN LEU PRO LEU GLY ASN TYR LYS LYS PRO LYS LEU
SEQRES 2 A 140 LEU TYR CYS SER ASN GLY GLY TYR PHE LEU ARG ILE LEU
SEQRES 3 A 140 PRO ASP GLY THR VAL ASP GLY THR LYS ASP ARG SER ASP
SEQRES 4 A 140 GLN HIS ILE GLN LEU GLN LEU ALA ALA GLU SER ILE GLY
SEQRES 5 A 140 GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN PHE LEU
SEQRES 6 A 140 ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN THR
SEQRES 7 A 140 PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU GLU
SEQRES 8 A 140 ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA GLU
SEQRES 9 A 140 LYS HIS TRP PHE VAL GLY LEU LYS LYS ASN GLY ARG SER
SEQRES 10 A 140 LYS LEU GLY PRO ARG THR HIS PHE GLY GLN LYS ALA ILE
SEQRES 11 A 140 LEU PHE LEU PRO LEU PRO VAL SER SER ASP
SEQRES 1 B 140 PHE ASN LEU PRO LEU GLY ASN TYR LYS LYS PRO LYS LEU
SEQRES 2 B 140 LEU TYR CYS SER ASN GLY GLY TYR PHE LEU ARG ILE LEU
SEQRES 3 B 140 PRO ASP GLY THR VAL ASP GLY THR LYS ASP ARG SER ASP
SEQRES 4 B 140 GLN HIS ILE GLN LEU GLN LEU ALA ALA GLU SER ILE GLY
SEQRES 5 B 140 GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN PHE LEU
SEQRES 6 B 140 ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN THR
SEQRES 7 B 140 PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU GLU
SEQRES 8 B 140 ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA GLU
SEQRES 9 B 140 LYS HIS TRP PHE VAL GLY LEU LYS LYS ASN GLY ARG SER
SEQRES 10 B 140 LYS LEU GLY PRO ARG THR HIS PHE GLY GLN LYS ALA ILE
SEQRES 11 B 140 LEU PHE LEU PRO LEU PRO VAL SER SER ASP
SEQRES 1 C 140 PHE ASN LEU PRO LEU GLY ASN TYR LYS LYS PRO LYS LEU
SEQRES 2 C 140 LEU TYR CYS SER ASN GLY GLY TYR PHE LEU ARG ILE LEU
SEQRES 3 C 140 PRO ASP GLY THR VAL ASP GLY THR LYS ASP ARG SER ASP
SEQRES 4 C 140 GLN HIS ILE GLN LEU GLN LEU ALA ALA GLU SER ILE GLY
SEQRES 5 C 140 GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN PHE LEU
SEQRES 6 C 140 ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN THR
SEQRES 7 C 140 PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU GLU
SEQRES 8 C 140 ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA GLU
SEQRES 9 C 140 LYS HIS TRP PHE VAL GLY LEU LYS LYS ASN GLY ARG SER
SEQRES 10 C 140 LYS LEU GLY PRO ARG THR HIS PHE GLY GLN LYS ALA ILE
SEQRES 11 C 140 LEU PHE LEU PRO LEU PRO VAL SER SER ASP
SEQRES 1 D 140 PHE ASN LEU PRO LEU GLY ASN TYR LYS LYS PRO LYS LEU
SEQRES 2 D 140 LEU TYR CYS SER ASN GLY GLY TYR PHE LEU ARG ILE LEU
SEQRES 3 D 140 PRO ASP GLY THR VAL ASP GLY THR LYS ASP ARG SER ASP
SEQRES 4 D 140 GLN HIS ILE GLN LEU GLN LEU ALA ALA GLU SER ILE GLY
SEQRES 5 D 140 GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN PHE LEU
SEQRES 6 D 140 ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN THR
SEQRES 7 D 140 PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU GLU
SEQRES 8 D 140 ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA GLU
SEQRES 9 D 140 LYS HIS TRP PHE VAL GLY LEU LYS LYS ASN GLY ARG SER
