Header list of 1hs7.pdb file
Complete list - b 23 2 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS 24-DEC-00 1HS7
TITLE VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNTAXIN VAM3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 23-119;
COMPND 5 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-KT
KEYWDS UP-AND-DOWN THREE-HELIX BUNDLE INSERTION PRECEDING PROLINE IN AN
KEYWDS 2 ALPHA-HELIX, ENDOCYTOSIS-EXOCYTOSIS COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR I.DULUBOVA,T.YAMAGUCHI,Y.WANG,T.C.SUDHOF,J.RIZO
REVDAT 3 23-FEB-22 1HS7 1 REMARK
REVDAT 2 24-FEB-09 1HS7 1 VERSN
REVDAT 1 07-MAR-01 1HS7 0
JRNL AUTH I.DULUBOVA,T.YAMAGUCHI,Y.WANG,T.C.SUDHOF,J.RIZO
JRNL TITL VAM3P STRUCTURE REVEALS CONSERVED AND DIVERGENT PROPERTIES
JRNL TITL 2 OF SYNTAXINS.
JRNL REF NAT.STRUCT.BIOL. V. 8 258 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11224573
JRNL DOI 10.1038/85012
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, CNS 0.9
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1771 TOTAL EXPERIMENTAL RESTRAINTS,
REMARK 3 1565 NOE DISTANCE RESTRAINTS, 130 HYDROGEN BOND RESTRAINTS, 76
REMARK 3 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1HS7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1000012558.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : 20 MM PHOSPHATE; 20 MM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.9 MM 15N-LABELED VAM3P N
REMARK 210 -TERMINAL DOMAIN; 20 MM
REMARK 210 PHOSPHATE PH 6.0, 30 C; 0.8 MM
REMARK 210 15N,13C-LABELED VAM3P N-TERMINAL
REMARK 210 DOMAIN; 20 MM PHOSPHATE PH 6.0,
REMARK 210 30 C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D
REMARK 210 NOESY; HNHA; 3D_13C-SEPARATED_
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7, NMRVIEW 4.1, CNS
REMARK 210 0.9
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST NOE
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE
REMARK 210 SPECTROSCOPY
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 ARG A 76 H GLU A 80 1.54
REMARK 500 O TYR A 62 H THR A 66 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
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 LYS A 54 -70.51 65.84
REMARK 500 1 ASP A 56 101.72 -42.35
REMARK 500 1 GLU A 67 -48.67 -136.54
REMARK 500 1 LEU A 68 -88.55 -70.91
REMARK 500 1 ASP A 94 -71.36 -47.34
REMARK 500 1 PHE A 116 65.90 -109.83
REMARK 500 2 LYS A 54 -65.40 68.11
REMARK 500 2 ASP A 56 119.22 -39.58
REMARK 500 2 GLU A 67 -46.90 -136.60
REMARK 500 2 LEU A 68 -89.08 -72.66
REMARK 500 2 ASP A 94 -71.27 -48.06
REMARK 500 2 PHE A 116 74.05 -118.13
REMARK 500 2 PRO A 117 -178.24 -66.00
REMARK 500 3 LYS A 54 -72.34 64.26
REMARK 500 3 ASP A 56 122.21 -39.96
REMARK 500 3 GLU A 67 -50.62 -133.62
REMARK 500 3 LEU A 68 -88.14 -69.38
REMARK 500 3 ASP A 94 -71.03 -48.92
REMARK 500 3 PHE A 116 73.74 -118.13
REMARK 500 3 PRO A 117 176.79 -57.18
REMARK 500 4 LYS A 54 -77.03 62.97
REMARK 500 4 ASP A 56 107.23 -38.00
REMARK 500 4 GLU A 67 -40.46 -135.64
REMARK 500 4 LEU A 68 -87.30 -68.67
REMARK 500 4 ASP A 94 -70.50 -47.64
REMARK 500 4 PHE A 116 66.28 -110.90
REMARK 500 5 LYS A 54 -65.10 68.03
REMARK 500 5 GLU A 67 -47.10 -137.20
REMARK 500 5 LEU A 68 -88.72 -72.31
REMARK 500 5 ASP A 94 -71.10 -49.04
REMARK 500 5 PHE A 116 73.64 -117.22
REMARK 500 5 PRO A 117 -168.94 -58.29
REMARK 500 6 LYS A 54 -75.64 62.88
REMARK 500 6 ASP A 56 107.56 -35.36
REMARK 500 6 GLU A 67 -52.56 -131.39
REMARK 500 6 LEU A 68 -88.28 -65.45
REMARK 500 6 ASP A 94 -71.25 -48.67
REMARK 500 6 PHE A 116 66.41 -112.47
REMARK 500 7 GLU A 67 -48.86 -136.75
REMARK 500 7 LEU A 68 -89.05 -69.79
REMARK 500 7 ASP A 94 -72.13 -47.30
REMARK 500 7 PHE A 116 74.31 -119.22
REMARK 500 7 PRO A 117 -160.46 -64.37
REMARK 500 8 LYS A 54 -68.32 66.74
REMARK 500 8 ASP A 56 117.71 -34.39
REMARK 500 8 GLU A 67 -49.18 -134.38
REMARK 500 8 LEU A 68 -87.52 -70.04
REMARK 500 8 ASP A 94 -71.47 -48.76
REMARK 500 8 PHE A 116 72.77 -115.87
REMARK 500 8 PRO A 117 179.44 -50.32
REMARK 500
REMARK 500 THIS ENTRY HAS 122 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1HS7 A 23 119 UNP Q12241 VAM3_YEAST 23 119
SEQRES 1 A 97 THR ASN GLN LYS THR LYS GLU LEU SER ASN LEU ILE GLU
SEQRES 2 A 97 THR PHE ALA GLU GLN SER ARG VAL LEU GLU LYS GLU CYS
SEQRES 3 A 97 THR LYS ILE GLY SER LYS ARG ASP SER LYS GLU LEU ARG
SEQRES 4 A 97 TYR LYS ILE GLU THR GLU LEU ILE PRO ASN CYS THR SER
SEQRES 5 A 97 VAL ARG ASP LYS ILE GLU SER ASN ILE LEU ILE HIS GLN
SEQRES 6 A 97 ASN GLY LYS LEU SER ALA ASP PHE LYS ASN LEU LYS THR
SEQRES 7 A 97 LYS TYR GLN SER LEU GLN GLN SER TYR ASN GLN ARG LYS
SEQRES 8 A 97 SER LEU PHE PRO LEU LYS
HELIX 1 1 ASN A 24 ILE A 51 1 28
HELIX 2 2 SER A 57 GLU A 67 1 11
HELIX 3 3 GLU A 67 ASN A 82 1 16
HELIX 4 4 ILE A 83 ASN A 88 1 6
HELIX 5 5 ASN A 88 PHE A 116 1 29
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