HEADER HYDROLASE/HYDROLASE INHIBITOR 06-JUN-01 1JBU
TITLE COAGULATION FACTOR VII ZYMOGEN (EGF2/PROTEASE) IN COMPLEX WITH
TITLE 2 INHIBITORY EXOSITE PEPTIDE A-183
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR VII;
COMPND 3 CHAIN: H;
COMPND 4 FRAGMENT: HEAVY CHAIN;
COMPND 5 SYNONYM: SERUM PROTHROMBIN CONVERSION ACCELERATOR;
COMPND 6 EC: 3.4.21.21;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: COAGULATION FACTOR VII;
COMPND 10 CHAIN: L;
COMPND 11 FRAGMENT: LIGHT CHAIN;
COMPND 12 SYNONYM: SERUM PROTHROMBIN CONVERSION ACCELERATOR;
COMPND 13 EC: 3.4.21.21;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: PEPTIDE EXOSITE INHIBITOR A-183;
COMPND 17 CHAIN: X;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HIGH-FIVE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PACGP67;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: HIGH-FIVE;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PACGP67;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 23 ORGANISM_TAXID: 562;
SOURCE 24 GENE: SYNTHETIC CONSTRUCT;
SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 27 EXPRESSION_SYSTEM_STRAIN: 27C7;
SOURCE 28 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 29 EXPRESSION_SYSTEM_PLASMID: PA-100-Z
KEYWDS SHIFTED REGISTRATION, BETA-STRANDS, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.EIGENBROT,D.KIRCHHOFER,M.S.DENNIS,L.SANTELL,R.A.LAZARUS,J.STAMOS,
AUTHOR 2 M.H.ULTSCH
REVDAT 7 16-AUG-23 1JBU 1 REMARK
REVDAT 6 31-JAN-18 1JBU 1 JRNL
REVDAT 5 24-JAN-18 1JBU 1 JRNL REMARK
REVDAT 4 13-JUL-11 1JBU 1 VERSN
REVDAT 3 24-FEB-09 1JBU 1 VERSN
REVDAT 2 01-APR-03 1JBU 1 JRNL
REVDAT 1 11-JUL-01 1JBU 0
JRNL AUTH C.EIGENBROT,D.KIRCHHOFER,M.S.DENNIS,L.SANTELL,R.A.LAZARUS,
JRNL AUTH 2 J.STAMOS,M.H.ULTSCH
JRNL TITL THE FACTOR VII ZYMOGEN STRUCTURE REVEALS REREGISTRATION OF
JRNL TITL 2 BETA STRANDS DURING ACTIVATION.
JRNL REF STRUCTURE V. 9 627 2001
JRNL REFN ISSN 0969-2126
JRNL PMID 11470437
JRNL DOI 10.1016/S0969-2126(01)00624-4
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.ROBERGE,L.SANTELL,M.S.DENNIS,C.EIGENBROT,M.A.DWYER,
REMARK 1 AUTH 2 R.A.LAZARUS
REMARK 1 TITL A NOVEL EXOSITE ON COAGULATION FACTOR VIIA AND ITS MOLECULAR
REMARK 1 TITL 2 INTERACTIONS WITH A NEW CLASS OF PEPTIDE INHIBITORS
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.W.BANNER,A.D'ARCY,C.CHENE,F.K.WINKLER,A.GUHA,
REMARK 1 AUTH 2 W.H.KONIGSBERG,Y.NEMERSON,D.KIRCHHOFER
REMARK 1 TITL THE CRYSTAL STRUCTURE OF THE COMPLEX OF BLOOD COAGULATION
REMARK 1 TITL 2 FACTOR VIIA WITH SOLUBLE TISSUE FACTOR
REMARK 1 REF NATURE V. 380 41 1996
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/380041A0
REMARK 1 REFERENCE 3
REMARK 1 AUTH E.ZHANG,R.ST.CHARLES,A.TULINSKY
REMARK 1 TITL STRUCTURE OF EXTRACELLULAR TISSUE FACTOR COMPLEXED WITH
REMARK 1 TITL 2 FACTOR VIIA INHIBITED WITH A BPTI MUTANT
REMARK 1 REF J.MOL.BIOL. V. 285 2089 1999
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1998.2452
REMARK 1 REFERENCE 4
REMARK 1 AUTH G.KEMBALL-COOK,D.J.JOHNSON,E.G.TUDDENHAM,K.HARLOS
REMARK 1 TITL CRYSTAL STRUCTURE OF ACTIVE SITE-INHIBITED HUMAN COAGULATION
REMARK 1 TITL 2 FACTOR VIIA (DES-GLA)
REMARK 1 REF J.STRUCT.BIOL. V. 127 213 1999
REMARK 1 REFN ISSN 1047-8477
REMARK 1 DOI 10.1006/JSBI.1999.4158
REMARK 1 REFERENCE 5
REMARK 1 AUTH A.C.PIKE,A.M.BRZOZOWSKI,S.M.ROBERTS,O.H.OLSEN,E.PERSSON
REMARK 1 TITL STRUCTURE OF HUMAN FACTOR VIIA AND ITS IMPLICATIONS FOR THE
REMARK 1 TITL 2 TRIGGERING OF BLOOD COAGULATION
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 96 8925 1999
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.96.16.8925
REMARK 1 REFERENCE 6
REMARK 1 AUTH M.S.DENNIS,C.EIGENBROT,N.J.SKELTON,M.H.ULTSCH,L.SANTELL,
REMARK 1 AUTH 2 M.A.DWYER,M.P.O'CONNELL,R.A.LAZARUS
REMARK 1 TITL PEPTIDE EXOSITE INHIBITORS OF FACTOR VIIA AS ANTICOAGULANTS
REMARK 1 REF NATURE V. 404 465 2000
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/35006574
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 98.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.200
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 33404
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) : 0.204
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100
