HEADER HEPARIN-BINDING PROTEIN 25-JUL-10 3O3Q
TITLE CRYSTAL STRUCTURE OF "L44F/M67I/L73V/A103G/DELETION 104-
TITLE 2 106/F108Y/V109L/L111I/C117V/R119G/DELETION 120-122" MUTANT FORM OF
TITLE 3 HUMAN ACIDIC FIBROBLAST GROWTH FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPARIN-BINDING GROWTH FACTOR 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: HBGF-1, ACIDIC FIBROBLAST GROWTH FACTOR, AFGF, BETA-
COMPND 5 ENDOTHELIAL CELL GROWTH FACTOR, ECGF-BETA;
COMPND 6 ENGINEERED: YES;
COMPND 7 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: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A(+)
KEYWDS BETA-TREFOIL, HEPARIN-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LEE,M.BLABER
REVDAT 4 06-SEP-23 3O3Q 1 REMARK SEQADV
REVDAT 3 17-JUL-19 3O3Q 1 REMARK
REVDAT 2 20-JUN-12 3O3Q 1 JRNL VERSN
REVDAT 1 23-FEB-11 3O3Q 0
JRNL AUTH J.LEE,S.I.BLABER,V.K.DUBEY,M.BLABER
JRNL TITL A POLYPEPTIDE "BUILDING BLOCK"TOP-DOWN SYMMETRIC
JRNL TITL 2 DECONSTRUCTION".
JRNL REF J.MOL.BIOL. V. 407 744 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21315087
JRNL DOI 10.1016/J.JMB.2011.02.002
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.070
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 66029
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3367
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 27.7167 - 3.4437 0.99 6741 363 0.1566 0.1703
REMARK 3 2 3.4437 - 2.7341 0.98 6691 362 0.1663 0.2003
REMARK 3 3 2.7341 - 2.3887 0.97 6659 323 0.1826 0.2182
REMARK 3 4 2.3887 - 2.1704 0.96 6547 335 0.1680 0.2121
REMARK 3 5 2.1704 - 2.0149 0.95 6431 379 0.1662 0.2129
REMARK 3 6 2.0149 - 1.8961 0.93 6272 341 0.1720 0.2084
REMARK 3 7 1.8961 - 1.8012 0.91 6234 337 0.1746 0.2120
REMARK 3 8 1.8012 - 1.7228 0.90 6092 312 0.1754 0.2343
REMARK 3 9 1.7228 - 1.6565 0.87 5934 324 0.1865 0.2299
REMARK 3 10 1.6565 - 1.6000 0.74 5061 291 0.1977 0.2386
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 : 0.36
REMARK 3 B_SOL : 43.87
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.040
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.64430
REMARK 3 B22 (A**2) : 0.97190
REMARK 3 B33 (A**2) : -2.61620
REMARK 3 B12 (A**2) : -0.87710
REMARK 3 B13 (A**2) : -1.84050
REMARK 3 B23 (A**2) : -0.95310
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 : 0.006 4084
REMARK 3 ANGLE : 1.006 5525
REMARK 3 CHIRALITY : 0.067 590
REMARK 3 PLANARITY : 0.005 712
REMARK 3 DIHEDRAL : 15.439 1475
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 3O3Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060626.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI MONOCHROMATOR
REMARK 200 OPTICS : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66029
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.34300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.860
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1JQZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM FORMATE, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 PHE A 1
REMARK 465 ASN A 2
REMARK 465 LEU A 3
REMARK 465 PRO A 4
REMARK 465 PRO A 5
REMARK 465 GLY A 6
REMARK 465 ASN A 7
REMARK 465 TYR A 8
REMARK 465 LYS A 9
REMARK 465 SER A 139
REMARK 465 ASP A 140
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 PHE B 1
