Header list of 1jav.pdb file
Complete list - 23 202 Bytes
HEADER VIRAL PROTEIN 31-MAY-01 1JAV
TITLE AVERAGE NMR SOLUTION STRUCTURE OF THE TRP-RICH PEPTIDE OF HIV GP41
TITLE 2 BOUND TO DPC MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSMEMBRANE GLYCOPROTEIN (GP41);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 665-683;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THE PEPTIDE IS NATURALLY FOUND IN HUMAN IMMUNODEFICIENCY VIRUS
SOURCE 5 (HIV).
KEYWDS AMPHIPATHIC ALPHA HELIX, VIRAL PROTEIN
EXPDTA SOLUTION NMR
AUTHOR D.J.SCHIBLI,R.C.MONTELARO,H.J.VOGEL
REVDAT 3 23-FEB-22 1JAV 1 REMARK LINK
REVDAT 2 24-FEB-09 1JAV 1 VERSN
REVDAT 1 17-OCT-01 1JAV 0
JRNL AUTH D.J.SCHIBLI,R.C.MONTELARO,H.J.VOGEL
JRNL TITL THE MEMBRANE-PROXIMAL TRYPTOPHAN-RICH REGION OF THE HIV
JRNL TITL 2 GLYCOPROTEIN, GP41, FORMS A WELL-DEFINED HELIX IN
JRNL TITL 3 DODECYLPHOSPHOCHOLINE MICELLES.
JRNL REF BIOCHEMISTRY V. 40 9570 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11583156
JRNL DOI 10.1021/BI010640U
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), A.T.BRUNGER, P.D.ADAMS,
REMARK 3 G.M.CLORE, W.L.DELANO, P.GROS, R.W.GROSSE-
REMARK 3 KUNSTLEVE, J.-S.JIANG, J.KUSZEWSKI, M.NILGES,
REMARK 3 N.S.PANNU, R.J.READ, L.M.RICE, T.SIMONSON,
REMARK 3 G.L.WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 STRUCTURES WERE INITIALLY GENERATED USING CNS. AMBIGUOUS AND
REMARK 3 UNASSIGNED NOE CONSTRAINTS
REMARK 3 WERE THEN USED IN CONJUCTION WITH MATRIX RELAXATION ANALYSIS USING
REMARK 3 THE PROGRAM ARIA.
REMARK 4
REMARK 4 1JAV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013567.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 3.51
REMARK 210 IONIC STRENGTH : 200 MM DPC-D38
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.6 MM SYNTHETIC GP41 PEPTIDE,
REMARK 210 200 MM PERDEUTERATED
REMARK 210 DODECYLPHOSPHOCHOLINE; 1.6 MM
REMARK 210 SYNTHETIC GP41 PEPTIDE, 200 MM
REMARK 210
REMARK 210 PERDEUTERATED DODECYLPHOSPHOCHOLIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.8, NMRVIEW 4.1.3, CNS
REMARK 210 1.0, ARIA 1.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 MATRIX RELAXATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: 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 TRP A 2 4.98 -69.61
REMARK 500 ALA A 3 5.45 -68.08
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 20
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JAU RELATED DB: PDB
REMARK 900 ENSEMBLE OF 40 NMR DERIVED STRUCTURES FOR THIS DEPOSITION
DBREF 1JAV A 1 19 UNP P04624 ENV_HV1H3 665 683
SEQRES 1 A 20 LYS TRP ALA SER LEU TRP ASN TRP PHE ASN ILE THR ASN
SEQRES 2 A 20 TRP LEU TRP TYR ILE LYS NH2
HET NH2 A 20 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 LYS A 1 SER A 4 5 4
HELIX 2 2 LEU A 5 ASN A 10 1 6
HELIX 3 3 ASN A 10 LYS A 19 1 10
LINK C LYS A 19 N NH2 A 20 1555 1555 1.33
SITE 1 AC1 2 ILE A 18 LYS A 19
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 - 23 202 Bytes