Header list of 1iou.pdb file
Complete list - b 23 2 Bytes
HEADER MEMBRANE PROTEIN 09-APR-01 1IOU TITLE SOLUTION STRUCTURE OF YKT6P (1-140) COMPND MOL_ID: 1; COMPND 2 MOLECULE: YKT6P; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-140; COMPND 5 SYNONYM: SYNAPTOBREVIN HOMOLOG 1; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 4 ORGANISM_TAXID: 4932; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SNARE, MEMBRANE PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.TOCHIO,M.M.K.TSUI,D.K.BANFIELD,M.ZHANG REVDAT 3 23-FEB-22 1IOU 1 REMARK SEQADV REVDAT 2 24-FEB-09 1IOU 1 VERSN REVDAT 1 06-MAY-03 1IOU 0 JRNL AUTH H.TOCHIO,M.M.K.TSUI,D.K.BANFIELD,M.ZHANG JRNL TITL AN AUTOINHIBITORY MECHANISM FOR NONSYNTAXIN SNARE PROTEINS JRNL TITL 2 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 : CNS 1.0, CNS 1.0 REMARK 3 AUTHORS : BRUNGER (CNS), BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1IOU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-APR-01. REMARK 100 THE DEPOSITION ID IS D_1000005130. 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 : 50MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1.5MM YKT6(1-140) U-15N,13C;50MM REMARK 210 PHOSPHATE BUFFER;20MM DTT;2MM REMARK 210 EDTA;D2O; 1.5MM YKT6(1-140) U- REMARK 210 15N;50MM PHOSPHATE BUFFER;20MM REMARK 210 DTT;2MM EDTA;10% D2O; 1.5MM REMARK 210 YKT6(1-140),13C;50MM PHOSPHATE REMARK 210 BUFFER;20MM DTT;2MM EDTA;D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING WITH TORSION REMARK 210 ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: NA 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 O TRP A 110 H ASP A 112 1.55 REMARK 500 O TRP A 110 N ASP A 112 2.14 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 11 96.30 -47.56 REMARK 500 1 LEU A 19 -73.35 -46.01 REMARK 500 1 PHE A 30 36.89 -81.77 REMARK 500 1 PHE A 31 -40.63 -140.35 REMARK 500 1 ALA A 53 153.29 59.66 REMARK 500 1 ASN A 63 40.00 -163.74 REMARK 500 1 GLN A 84 45.17 -90.83 REMARK 500 1 PRO A 86 144.82 -34.71 REMARK 500 1 PRO A 106 149.98 -27.62 REMARK 500 1 ALA A 111 -68.87 46.67 REMARK 500 1 VAL A 113 -62.63 70.94 REMARK 500 1 THR A 114 -1.59 66.68 REMARK 500 1 GLU A 115 109.40 -164.60 REMARK 500 1 ASN A 117 72.48 -115.29 REMARK 500 1 LEU A 120 27.31 -155.04 REMARK 500 1 MET A 122 60.78 67.21 REMARK 500 1 GLN A 133 -32.80 -33.27 REMARK 500 1 SER A 136 -55.68 -150.55 REMARK 500 1 GLN A 137 -17.03 82.67 REMARK 500 2 SER A 11 86.10 -62.94 REMARK 500 2 GLU A 18 -171.46 159.42 REMARK 500 2 LEU A 19 -123.47 36.44 REMARK 500 2 PHE A 30 30.68 -94.71 REMARK 500 2 PHE A 31 -47.37 -139.22 REMARK 500 2 ALA A 53 157.05 56.98 REMARK 500 2 ASN A 63 -45.21 -173.07 REMARK 500 2 ARG A 71 -178.54 -67.10 REMARK 500 2 GLU A 73 109.84 179.02 REMARK 500 2 GLN A 84 39.31 -89.41 REMARK 500 2 PRO A 86 150.69 -31.91 REMARK 500 2 ALA A 104 -19.96 -45.00 REMARK 500 2 HIS A 105 136.16 -175.24 REMARK 500 2 PRO A 106 169.50 -39.22 REMARK 500 2 ALA A 111 -66.72 46.77 REMARK 500 2 ASP A 112 63.42 -153.29 REMARK 500 2 VAL A 113 -32.81 -35.70 REMARK 500 2 THR A 114 27.18 40.74 REMARK 500 2 GLU A 115 41.80 -172.02 REMARK 500 2 ASN A 117 -156.03 -173.33 REMARK 500 2 LYS A 121 168.57 66.82 REMARK 500 2 MET A 122 72.58 -177.32 REMARK 500 2 LYS A 123 -28.78 -39.47 REMARK 500 2 GLN A 124 -75.63 -65.16 REMARK 500 2 GLN A 133 -22.32 -39.31 REMARK 500 2 SER A 136 77.09 -176.63 REMARK 500 2 ALA A 138 78.59 86.48 REMARK 500 3 ARG A 2 102.47 -165.95 REMARK 500 3 SER A 11 98.35 -58.63 REMARK 500 3 LEU A 19 -84.74 -75.05 REMARK 500 3 LEU A 25 74.77 -115.50 REMARK 500 REMARK 500 THIS ENTRY HAS 414 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1H8M RELATED DB: PDB REMARK 900 1H8M IS THE MINIMIZED AVERAGE STRUCTURE DBREF 1IOU A 1 140 UNP P36015 YKT6_YEAST 1 140 SEQADV 1IOU GLU A 55 UNP P36015 GLN 55 CONFLICT SEQADV 1IOU 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 ALA A 104 1 19 HELIX 3 3 PRO A 106 ALA A 111 1 6 HELIX 4 4 MET A 122 TYR A 132 1 11 HELIX 5 5 SER A 136 ALA A 140 5 5 SHEET 1 A 5 LYS A 15 LYS A 23 0 SHEET 2 A 5 TYR A 5 GLY A 12 -1 O ILE A 6 N VAL A 22 SHEET 3 A 5 CYS A 76 ILE A 80 -1 O CYS A 76 N PHE A 9 SHEET 4 A 5 TYR A 64 TYR A 69 -1 O HIS A 67 N LEU A 79 SHEET 5 A 5 ARG A 56 GLU A 61 -1 N GLN A 57 O VAL A 68 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