[English] 日本語
Yorodumi- PDB-1jzp: Modified Peptide A (D18-A1) of the Rabbit Skeletal Dihydropyridin... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1jzp | ||||||
---|---|---|---|---|---|---|---|
Title | Modified Peptide A (D18-A1) of the Rabbit Skeletal Dihydropyridine Receptor | ||||||
Components | Skeletal Dihydropydrine Receptor | ||||||
Keywords | SIGNALING PROTEIN / Alpha helical peptide / DHPR / D-isomer | ||||||
Function / homology | Function and homology information positive regulation of muscle contraction / L-type voltage-gated calcium channel complex / cellular response to caffeine / voltage-gated calcium channel activity / release of sequestered calcium ion into cytosol / regulation of ryanodine-sensitive calcium-release channel activity / T-tubule / muscle contraction / calcium ion transmembrane transport / transmembrane transporter binding ...positive regulation of muscle contraction / L-type voltage-gated calcium channel complex / cellular response to caffeine / voltage-gated calcium channel activity / release of sequestered calcium ion into cytosol / regulation of ryanodine-sensitive calcium-release channel activity / T-tubule / muscle contraction / calcium ion transmembrane transport / transmembrane transporter binding / calmodulin binding / metal ion binding / plasma membrane Similarity search - Function | ||||||
Method | SOLUTION NMR / Distance Geometry Simulated annealing refinement | ||||||
Authors | Green, D. / Pace, S. / Sakowska, M. / Dulhunty, A.F. / Casarotto, M.G. | ||||||
Citation | Journal: Biochem.J. / Year: 2003 Title: The three-dimensional structural surface of two beta-sheet scorpion toxins mimics that of an alpha-helical dihydropyridine receptor segment. Authors: Green, D. / Pace, S. / Curtis, S.M. / Sakowska, M. / Lamb, G.D. / Dulhunty, A.F. / Casarotto, M.G. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1jzp.cif.gz | 13.1 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1jzp.ent.gz | 9.6 KB | Display | PDB format |
PDBx/mmJSON format | 1jzp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jz/1jzp ftp://data.pdbj.org/pub/pdb/validation_reports/jz/1jzp | HTTPS FTP |
---|
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein/peptide | Mass: 2337.772 Da / Num. of mol.: 1 / Fragment: D18-A1 / Mutation: Arg688 from L to D isomer / Source method: obtained synthetically Details: This sequence is a modification of a segment of a protein that occurs naturally in rabbit skeletal muscle. References: UniProt: P07293*PLUS |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||
NMR details | Text: This structure was determined by using standard 2D homonuclear techniques. |
-Sample preparation
Details | Contents: 2-3 mM DHPR peptide, unbuffered / Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | pH: 5.0 / Pressure: 1 atm / Temperature: 278 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
---|---|
Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
-Processing
NMR software | Name: X-PLOR / Version: 3.851 / Developer: Brunger / Classification: refinement |
---|---|
Refinement | Method: Distance Geometry Simulated annealing refinement / Software ordinal: 1 Details: The structure is based on a total of 239 restraints of which 222 are NOE-derived, 12 are dihedral angle restraints and 5 are distance restraints from hydrogen bonds. |
NMR representative | Selection criteria: closest to the average |
NMR ensemble | Conformers calculated total number: 17 / Conformers submitted total number: 1 |