[English] 日本語
Yorodumi- PDB-1omv: non-myristoylated bovine recoverin (E85Q mutant) with calcium bou... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1omv | ||||||
---|---|---|---|---|---|---|---|
Title | non-myristoylated bovine recoverin (E85Q mutant) with calcium bound to EF-hand 3 | ||||||
Components | recoverin | ||||||
Keywords | METAL BINDING PROTEIN / EF-hand / helix-loop-helix | ||||||
Function / homology | Function and homology information Inactivation, recovery and regulation of the phototransduction cascade / regulation of calcium ion transport / phototransduction / photoreceptor outer segment / photoreceptor inner segment / visual perception / perikaryon / calcium ion binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Weiergraber, O.H. / Granzin, J. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2003 Title: Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin Authors: Weiergraber, O.H. / Senin, I.I. / Philippov, P.P. / Granzin, J. / Koch, K.-W. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1omv.cif.gz | 53.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1omv.ent.gz | 37.6 KB | Display | PDB format |
PDBx/mmJSON format | 1omv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1omv_validation.pdf.gz | 428.7 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1omv_full_validation.pdf.gz | 434.2 KB | Display | |
Data in XML | 1omv_validation.xml.gz | 10.5 KB | Display | |
Data in CIF | 1omv_validation.cif.gz | 13.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/om/1omv ftp://data.pdbj.org/pub/pdb/validation_reports/om/1omv | HTTPS FTP |
-Related structure data
Related structure data | 1omrSC S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 23234.223 Da / Num. of mol.: 1 / Mutation: E85Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Gene: RCV1 / Plasmid: pET11d / Production host: Escherichia coli (E. coli) / Strain (production host): rec/BL21 / References: UniProt: P21457 |
---|---|
#2: Chemical | ChemComp-CA / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.26 % | |||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 8 Details: ammonium sulfate, TRIS, calcium chloride, magnesium chloride, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Apr 21, 2002 / Details: mirrors |
Radiation | Monochromator: mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→59.76 Å / Num. all: 19464 / Num. obs: 19464 / % possible obs: 99.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Biso Wilson estimate: 19.5 Å2 / Rmerge(I) obs: 0.074 / Rsym value: 0.074 / Net I/σ(I): 4.7 |
Reflection shell | Resolution: 1.8→1.84 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.178 / Mean I/σ(I) obs: 3.1 / Num. unique all: 1454 / Rsym value: 0.178 / % possible all: 100 |
Reflection | *PLUS Highest resolution: 1.9 Å / Num. obs: 16253 / Rmerge(I) obs: 0.087 |
Reflection shell | *PLUS % possible obs: 100 % / Rmerge(I) obs: 0.208 |
-Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1OMR Resolution: 1.9→59.63 Å / Isotropic thermal model: anisotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: Residues 2-6, 75-77 and 198-202 could not be defined in electron density.
| |||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.3 Å2
| |||||||||||||||||||||||||
Refine analyze |
| |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→59.63 Å
| |||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||
LS refinement shell | Resolution: 1.9→1.94 Å / Rfactor Rfree error: 0.039
| |||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rwork: 0.24 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
|