REMARK 465 ASN B 2
REMARK 465 LEU B 3
REMARK 465 PRO B 4
REMARK 465 PRO B 5
REMARK 465 GLY B 6
REMARK 465 ASN B 7
REMARK 465 TYR B 8
REMARK 465 LYS B 9
REMARK 465 SER B 138
REMARK 465 SER B 139
REMARK 465 ASP B 140
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 PHE C 1
REMARK 465 ASN C 2
REMARK 465 LEU C 3
REMARK 465 PRO C 4
REMARK 465 PRO C 5
REMARK 465 GLY C 6
REMARK 465 ASN C 7
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
REMARK 465 PHE D 1
REMARK 465 ASN D 2
REMARK 465 LEU D 3
REMARK 465 PRO D 4
REMARK 465 PRO D 5
REMARK 465 GLY D 6
REMARK 465 ASN D 7
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 GLU C 91 CG CD OE1 OE2
REMARK 470 GLU D 91 CG CD OE1 OE2
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 HIS A 93 -9.63 86.49
REMARK 500 HIS B 93 -10.13 89.06
REMARK 500 GLU C 49 -76.99 -85.95
REMARK 500 GLU D 49 -81.91 -80.53
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 GOL B 141
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 141
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JQZ RELATED DB: PDB
REMARK 900 HUMAN ACIDIC FIBROBLAST GROWTH FACTOR. 141 AMINO ACID FORM WITH
REMARK 900 AMINO TERMINAL HIS TAG
REMARK 900 RELATED ID: 3O49 RELATED DB: PDB
REMARK 900 RELATED ID: 3O4A RELATED DB: PDB
REMARK 900 RELATED ID: 3O4B RELATED DB: PDB
REMARK 900 RELATED ID: 3O4C RELATED DB: PDB
REMARK 900 RELATED ID: 3O4D RELATED DB: PDB
REMARK 900 RELATED ID: 3O4E RELATED DB: PDB
DBREF 3O3Q A 1 140 UNP P05230 FGF1_HUMAN 16 155
DBREF 3O3Q B 1 140 UNP P05230 FGF1_HUMAN 16 155
DBREF 3O3Q C 1 140 UNP P05230 FGF1_HUMAN 16 155
DBREF 3O3Q D 1 140 UNP P05230 FGF1_HUMAN 16 155
SEQADV 3O3Q HIS A -5 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS A -4 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS A -3 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS A -2 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS A -1 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS A 0 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q PHE A 44 UNP P05230 LEU 59 ENGINEERED MUTATION
SEQADV 3O3Q ILE A 67 UNP P05230 MET 82 ENGINEERED MUTATION
SEQADV 3O3Q VAL A 73 UNP P05230 LEU 88 ENGINEERED MUTATION
SEQADV 3O3Q GLY A 103 UNP P05230 ALA 118 ENGINEERED MUTATION
SEQADV 3O3Q A UNP P05230 GLU 119 DELETION
SEQADV 3O3Q A UNP P05230 LYS 120 DELETION
SEQADV 3O3Q A UNP P05230 ASN 121 DELETION
SEQADV 3O3Q TYR A 108 UNP P05230 PHE 123 ENGINEERED MUTATION
SEQADV 3O3Q LEU A 109 UNP P05230 VAL 124 ENGINEERED MUTATION
SEQADV 3O3Q ILE A 111 UNP P05230 LEU 126 ENGINEERED MUTATION
SEQADV 3O3Q VAL A 117 UNP P05230 CYS 132 ENGINEERED MUTATION
SEQADV 3O3Q GLY A 119 UNP P05230 ARG 134 ENGINEERED MUTATION
SEQADV 3O3Q A UNP P05230 GLY 135 DELETION
SEQADV 3O3Q A UNP P05230 PRO 136 DELETION
SEQADV 3O3Q A UNP P05230 ARG 137 DELETION
SEQADV 3O3Q HIS B -5 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS B -4 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS B -3 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS B -2 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS B -1 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS B 0 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q PHE B 44 UNP P05230 LEU 59 ENGINEERED MUTATION
SEQADV 3O3Q ILE B 67 UNP P05230 MET 82 ENGINEERED MUTATION
