Header list of 1whe.pdb file
Complete list - v 29 2 Bytes
HEADER GLYCOPROTEIN 18-JUN-96 1WHE TITLE COAGULATION FACTOR, NMR, 20 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 APO FORM OF THE FRAGMENT CONTAINING THE GLA AND N- COMPND 6 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 20 AUTHOR M.SUNNERHAGEN,G.A.OLAH,J.STENFLO,S.FORSEN,T.DRAKENBERG,J.TREWHELLA REVDAT 4 29-NOV-17 1WHE 1 HELIX REVDAT 3 20-JUN-12 1WHE 1 HETNAM VERSN REVDAT 2 24-FEB-09 1WHE 1 VERSN REVDAT 1 15-MAY-97 1WHE 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 1WHE 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_1000177194. 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 : 20 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: 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 1 TYR A 68 CB - CG - CD2 ANGL. DEV. = -4.1 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 1 ASN A 2 -168.06 51.13 REMARK 500 1 SER A 3 -39.20 -152.29 REMARK 500 1 PHE A 4 -83.58 -75.15 REMARK 500 1 LEU A 5 179.24 -58.05 REMARK 500 1 CGU A 6 -74.07 79.12 REMARK 500 1 GLN A 10 177.22 170.74 REMARK 500 1 ASN A 12 -133.32 -169.66 REMARK 500 1 LEU A 13 -33.02 -151.19 REMARK 500 1 CGU A 14 -66.83 -155.54 REMARK 500 1 LEU A 18 45.23 -102.97 REMARK 500 1 CGU A 19 -158.32 -145.83 REMARK 500 1 LEU A 24 36.02 -177.41 REMARK 500 1 CGU A 25 -91.81 -80.07 REMARK 500 1 VAL A 30 50.18 -90.17 REMARK 500 1 PHE A 31 -57.53 -127.35 REMARK 500 1 CGU A 32 -42.36 82.41 REMARK 500 1 ASP A 38 -101.89 -56.34 REMARK 500 1 CGU A 39 -55.42 -27.36 REMARK 500 1 PHE A 40 -77.36 -39.43 REMARK 500 1 TRP A 41 -95.57 -82.09 REMARK 500 1 SER A 42 52.83 33.20 REMARK 500 1 LYS A 43 54.21 78.86 REMARK 500 1 TYR A 44 82.32 -38.86 REMARK 500 1 ASP A 46 -150.63 31.08 REMARK 500 1 ASP A 48 18.41 56.10 REMARK 500 1 GLN A 49 101.00 23.48 REMARK 500 1 CYS A 50 13.62 99.22 REMARK 500 1 HIS A 53 102.78 50.77 REMARK 500 1 BHD A 63 145.51 57.67 REMARK 500 1 ILE A 65 113.89 -35.90 REMARK 500 1 CYS A 81 27.91 46.86 REMARK 500 2 ASN A 2 -179.90 167.24 REMARK 500 2 SER A 3 27.84 44.53 REMARK 500 2 PHE A 4 82.10 -66.98 REMARK 500 2 CGU A 6 -64.30 82.37 REMARK 500 2 GLN A 10 103.59 62.08 REMARK 500 2 ASN A 12 -146.68 -178.86 REMARK 500 2 LEU A 13 -106.92 -169.56 REMARK 500 2 CGU A 14 -62.46 -105.76 REMARK 500 2 LEU A 18 36.96 -90.21 REMARK 500 2 CYS A 22 163.80 -43.12 REMARK 500 2 LEU A 24 -65.74 82.63 REMARK 500 2 VAL A 30 54.35 -103.09 REMARK 500 2 PHE A 31 -49.85 -132.55 REMARK 500 2 CGU A 32 -47.65 85.05 REMARK 500 2 THR A 37 -29.08 -38.67 REMARK 500 2 ASP A 38 -86.83 -75.20 REMARK 500 2 PHE A 40 -80.68 -37.94 REMARK 500 2 TRP A 41 -88.97 -81.83 REMARK 500 2 SER A 42 -92.01 47.24 REMARK 500 REMARK 500 THIS ENTRY HAS 532 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1WHE A 1 86 UNP P00743 FA10_BOVIN 41 126 SEQADV 1WHE CGU A 6 UNP P00743 GLU 46 MODIFIED RESIDUE SEQADV 1WHE CGU A 7 UNP P00743 GLU 47 MODIFIED RESIDUE SEQADV 1WHE CGU A 14 UNP P00743 GLU 54 MODIFIED RESIDUE SEQADV 1WHE CGU A 16 UNP P00743 GLU 56 MODIFIED RESIDUE SEQADV 1WHE CGU A 19 UNP P00743 GLU 59 MODIFIED RESIDUE SEQADV 1WHE CGU A 20 UNP P00743 GLU 60 MODIFIED RESIDUE SEQADV 1WHE CGU A 25 UNP P00743 GLU 65 MODIFIED RESIDUE SEQADV 1WHE CGU A 26 UNP P00743 GLU 66 MODIFIED RESIDUE SEQADV 1WHE CGU A 29 UNP P00743 GLU 69 MODIFIED RESIDUE SEQADV 1WHE CGU A 32 UNP P00743 GLU 72 MODIFIED RESIDUE SEQADV 1WHE CGU A 35 UNP P00743 GLU 75 MODIFIED RESIDUE SEQADV 1WHE CGU A 39 UNP P00743 GLU 79 MODIFIED RESIDUE SEQADV 1WHE 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 1WHE CGU A 6 GLU GAMMA-CARBOXY-GLUTAMIC ACID MODRES 1WHE CGU A 7 GLU GAMMA-CARBOXY-GLUTAMIC ACID MODRES 1WHE CGU A 14 GLU GAMMA-CARBOXY-GLUTAMIC ACID MODRES 1WHE CGU A 16 GLU GAMMA-CARBOXY-GLUTAMIC ACID MODRES 1WHE CGU A 19 GLU GAMMA-CARBOXY-GLUTAMIC ACID MODRES 1WHE CGU A 20 GLU GAMMA-CARBOXY-GLUTAMIC ACID MODRES 1WHE CGU A 25 GLU GAMMA-CARBOXY-GLUTAMIC ACID MODRES 1WHE CGU A 26 GLU GAMMA-CARBOXY-GLUTAMIC ACID MODRES 1WHE CGU A 29 GLU GAMMA-CARBOXY-GLUTAMIC ACID MODRES 1WHE CGU A 32 GLU GAMMA-CARBOXY-GLUTAMIC ACID MODRES 1WHE CGU A 35 GLU GAMMA-CARBOXY-GLUTAMIC ACID MODRES 1WHE CGU A 39 GLU GAMMA-CARBOXY-GLUTAMIC ACID MODRES 1WHE 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 1.31 LINK C CGU A 6 N CGU A 7 1555 1555 1.31 LINK C CGU A 7 N VAL A 8 1555 1555 1.29 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 1.30 LINK C CGU A 16 N CYS A 17 1555 1555 1.30 LINK N CGU A 19 C LEU A 18 1555 1555 1.31 LINK C CGU A 19 N CGU A 20 1555 1555 1.31 LINK C CGU A 20 N ALA A 21 1555 1555 1.30 LINK N CGU A 25 C LEU A 24 1555 1555 1.31 LINK C CGU A 25 N CGU A 26 1555 1555 1.31 LINK C CGU A 26 N ALA A 27 1555 1555 1.30 LINK N CGU A 29 C ARG A 28 1555 1555 1.30 LINK C CGU A 29 N VAL A 30 1555 1555 1.31 LINK N CGU A 32 C PHE A 31 1555 1555 1.31 LINK C CGU A 32 N ASP A 33 1555 1555 1.31 LINK N CGU A 35 C ALA A 34 1555 1555 1.31 LINK C CGU A 35 N GLN A 36 1555 1555 1.31 LINK N CGU A 39 C ASP A 38 1555 1555 1.31 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 1.30 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
Complete list - v 29 2 Bytes