Header list of 1mxq.pdb file
Complete list - 25 20 Bytes
HEADER NEUROPEPTIDE 03-OCT-02 1MXQ
TITLE SOLUTION STRUCTURE OF THE TACHYKININ PEPTIDE ELEDOISIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELEDOISIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: ELEDONE MOSCHATA;
SOURCE 4 ORGANISM_TAXID: 6641
KEYWDS HELIX, 3 10 HELIX, LIPID INDUCED CONFORMATION, DPC MICELLES,
KEYWDS 2 NEUROPEPTIDE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.C.GRACE,I.R.CHANDRASHEKAR,S.M.COWSIK
REVDAT 4 25-DEC-19 1MXQ 1 SEQADV SEQRES HET HETNAM
REVDAT 4 2 1 FORMUL
REVDAT 3 09-OCT-19 1MXQ 1 SOURCE REMARK LINK
REVDAT 2 24-FEB-09 1MXQ 1 VERSN
REVDAT 1 18-FEB-03 1MXQ 0
JRNL AUTH R.C.GRACE,I.R.CHANDRASHEKAR,S.M.COWSIK
JRNL TITL SOLUTION STRUCTURE OF THE TACHYKININ PEPTIDE ELEDOISIN
JRNL REF BIOPHYS.J. V. 84 655 2003
JRNL REFN ISSN 0006-3495
JRNL PMID 12524318
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5
REMARK 3 AUTHORS : GNTERT, P., AND K. WTHRICH (DYANA), GNTERT, P.,
REMARK 3 AND K. WTHRICH (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MXQ 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_1000017287.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NO SALTS USED
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MG OF ELEDOISIN 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 : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.8
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 1MXQ A 1 11 UNP P01293 TKN_ELEMOX 1 11
SEQRES 1 A 11 PCA PRO SER LYS ASP ALA PHE ILE GLY LEU MET
MODRES 1MXQ PCA A 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 14
HETNAM PCA PYROGLUTAMIC ACID
FORMUL 1 PCA C5 H7 N O3
HELIX 1 1 ASP A 5 MET A 11 1 7
LINK C PCA A 1 N PRO A 2 1555 1555 1.36
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 - 25 20 Bytes