+Open data
-Basic information
Entry | Database: PDB / ID: 1f0c | ||||||
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Title | STRUCTURE OF THE VIRAL SERPIN CRMA | ||||||
Components | (ICE INHIBITOR) x 2 | ||||||
Keywords | VIRAL PROTEIN / Apoptosis / caspase inhibitor / protease inhibitor / serpin | ||||||
Function / homology | Function and homology information : / Microbial modulation of RIPK1-mediated regulated necrosis / cysteine-type endopeptidase inhibitor activity / protein sequestering activity / Regulation of TNFR1 signaling / serine-type endopeptidase inhibitor activity / : / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / host cell cytoplasm / extracellular space / cytoplasm Similarity search - Function | ||||||
Biological species | Cowpox virus | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.26 Å | ||||||
Authors | Renatus, M. / Zhou, Q. / Stennicke, H.R. / Snipas, S.J. / Turk, D. / Bankston, L.A. / Liddington, R.C. / Salvesen, G.S. | ||||||
Citation | Journal: Structure Fold.Des. / Year: 2000 Title: Crystal structure of the apoptotic suppressor CrmA in its cleaved form. Authors: Renatus, M. / Zhou, Q. / Stennicke, H.R. / Snipas, S.J. / Turk, D. / Bankston, L.A. / Liddington, R.C. / Salvesen, G.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1f0c.cif.gz | 81.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1f0c.ent.gz | 60.5 KB | Display | PDB format |
PDBx/mmJSON format | 1f0c.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f0/1f0c ftp://data.pdbj.org/pub/pdb/validation_reports/f0/1f0c | 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: 34021.449 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-305 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Cowpox virus / Genus: Orthopoxvirus / Plasmid: PET23D / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) Keywords: PROTEIN HAS BEEN CLEAVED WITH SUBTILISIN CARLSBERG References: UniProt: P07385 |
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#2: Protein/peptide | Mass: 4106.662 Da / Num. of mol.: 1 / Fragment: RESIDUES 306-341 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Cowpox virus / Genus: Orthopoxvirus / Plasmid: PET23D / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) Keywords: PROTEIN HAS BEEN CLEAVED WITH SUBTILISIN CARLSBERG References: UniProt: P07385 |
#3: Chemical | ChemComp-DTT / |
#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: 3 Å3/Da / Density % sol: 58.93 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 296 K / Method: vapor diffusion Details: 0.1 M Na-Acetate, 15% PEG 4000, 0.1 M MgCl2, VAPOR DIFFUSION, temperature 296K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 23 ℃ / pH: 5 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.15 |
Detector | Type: BRANDEIS - B4 / Detector: CCD / Date: Sep 23, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.15 Å / Relative weight: 1 |
Reflection | Resolution: 2.26→35 Å / Num. all: 75617 / Num. obs: 21897 / % possible obs: 96.2 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.5 % / Biso Wilson estimate: 35.9 Å2 / Rmerge(I) obs: 0.051 / Net I/σ(I): 26.3 |
Reflection shell | Resolution: 2.26→2.31 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.281 / % possible all: 94.1 |
Reflection | *PLUS Num. measured all: 75617 |
Reflection shell | *PLUS % possible obs: 94.7 % |
-Processing
Software |
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Refinement | Resolution: 2.26→500 Å / σ(F): 2 / σ(I): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.26→500 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 50 Å / σ(F): 2 / Rfactor obs: 0.2277 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS |