+Open data
-Basic information
Entry | Database: PDB / ID: 1oop | ||||||
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Title | The Crystal Structure of Swine Vesicular Disease Virus | ||||||
Components | (Coat protein ...) x 4 | ||||||
Keywords | VIRUS / PICORNAVIRUS STRUCTURE / VIRUS/VIRAL PROTEIN / VIRUS-RECEPTOR INTERACTIONS / HOST ADAPTATION / CAR / DAF / COXSACKIEVIRUS / Icosahedral virus | ||||||
Function / homology | Function and homology information : / positive stranded viral RNA replication / RNA-protein covalent cross-linking / : / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid ...: / positive stranded viral RNA replication / RNA-protein covalent cross-linking / : / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / : / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / RNA helicase activity / DNA replication / induction by virus of host autophagy / RNA-directed RNA polymerase / symbiont-mediated suppression of host gene expression / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / host cell nucleus / virion attachment to host cell / structural molecule activity / RNA binding / ATP binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | Swine vesicular disease virus | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å | ||||||
Authors | Fry, E.E. / Knowles, N.J. / Newman, J.W.I. / Wilsden, G. / Rao, Z. / King, A.M.Q. / Stuart, D.I. | ||||||
Citation | Journal: J.Virol. / Year: 2003 Title: Crystal Structure of Swine Vesicular Disease Virus and Implications for Host Adaptation Authors: Fry, E.E. / Knowles, N.J. / Newman, J.W.I. / Wilsden, G. / Rao, Z. / King, A.M.Q. / Stuart, D.I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1oop.cif.gz | 168.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1oop.ent.gz | 131.9 KB | Display | PDB format |
PDBx/mmJSON format | 1oop.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oo/1oop ftp://data.pdbj.org/pub/pdb/validation_reports/oo/1oop | 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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2 |
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3 |
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4 |
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5 |
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Unit cell |
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Symmetry | Point symmetry: (Hermann–Mauguin notation: 532 / Schoenflies symbol: I (icosahedral)) |
-Components
-Coat protein ... , 4 types, 4 molecules ABCD
#1: Protein | Mass: 31538.373 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Swine vesicular disease virus (STRAIN UKG/27/72) Genus: Enterovirus / Species: Human enterovirus B / Strain: UKG-27-72 / References: UniProt: P13900 |
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#2: Protein | Mass: 28652.350 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Swine vesicular disease virus (STRAIN UKG/27/72) Genus: Enterovirus / Species: Human enterovirus B / Strain: UKG-27-72 / References: UniProt: P13900 |
#3: Protein | Mass: 26084.574 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Swine vesicular disease virus (STRAIN UKG/27/72) Genus: Enterovirus / Species: Human enterovirus B / Strain: UKG-27-72 / References: UniProt: P13900 |
#4: Protein | Mass: 7457.220 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Swine vesicular disease virus (STRAIN UKG/27/72) Genus: Enterovirus / Species: Human enterovirus B / Strain: UKG-27-72 / References: UniProt: P13900 |
-Non-polymers , 2 types, 2 molecules
#5: Chemical | ChemComp-SPH / |
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#6: Chemical | ChemComp-MYR / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.6 Details: 15-25% saturated ammonium sulfate, 100mM phosphate buffer, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K | ||||||||||||||||||||||||
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Crystal grow | *PLUS | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX14.2 / Wavelength: 0.979 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Feb 29, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 3→20 Å / Num. obs: 406689 / % possible obs: 49.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.207 / Net I/σ(I): 5.1 |
Reflection shell | Resolution: 3→3.11 Å / Rmerge(I) obs: 0.482 / % possible all: 45.9 |
Reflection shell | *PLUS % possible obs: 46 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: Coxsackievirus A9 Resolution: 3→15 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: A free R value is absent because the high non-crystallographic symmetry of viruses makes this less relevant.
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Displacement parameters | Biso mean: 14 Å2 | ||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→15 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 3 Å / Lowest resolution: 15 Å | ||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||
Displacement parameters | *PLUS |