HEADER GLYCOPROTEIN 18-JUN-96 1WHF
TITLE COAGULATION FACTOR, NMR, 15 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR X;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.21.6;
COMPND 5 OTHER_DETAILS: THE 1 CA FORM OF THE FRAGMENT CONTAINING THE GLA AND
COMPND 6 N-TERMINAL EGF-LIKE MODULE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS GLYCOPROTEIN, HYDROLASE, SERINE PROTEASE, PLASMA, BLOOD COAGULATION
KEYWDS 2 FACTOR
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR M.SUNNERHAGEN,G.A.OLAH,J.STENFLO,S.FORSEN,T.DRAKENBERG,J.TREWHELLA
REVDAT 4 29-NOV-17 1WHF 1 HELIX
REVDAT 3 20-JUN-12 1WHF 1 HETNAM VERSN
REVDAT 2 24-FEB-09 1WHF 1 VERSN
REVDAT 1 15-MAY-97 1WHF 0
JRNL AUTH M.SUNNERHAGEN,G.A.OLAH,J.STENFLO,S.FORSEN,T.DRAKENBERG,
JRNL AUTH 2 J.TREWHELLA
JRNL TITL THE RELATIVE ORIENTATION OF GLA AND EGF DOMAINS IN
JRNL TITL 2 COAGULATION FACTOR X IS ALTERED BY CA2+ BINDING TO THE FIRST
JRNL TITL 3 EGF DOMAIN. A COMBINED NMR-SMALL ANGLE X-RAY SCATTERING
JRNL TITL 4 STUDY.
JRNL REF BIOCHEMISTRY V. 35 11547 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8794734
JRNL DOI 10.1021/BI960633J
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.SUNNERHAGEN,S.FORSEN,A.M.HOFFREN,T.DRAKENBERG,O.TELEMAN,
REMARK 1 AUTH 2 J.STENFLO
REMARK 1 TITL STRUCTURE OF THE CA(2+)-FREE GLA DOMAIN SHEDS LIGHT ON
REMARK 1 TITL 2 MEMBRANE BINDING OF BLOOD COAGULATION PROTEINS
REMARK 1 REF NAT.STRUCT.BIOL. V. 2 504 1995
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.SELANDER-SUNNERHAGEN,M.ULLNER,E.PERSSON,O.TELEMAN,
REMARK 1 AUTH 2 J.STENFLO,T.DRAKENBERG
REMARK 1 TITL HOW AN EPIDERMAL GROWTH FACTOR (EGF)-LIKE DOMAIN BINDS
REMARK 1 TITL 2 CALCIUM. HIGH RESOLUTION NMR STRUCTURE OF THE CALCIUM FORM
REMARK 1 TITL 3 OF THE NH2-TERMINAL EGF-LIKE DOMAIN IN COAGULATION FACTOR X
REMARK 1 REF J.BIOL.CHEM. V. 267 19642 1992
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.ULLNER,M.SELANDER,E.PERSSON,J.STENFLO,T.DRAKENBERG,
REMARK 1 AUTH 2 O.TELEMAN
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE APO FORM OF THE
REMARK 1 TITL 2 N-TERMINAL EGF-LIKE MODULE OF BLOOD COAGULATION FACTOR X AS
REMARK 1 TITL 3 DETERMINED BY NMR SPECTROSCOPY AND SIMULATED FOLDING
REMARK 1 REF BIOCHEMISTRY V. 31 5974 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WHF 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_1000177195.
