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- PDB-8ey3: Contact-dependent growth inhibition (CDI) immunity protein from E... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8ey3 | ||||||
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Title | Contact-dependent growth inhibition (CDI) immunity protein from E. coli O32:H37 | ||||||
![]() | Cys_rich_CPCC domain-containing protein | ||||||
![]() | TOXIN / CDI | ||||||
Function / homology | Cysteine-rich CPCC domain / Cysteine-rich CPCC / : / Cysteine-rich CPCC domain-containing protein![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Michalska, K. / Stols, L. / Eschenfeldt, W. / Goulding, C.W. / Hayes, C.S. / Joachimiak, A. / Midwest Center for Structural Genomics (MCSG) / Center for Structural Genomics of Infectious Diseases (CSGID) | ||||||
Funding support | ![]()
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![]() | ![]() Title: Contact-dependent growth inhibition (CDI) immunity protein from E. coli O32:H37 Authors: Michalska, K. / Stols, L. / Eschenfeldt, W. / Goulding, C.W. / Hayes, C.S. / Joachimiak, A. / Midwest Center for Structural Genomics (MCSG) / Center for Structural Genomics of Infectious Diseases (CSGID) | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 64.7 KB | Display | ![]() |
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PDB format | ![]() | 38.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 932.4 KB | Display | ![]() |
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Full document | ![]() | 932.4 KB | Display | |
Data in XML | ![]() | 6.5 KB | Display | |
Data in CIF | ![]() | 8.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 6950.540 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: B6R12_004683, B6R15_004523, C0P57_003609, D9E49_27105, DAH20_21150, DEN92_22940, DEN93_17480, DEO13_20945, DEO14_22190, DEO15_23150, E5S48_23695, E5S53_25065, E5S55_25155, FHQ91_23985, FJQ51_ ...Gene: B6R12_004683, B6R15_004523, C0P57_003609, D9E49_27105, DAH20_21150, DEN92_22940, DEN93_17480, DEO13_20945, DEO14_22190, DEO15_23150, E5S48_23695, E5S53_25065, E5S55_25155, FHQ91_23985, FJQ51_24360, FJQ53_24775, GF698_05830, GQW68_24765 Plasmid: pMCSG63 / Production host: ![]() ![]() | ||||
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#2: Chemical | ChemComp-FE / | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Has ligand of interest | Y | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.77 Å3/Da / Density % sol: 30.62 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / Details: 2.4 M sodium malonate pH 7.0 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 29, 2015 / Details: mirrors |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
Reflection | Resolution: 1→30 Å / Num. obs: 27034 / % possible obs: 98 % / Observed criterion σ(I): -3 / Redundancy: 4.7 % / Biso Wilson estimate: 16.26 Å2 / Rmerge(I) obs: 0.037 / Net I/σ(I): 33.52 |
Reflection shell | Resolution: 1→1.02 Å / Rmerge(I) obs: 0.299 / Mean I/σ(I) obs: 2.01 / Num. unique obs: 1028 / CC1/2: 0.869 / % possible all: 75.4 |
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Processing
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Refinement | Method to determine structure: ![]() Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 19.92 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1→29.15 Å
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Refine LS restraints |
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LS refinement shell |
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