+Open data
-Basic information
Entry | Database: PDB / ID: 6b26 | ||||||
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Title | Crystal structure of human STAC2 Tandem SH3 Domains (296-411) | ||||||
Components | SH3 and cysteine-rich domain-containing protein 2 | ||||||
Keywords | PROTEIN BINDING / Excitation-contraction coupling / ion channel adaptor protein | ||||||
Function / homology | Function and homology information positive regulation of voltage-gated calcium channel activity / skeletal muscle contraction / positive regulation of protein localization to plasma membrane / cytoplasmic side of plasma membrane / sarcolemma / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.2 Å | ||||||
Authors | Wong King Yuen, S.M. / Van Petegem, F. | ||||||
Funding support | Canada, 1items
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Citation | Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2017 Title: Structural insights into binding of STAC proteins to voltage-gated calcium channels. Authors: Wong King Yuen, S.M. / Campiglio, M. / Tung, C.C. / Flucher, B.E. / Van Petegem, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6b26.cif.gz | 73.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6b26.ent.gz | 53.8 KB | Display | PDB format |
PDBx/mmJSON format | 6b26.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6b26_validation.pdf.gz | 399.6 KB | Display | wwPDB validaton report |
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Full document | 6b26_full_validation.pdf.gz | 399.7 KB | Display | |
Data in XML | 6b26_validation.xml.gz | 9.1 KB | Display | |
Data in CIF | 6b26_validation.cif.gz | 13.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b2/6b26 ftp://data.pdbj.org/pub/pdb/validation_reports/b2/6b26 | HTTPS FTP |
-Related structure data
Related structure data | 6b25C 6b27C 6b28C 6b29C 2dl4S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 13471.185 Da / Num. of mol.: 1 / Fragment: residues 296-411 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: STAC2 / Production host: Escherichia coli (E. coli) / References: UniProt: Q6ZMT1 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.47 Å3/Da / Density % sol: 50.11 % |
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Crystal grow | Temperature: 277.15 K / Method: microdialysis / pH: 7.4 / Details: 150mM KCl, 10mM HEPES, 2mM TCEP |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 0.97946 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: May 6, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97946 Å / Relative weight: 1 |
Reflection | Resolution: 1.2→32.95 Å / Num. obs: 41292 / % possible obs: 99.3 % / Redundancy: 4.4 % / Rmerge(I) obs: 0.02397 / Net I/σ(I): 29.89 |
Reflection shell | Resolution: 1.2→1.24 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.2007 / Mean I/σ(I) obs: 5.84 / % possible all: 98.95 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2DL4 Resolution: 1.2→32.95 Å / Cor.coef. Fo:Fc: 0.974 / Cor.coef. Fo:Fc free: 0.968 / SU B: 1.042 / SU ML: 0.022 / SU R Cruickshank DPI: 0.0393 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.039 / ESU R Free: 0.037 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 50.72 Å2 / Biso mean: 14.152 Å2 / Biso min: 6.4 Å2
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Refinement step | Cycle: final / Resolution: 1.2→32.95 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.2→1.231 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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