Header list of 1myu.pdb file
Complete list - 9 20 Bytes
HEADER NEUROPEPTIDE 04-OCT-02 1MYU
TITLE LIPID INDUCED CONFORMATION OF THE TACHYKININ PEPTIDE KASSININ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KASSININ;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: KASSINA SENEGALENSIS;
SOURCE 4 ORGANISM_TAXID: 8415
KEYWDS HELICAL CORE, 3-10 HELIX, LIPID INDUCED CONFORMATION, DPC MICELLES,
KEYWDS 2 NEUROPEPTIDE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.C.GRACE,A.M.LYNN,S.M.COWSIK
REVDAT 3 09-OCT-19 1MYU 1 SOURCE JRNL REMARK ATOM
REVDAT 2 24-FEB-09 1MYU 1 VERSN
REVDAT 1 16-OCT-02 1MYU 0
JRNL AUTH R.C.GRACE,A.M.LYNN,S.M.COWSIK
JRNL TITL LIPID INDUCED CONFORMATION OF THE TACHYKININ PEPTIDE
JRNL TITL 2 KASSININ.
JRNL REF J.BIOMOL.STRUCT.DYN. V. 18 623-5 2001
JRNL REFN ISSN 0739-1102
JRNL PMID 11245256
JRNL DOI 10.1080/07391102.2001.10506693
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 95.0, DYANA 1.5
REMARK 3 AUTHORS : MSI (FELIX), GUNTERT, P., AND K. WTHRICH (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 150 RESTRAINTS, 142 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 8 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1MYU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017308.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NO SALTS USED
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 5MG OF KASSININ IN 0.4ML 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 : AM
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
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 1MYU A 1 12 UNP P08611 TKN_KASSE 1 12
SEQRES 1 A 12 ASP VAL PRO LYS SER ASP GLN PHE VAL GLY LEU MET
HELIX 1 1 PRO A 3 MET A 12 1 10
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 - 9 20 Bytes