Header list of 1g4f.pdb file
Complete list - b 23 2 Bytes
HEADER SIGNALING PROTEIN 27-OCT-00 1G4F
TITLE NMR STRUCTURE OF THE FIFTH DOMAIN OF HUMAN BETA2-GLYCOPROTEIN I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA2-GLYCOPROTEIN I;
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;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS SHORT CONSENSUS REPEAT, SUSHI-DOMAIN, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.HOSHINO,Y.HAGIHARA,I.NISHII,T.YAMAZAKI,H.KATO,Y.GOTO
REVDAT 4 23-FEB-22 1G4F 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1G4F 1 VERSN
REVDAT 2 28-MAR-01 1G4F 1 JRNL
REVDAT 1 15-NOV-00 1G4F 0
JRNL AUTH M.HOSHINO,Y.HAGIHARA,I.NISHII,T.YAMAZAKI,H.KATO,Y.GOTO
JRNL TITL IDENTIFICATION OF THE PHOSPHOLIPID-BINDING SITE OF HUMAN
JRNL TITL 2 BETA(2)-GLYCOPROTEIN I DOMAIN V BY HETERONUCLEAR MAGNETIC
JRNL TITL 3 RESONANCE.
JRNL REF J.MOL.BIOL. V. 304 927 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 11124037
JRNL DOI 10.1006/JMBI.2000.4243
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.841, X-PLOR 3.841
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1402 RESTRAINTS, 1288 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 88
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 26 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS
REMARK 4
REMARK 4 1G4F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012219.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 0.12
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM BETA2-GLYCOPROTEIN I DOMAIN
REMARK 210 V U-15N; 20MM NA-PHOSPHATE
REMARK 210 BUFFER, PH 6.0; 90% H2O, 10% D2O;
REMARK 210 1MM BETA2-GLYCOPROTEIN I DOMAIN
REMARK 210 V U-15N,13C; 20MM NA-PHOSPHATE
REMARK 210 BUFFER, PD 6.0; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_ROESY; HNCO-TROSY;
REMARK 210 HMQC-J; HNHB; HN(CO)HB; N15-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 18
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 H CYS A 5 O MET A 31 1.48
REMARK 500 O ASP A 79 H ASP A 82 1.50
REMARK 500 H GLY A 34 O CYS A 56 1.50
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 LEU A 7 101.39 -40.84
REMARK 500 1 LYS A 11 41.32 -157.18
REMARK 500 1 PHE A 27 43.84 -109.62
REMARK 500 1 ASN A 29 40.13 -102.53
REMARK 500 1 ASP A 58 87.34 -50.51
REMARK 500 1 SER A 72 -91.25 47.29
REMARK 500 1 PHE A 75 -166.64 45.75
REMARK 500 1 TRP A 76 -167.23 63.33
REMARK 500 1 LYS A 77 32.69 -151.93
REMARK 500 1 THR A 78 80.53 -156.57
REMARK 500 1 SER A 81 -19.74 -49.28
REMARK 500 2 SER A 4 171.86 -49.49
REMARK 500 2 CYS A 5 -147.72 -100.77
REMARK 500 2 LEU A 7 99.32 -38.39
REMARK 500 2 LYS A 11 43.95 -160.36
REMARK 500 2 VAL A 14 -164.96 -117.56
REMARK 500 2 ASP A 53 145.17 -38.81
REMARK 500 2 ASP A 58 90.17 -33.58
REMARK 500 2 GLU A 62 78.72 -100.38
REMARK 500 2 VAL A 63 154.81 -43.62
REMARK 500 2 GLU A 69 86.08 -63.97
REMARK 500 2 PHE A 75 -154.28 -159.88
REMARK 500 2 LYS A 77 -36.61 -144.68
REMARK 500 2 THR A 78 87.66 47.00