REMARK 3 FREE R VALUE TEST SET COUNT : 698
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3230
REMARK 3 BIN R VALUE (WORKING SET) : 0.3130
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 59
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.044
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2415
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 198
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.01000
REMARK 3 B22 (A**2) : 0.50000
REMARK 3 B33 (A**2) : -0.25000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.21
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.26
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.100
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.970 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.470 ; 4.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.070 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.900 ; 6.000
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 : MSI_XPLOR_PARHCSDX
REMARK 3 PARAMETER FILE 2 : PARAM.SO4
REMARK 3 PARAMETER FILE 3 : PARWAT.PRO
REMARK 3 PARAMETER FILE 4 : PARAM.BDN
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : MSI_XPLOR_TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOP.SO4
REMARK 3 TOPOLOGY FILE 3 : TOPWAT.PRO
REMARK 3 TOPOLOGY FILE 4 : TOP.BDN
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JBU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013599.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-99
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 : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.05
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC (QUANTUM)
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33624
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.044
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.77
REMARK 200 R MERGE FOR SHELL (I) : 0.42200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1DAN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, AMMONIUM SULFATE, GLYCEROL, PEG
REMARK 280 400, BENZAMIDINE, CALCIUM CHLORIDE, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 33.72000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.42000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.25500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.42000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.72000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.25500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, X
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 -33.72000
REMARK 350 BIOMT2 1 0.000000 -1.000000 0.000000 42.25500
REMARK 350 BIOMT3 1 0.000000 0.000000 -1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, X
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 ILE H 16
REMARK 465 VAL H 17
REMARK 465 GLY H 18
REMARK 465 GLY H 19
REMARK 465 LEU H 73
REMARK 465 SER H 74
REMARK 465 GLU H 75
REMARK 465 GLY H 143
REMARK 465 GLN H 144
REMARK 465 LEU H 145
REMARK 465 LEU H 146
REMARK 465 ASP H 147
REMARK 465 ARG H 148
REMARK 465 GLY H 149
REMARK 465 ALA H 150
REMARK 465 ARG L 144
REMARK 465 ASN L 145
REMARK 465 ALA L 146
REMARK 465 SER L 147
REMARK 465 LYS L 148
REMARK 465 PRO L 149
REMARK 465 GLN L 150
REMARK 465 GLY L 151
REMARK 465 ARG L 152
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ASP H 72
REMARK 475 HIS H 76
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS H 24 CE NZ
REMARK 480 ASP H 77 CG OD1 OD2
REMARK 480 VAL H 170E CG1 CG2
REMARK 480 SER H 188A OG
REMARK 480 LYS H 188 CG CD CE NZ
REMARK 480 ASP H 189 CG OD1 OD2
REMARK 480 SER H 190 OG
REMARK 480 GLU L 116 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 LEU H 68 CA - CB - CG ANGL. DEV. = 14.3 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 LYS H 24 19.76 59.63
REMARK 500 ASN H 63 -177.70 -172.79
REMARK 500 ASP H 77 -30.06 71.48
REMARK 500 SER H 190 -1.47 -165.89
REMARK 500 LYS H 192 -72.31 -55.68
REMARK 500 ALA H 221A 167.36 71.64
REMARK 500 GLN L 100 -95.12 -118.35
REMARK 500 THR L 108 -179.08 -64.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE AUTHORS ARE UNCERTAIN OF THE TRUE IDENTITY OF THE
REMARK 600 HET GROUP BEN, AND USED BENZAMIDINE AS A CONVENIENCE.
