+Open data
-Basic information
Entry | Database: PDB / ID: 3q1c | ||||||
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Title | Structure of EspG Protein | ||||||
Components | LEE-encoded effector EspG | ||||||
Keywords | SIGNALING PROTEIN / VirA fold / virulence factor / PAK recruitment and activation / p21 activated kinase | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Escherichia coli O127:H6 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.596 Å | ||||||
Authors | Spiller, B.W. / Germane, K.L. | ||||||
Citation | Journal: Biochemistry / Year: 2011 Title: Structural and Functional Studies Indicate That the EPEC Effector, EspG, Directly Binds p21-Activated Kinase. Authors: Germane, K.L. / Spiller, B.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3q1c.cif.gz | 157.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3q1c.ent.gz | 123.3 KB | Display | PDB format |
PDBx/mmJSON format | 3q1c.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3q1c_validation.pdf.gz | 424.9 KB | Display | wwPDB validaton report |
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Full document | 3q1c_full_validation.pdf.gz | 431.5 KB | Display | |
Data in XML | 3q1c_validation.xml.gz | 19.5 KB | Display | |
Data in CIF | 3q1c_validation.cif.gz | 30 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q1/3q1c ftp://data.pdbj.org/pub/pdb/validation_reports/q1/3q1c | HTTPS FTP |
-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: 39879.578 Da / Num. of mol.: 1 / Fragment: UNP residues 44-398 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli O127:H6 (bacteria) / Strain: E2348/69 / EPEC / Gene: E2348C_3970, E2348_C_3970, espG Plasmid details: An N-terminal 6His tag was cleaved with Thrombin. Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: B7UMC8 |
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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: 3.12 Å3/Da / Density % sol: 60.52 % |
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Crystal grow | Method: vapor diffusion, hanging drop Details: 2.0-11.0% PEG8000, 100 mM Bis-Tris, pH 6.25-7.5, VAPOR DIFFUSION, HANGING DROP, temperature range 268-291K PH range: 6.25-7.5 |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9795 | |||||||||||
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 16, 2009 | |||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 | |||||||||||
Reflection | Resolution: 1.595→32.958 Å / Num. obs: 60098 / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.8 % / Biso Wilson estimate: 21.2 Å2 / Rmerge(I) obs: 0.035 / Net I/σ(I): 32 | |||||||||||
Reflection shell |
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-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 1.596→32.093 Å / SU ML: 0.18 / σ(F): 0 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.61 Å / VDW probe radii: 0.9 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 56.988 Å2 / ksol: 0.394 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refine analyze | Luzzati sigma a obs: 0.18 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.596→32.093 Å
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Refine LS restraints |
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LS refinement shell |
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