SEQRES 10 D 140 LYS LEU GLY PRO ARG THR HIS PHE GLY GLN LYS ALA ILE
SEQRES 11 D 140 LEU PHE LEU PRO LEU PRO VAL SER SER ASP
SEQRES 1 E 140 PHE ASN LEU PRO LEU GLY ASN TYR LYS LYS PRO LYS LEU
SEQRES 2 E 140 LEU TYR CYS SER ASN GLY GLY TYR PHE LEU ARG ILE LEU
SEQRES 3 E 140 PRO ASP GLY THR VAL ASP GLY THR LYS ASP ARG SER ASP
SEQRES 4 E 140 GLN HIS ILE GLN LEU GLN LEU ALA ALA GLU SER ILE GLY
SEQRES 5 E 140 GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN PHE LEU
SEQRES 6 E 140 ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN THR
SEQRES 7 E 140 PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU GLU
SEQRES 8 E 140 ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA GLU
SEQRES 9 E 140 LYS HIS TRP PHE VAL GLY LEU LYS LYS ASN GLY ARG SER
SEQRES 10 E 140 LYS LEU GLY PRO ARG THR HIS PHE GLY GLN LYS ALA ILE
SEQRES 11 E 140 LEU PHE LEU PRO LEU PRO VAL SER SER ASP
SEQRES 1 F 140 PHE ASN LEU PRO LEU GLY ASN TYR LYS LYS PRO LYS LEU
SEQRES 2 F 140 LEU TYR CYS SER ASN GLY GLY TYR PHE LEU ARG ILE LEU
SEQRES 3 F 140 PRO ASP GLY THR VAL ASP GLY THR LYS ASP ARG SER ASP
SEQRES 4 F 140 GLN HIS ILE GLN LEU GLN LEU ALA ALA GLU SER ILE GLY
SEQRES 5 F 140 GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN PHE LEU
SEQRES 6 F 140 ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN THR
SEQRES 7 F 140 PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU GLU
SEQRES 8 F 140 ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA GLU
SEQRES 9 F 140 LYS HIS TRP PHE VAL GLY LEU LYS LYS ASN GLY ARG SER
SEQRES 10 F 140 LYS LEU GLY PRO ARG THR HIS PHE GLY GLN LYS ALA ILE
SEQRES 11 F 140 LEU PHE LEU PRO LEU PRO VAL SER SER ASP
SEQRES 1 G 140 PHE ASN LEU PRO LEU GLY ASN TYR LYS LYS PRO LYS LEU
SEQRES 2 G 140 LEU TYR CYS SER ASN GLY GLY TYR PHE LEU ARG ILE LEU
SEQRES 3 G 140 PRO ASP GLY THR VAL ASP GLY THR LYS ASP ARG SER ASP
SEQRES 4 G 140 GLN HIS ILE GLN LEU GLN LEU ALA ALA GLU SER ILE GLY
SEQRES 5 G 140 GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN PHE LEU
SEQRES 6 G 140 ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN THR
SEQRES 7 G 140 PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU GLU
SEQRES 8 G 140 ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA GLU
SEQRES 9 G 140 LYS HIS TRP PHE VAL GLY LEU LYS LYS ASN GLY ARG SER
SEQRES 10 G 140 LYS LEU GLY PRO ARG THR HIS PHE GLY GLN LYS ALA ILE
SEQRES 11 G 140 LEU PHE LEU PRO LEU PRO VAL SER SER ASP
SEQRES 1 H 140 PHE ASN LEU PRO LEU GLY ASN TYR LYS LYS PRO LYS LEU
SEQRES 2 H 140 LEU TYR CYS SER ASN GLY GLY TYR PHE LEU ARG ILE LEU
SEQRES 3 H 140 PRO ASP GLY THR VAL ASP GLY THR LYS ASP ARG SER ASP
SEQRES 4 H 140 GLN HIS ILE GLN LEU GLN LEU ALA ALA GLU SER ILE GLY
SEQRES 5 H 140 GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN PHE LEU
SEQRES 6 H 140 ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN THR
SEQRES 7 H 140 PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU GLU
