Header list of 1h8m.pdb file
Complete list - 25 20 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS 10-FEB-01 1H8M
TITLE SOLUTION STRUCTURE OF YKT6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNAPTOBREVIN HOMOLOG 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932
KEYWDS ENDOCYTOSIS/EXOCYTOSIS, TRANSMEMBRANE LIPOPROTEIN,
KEYWDS 2 PRENYLATION
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR H.TOCHIO,M.M.K.TSUI,D.K.BANFIELD,M.ZHANG
REVDAT 3 24-FEB-09 1H8M 1 VERSN
REVDAT 2 04-JUL-03 1H8M 1 SOURCE
REVDAT 1 07-AUG-01 1H8M 0
JRNL AUTH H.TOCHIO,M.M.K.TSUI,D.K.BANFIELD,M.ZHANG
JRNL TITL AN AUTOINHIBITORY MECHANISM FOR NONSYNTAXIN SNARE
JRNL TITL 2 PROTEINS REVEALED BY THE STRUCTURE OF YKT6P
JRNL REF SCIENCE V. 293 698 2001
JRNL REFN ISSN 0036-8075
JRNL PMID 11474112
JRNL DOI 10.1126/SCIENCE.1062950
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : 1.0
REMARK 3 AUTHORS : BRUNGER STRUCTURAL STATISTICS: RMSD SD NOE
REMARK 3 DISTANCE RESTRAINTS (2350) 0.025 A 0.001 A
REMARK 3 DIHEDRAL ANGLE RESTRAINTS (157) 0.584 DEG 0.036
REMARK 3 DEG BONDS 0.003 A 0.000 A ANGLES 0.435 DEG 0.012
REMARK 3 DEG IMPROPERS 0.336 DEG 0.014 DEG DIHEDRALS
REMARK 3 29.969 DEG 0.887 DEG ENOE -30.74 40.95 ECDIH
REMARK 3 3.28 0.40 EBOND 14.68 1.25 EANGLE 115.61 6.40 EI
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1H8M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-FEB-01.
REMARK 100 THE PDBE ID CODE IS EBI-5885.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
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 : NULL
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 HB ILE A 6 - HG13 ILE A 129 1.58
REMARK 500 HB VAL A 8 - HB3 LEU A 19 1.56
REMARK 500 HE1 PHE A 9 - HB VAL A 78 1.59
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 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 GLU A 18 104.16 -49.77
REMARK 500 LEU A 25 74.10 -114.02
REMARK 500 ASN A 63 -42.59 -179.73
REMARK 500 SER A 72 36.35 -98.57
REMARK 500 PRO A 86 161.29 -47.53
REMARK 500 PRO A 106 149.46 -33.00
REMARK 500 ALA A 111 55.52 37.24
REMARK 500 ASP A 112 -38.63 100.86
REMARK 500 VAL A 113 104.85 59.45
REMARK 500 GLU A 115 96.96 -161.94
REMARK 500 ASN A 117 177.80 175.55
REMARK 500 LYS A 121 178.90 61.75
REMARK 500 MET A 122 105.33 -165.00
REMARK 500 GLN A 124 -70.79 -66.82
REMARK 500 GLN A 133 -36.39 -39.01
REMARK 500 ASP A 134 -173.51 -62.22
REMARK 500 SER A 136 -33.58 -150.10
REMARK 500 ASP A 139 60.94 60.98
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1H8M A 1 140 UNP P36015 YKT6_YEAST 1 140
SEQADV 1H8M GLU A 55 UNP P36015 GLN 55 CONFLICT
SEQADV 1H8M GLN A 84 UNP P36015 GLU 84 CONFLICT
SEQRES 1 A 140 MET ARG ILE TYR TYR ILE GLY VAL PHE ARG SER GLY GLY
SEQRES 2 A 140 GLU LYS ALA LEU GLU LEU SER GLU VAL LYS ASP LEU SER
SEQRES 3 A 140 GLN PHE GLY PHE PHE GLU ARG SER SER VAL GLY GLN PHE
SEQRES 4 A 140 MET THR PHE PHE ALA GLU THR VAL ALA SER ARG THR GLY
SEQRES 5 A 140 ALA GLY GLU ARG GLN SER ILE GLU GLU GLY ASN TYR ILE
SEQRES 6 A 140 GLY HIS VAL TYR ALA ARG SER GLU GLY ILE CYS GLY VAL
SEQRES 7 A 140 LEU ILE THR ASP LYS GLN TYR PRO VAL ARG PRO ALA TYR
SEQRES 8 A 140 THR LEU LEU ASN LYS ILE LEU ASP GLU TYR LEU VAL ALA
SEQRES 9 A 140 HIS PRO LYS GLU GLU TRP ALA ASP VAL THR GLU THR ASN
SEQRES 10 A 140 ASP ALA LEU LYS MET LYS GLN LEU ASP THR TYR ILE SER
SEQRES 11 A 140 LYS TYR GLN ASP PRO SER GLN ALA ASP ALA
HELIX 1 1 PHE A 31 THR A 51 1 21
HELIX 2 2 PRO A 86 HIS A 105 1 20
HELIX 3 3 PRO A 106 ALA A 111 1 6
HELIX 4 4 MET A 122 TYR A 132 1 11
SHEET 1 A 5 ALA A 16 LYS A 23 0
SHEET 2 A 5 ILE A 3 SER A 11 -1 O ILE A 6 N VAL A 22
SHEET 3 A 5 ILE A 75 THR A 81 -1 O CYS A 76 N PHE A 9
SHEET 4 A 5 ILE A 65 TYR A 69 -1 O ILE A 65 N THR A 81
SHEET 5 A 5 ILE A 59 GLU A 60 -1 N ILE A 59 O GLY A 66
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
Complete list - 25 20 Bytes