Header list of 1bf9.pdb file
Complete list - v 29 2 Bytes
HEADER BLOOD COAGULATION 28-MAY-98 1BF9
TITLE N-TERMINAL EGF-LIKE DOMAIN FROM HUMAN FACTOR VII, NMR, 23 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FACTOR VII;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL EGF-LIKE DOMAIN;
COMPND 5 EC: 3.4.21.21;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: BLOOD
KEYWDS BLOOD COAGULATION, EGF, HYDROLASE, SERINE PROTEASE
EXPDTA SOLUTION NMR
NUMMDL 23
AUTHOR A.MURANYI,B.E.FINN,G.P.GIPPERT,S.FORSEN,J.STENFLO,T.DRAKENBERG
REVDAT 3 29-NOV-17 1BF9 1 REMARK HELIX
REVDAT 2 24-FEB-09 1BF9 1 VERSN
REVDAT 1 16-FEB-99 1BF9 0
JRNL AUTH A.MURANYI,B.E.FINN,G.P.GIPPERT,S.FORSEN,J.STENFLO,
JRNL AUTH 2 T.DRAKENBERG
JRNL TITL SOLUTION STRUCTURE OF THE N-TERMINAL EGF-LIKE DOMAIN FROM
JRNL TITL 2 HUMAN FACTOR VII.
JRNL REF BIOCHEMISTRY V. 37 10605 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9692950
JRNL DOI 10.1021/BI980522F
REMARK 1
REMARK 1 REFERENCE 1
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 REFERENCE 2
REMARK 1 AUTH M.BARON,D.G.NORMAN,T.S.HARVEY,P.A.HANDFORD,M.MAYHEW,A.G.TSE,
REMARK 1 AUTH 2 G.G.BROWNLEE,I.D.CAMPBELL
REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF THE FIRST EGF-LIKE MODULE
REMARK 1 TITL 2 OF HUMAN FACTOR IX: COMPARISON WITH EGF AND TGF-ALPHA
REMARK 1 REF PROTEIN SCI. V. 1 81 1992
REMARK 1 REFN ISSN 0961-8368
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 : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BF9 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_1000171685.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.6
REMARK 210 IONIC STRENGTH : NO SALT ADDED
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : H2O AND D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; 2Q; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : OMEGA; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : GE; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY EMBEDDING
REMARK 210 WITHOUT METRIZATION FOLLOWED BY
REMARK 210 RESTRAINED SIMULATED ANNEALING
REMARK 210 AND SIMULATED ANNEALING
REMARK 210 REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO DISTANCE RESTRAINT VIOLATED
REMARK 210 BY MORE THAN 0.2 ANGSTROM AND NO
REMARK 210 DIHEDRAL ANGLE RESTRAINTS
REMARK 210 VIOLATED BY MORE THAN 2 DEGREES
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: 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 46 109.49 61.74
REMARK 500 1 CYS A 50 43.70 -83.55
REMARK 500 1 SER A 53 70.49 50.91
REMARK 500 1 GLN A 64 -165.64 -103.79
REMARK 500 1 SER A 67 -112.44 179.36
REMARK 500 1 CYS A 72 179.43 -58.41
REMARK 500 1 THR A 83 76.71 -104.24
REMARK 500 2 ASP A 48 -89.63 -60.91
REMARK 500 2 GLN A 49 -58.73 -129.15
REMARK 500 2 LEU A 65 -82.03 -51.02
REMARK 500 2 GLN A 66 -31.42 -36.18