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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
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 1 SER A 3 -135.35 -167.06
REMARK 500 1 CGU A 7 57.46 -141.32
REMARK 500 1 VAL A 8 96.06 -39.93
REMARK 500 1 GLN A 10 130.98 168.03
REMARK 500 1 LEU A 13 -125.69 -77.18
REMARK 500 1 CYS A 17 42.51 -84.56
REMARK 500 1 CGU A 19 -142.47 -112.10
REMARK 500 1 SER A 23 -35.27 -175.96
REMARK 500 1 LEU A 24 -36.99 -165.21
REMARK 500 1 CGU A 29 -8.26 80.82
REMARK 500 1 ASP A 33 88.45 -37.71
REMARK 500 1 SER A 42 87.74 42.13
REMARK 500 1 LYS A 43 5.55 115.19
REMARK 500 1 TYR A 44 -95.34 -80.70
REMARK 500 1 LYS A 45 55.30 12.61
REMARK 500 1 ASP A 46 16.76 -143.98
REMARK 500 1 ASP A 48 7.16 88.55
REMARK 500 1 GLN A 49 -23.44 72.47
REMARK 500 1 HIS A 53 63.33 65.85
REMARK 500 1 HIS A 60 -164.04 -79.23
REMARK 500 1 ILE A 65 -165.22 34.59
REMARK 500 1 ASP A 67 -171.75 85.58
REMARK 500 1 THR A 71 118.41 -160.15
REMARK 500 1 ASN A 80 30.19 -94.06
REMARK 500 1 SER A 84 94.42 -66.73
REMARK 500 2 CGU A 7 57.11 -110.73
REMARK 500 2 VAL A 8 99.12 -39.59
REMARK 500 2 GLN A 10 58.26 89.76
REMARK 500 2 CGU A 14 -66.40 -157.13
REMARK 500 2 CGU A 16 -1.09 -53.61
REMARK 500 2 CYS A 17 -45.41 115.90
REMARK 500 2 LEU A 18 -103.43 113.67
REMARK 500 2 CGU A 19 -145.99 -89.91
REMARK 500 2 ALA A 21 -32.18 -35.22
REMARK 500 2 LEU A 24 -5.27 77.74
REMARK 500 2 ALA A 27 -8.94 -58.28
REMARK 500 2 ARG A 28 -78.21 -79.94
REMARK 500 2 SER A 42 92.86 36.84
REMARK 500 2 LYS A 43 -33.33 123.14
REMARK 500 2 TYR A 44 -73.66 -55.05
REMARK 500 2 LYS A 45 68.96 -0.69
REMARK 500 2 ASP A 46 28.00 -160.45
REMARK 500 2 GLN A 49 -10.63 70.53
REMARK 500 2 HIS A 53 66.08 68.84
REMARK 500 2 ILE A 65 -67.42 -94.37
REMARK 500 2 ASP A 67 -149.47 175.54
REMARK 500 2 TYR A 68 -165.10 -160.43
REMARK 500 2 CYS A 81 71.70 55.84
REMARK 500 2 SER A 84 108.88 -55.22
REMARK 500 3 VAL A 8 96.80 -40.06
REMARK 500
REMARK 500 THIS ENTRY HAS 338 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1WHF A 1 86 UNP P00743 FA10_BOVIN 41 126
SEQADV 1WHF CGU A 6 UNP P00743 GLU 46 MODIFIED RESIDUE
SEQADV 1WHF CGU A 7 UNP P00743 GLU 47 MODIFIED RESIDUE
SEQADV 1WHF CGU A 14 UNP P00743 GLU 54 MODIFIED RESIDUE
SEQADV 1WHF CGU A 16 UNP P00743 GLU 56 MODIFIED RESIDUE
SEQADV 1WHF CGU A 19 UNP P00743 GLU 59 MODIFIED RESIDUE
SEQADV 1WHF CGU A 20 UNP P00743 GLU 60 MODIFIED RESIDUE
SEQADV 1WHF CGU A 25 UNP P00743 GLU 65 MODIFIED RESIDUE
SEQADV 1WHF CGU A 26 UNP P00743 GLU 66 MODIFIED RESIDUE
SEQADV 1WHF CGU A 29 UNP P00743 GLU 69 MODIFIED RESIDUE
SEQADV 1WHF CGU A 32 UNP P00743 GLU 72 MODIFIED RESIDUE
SEQADV 1WHF CGU A 35 UNP P00743 GLU 75 MODIFIED RESIDUE
SEQADV 1WHF CGU A 39 UNP P00743 GLU 79 MODIFIED RESIDUE
SEQADV 1WHF BHD A 63 UNP P00743 ASP 103 MODIFIED RESIDUE
SEQRES 1 A 86 ALA ASN SER PHE LEU CGU CGU VAL LYS GLN GLY ASN LEU
SEQRES 2 A 86 CGU ARG CGU CYS LEU CGU CGU ALA CYS SER LEU CGU CGU
