HEADER BLOOD CLOTTING 19-FEB-99 1F7E
TITLE THE FIRST EGF-LIKE DOMAIN FROM HUMAN BLOOD COAGULATION FVII, NMR, 20
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (BLOOD COAGULATION FACTOR VII);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIRST EGF-LIKE DOMAIN (RESIDUES 45-87);
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: CALCIUM BOUND FORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FACTOR VII, BLOOD COAGULATION, EGF-LIKE DOMAIN, BLOOD CLOTTING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.-H.KAO,G.F.LEE,Y.WANG,M.A.STAROVASNIK,R.F.KELLEY,M.W.SPELLMAN,
AUTHOR 2 L.LERNER
REVDAT 5 27-DEC-23 1F7E 1 REMARK
REVDAT 4 16-FEB-22 1F7E 1 REMARK
REVDAT 3 24-FEB-09 1F7E 1 VERSN
REVDAT 2 01-APR-03 1F7E 1 JRNL
REVDAT 1 16-JUN-99 1F7E 0
JRNL AUTH Y.H.KAO,G.F.LEE,Y.WANG,M.A.STAROVASNIK,R.F.KELLEY,
JRNL AUTH 2 M.W.SPELLMAN,L.LERNER
JRNL TITL THE EFFECT OF O-FUCOSYLATION ON THE FIRST EGF-LIKE DOMAIN
JRNL TITL 2 FROM HUMAN BLOOD COAGULATION FACTOR VII.
JRNL REF BIOCHEMISTRY V. 38 7097 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10353820
JRNL DOI 10.1021/BI990234Z
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1F7E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-99.
REMARK 100 THE DEPOSITION ID IS D_1000000508.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 400MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2Q; TOCSY; NOESY; 1H
REMARK 210 -15N HSQC; 3D 1H-15N NOESY-HSQC;
REMARK 210 3D 1H-15N TOCSY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA 500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX, X-PLOR
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY -
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND
REMARK 210 LOWEST XPLOR ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: DETAILS ARE INCLUDED IN THE PUBLICATION.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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
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 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 1 ASP A 46 53.44 -163.47
REMARK 500 1 LEU A 65 97.29 53.91
REMARK 500 1 GLN A 66 -77.29 62.94
REMARK 500 1 SER A 67 -165.99 -62.07
REMARK 500 1 PHE A 71 66.77 -102.48
REMARK 500 1 SER A 89 -86.63 55.58
REMARK 500 2 ASP A 46 48.71 -91.55
REMARK 500 2 CYS A 50 49.68 -93.66
REMARK 500 2 SER A 53 72.51 51.19
REMARK 500 2 LEU A 65 100.91 53.84
REMARK 500 2 ASP A 86 44.74 -92.65
REMARK 500 2 ASP A 87 -71.80 -168.41
REMARK 500 2 SER A 89 108.78 -167.72
REMARK 500 3 ASP A 46 -64.17 -156.74
REMARK 500 3 CYS A 50 48.73 -91.45
REMARK 500 3 SER A 53 80.79 51.18
REMARK 500 3 LEU A 65 151.17 61.40
REMARK 500 3 GLN A 66 -80.54 60.38
REMARK 500 3 SER A 67 -156.56 -109.84
REMARK 500 3 CYS A 72 -171.86 -66.85
REMARK 500 3 ASP A 87 -172.48 52.84
REMARK 500 4 ASP A 46 84.86 -167.11
REMARK 500 4 CYS A 50 30.43 -96.95
REMARK 500 4 SER A 53 71.03 50.69
REMARK 500 4 LEU A 65 104.33 55.63
REMARK 500 5 CYS A 50 51.88 -100.16
REMARK 500 5 SER A 53 80.87 51.49
REMARK 500 5 LEU A 65 -156.73 53.88
REMARK 500 5 PHE A 71 68.68 -107.26
REMARK 500 6 ASP A 46 48.53 -91.71
REMARK 500 6 CYS A 50 46.04 -93.15
REMARK 500 6 SER A 53 72.75 46.53
REMARK 500 6 LEU A 65 152.20 60.59
REMARK 500 6 GLN A 66 -82.27 58.99
REMARK 500 6 SER A 67 -154.79 -112.80
REMARK 500 7 GLN A 56 -151.52 -122.42
REMARK 500 7 GLN A 64 -168.58 -110.10
REMARK 500 7 ASP A 87 -179.61 52.85
REMARK 500 8 CYS A 50 48.01 -91.76
REMARK 500 8 SER A 53 81.81 51.67
REMARK 500 8 GLN A 64 55.38 -112.67
REMARK 500 8 LEU A 65 110.54 58.27
REMARK 500 8 GLN A 66 -73.53 65.30
REMARK 500 9 CYS A 50 49.51 -91.81
REMARK 500 9 SER A 53 77.46 51.09
REMARK 500 9 GLN A 64 -168.94 -102.75
REMARK 500 9 SER A 67 -167.19 -169.06
REMARK 500 9 CYS A 72 -166.75 -108.61
REMARK 500 9 LYS A 85 -171.25 -60.88
REMARK 500 9 ASP A 86 -69.27 63.09
REMARK 500
REMARK 500 THIS ENTRY HAS 125 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1F7E A 45 87 UNP P08709 FA7_HUMAN 83 125
SEQADV 1F7E GLY A 88 UNP P08709 SEE REMARK 999
SEQADV 1F7E SER A 89 UNP P08709 SEE REMARK 999
SEQADV 1F7E ALA A 90 UNP P08709 SEE REMARK 999
SEQRES 1 A 46 SER ASP GLY ASP GLN CYS ALA SER SER PRO CYS GLN ASN
SEQRES 2 A 46 GLY GLY SER CYS LYS ASP GLN LEU GLN SER TYR ILE CYS
SEQRES 3 A 46 PHE CYS LEU PRO ALA PHE GLU GLY ARG ASN CYS GLU THR
SEQRES 4 A 46 HIS LYS ASP ASP GLY SER ALA
SHEET 1 S1 2 SER A 60 ASP A 63 0
SHEET 2 S1 2 TYR A 68 PHE A 71 -1
SHEET 1 S2 2 PHE A 76 GLU A 77 0
SHEET 2 S2 2 THR A 83 HIS A 84 -1
SSBOND 1 CYS A 50 CYS A 61 1555 1555 2.02
SSBOND 2 CYS A 55 CYS A 70 1555 1555 2.02
SSBOND 3 CYS A 72 CYS A 81 1555 1555 2.02
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END