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 SO4 H 308
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN H 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN X OF PEPTIDE EXOSITE
REMARK 800 INHIBITOR A-183
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DAN RELATED DB: PDB
REMARK 900 TISSUE FACTOR/FACTOR VIIA COMPLEX
REMARK 900 RELATED ID: 1FAK RELATED DB: PDB
REMARK 900 TISSUE FACTOR/FACTOR VIIA/BPTI COMPLEX
REMARK 900 RELATED ID: 1QFK RELATED DB: PDB
REMARK 900 FACTOR VIIA DES-GLA
REMARK 900 RELATED ID: 1CVW RELATED DB: PDB
REMARK 900 FACTOR VIIA DES-GLA
REMARK 900 RELATED ID: 1DVA RELATED DB: PDB
REMARK 900 FACTOR VIIA(DES-GLA)/PEPTIDE E-76 COMPLEX
DBREF 1JBU H 16 257 UNP P08709 FA7_HUMAN 213 466
DBREF 1JBU L 90 152 UNP P08709 FA7_HUMAN 150 212
DBREF 1JBU X 1 15 PDB 1JBU 1JBU 1 15
SEQRES 1 H 254 ILE VAL GLY GLY LYS VAL CYS PRO LYS GLY GLU CYS PRO
SEQRES 2 H 254 TRP GLN VAL LEU LEU LEU VAL ASN GLY ALA GLN LEU CYS
SEQRES 3 H 254 GLY GLY THR LEU ILE ASN THR ILE TRP VAL VAL SER ALA
SEQRES 4 H 254 ALA HIS CYS PHE ASP LYS ILE LYS ASN TRP ARG ASN LEU
SEQRES 5 H 254 ILE ALA VAL LEU GLY GLU HIS ASP LEU SER GLU HIS ASP
SEQRES 6 H 254 GLY ASP GLU GLN SER ARG ARG VAL ALA GLN VAL ILE ILE
SEQRES 7 H 254 PRO SER THR TYR VAL PRO GLY THR THR ASN HIS ASP ILE
SEQRES 8 H 254 ALA LEU LEU ARG LEU HIS GLN PRO VAL VAL LEU THR ASP
SEQRES 9 H 254 HIS VAL VAL PRO LEU CYS LEU PRO GLU ARG THR PHE SER
SEQRES 10 H 254 GLU ARG THR LEU ALA PHE VAL ARG PHE SER LEU VAL SER
SEQRES 11 H 254 GLY TRP GLY GLN LEU LEU ASP ARG GLY ALA THR ALA LEU
SEQRES 12 H 254 GLU LEU MET VAL LEU ASN VAL PRO ARG LEU MET THR GLN
SEQRES 13 H 254 ASP CYS LEU GLN GLN SER ARG LYS VAL GLY ASP SER PRO
SEQRES 14 H 254 ASN ILE THR GLU TYR MET PHE CYS ALA GLY TYR SER ASP
SEQRES 15 H 254 GLY SER LYS ASP SER CYS LYS GLY ASP SER GLY GLY PRO
SEQRES 16 H 254 HIS ALA THR HIS TYR ARG GLY THR TRP TYR LEU THR GLY
SEQRES 17 H 254 ILE VAL SER TRP GLY GLN GLY CYS ALA THR VAL GLY HIS
SEQRES 18 H 254 PHE GLY VAL TYR THR ARG VAL SER GLN TYR ILE GLU TRP
SEQRES 19 H 254 LEU GLN LYS LEU MET ARG SER GLU PRO ARG PRO GLY VAL
SEQRES 20 H 254 LEU LEU ARG ALA PRO PHE PRO
SEQRES 1 L 63 ILE CYS VAL ASN GLU ASN GLY GLY CYS GLU GLN TYR CYS
SEQRES 2 L 63 SER ASP HIS THR GLY THR LYS ARG SER CYS ARG CYS HIS
SEQRES 3 L 63 GLU GLY TYR SER LEU LEU ALA ASP GLY VAL SER CYS THR
SEQRES 4 L 63 PRO THR VAL GLU TYR PRO CYS GLY LYS ILE PRO ILE LEU
SEQRES 5 L 63 GLU LYS ARG ASN ALA SER LYS PRO GLN GLY ARG
SEQRES 1 X 15 GLU GLU TRP GLU VAL LEU CYS TRP THR TRP GLU THR CYS
SEQRES 2 X 15 GLU ARG
HET SO4 H 308 5
HET BEN H 300 9
HETNAM SO4 SULFATE ION
HETNAM BEN BENZAMIDINE
FORMUL 4 SO4 O4 S 2-
FORMUL 5 BEN C7 H8 N2
FORMUL 6 HOH *198(H2 O)