SEQRES 3 A 86 ALA ARG CGU VAL PHE CGU ASP ALA CGU GLN THR ASP CGU
SEQRES 4 A 86 PHE TRP SER LYS TYR LYS ASP GLY ASP GLN CYS GLU GLY
SEQRES 5 A 86 HIS PRO CYS LEU ASN GLN GLY HIS CYS LYS BHD GLY ILE
SEQRES 6 A 86 GLY ASP TYR THR CYS THR CYS ALA GLU GLY PHE GLU GLY
SEQRES 7 A 86 LYS ASN CYS GLU PHE SER THR ARG
MODRES 1WHF CGU A 6 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1WHF CGU A 7 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1WHF CGU A 14 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1WHF CGU A 16 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1WHF CGU A 19 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1WHF CGU A 20 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1WHF CGU A 25 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1WHF CGU A 26 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1WHF CGU A 29 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1WHF CGU A 32 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1WHF CGU A 35 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1WHF CGU A 39 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 1WHF BHD A 63 ASP (3S)-3-HYDROXY-L-ASPARTIC ACID
HET CGU A 6 17
HET CGU A 7 17
HET CGU A 14 17
HET CGU A 16 17
HET CGU A 19 17
HET CGU A 20 17
HET CGU A 25 17
HET CGU A 26 17
HET CGU A 29 17
HET CGU A 32 17
HET CGU A 35 17
HET CGU A 39 17
HET BHD A 63 13
HETNAM CGU GAMMA-CARBOXY-GLUTAMIC ACID
HETNAM BHD (3S)-3-HYDROXY-L-ASPARTIC ACID
HETSYN BHD BETA-HYDROXYASPARTIC ACID
FORMUL 1 CGU 12(C6 H9 N O6)
FORMUL 1 BHD C4 H7 N O5
HELIX 1 A1 LEU A 13 LEU A 18 1 6
HELIX 2 A2 CGU A 20 VAL A 30 1 11
HELIX 3 A3 ALA A 34 TRP A 41 1 8
SHEET 1 S1 2 GLY A 59 BHD A 63 0
SHEET 2 S1 2 TYR A 68 CYS A 72 -1
SHEET 1 S2 2 PHE A 76 GLU A 77 0
SHEET 2 S2 2 PHE A 83 SER A 84 -1
SSBOND 1 CYS A 17 CYS A 22 1555 1555 2.02
SSBOND 2 CYS A 50 CYS A 61 1555 1555 2.02
SSBOND 3 CYS A 55 CYS A 70 1555 1555 2.02
SSBOND 4 CYS A 72 CYS A 81 1555 1555 2.02
LINK N CGU A 6 C LEU A 5 1555 1555 1.30
LINK C CGU A 6 N CGU A 7 1555 1555 1.30
LINK C CGU A 7 N VAL A 8 1555 1555 1.31
LINK N CGU A 14 C LEU A 13 1555 1555 1.31
LINK C CGU A 14 N ARG A 15 1555 1555 1.30
LINK N CGU A 16 C ARG A 15 1555 1555 1.31
LINK C CGU A 16 N CYS A 17 1555 1555 1.31
LINK N CGU A 19 C LEU A 18 1555 1555 1.29
LINK C CGU A 19 N CGU A 20 1555 1555 1.30
LINK C CGU A 20 N ALA A 21 1555 1555 1.31
LINK N CGU A 25 C LEU A 24 1555 1555 1.30
LINK C CGU A 25 N CGU A 26 1555 1555 1.31
LINK C CGU A 26 N ALA A 27 1555 1555 1.31
LINK N CGU A 29 C ARG A 28 1555 1555 1.29
LINK C CGU A 29 N VAL A 30 1555 1555 1.32
LINK N CGU A 32 C PHE A 31 1555 1555 1.31
LINK C CGU A 32 N ASP A 33 1555 1555 1.30
LINK N CGU A 35 C ALA A 34 1555 1555 1.30
LINK C CGU A 35 N GLN A 36 1555 1555 1.31
LINK N CGU A 39 C ASP A 38 1555 1555 1.32
LINK C CGU A 39 N PHE A 40 1555 1555 1.30
LINK N BHD A 63 C LYS A 62 1555 1555 1.31
LINK C BHD A 63 N GLY A 64 1555 1555 1.31
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
