HEADER COAGULATION FACTOR 26-FEB-95 1CFH
TITLE STRUCTURE OF THE METAL-FREE GAMMA-CARBOXYGLUTAMIC ACID-RICH MEMBRANE
TITLE 2 BINDING REGION OF FACTOR IX BY TWO-DIMENSIONAL NMR SPECTROSCOPY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR IX;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS COAGULATION FACTOR
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR S.J.FREEDMAN,B.C.FURIE,B.FURIE,J.D.BALEJA
REVDAT 3 16-FEB-22 1CFH 1 REMARK LINK
REVDAT 2 24-FEB-09 1CFH 1 VERSN
REVDAT 1 10-JUL-95 1CFH 0
JRNL AUTH S.J.FREEDMAN,B.C.FURIE,B.FURIE,J.D.BALEJA
JRNL TITL STRUCTURE OF THE METAL-FREE GAMMA-CARBOXYGLUTAMIC ACID-RICH
JRNL TITL 2 MEMBRANE BINDING REGION OF FACTOR IX BY TWO-DIMENSIONAL NMR
JRNL TITL 3 SPECTROSCOPY.
JRNL REF J.BIOL.CHEM. V. 270 7980 1995
JRNL REFN ISSN 0021-9258
JRNL PMID 7713897
JRNL DOI 10.1074/JBC.270.14.7980
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII
REMARK 3 AUTHORS : BIOSYM TECHNOLOGIES INC.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CFH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172293.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 48
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 49
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 50
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 51
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 52
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 53
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 54
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 55
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 56
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 58
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 59
DBREF 1CFH A 1 47 UNP P00740 FA9_HUMAN 47 93
SEQRES 1 A 47 TYR ASN SER GLY LYS LEU GLU GLU PHE VAL GLN GLY ASN
SEQRES 2 A 47 LEU GLU ARG GLU CYS MET GLU GLU LYS CYS SER PHE GLU
SEQRES 3 A 47 GLU ALA ARG GLU VAL PHE GLU ASN THR GLU ARG THR THR
SEQRES 4 A 47 GLU PHE TRP LYS GLN TYR VAL ASP
HET FMT A 48 3
HET FMT A 49 3
HET FMT A 50 3
HET FMT A 51 3
HET FMT A 52 3
HET FMT A 53 3
HET FMT A 54 3
HET FMT A 55 3
HET FMT A 56 3
HET FMT A 57 3
HET FMT A 58 3
HET FMT A 59 3
HETNAM FMT FORMIC ACID
FORMUL 2 FMT 12(C H2 O2)
HELIX 1 1 ARG A 37 VAL A 46 1 10
SSBOND 1 CYS A 18 CYS A 23 1555 1555 2.03
LINK CG GLU A 7 C FMT A 48 1555 1555 1.54
LINK CG GLU A 8 C FMT A 49 1555 1555 1.54
LINK CG GLU A 15 C FMT A 50 1555 1555 1.54
LINK CG GLU A 17 C FMT A 51 1555 1555 1.54
LINK CG GLU A 20 C FMT A 52 1555 1555 1.54
LINK CG GLU A 21 C FMT A 53 1555 1555 1.54
LINK CG GLU A 26 C FMT A 54 1555 1555 1.54
LINK CG GLU A 27 C FMT A 55 1555 1555 1.54
LINK CG GLU A 30 C FMT A 56 1555 1555 1.54
LINK CG GLU A 33 C FMT A 57 1555 1555 1.54
LINK CG GLU A 36 C FMT A 58 1555 1555 1.54
LINK CG GLU A 40 C FMT A 59 1555 1555 1.54
SITE 1 AC1 2 GLU A 7 GLU A 8
SITE 1 AC2 2 TYR A 1 GLU A 8
SITE 1 AC3 1 GLU A 15
SITE 1 AC4 2 GLU A 17 LYS A 22
SITE 1 AC5 1 GLU A 20
SITE 1 AC6 2 GLU A 21 SER A 24
SITE 1 AC7 1 GLU A 26
SITE 1 AC8 1 GLU A 27
SITE 1 AC9 3 GLU A 30 VAL A 31 PHE A 32
SITE 1 BC1 2 PHE A 32 GLU A 33
SITE 1 BC2 1 GLU A 36
SITE 1 BC3 1 GLU A 40
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