REMARK 500 2 ASP A 79 -159.27 -87.62
REMARK 500 2 ALA A 80 -28.27 -39.43
REMARK 500 3 ALA A 3 -146.64 -86.34
REMARK 500 3 SER A 4 -157.78 -133.48
REMARK 500 3 LEU A 7 104.99 -45.41
REMARK 500 3 LYS A 11 40.20 -160.82
REMARK 500 3 ASN A 29 37.78 -99.86
REMARK 500 3 ASP A 58 73.56 -58.49
REMARK 500 3 HIS A 70 -68.62 -96.48
REMARK 500 3 SER A 71 -42.05 173.42
REMARK 500 3 SER A 72 99.70 63.69
REMARK 500 3 LEU A 73 -172.66 53.64
REMARK 500 3 TRP A 76 173.64 -59.82
REMARK 500 4 SER A 4 -155.95 -61.39
REMARK 500 4 CYS A 5 -163.25 -122.28
REMARK 500 4 LEU A 7 100.75 -41.14
REMARK 500 4 VAL A 9 -147.53 -106.23
REMARK 500 4 ASP A 58 98.61 -45.09
REMARK 500 4 PHE A 67 159.37 56.15
REMARK 500 4 LYS A 68 73.70 -110.30
REMARK 500 4 GLU A 69 -171.22 -64.38
REMARK 500 4 SER A 72 -141.97 -108.82
REMARK 500 4 LEU A 73 -160.33 46.26
REMARK 500 4 TRP A 76 55.63 -147.01
REMARK 500 4 THR A 78 72.34 52.45
REMARK 500 5 SER A 4 -172.69 -66.73
REMARK 500
REMARK 500 THIS ENTRY HAS 238 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 20 0.16 SIDE CHAIN
REMARK 500 2 ARG A 20 0.18 SIDE CHAIN
REMARK 500 3 ARG A 20 0.32 SIDE CHAIN
REMARK 500 4 ARG A 20 0.29 SIDE CHAIN
REMARK 500 5 ARG A 20 0.29 SIDE CHAIN
REMARK 500 6 ARG A 20 0.21 SIDE CHAIN
REMARK 500 7 ARG A 20 0.24 SIDE CHAIN
REMARK 500 8 ARG A 20 0.28 SIDE CHAIN
REMARK 500 9 ARG A 20 0.15 SIDE CHAIN
REMARK 500 10 ARG A 20 0.24 SIDE CHAIN
REMARK 500 11 ARG A 20 0.24 SIDE CHAIN
REMARK 500 12 ARG A 20 0.28 SIDE CHAIN
REMARK 500 13 ARG A 20 0.17 SIDE CHAIN
REMARK 500 14 ARG A 20 0.20 SIDE CHAIN
REMARK 500 15 ARG A 20 0.26 SIDE CHAIN
REMARK 500 16 ARG A 20 0.26 SIDE CHAIN
REMARK 500 17 ARG A 20 0.08 SIDE CHAIN
REMARK 500 18 ARG A 20 0.29 SIDE CHAIN
REMARK 500 19 ARG A 20 0.30 SIDE CHAIN
REMARK 500 20 ARG A 20 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G4G RELATED DB: PDB
REMARK 900 1G4G CONTAINS THE ENERGY MINIMIZED AVERAGE STRUCTURE OF THIS ENTRY
DBREF 1G4F A 1 86 UNP P02749 APOH_HUMAN 260 345
SEQADV 1G4F THR A 1 UNP P02749 CYS 260 CONFLICT
SEQADV 1G4F LEU A 7 UNP P02749 VAL 266 VARIANT
SEQRES 1 A 86 THR LYS ALA SER CYS LYS LEU PRO VAL LYS LYS ALA THR
SEQRES 2 A 86 VAL VAL TYR GLN GLY GLU ARG VAL LYS ILE GLN GLU LYS
SEQRES 3 A 86 PHE LYS ASN GLY MET LEU HIS GLY ASP LYS VAL SER PHE
SEQRES 4 A 86 PHE CYS LYS ASN LYS GLU LYS LYS CYS SER TYR THR GLU
SEQRES 5 A 86 ASP ALA GLN CYS ILE ASP GLY THR ILE GLU VAL PRO LYS
SEQRES 6 A 86 CYS PHE LYS GLU HIS SER SER LEU ALA PHE TRP LYS THR
SEQRES 7 A 86 ASP ALA SER ASP VAL LYS PRO CYS
HELIX 1 1 ILE A 23 PHE A 27 1 5
HELIX 2 2 ASP A 79 VAL A 83 5 5
SHEET 1 A 2 THR A 13 TYR A 16 0
SHEET 2 A 2 GLU A 19 LYS A 22 -1 O GLU A 19 N TYR A 16
SHEET 1 B 3 LYS A 36 ASN A 43 0
SHEET 2 B 3 CYS A 48 ILE A 57 -1 O CYS A 48 N ASN A 43
SHEET 3 B 3 THR A 60 ILE A 61 -1 O THR A 60 N ILE A 57
SSBOND 1 CYS A 5 CYS A 56 1555 1555 2.02
SSBOND 2 CYS A 41 CYS A 66 1555 1555 2.02
SSBOND 3 CYS A 48 CYS A 86 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 - b 23 2 Bytes