Header list of 1d7n.pdb file
Complete list - 16 20 Bytes
HEADER TOXIN 19-OCT-99 1D7N
TITLE SOLUTION STRUCTURE ANALYSIS OF THE MASTOPARAN WITH DETERGENTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (WASP VENOM PEPTIDE (MASTOPARAN));
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VESPULA LEWISII;
SOURCE 3 ORGANISM_TAXID: 7452;
SOURCE 4 SECRETION: VENOM
KEYWDS SODIUM DODECYL SULFATE BOUND CONFORMATION, IMMUNE SYSTEM, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR Y.HORI,M.DEMURA,M.IWADATE,T.NIIDOME,H.AOYAGI,T.ASAKURA
REVDAT 3 16-FEB-22 1D7N 1 REMARK LINK
REVDAT 2 24-FEB-09 1D7N 1 VERSN
REVDAT 1 20-JUN-01 1D7N 0
JRNL AUTH Y.HORI,M.DEMURA,M.IWADATE,A.S.ULRICH,T.NIIDOME,H.AOYAGI,
JRNL AUTH 2 T.ASAKURA
JRNL TITL INTERACTION OF MASTOPARAN WITH MEMBRANES STUDIED BY 1H-NMR
JRNL TITL 2 SPECTROSCOPY IN DETERGENT MICELLES AND BY SOLID-STATE 2H-NMR
JRNL TITL 3 AND 15N-NMR SPECTROSCOPY IN ORIENTED LIPID BILAYERS.
JRNL REF EUR.J.BIOCHEM. V. 268 302 2001
JRNL REFN ISSN 0014-2956
JRNL PMID 11168364
JRNL DOI 10.1046/J.1432-1033.2001.01880.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII MSI NMRCHITECT 95.0
REMARK 3 AUTHORS : MSI
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 94 NOE-DERIVED DISTANCE CONSTRAINTS.
REMARK 4
REMARK 4 1D7N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1000009865.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303.15
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 5MM MASTOPARAN SODIUM DODECYL
REMARK 210 SULFATE- D25; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : A
REMARK 210 SPECTROMETER MANUFACTURER : JEOL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DGII MSI
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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: 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
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 2 ASN A 2 -33.14 83.68
REMARK 500 5 ASN A 2 53.64 -142.77
REMARK 500 6 ASN A 2 -71.39 -58.59
REMARK 500 6 LEU A 3 -56.43 91.68
REMARK 500 7 LEU A 3 -43.14 91.61
REMARK 500 7 LYS A 12 -76.98 -92.05
REMARK 500 7 ILE A 13 31.73 85.80
REMARK 500 8 ASN A 2 -72.99 -76.80
REMARK 500 8 LEU A 3 -38.97 88.66
REMARK 500 9 LEU A 3 -43.29 92.28
REMARK 500 10 LYS A 12 -75.70 -100.98
REMARK 500 10 ILE A 13 20.12 85.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 15
DBREF 1D7N A 1 14 UNP P01514 MAST_VESLE 1 14
SEQRES 1 A 15 ILE ASN LEU LYS ALA LEU ALA ALA LEU ALA LYS LYS ILE
SEQRES 2 A 15 LEU NH2
HET NH2 A 15 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 LEU A 3 LYS A 12 1 10
LINK C LEU A 14 N NH2 A 15 1555 1555 1.33
SITE 1 AC1 1 LEU A 14
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 - 16 20 Bytes