Header list of 1n6t.pdb file
Complete list - 6 20 Bytes
HEADER NEUROPEPTIDE 12-NOV-02 1N6T TITLE SOLUTION STRUCTURE OF THE TACHYKININ PEPTIDE NEUROKININ A COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUROKININ A; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN MAMMALIAN NEURONAL SOURCE 4 TISSUE. KEYWDS HELIX, 3 10 HELIX, LIPID INDUCED CONFORMATION, DPC MICELLES, KEYWDS 2 NEUROPEPTIDE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR I.R.CHANDRASHEKAR,S.M.COWSIK REVDAT 3 06-NOV-19 1N6T 1 JRNL REMARK REVDAT 2 24-FEB-09 1N6T 1 VERSN REVDAT 1 16-DEC-03 1N6T 0 JRNL AUTH I.R.CHANDRASHEKAR,S.M.COWSIK JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE MAMMALIAN TACHYKININ JRNL TITL 2 PEPTIDE NEUROKININ A BOUND TO LIPID MICELLES. JRNL REF BIOPHYS.J. V. 85 4002 2003 JRNL REFN ISSN 0006-3495 JRNL PMID 14645089 JRNL DOI 10.1016/S0006-3495(03)74814-0 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5 REMARK 3 AUTHORS : P.GUNTERT, C.MUMENTHALER, K.WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1N6T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-NOV-02. REMARK 100 THE DEPOSITION ID IS D_1000017590. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 305 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : NO SALTS USED REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 5MG OF NEUROKININ A IN 0.5ML OF REMARK 210 WATER (90% H2O, 10% D2O, PH 5.0) REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.1 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED REMARK 210 ANNEALING(DYANA) REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 1N6T A 1 10 UNP P19851 TKNB_CHICK 1 10 SEQRES 1 A 10 HIS LYS THR ASP SER PHE VAL GLY LEU MET HELIX 1 1 THR A 3 MET A 10 5 8 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 - 6 20 Bytes