SEQADV 3O3Q VAL B 73 UNP P05230 LEU 88 ENGINEERED MUTATION
SEQADV 3O3Q GLY B 103 UNP P05230 ALA 118 ENGINEERED MUTATION
SEQADV 3O3Q B UNP P05230 GLU 119 DELETION
SEQADV 3O3Q B UNP P05230 LYS 120 DELETION
SEQADV 3O3Q B UNP P05230 ASN 121 DELETION
SEQADV 3O3Q TYR B 108 UNP P05230 PHE 123 ENGINEERED MUTATION
SEQADV 3O3Q LEU B 109 UNP P05230 VAL 124 ENGINEERED MUTATION
SEQADV 3O3Q ILE B 111 UNP P05230 LEU 126 ENGINEERED MUTATION
SEQADV 3O3Q VAL B 117 UNP P05230 CYS 132 ENGINEERED MUTATION
SEQADV 3O3Q GLY B 119 UNP P05230 ARG 134 ENGINEERED MUTATION
SEQADV 3O3Q B UNP P05230 GLY 135 DELETION
SEQADV 3O3Q B UNP P05230 PRO 136 DELETION
SEQADV 3O3Q B UNP P05230 ARG 137 DELETION
SEQADV 3O3Q HIS C -5 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS C -4 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS C -3 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS C -2 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS C -1 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS C 0 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q PHE C 44 UNP P05230 LEU 59 ENGINEERED MUTATION
SEQADV 3O3Q ILE C 67 UNP P05230 MET 82 ENGINEERED MUTATION
SEQADV 3O3Q VAL C 73 UNP P05230 LEU 88 ENGINEERED MUTATION
SEQADV 3O3Q GLY C 103 UNP P05230 ALA 118 ENGINEERED MUTATION
SEQADV 3O3Q C UNP P05230 GLU 119 DELETION
SEQADV 3O3Q C UNP P05230 LYS 120 DELETION
SEQADV 3O3Q C UNP P05230 ASN 121 DELETION
SEQADV 3O3Q TYR C 108 UNP P05230 PHE 123 ENGINEERED MUTATION
SEQADV 3O3Q LEU C 109 UNP P05230 VAL 124 ENGINEERED MUTATION
SEQADV 3O3Q ILE C 111 UNP P05230 LEU 126 ENGINEERED MUTATION
SEQADV 3O3Q VAL C 117 UNP P05230 CYS 132 ENGINEERED MUTATION
SEQADV 3O3Q GLY C 119 UNP P05230 ARG 134 ENGINEERED MUTATION
SEQADV 3O3Q C UNP P05230 GLY 135 DELETION
SEQADV 3O3Q C UNP P05230 PRO 136 DELETION
SEQADV 3O3Q C UNP P05230 ARG 137 DELETION
SEQADV 3O3Q HIS D -5 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS D -4 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS D -3 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS D -2 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS D -1 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q HIS D 0 UNP P05230 EXPRESSION TAG
SEQADV 3O3Q PHE D 44 UNP P05230 LEU 59 ENGINEERED MUTATION
SEQADV 3O3Q ILE D 67 UNP P05230 MET 82 ENGINEERED MUTATION
SEQADV 3O3Q VAL D 73 UNP P05230 LEU 88 ENGINEERED MUTATION
SEQADV 3O3Q GLY D 103 UNP P05230 ALA 118 ENGINEERED MUTATION
SEQADV 3O3Q D UNP P05230 GLU 119 DELETION
SEQADV 3O3Q D UNP P05230 LYS 120 DELETION
SEQADV 3O3Q D UNP P05230 ASN 121 DELETION
SEQADV 3O3Q TYR D 108 UNP P05230 PHE 123 ENGINEERED MUTATION
SEQADV 3O3Q LEU D 109 UNP P05230 VAL 124 ENGINEERED MUTATION
SEQADV 3O3Q ILE D 111 UNP P05230 LEU 126 ENGINEERED MUTATION
SEQADV 3O3Q VAL D 117 UNP P05230 CYS 132 ENGINEERED MUTATION
SEQADV 3O3Q GLY D 119 UNP P05230 ARG 134 ENGINEERED MUTATION
SEQADV 3O3Q D UNP P05230 GLY 135 DELETION
SEQADV 3O3Q D UNP P05230 PRO 136 DELETION
SEQADV 3O3Q D UNP P05230 ARG 137 DELETION
SEQRES 1 A 140 HIS HIS HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY ASN
SEQRES 2 A 140 TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY
SEQRES 3 A 140 HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY
SEQRES 4 A 140 THR ARG ASP ARG SER ASP GLN HIS ILE GLN PHE GLN LEU
