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Yorodumi- PDB-1sji: Comparing skeletal and cardiac calsequestrin structures and their... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1sji | ||||||
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Title | Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization | ||||||
Components | Calsequestrin, cardiac muscle isoform | ||||||
Keywords | METAL BINDING PROTEIN / calsequestrin / Glycoprotein / Calcium-binding / Muscle protein | ||||||
Function / homology | Function and homology information sarcoplasmic reticulum lumen / regulation of release of sequestered calcium ion into cytosol / negative regulation of ryanodine-sensitive calcium-release channel activity / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / sarcoplasmic reticulum / Z disc / calcium ion binding Similarity search - Function | ||||||
Biological species | Canis lupus familiaris (dog) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Park, H.J. / Park, I.Y. / Kim, E.J. / Youn, B. / Fields, K. / Dunker, A.K. / Kang, C.H. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2004 Title: Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization. Authors: Park, H.J. / Park, I.Y. / Kim, E.J. / Youn, B. / Fields, K. / Dunker, A.K. / Kang, C.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1sji.cif.gz | 153 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1sji.ent.gz | 121.8 KB | Display | PDB format |
PDBx/mmJSON format | 1sji.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sj/1sji ftp://data.pdbj.org/pub/pdb/validation_reports/sj/1sji | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 40745.855 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Canis lupus familiaris (dog) / Species: Canis lupus / Strain: familiaris / Gene: CASQ2 / Plasmid: pTYB1 / Production host: Escherichia coli (E. coli) / References: UniProt: P12637 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.23 Å3/Da / Density % sol: 61.89 % |
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Crystal grow | Temperature: 282 K / Method: vapor diffusion, hanging drop / pH: 8.2 Details: PEG400 Na citrate DM Tris-HCl, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 282K |
-Data collection
Diffraction | Mean temperature: 103 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1.5621 Å |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Jan 1, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5621 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→10 Å / Num. all: 8809 / Num. obs: 8778 / % possible obs: 89.6 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 8.4 % / Rmerge(I) obs: 0.052 / Rsym value: 0.041 |
Reflection shell | Resolution: 2.45→2.57 Å / % possible all: 66.02 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.4→10 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.4→10 Å
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Refine LS restraints |
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