Header list of 2b19.pdb file
Complete list - 9 20 Bytes
HEADER NEUROPEPTIDE 15-SEP-05 2B19
TITLE SOLUTION STRUCTURE OF MAMMALIAN TACHYKININ PEPTIDE, NEUROPEPTIDE K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROPEPTIDE K;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NPK;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: CHEMICAL SYNTHESIS
KEYWDS HELIX, 3 10 HELIX, LIPID INDUCED CONFORMATION, DPC MICELLES,
KEYWDS 2 NEUROPEPTIDE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.DIKE,S.M.COWSIK
REVDAT 3 09-MAR-22 2B19 1 REMARK
REVDAT 2 24-FEB-09 2B19 1 VERSN
REVDAT 1 19-SEP-06 2B19 0
JRNL AUTH A.DIKE,S.M.COWSIK
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF NEUROPEPTIDE K BOUND TO
JRNL TITL 2 DODECYLPHOSPHOCHOLINE MICELLES
JRNL REF BIOCHEMISTRY V. 45 2994 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16503654
JRNL DOI 10.1021/BI052287O
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5
REMARK 3 AUTHORS : P.GUNTERT, C.MUMENTHALER, K.WUTHRICH (DYANA),
REMARK 3 P.GUNTERT, C.MUMENTHALER, K.WUTHRICH (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2B19 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034549.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : NO SALTS USED
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 146MM PERDEUTERATED DPC; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
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
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ALA A 2 H SER A 5 1.56
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2B19 A 1 36 UNP Q53GH4 Q53GH4_HUMAN 72 107
SEQRES 1 A 36 ASP ALA ASP SER SER ILE GLU LYS GLN VAL ALA LEU LEU
SEQRES 2 A 36 LYS ALA LEU TYR GLY HIS GLY GLN ILE SER HIS LYS ARG
SEQRES 3 A 36 HIS LYS THR ASP SER PHE VAL GLY LEU MET
HELIX 1 1 ASP A 1 LYS A 8 5 8
HELIX 2 2 GLN A 9 GLY A 18 1 10
HELIX 3 3 GLY A 20 LYS A 25 1 6
HELIX 4 4 ARG A 26 SER A 31 1 6
HELIX 5 5 PHE A 32 MET A 36 5 5
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