+Open data
-Basic information
Entry | Database: PDB / ID: 4mew | ||||||
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Title | Structure of the core fragment of human PR70 | ||||||
Components | Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta | ||||||
Keywords | hydrolase / cell cycle / EF-hands / Protein Phosphatase / Calcium Binding / METAL BINDING PROTEIN | ||||||
Function / homology | Function and homology information protein phosphatase type 2A complex / Inhibition of replication initiation of damaged DNA by RB1/E2F1 / protein phosphatase regulator activity / Cyclin A/B1/B2 associated events during G2/M transition / protein dephosphorylation / Cyclin D associated events in G1 / regulation of cell cycle / calcium ion binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.993 Å | ||||||
Authors | Dovega, R.B. / Quistgaard, E.M. / Tsutakawa, S. / Anandapadamanaban, M. / Low, C. / Nordlund, P. | ||||||
Citation | Journal: Plos One / Year: 2014 Title: Structural and Biochemical Characterization of Human PR70 in Isolation and in Complex with the Scaffolding Subunit of Protein Phosphatase 2A. Authors: Dovega, R. / Tsutakawa, S. / Quistgaard, E.M. / Anandapadamanaban, M. / Low, C. / Nordlund, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4mew.cif.gz | 158.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4mew.ent.gz | 130.8 KB | Display | PDB format |
PDBx/mmJSON format | 4mew.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/me/4mew ftp://data.pdbj.org/pub/pdb/validation_reports/me/4mew | 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: 41866.066 Da / Num. of mol.: 1 / Fragment: Residues 130-483 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PPP2R3B, PPP2R3L / Plasmid: pNIC28-Bsa4 / Production host: Escherichia coli (E. coli) / Strain (production host): Bl21(DE3) / References: UniProt: Q9Y5P8 | ||||
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#2: Chemical | #3: Chemical | #4: 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: 2.05 Å3/Da / Density % sol: 40.14 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion / pH: 7.5 Details: 0.1 M Tris-HCl, 16% PEG 2000 monomethyl ether, 0.15 M trimethylamine N-oxide, pH 7.5, VAPOR DIFFUSION, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9796 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 22, 2012 |
Radiation | Monochromator: Double crystal, Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9796 Å / Relative weight: 1 |
Reflection | Resolution: 1.99→37.23 Å / Num. all: 45116 / Num. obs: 45116 / % possible obs: 99.1 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rsym value: 0.097 / Net I/σ(I): 13.8 |
Reflection shell | Resolution: 1.99→2.04 Å / Mean I/σ(I) obs: 2.42 / Num. unique all: 3010 / Rsym value: 0.601 / % possible all: 89 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 1.993→37.23 Å / SU ML: 0.2 / σ(F): 1.51 / Phase error: 20.63 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.993→37.23 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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