SEQRES 5 A 140 SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR
SEQRES 6 A 140 GLU THR GLY GLN TYR LEU ALA ILE ASP THR ASP GLY LEU
SEQRES 7 A 140 VAL TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE
SEQRES 8 A 140 LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE
SEQRES 9 A 140 SER LYS LYS HIS GLY TRP TYR LEU GLY ILE LYS LYS ASN
SEQRES 10 A 140 GLY SER VAL LYS GLY THR HIS TYR GLY GLN LYS ALA ILE
SEQRES 11 A 140 LEU PHE LEU PRO LEU PRO VAL SER SER ASP
SEQRES 1 B 140 HIS HIS HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY ASN
SEQRES 2 B 140 TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY
SEQRES 3 B 140 HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY
SEQRES 4 B 140 THR ARG ASP ARG SER ASP GLN HIS ILE GLN PHE GLN LEU
SEQRES 5 B 140 SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR
SEQRES 6 B 140 GLU THR GLY GLN TYR LEU ALA ILE ASP THR ASP GLY LEU
SEQRES 7 B 140 VAL TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE
SEQRES 8 B 140 LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE
SEQRES 9 B 140 SER LYS LYS HIS GLY TRP TYR LEU GLY ILE LYS LYS ASN
SEQRES 10 B 140 GLY SER VAL LYS GLY THR HIS TYR GLY GLN LYS ALA ILE
SEQRES 11 B 140 LEU PHE LEU PRO LEU PRO VAL SER SER ASP
SEQRES 1 C 140 HIS HIS HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY ASN
SEQRES 2 C 140 TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY
SEQRES 3 C 140 HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY
SEQRES 4 C 140 THR ARG ASP ARG SER ASP GLN HIS ILE GLN PHE GLN LEU
SEQRES 5 C 140 SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR
SEQRES 6 C 140 GLU THR GLY GLN TYR LEU ALA ILE ASP THR ASP GLY LEU
SEQRES 7 C 140 VAL TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE
SEQRES 8 C 140 LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE
SEQRES 9 C 140 SER LYS LYS HIS GLY TRP TYR LEU GLY ILE LYS LYS ASN
SEQRES 10 C 140 GLY SER VAL LYS GLY THR HIS TYR GLY GLN LYS ALA ILE
SEQRES 11 C 140 LEU PHE LEU PRO LEU PRO VAL SER SER ASP
SEQRES 1 D 140 HIS HIS HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY ASN
SEQRES 2 D 140 TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY
SEQRES 3 D 140 HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY
SEQRES 4 D 140 THR ARG ASP ARG SER ASP GLN HIS ILE GLN PHE GLN LEU
SEQRES 5 D 140 SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR
SEQRES 6 D 140 GLU THR GLY GLN TYR LEU ALA ILE ASP THR ASP GLY LEU
SEQRES 7 D 140 VAL TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE
SEQRES 8 D 140 LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE
SEQRES 9 D 140 SER LYS LYS HIS GLY TRP TYR LEU GLY ILE LYS LYS ASN
SEQRES 10 D 140 GLY SER VAL LYS GLY THR HIS TYR GLY GLN LYS ALA ILE
SEQRES 11 D 140 LEU PHE LEU PRO LEU PRO VAL SER SER ASP
HET GOL B 141 6
HET GOL D 141 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 7 HOH *578(H2 O)
HELIX 1 1 GLN A 127 ILE A 130 5 4
HELIX 2 2 GLN B 127 ILE B 130 5 4
HELIX 3 3 ASN C 80 CYS C 83 5 4
HELIX 4 4 GLU C 91 HIS C 93 5 3
HELIX 5 5 GLN C 127 ILE C 130 5 4
HELIX 6 6 ASN D 80 GLU D 82 5 3
HELIX 7 7 GLU D 91 HIS D 93 5 3
HELIX 8 8 GLN D 127 ILE D 130 5 4
SHEET 1 A 4 VAL A 31 THR A 34 0
SHEET 2 A 4 HIS A 21 ILE A 25 -1 N PHE A 22 O THR A 34
