Header list of 1jzp.pdb file
Complete list - 23 202 Bytes
HEADER SIGNALING PROTEIN 17-SEP-01 1JZP
TITLE MODIFIED PEPTIDE A (D18-A1) OF THE RABBIT SKELETAL DIHYDROPYRIDINE
TITLE 2 RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SKELETAL DIHYDROPYDRINE RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: D18-A1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE IS A MODIFICATION OF A SEGMENT OF A
SOURCE 4 PROTEIN THAT OCCURS NATURALLY IN RABBIT SKELETAL MUSCLE.
KEYWDS ALPHA HELICAL PEPTIDE, DHPR, D-ISOMER, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR D.GREEN,S.PACE,M.SAKOWSKA,A.F.DULHUNTY,M.G.CASAROTTO
REVDAT 4 23-FEB-22 1JZP 1 REMARK LINK
REVDAT 3 24-FEB-09 1JZP 1 VERSN
REVDAT 2 31-MAY-05 1JZP 1 JRNL
REVDAT 1 20-MAR-02 1JZP 0
JRNL AUTH D.GREEN,S.PACE,S.M.CURTIS,M.SAKOWSKA,G.D.LAMB,A.F.DULHUNTY,
JRNL AUTH 2 M.G.CASAROTTO
JRNL TITL THE THREE-DIMENSIONAL STRUCTURAL SURFACE OF TWO BETA-SHEET
JRNL TITL 2 SCORPION TOXINS MIMICS THAT OF AN ALPHA-HELICAL
JRNL TITL 3 DIHYDROPYRIDINE RECEPTOR SEGMENT.
JRNL REF BIOCHEM.J. V. 370 517 2003
JRNL REFN ISSN 0264-6021
JRNL PMID 12429019
JRNL DOI 10.1042/BJ20021488
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURE IS BASED ON A TOTAL OF 239 RESTRAINTS OF WHICH 222
REMARK 3 ARE NOE-DERIVED, 12 ARE DIHEDRAL ANGLE RESTRAINTS AND 5 ARE
REMARK 3 DISTANCE RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1JZP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014377.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2-3 MM DHPR PEPTIDE, UNBUFFERED
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 17
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED BY 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: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 6 -45.50 178.70
REMARK 500 ARG A 18 32.54 -90.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 11 0.14 SIDE CHAIN
REMARK 500 ARG A 13 0.27 SIDE CHAIN
REMARK 500 ARG A 14 0.20 SIDE CHAIN
REMARK 500 ARG A 18 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 21
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DU1 RELATED DB: PDB
REMARK 900 PEPTIDE FRAGMENT THR671-LEU690 OF THE RABBIT SKELETAL
REMARK 900 DIHYDROPYRIDINE RECEPTOR
DBREF 1JZP A 1 21 PDB 1JZP 1JZP 1 21
SEQRES 1 A 21 THR SER ALA GLN LYS ALA LYS ALA GLU GLU ARG LYS ARG
SEQRES 2 A 21 ARG LYS MET SER ARG GLY LEU NH2
HET NH2 A 21 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 THR A 1 LYS A 5 5 5
HELIX 2 2 ALA A 6 GLY A 19 1 14
LINK C LEU A 20 N NH2 A 21 1555 1555 1.31
SITE 1 AC1 2 GLY A 19 LEU A 20
CRYST1 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