SEQRES 8 H 140 ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA GLU
SEQRES 9 H 140 LYS HIS TRP PHE VAL GLY LEU LYS LYS ASN GLY ARG SER
SEQRES 10 H 140 LYS LEU GLY PRO ARG THR HIS PHE GLY GLN LYS ALA ILE
SEQRES 11 H 140 LEU PHE LEU PRO LEU PRO VAL SER SER ASP
HET GU4 I 1 27
HET YYJ I 2 28
HET GU4 J 1 27
HET YYJ J 2 28
HET GU4 K 1 27
HET YYJ K 2 28
HET GU4 L 1 27
HET YYJ L 2 28
HET GU4 M 1 27
HET YYJ M 2 28
HET GU4 N 1 27
HET YYJ N 2 28
HET GU4 O 1 27
HET YYJ O 2 28
HET GU4 P 1 27
HET YYJ P 2 28
HETNAM GU4 2,3,4,6-TETRA-O-SULFONATO-ALPHA-D-GLUCOPYRANOSE
HETNAM YYJ 1,3,4,6-TETRA-O-SULFO-BETA-D-FRUCTOFURANOSE
HETSYN GU4 2,3,4,6-TETRA-O-SULFONATO-ALPHA-D-GLUCOSE; 2,3,4,6-
HETSYN 2 GU4 TETRA-O-SULFONATO-D-GLUCOSE; 2,3,4,6-TETRA-O-
HETSYN 3 GU4 SULFONATO-GLUCOSE
FORMUL 9 GU4 8(C6 H12 O18 S4)
FORMUL 9 YYJ 8(C6 H12 O18 S4)
HELIX 1 1 ASP A 39 ILE A 42 5 4
HELIX 2 2 ASN A 80 LEU A 84 5 5
HELIX 3 3 GLY A 120 THR A 123 5 4
HELIX 4 4 LYS B 101 ALA B 103 5 3
HELIX 5 5 LEU B 119 THR B 123 5 5
HELIX 6 6 ASN C 80 CYS C 83 5 4
HELIX 7 7 GLY C 120 THR C 123 5 4
HELIX 8 8 LEU D 119 THR D 123 5 5
HELIX 9 9 ASN E 80 CYS E 83 5 4
HELIX 10 10 GLY E 120 THR E 123 5 4
HELIX 11 11 ASP F 39 ILE F 42 5 4
HELIX 12 12 ASN F 80 CYS F 83 5 4
HELIX 13 13 LEU F 119 THR F 123 5 5
HELIX 14 14 ASP G 39 ILE G 42 5 4
HELIX 15 15 ASN G 80 CYS G 83 5 4
HELIX 16 16 LEU G 119 THR G 123 5 5
HELIX 17 17 ASP H 39 ILE H 42 5 4
HELIX 18 18 ASN H 80 LEU H 84 5 5
HELIX 19 19 GLY H 120 THR H 123 5 4
HELIX 20 20 GLN H 127 ILE H 130 5 4
SHEET 1 A 2 LEU A 13 CYS A 16 0
SHEET 2 A 2 PHE A 132 LEU A 135 -1 N LEU A 133 O TYR A 15
SHEET 1 B 2 PHE A 22 ILE A 25 0
SHEET 2 B 2 VAL A 31 THR A 34 -1 O ASP A 32 N ARG A 24
SHEET 1 C 2 LEU A 44 LEU A 46 0
SHEET 2 C 2 ILE A 56 SER A 58 -1 N LYS A 57 O GLN A 45
SHEET 1 D 2 PHE A 64 MET A 67 0
SHEET 2 D 2 LEU A 73 SER A 76 -1 O TYR A 74 N ALA A 66
SHEET 1 E 2 ARG A 88 LEU A 89 0
SHEET 2 E 2 ASN A 95 THR A 96 -1 O THR A 96 N ARG A 88
SHEET 1 F 7 LYS B 12 CYS B 16 0
SHEET 2 F 7 GLN B 43 SER B 50 -1 N LEU B 44 O LYS B 12
SHEET 3 F 7 GLU B 53 SER B 58 -1 N GLU B 53 O SER B 50
SHEET 4 F 7 PHE B 85 LEU B 89 -1 N PHE B 85 O VAL B 54
SHEET 5 F 7 ASN B 95 SER B 99 -1 O THR B 96 N ARG B 88
SHEET 6 F 7 PHE B 132 LEU B 135 -1 O PHE B 132 N ASN B 95
SHEET 7 F 7 LYS B 12 CYS B 16 -1 O LEU B 13 N LEU B 135
SHEET 1 G 2 ARG B 24 LEU B 26 0
SHEET 2 G 2 THR B 30 ASP B 32 -1 O THR B 30 N LEU B 26
SHEET 1 H 2 PHE B 64 MET B 67 0
SHEET 2 H 2 LEU B 73 SER B 76 -1 N TYR B 74 O ALA B 66
SHEET 1 I 7 GLU C 53 VAL C 54 0
SHEET 2 I 7 PHE C 85 GLU C 87 -1 O PHE C 85 N VAL C 54
SHEET 3 I 7 ASN C 95 SER C 99 -1 O ILE C 98 N LEU C 86
SHEET 4 I 7 LEU C 131 LEU C 135 -1 O PHE C 132 N ASN C 95
SHEET 5 I 7 LYS C 12 CYS C 16 -1 O LEU C 13 N LEU C 135
SHEET 6 I 7 GLN C 43 GLN C 45 -1 O LEU C 44 N LYS C 12
SHEET 7 I 7 LYS C 57 SER C 58 -1 N LYS C 57 O GLN C 45