HELIX 1 1 CYS H 22 GLU H 26 5 5
HELIX 2 2 ALA H 55 ASP H 60 5 6
HELIX 3 3 GLU H 125 THR H 129C 1 8
HELIX 4 4 LEU H 129D VAL H 129G 5 4
HELIX 5 5 PRO H 161 LEU H 163 5 3
HELIX 6 6 MET H 164 LEU H 169 1 6
HELIX 7 7 GLN H 170 ARG H 170C 5 4
HELIX 8 8 ASN H 175 TYR H 179 1 5
HELIX 9 9 SER H 190 SER H 195 1 6
HELIX 10 10 TYR H 234 SER H 244 1 11
HELIX 11 11 ASN L 93 CYS L 98 5 6
HELIX 12 12 ILE L 138 LYS L 143 1 6
SHEET 1 A 8 GLU X 4 CYS X 7 0
SHEET 2 A 8 LEU H 251 ALA H 254 -1 O LEU H 251 N LEU X 6
SHEET 3 A 8 GLU H 80 PRO H 91 1 O VAL H 88 N LEU H 252
SHEET 4 A 8 ILE H 65 GLY H 69 -1 N ALA H 66 O ARG H 83
SHEET 5 A 8 GLN H 30 VAL H 35 -1 O LEU H 32 N VAL H 67
SHEET 6 A 8 ALA H 39 LEU H 46 -1 N ALA H 39 O VAL H 35
SHEET 7 A 8 TRP H 51 SER H 54 -1 N VAL H 53 O THR H 45
SHEET 8 A 8 ALA H 104 LEU H 108 -1 O ALA H 104 N SER H 54
SHEET 1 B 6 LEU H 153 LEU H 158 0
SHEET 2 B 6 PHE H 135 GLY H 140 -1 O SER H 136 N VAL H 157
SHEET 3 B 6 PRO H 198 TYR H 203 -1 O PRO H 198 N SER H 139
SHEET 4 B 6 THR H 206 TRP H 215 -1 O THR H 206 N TYR H 203
SHEET 5 B 6 HIS H 224 ARG H 230 -1 N VAL H 227 O TRP H 215
SHEET 6 B 6 MET H 180 SER H 185 -1 O PHE H 181 N TYR H 228
SHEET 1 C 2 TYR L 101 SER L 103 0
SHEET 2 C 2 SER L 111 ARG L 113 -1 O SER L 111 N SER L 103
SHEET 1 D 2 TYR L 118 LEU L 120 0
SHEET 2 D 2 CYS L 127 PRO L 129 -1 N THR L 128 O SER L 119
SSBOND 1 CYS H 22 CYS H 27 1555 1555 2.04
SSBOND 2 CYS H 42 CYS H 58 1555 1555 2.03
SSBOND 3 CYS H 122 CYS L 135 1555 1555 2.03
SSBOND 4 CYS H 168 CYS H 182 1555 1555 2.04
SSBOND 5 CYS H 191 CYS H 220 1555 1555 2.03
SSBOND 6 CYS L 91 CYS L 102 1555 1555 2.03
SSBOND 7 CYS L 98 CYS L 112 1555 1555 2.03
SSBOND 8 CYS L 114 CYS L 127 1555 1555 2.04
SSBOND 9 CYS X 7 CYS X 13 1555 1555 2.04
CISPEP 1 PHE H 256 PRO H 257 0 0.07
SITE 1 AC1 2 ARG H 84 ALA L 122
SITE 1 AC2 3 VAL H 35 ASN H 37 LYS H 60C
SITE 1 AC3 44 PHE H 59 ASP H 60 LYS H 60A ILE H 60B
SITE 2 AC3 44 TRP H 61 LEU H 64 VAL H 85 ILE H 89
SITE 3 AC3 44 ILE H 90 ARG H 134 LEU H 158 ASN H 159
SITE 4 AC3 44 TYR H 184 GLY H 184A SER H 185 ASP H 186
SITE 5 AC3 44 GLY H 187 PHE H 225 LYS H 240 LEU H 241
SITE 6 AC3 44 SER H 244 ARG H 247 GLY H 249 VAL H 250
SITE 7 AC3 44 LEU H 251 LEU H 252 ARG H 253 PRO H 255
SITE 8 AC3 44 HOH H 445 HOH H 520 HOH H 526 HOH X 404
SITE 9 AC3 44 HOH X 429 HOH X 439 HOH X 458 HOH X 464
SITE 10 AC3 44 HOH X 465 HOH X 470 HOH X 471 HOH X 492
SITE 11 AC3 44 HOH X 511 HOH X 515 HOH X 578 HOH X 596
CRYST1 67.440 84.510 84.840 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 0.014828 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011833 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011787 0.00000
(ATOM LINES ARE NOT SHOWN.)
END