SHEET 3 A 4 LYS A 12 CYS A 16 -1 N CYS A 16 O HIS A 21
SHEET 4 A 4 PHE A 132 PRO A 136 -1 O LEU A 133 N TYR A 15
SHEET 1 B 2 PHE A 44 GLN A 45 0
SHEET 2 B 2 LYS A 57 SER A 58 -1 O LYS A 57 N GLN A 45
SHEET 1 C 4 ALA A 48 SER A 50 0
SHEET 2 C 4 GLU A 53 VAL A 54 -1 O GLU A 53 N SER A 50
SHEET 3 C 4 PHE A 85 LEU A 89 -1 O PHE A 85 N VAL A 54
SHEET 4 C 4 ASN A 95 SER A 99 -1 O ILE A 98 N LEU A 86
SHEET 1 D 2 TYR A 64 ILE A 67 0
SHEET 2 D 2 VAL A 73 SER A 76 -1 O SER A 76 N TYR A 64
SHEET 1 E 2 TYR A 108 ILE A 111 0
SHEET 2 E 2 VAL A 117 THR A 123 -1 O THR A 123 N TYR A 108
SHEET 1 F 5 VAL B 31 THR B 34 0
SHEET 2 F 5 HIS B 21 ILE B 25 -1 N PHE B 22 O THR B 34
SHEET 3 F 5 LYS B 12 CYS B 16 -1 N CYS B 16 O HIS B 21
SHEET 4 F 5 GLN B 43 GLN B 45 -1 O PHE B 44 N LYS B 12
SHEET 5 F 5 LYS B 57 SER B 58 -1 O LYS B 57 N GLN B 45
SHEET 1 G 4 VAL B 31 THR B 34 0
SHEET 2 G 4 HIS B 21 ILE B 25 -1 N PHE B 22 O THR B 34
SHEET 3 G 4 LYS B 12 CYS B 16 -1 N CYS B 16 O HIS B 21
SHEET 4 G 4 PHE B 132 PRO B 136 -1 O LEU B 133 N TYR B 15
SHEET 1 H 4 ALA B 48 SER B 50 0
SHEET 2 H 4 GLU B 53 VAL B 54 -1 O GLU B 53 N SER B 50
SHEET 3 H 4 PHE B 85 LEU B 89 -1 O PHE B 85 N VAL B 54
SHEET 4 H 4 ASN B 95 SER B 99 -1 O ILE B 98 N LEU B 86
SHEET 1 I 2 TYR B 64 ILE B 67 0
SHEET 2 I 2 VAL B 73 SER B 76 -1 O SER B 76 N TYR B 64
SHEET 1 J 2 TYR B 108 ILE B 111 0
SHEET 2 J 2 VAL B 117 THR B 123 -1 O THR B 123 N TYR B 108
SHEET 1 K 7 LYS C 12 CYS C 16 0
SHEET 2 K 7 GLN C 43 ALA C 48 -1 O PHE C 44 N LYS C 12
SHEET 3 K 7 GLU C 53 SER C 58 -1 O LYS C 57 N GLN C 45
SHEET 4 K 7 PHE C 85 LEU C 89 -1 O PHE C 85 N VAL C 54
SHEET 5 K 7 ASN C 95 SER C 99 -1 O ILE C 98 N LEU C 86
SHEET 6 K 7 PHE C 132 PRO C 136 -1 O PHE C 132 N ASN C 95
SHEET 7 K 7 LYS C 12 CYS C 16 -1 N LEU C 13 O LEU C 135
SHEET 1 L 2 PHE C 22 ILE C 25 0
SHEET 2 L 2 VAL C 31 THR C 34 -1 O THR C 34 N PHE C 22
SHEET 1 M 2 TYR C 64 ILE C 67 0
SHEET 2 M 2 VAL C 73 SER C 76 -1 O SER C 76 N TYR C 64
SHEET 1 N 2 TYR C 108 ILE C 111 0
SHEET 2 N 2 VAL C 117 THR C 123 -1 O THR C 123 N TYR C 108
SHEET 1 O 7 LYS D 12 CYS D 16 0
SHEET 2 O 7 GLN D 43 ALA D 48 -1 O PHE D 44 N LYS D 12
SHEET 3 O 7 GLU D 53 SER D 58 -1 O LYS D 57 N GLN D 45
SHEET 4 O 7 LEU D 84 LEU D 89 -1 O PHE D 85 N VAL D 54
SHEET 5 O 7 ASN D 95 SER D 99 -1 O ILE D 98 N LEU D 86
SHEET 6 O 7 PHE D 132 PRO D 136 -1 O PHE D 132 N ASN D 95
SHEET 7 O 7 LYS D 12 CYS D 16 -1 N LEU D 13 O LEU D 135
SHEET 1 P 2 PHE D 22 ILE D 25 0
SHEET 2 P 2 VAL D 31 THR D 34 -1 O THR D 34 N PHE D 22
SHEET 1 Q 2 TYR D 64 ILE D 67 0
SHEET 2 Q 2 VAL D 73 SER D 76 -1 O SER D 76 N TYR D 64
SHEET 1 R 2 TYR D 108 ILE D 111 0
SHEET 2 R 2 VAL D 117 THR D 123 -1 O THR D 123 N TYR D 108
SITE 1 AC1 10 HIS B 102 GLY B 103 HIS B 124 HOH B 160
SITE 2 AC1 10 HOH B 297 HOH B 346 HOH B 517 ARG C 37
SITE 3 AC1 10 PRO C 136 SER C 138
SITE 1 AC2 12 HIS A 102 GLY A 103 TRP A 107 HIS A 124
SITE 2 AC2 12 HOH A 168 HOH A 296 HOH A 300 ARG D 37
SITE 3 AC2 12 PRO D 136 SER D 138 SER D 139 HOH D 412
CRYST1 46.920 56.890 61.920 64.94 89.76 71.27 P 1 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 0.021313 -0.007226 0.003500 0.00000
SCALE2 0.000000 0.018561 -0.009245 0.00000
SCALE3 0.000000 0.000000 0.018042 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
