Header list of 1lb0.pdb file
Complete list - 23 202 Bytes
HEADER VIRAL PROTEIN 01-APR-02 1LB0 TITLE NMR STRUCTURE OF HIV-1 GP41 659-671 13-MER PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: GP41; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 659-671; COMPND 5 SYNONYM: TRANSMEMBRANE GLYCOPROTEIN; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE SOURCE 4 OF THE PEPTIDE IS NATURALLY FOUND IN HIV-1 VIRUS. KEYWDS 3-10 HELIX, GP41 ENVELOPE PROTEIN, VIRAL PROTEIN EXPDTA SOLUTION NMR AUTHOR Z.BIRON REVDAT 3 23-FEB-22 1LB0 1 REMARK REVDAT 2 24-FEB-09 1LB0 1 VERSN REVDAT 1 04-DEC-02 1LB0 0 JRNL AUTH Z.BIRON,S.KHARE,A.O.SAMSON,Y.HAYEK,F.NAIDER,J.ANGLISTER JRNL TITL A MONOMERIC 3(10)-HELIX IS FORMED IN WATER BY A 13-RESIDUE JRNL TITL 2 PEPTIDE REPRESENTING THE NEUTRALIZING DETERMINANT OF HIV-1 JRNL TITL 3 ON GP41(,). JRNL REF BIOCHEMISTRY V. 41 12687 2002 JRNL REFN ISSN 0006-2960 JRNL PMID 12379111 JRNL DOI 10.1021/BI026261Y REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AURELIA AMIX 2.8.11, CNS REMARK 3 AUTHORS : BRUKER (AURELIA), A.T.BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 212 RESTRAINTS, 202 ARE NOE- REMARK 3 DERIVED REMARK 3 DISTANCE CONSTRAINTS, 9 DIHEDRAL ANGLE RESTRAINTS,1 DISTANCE REMARK 3 RESTRAINT REMARK 3 FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1LB0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-02. REMARK 100 THE DEPOSITION ID IS D_1000015800. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 277 REMARK 210 PH : 7.7 REMARK 210 IONIC STRENGTH : 0.1MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 3.5MM GP41659-671; 50MM 50MM REMARK 210 AMMONIUM ACETATE BUFFER.; 5 MM REMARK 210 GP41659-671; 50MM 50MM AMMONIUM REMARK 210 ACETATE BUFFER REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.0, CNS 1.1 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING 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 DBREF 1LB0 A 1 13 UNP P31872 ENV_HV1W1 659 671 SEQRES 1 A 13 GLU LEU LEU GLU LEU ASP LYS TRP ALA SER LEU TRP ASN HELIX 1 1 LEU A 3 ASN A 13 5 11 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