SHEET 1 J 2 PHE C 22 ILE C 25 0
SHEET 2 J 2 VAL C 31 THR C 34 -1 O ASP C 32 N ARG C 24
SHEET 1 K 2 PHE C 64 MET C 67 0
SHEET 2 K 2 LEU C 73 SER C 76 -1 N TYR C 74 O ALA C 66
SHEET 1 L 2 LEU D 13 LEU D 14 0
SHEET 2 L 2 PRO D 134 LEU D 135 -1 O LEU D 135 N LEU D 13
SHEET 1 M 2 PHE D 22 LEU D 26 0
SHEET 2 M 2 THR D 30 THR D 34 -1 O THR D 30 N LEU D 26
SHEET 1 N 4 LEU D 44 ALA D 47 0
SHEET 2 N 4 GLU D 53 SER D 58 -1 O TYR D 55 N ALA D 47
SHEET 3 N 4 PHE D 85 LEU D 86 -1 N PHE D 85 O VAL D 54
SHEET 4 N 4 ILE D 98 SER D 99 -1 O ILE D 98 N LEU D 86
SHEET 1 O 2 PHE D 64 MET D 67 0
SHEET 2 O 2 LEU D 73 SER D 76 -1 O TYR D 74 N ALA D 66
SHEET 1 P 4 THR E 30 THR E 34 0
SHEET 2 P 4 TYR E 21 LEU E 26 -1 N PHE E 22 O THR E 34
SHEET 3 P 4 LEU E 13 CYS E 16 -1 O LEU E 14 N LEU E 23
SHEET 4 P 4 PHE E 132 LEU E 135 -1 N LEU E 133 O TYR E 15
SHEET 1 Q 2 LEU E 44 LEU E 46 0
SHEET 2 Q 2 ILE E 56 SER E 58 -1 N LYS E 57 O GLN E 45
SHEET 1 R 2 PHE E 64 MET E 67 0
SHEET 2 R 2 LEU E 73 SER E 76 -1 N TYR E 74 O ALA E 66
SHEET 1 S 2 PHE E 85 GLU E 87 0
SHEET 2 S 2 TYR E 97 SER E 99 -1 O ILE E 98 N LEU E 86
SHEET 1 T 2 LEU F 13 CYS F 16 0
SHEET 2 T 2 PHE F 132 LEU F 135 -1 N LEU F 133 O TYR F 15
SHEET 1 U 2 PHE F 22 ILE F 25 0
SHEET 2 U 2 VAL F 31 THR F 34 -1 O ASP F 32 N ARG F 24
SHEET 1 V 2 LEU F 44 GLN F 45 0
SHEET 2 V 2 LYS F 57 SER F 58 -1 O LYS F 57 N GLN F 45
SHEET 1 W 2 PHE F 64 MET F 67 0
SHEET 2 W 2 LEU F 73 SER F 76 -1 O TYR F 74 N ALA F 66
SHEET 1 X 2 PHE F 85 GLU F 87 0
SHEET 2 X 2 TYR F 97 SER F 99 -1 O ILE F 98 N LEU F 86
SHEET 1 Y 2 LEU G 13 LEU G 14 0
SHEET 2 Y 2 PRO G 134 LEU G 135 -1 O LEU G 135 N LEU G 13
SHEET 1 Z 2 LEU G 23 ILE G 25 0
SHEET 2 Z 2 VAL G 31 GLY G 33 -1 O ASP G 32 N ARG G 24
SHEET 1 AA 2 LEU G 44 GLN G 45 0
SHEET 2 AA 2 LYS G 57 SER G 58 -1 O LYS G 57 N GLN G 45
SHEET 1 AB 2 PHE G 85 LEU G 86 0
SHEET 2 AB 2 ILE G 98 SER G 99 -1 O ILE G 98 N LEU G 86
SHEET 1 AC 2 LEU H 13 CYS H 16 0
SHEET 2 AC 2 PHE H 132 LEU H 135 -1 N LEU H 133 O TYR H 15
SHEET 1 AD 2 PHE H 22 ILE H 25 0
SHEET 2 AD 2 VAL H 31 THR H 34 -1 O ASP H 32 N ARG H 24
SHEET 1 AE 2 LEU H 44 LEU H 46 0
SHEET 2 AE 2 ILE H 56 SER H 58 -1 N LYS H 57 O GLN H 45
SHEET 1 AF 2 PHE H 64 MET H 67 0
SHEET 2 AF 2 LEU H 73 SER H 76 -1 O TYR H 74 N ALA H 66
LINK C1 GU4 I 1 O2 YYJ I 2 1555 1555 1.45
LINK C1 GU4 J 1 O2 YYJ J 2 1555 1555 1.42
LINK C1 GU4 K 1 O2 YYJ K 2 1555 1555 1.41
LINK C1 GU4 L 1 O2 YYJ L 2 1555 1555 1.44
LINK C1 GU4 M 1 O2 YYJ M 2 1555 1555 1.39
LINK C1 GU4 N 1 O2 YYJ N 2 1555 1555 1.42
LINK C1 GU4 O 1 O2 YYJ O 2 1555 1555 1.40
LINK C1 GU4 P 1 O2 YYJ P 2 1555 1555 1.44
CRYST1 110.600 110.600 172.200 90.00 90.00 120.00 P 32 2 1 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 0.009042 0.005220 0.000000 0.00000
SCALE2 0.000000 0.010440 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005807 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