REMARK 500 2 SER A 67 -153.43 169.91
REMARK 500 2 CYS A 72 -159.53 41.13
REMARK 500 3 GLN A 49 -83.13 40.53
REMARK 500 3 CYS A 50 43.23 -80.79
REMARK 500 3 SER A 53 86.30 67.74
REMARK 500 3 CYS A 55 151.69 -42.45
REMARK 500 3 SER A 67 -134.90 179.63
REMARK 500 3 CYS A 72 -160.53 -105.43
REMARK 500 3 GLU A 77 114.82 -170.21
REMARK 500 3 ASN A 80 19.54 -152.20
REMARK 500 3 THR A 83 75.82 -118.04
REMARK 500 4 ASP A 48 -83.64 -175.07
REMARK 500 4 SER A 53 76.93 67.52
REMARK 500 4 SER A 67 -131.13 -178.96
REMARK 500 4 CYS A 72 -159.27 -74.92
REMARK 500 4 ASN A 80 27.75 -152.71
REMARK 500 4 THR A 83 67.67 -111.92
REMARK 500 5 ASP A 46 -100.75 -179.37
REMARK 500 5 ASP A 48 -82.82 -176.50
REMARK 500 5 SER A 52 18.93 -149.50
REMARK 500 5 SER A 53 72.60 54.29
REMARK 500 5 SER A 67 -123.59 179.04
REMARK 500 5 CYS A 72 177.82 -59.25
REMARK 500 5 GLU A 77 113.82 -167.22
REMARK 500 5 ASN A 80 21.89 -140.07
REMARK 500 5 CYS A 81 18.93 53.98
REMARK 500 6 ASP A 48 -99.89 -178.19
REMARK 500 6 GLN A 49 -59.03 -130.43
REMARK 500 6 CYS A 50 41.22 -81.57
REMARK 500 6 SER A 53 75.07 58.26
REMARK 500 6 GLN A 64 -165.07 -106.79
REMARK 500 6 SER A 67 -132.90 -178.17
REMARK 500 6 CYS A 72 -175.37 -56.97
REMARK 500 6 GLU A 77 -36.14 -161.67
REMARK 500 6 THR A 83 66.41 -103.97
REMARK 500 6 HIS A 84 108.13 -50.20
REMARK 500 7 ASP A 46 -40.16 -163.31
REMARK 500 7 ASP A 48 117.88 58.87
REMARK 500 7 SER A 53 77.46 58.97
REMARK 500
REMARK 500 THIS ENTRY HAS 190 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 79 0.24 SIDE CHAIN
REMARK 500 2 ARG A 79 0.30 SIDE CHAIN
REMARK 500 3 ARG A 79 0.31 SIDE CHAIN
REMARK 500 4 ARG A 79 0.20 SIDE CHAIN
REMARK 500 5 ARG A 79 0.25 SIDE CHAIN
REMARK 500 6 ARG A 79 0.18 SIDE CHAIN
REMARK 500 7 ARG A 79 0.23 SIDE CHAIN
REMARK 500 8 ARG A 79 0.31 SIDE CHAIN
REMARK 500 9 ARG A 79 0.18 SIDE CHAIN
REMARK 500 10 ARG A 79 0.28 SIDE CHAIN
REMARK 500 11 ARG A 79 0.29 SIDE CHAIN
REMARK 500 12 ARG A 79 0.30 SIDE CHAIN
REMARK 500 13 ARG A 79 0.16 SIDE CHAIN
REMARK 500 14 ARG A 79 0.25 SIDE CHAIN
REMARK 500 15 ARG A 79 0.32 SIDE CHAIN
REMARK 500 16 ARG A 79 0.13 SIDE CHAIN
REMARK 500 17 ARG A 79 0.29 SIDE CHAIN
REMARK 500 18 ARG A 79 0.32 SIDE CHAIN
REMARK 500 19 ARG A 79 0.29 SIDE CHAIN
REMARK 500 20 ARG A 79 0.27 SIDE CHAIN
REMARK 500 21 ARG A 79 0.28 SIDE CHAIN
REMARK 500 22 ARG A 79 0.09 SIDE CHAIN
REMARK 500 23 ARG A 79 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BF9 A 45 85 UNP P08709 FA7_HUMAN 105 145
SEQRES 1 A 41 SER ASP GLY ASP GLN CYS ALA SER SER PRO CYS GLN ASN
SEQRES 2 A 41 GLY GLY SER CYS LYS ASP GLN LEU GLN SER TYR ILE CYS
SEQRES 3 A 41 PHE CYS LEU PRO ALA PHE GLU GLY ARG ASN CYS GLU THR
SEQRES 4 A 41 HIS LYS
HELIX 1 1 ASP A 48 SER A 52 5 5
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
Complete list - v 29 2 Bytes