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Open data
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Basic information
| Entry | Database: PDB / ID: 1skv | ||||||
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| Title | Crystal Structure of D-63 from Sulfolobus Spindle Virus 1 | ||||||
Components | Hypothetical 7.5 kDa protein | ||||||
Keywords | VIRAL PROTEIN / Sulfolobus Spindle Virus / SSV / Archaeal / Crenarchaeal / Helix-Turn-Helix / Four Helix Bundle | ||||||
| Function / homology | Hypothetical protein D-63 / : / Sulfolobus spindle-shape virus 1, protein D-63 / Helix hairpin bin / Helix hairpin bin domain superfamily / Helix Hairpins / Orthogonal Bundle / Mainly Alpha / Protein D-63 Function and homology information | ||||||
| Biological species | ![]() Sulfolobus virus 1 | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.6 Å | ||||||
Authors | Kraft, P. / Kummel, D. / Oeckinghaus, A. / Gauss, G.H. / Wiedenheft, B. / Young, M. / Lawrence, C.M. | ||||||
Citation | Journal: J.Virol. / Year: 2004Title: Structure of d-63 from sulfolobus spindle-shaped virus 1: surface properties of the dimeric four-helix bundle suggest an adaptor protein function Authors: Kraft, P. / Oeckinghaus, A. / Gauss, G.H. / Wiedenheft, B. / Young, M. / Lawrence, C.M. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1skv.cif.gz | 60 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1skv.ent.gz | 46.1 KB | Display | PDB format |
| PDBx/mmJSON format | 1skv.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1skv_validation.pdf.gz | 441.9 KB | Display | wwPDB validaton report |
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| Full document | 1skv_full_validation.pdf.gz | 449.6 KB | Display | |
| Data in XML | 1skv_validation.xml.gz | 12.2 KB | Display | |
| Data in CIF | 1skv_validation.cif.gz | 15.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sk/1skv ftp://data.pdbj.org/pub/pdb/validation_reports/sk/1skv | HTTPS FTP |
-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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| 2 | ![]()
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| Unit cell |
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| Details | The biological assembly is the AB dimer / The biological assembly is the CD dimer |
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Components
| #1: Protein | Mass: 8402.422 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Sulfolobus virus 1 / Genus: Fusellovirus / Gene: D-63 / Plasmid: pDest14 / Production host: ![]() #2: Water | ChemComp-HOH / | Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 2.99 Å3/Da / Density % sol: 58.48 % |
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| Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5 Details: Ammonium Sulfate, ammonium acetate, PEG 4000, NaCl, Tris, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
| Diffraction | Mean temperature: 100 K | ||||||||||||
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| Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 14-BM-D / Wavelength: 0.9778, 0.9787, 0.9789 | ||||||||||||
| Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Aug 16, 2002 | ||||||||||||
| Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
| Radiation wavelength |
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| Reflection | Resolution: 2.6→20 Å / Num. all: 10225 / Num. obs: 10095 / % possible obs: 98.7 % / Observed criterion σ(F): -1.5 / Observed criterion σ(I): -3 / Redundancy: 8.6 % / Rmerge(I) obs: 0.043 / Net I/σ(I): 42 | ||||||||||||
| Reflection shell | Resolution: 2.6→2.7 Å / Redundancy: 9.7 % / Rmerge(I) obs: 0.212 / Mean I/σ(I) obs: 9 / Num. unique all: 1121 / % possible all: 99.5 |
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Processing
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| Refinement | Method to determine structure: MAD / Resolution: 2.6→15 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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| Displacement parameters | Biso mean: 58 Å2
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| Refine analyze |
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| Refinement step | Cycle: LAST / Resolution: 2.6→15 Å
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| Refine LS restraints |
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Sulfolobus virus 1
X-RAY DIFFRACTION
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