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Yorodumi- PDB-1fod: STRUCTURE OF A MAJOR IMMUNOGENIC SITE ON FOOT-AND-MOUTH DISEASE VIRUS -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fod | ||||||
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Title | STRUCTURE OF A MAJOR IMMUNOGENIC SITE ON FOOT-AND-MOUTH DISEASE VIRUS | ||||||
Components | (FOOT AND MOUTH DISEASE VIRUSFoot-and-mouth disease virus) x 4 | ||||||
Keywords | VIRUS / Icosahedral virus | ||||||
Function / homology | Function and homology information icosahedral viral capsid / host cell cytoplasm / symbiont entry into host cell / virion attachment to host cell / structural molecule activity / cytoplasm Similarity search - Function | ||||||
Biological species | Foot-and-mouth disease virus | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.6 Å | ||||||
Authors | Logan, D.T. / Lea, S. / Lewis, R. / Stuart, D. / Fry, E. | ||||||
Citation | Journal: Nature / Year: 1993 Title: Structure of a major immunogenic site on foot-and-mouth disease virus. Authors: Logan, D. / Abu-Ghazaleh, R. / Blakemore, W. / Curry, S. / Jackson, T. / King, A. / Lea, S. / Lewis, R. / Newman, J. / Parry, N. / Rowlands, D. / Stuart, D. / Fry, E. #1: Journal: Semin.Virol. / Year: 1990 Title: Architecture and Topography of an Aphthovirus Authors: Fry, E. / Logan, D. / Acharya, R. / Fox, G. / Rowlands, D. / Brown, F. / Stuart, D. #2: Journal: Nature / Year: 1990 Title: Structural and Serological Evidence for a Novel Mechanism of Antigenic Variation in Foot-and-Mouth Disease Virus Authors: Parry, N. / Fox, G. / Rowlands, D. / Brown, F. / Fry, E. / Acharya, R. / Logan, D. / Stuart, D. #3: Journal: Nature / Year: 1989 Title: The Three-Dimensional Structure of Foot-and-Mouth Disease Virus at 2.9 Angstroms Resolution Authors: Acharya, R. / Fry, E. / Stuart, D. / Fox, G. / Rowlands, D. / Brown, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fod.cif.gz | 145.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fod.ent.gz | 114.1 KB | Display | PDB format |
PDBx/mmJSON format | 1fod.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fo/1fod ftp://data.pdbj.org/pub/pdb/validation_reports/fo/1fod | 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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6 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 1 111 / 2: CIS PROLINE - PRO 2 84 | ||||||||||||||||||
Symmetry | Point symmetry: (Hermann–Mauguin notation: 532 / Schoenflies symbol: I (icosahedral)) | ||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 23814.158 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Foot-and-mouth disease virus / Genus: Aphthovirus / Strain: STRAIN BFS, 1860 / References: UniProt: Q84771 |
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#2: Protein | Mass: 24373.455 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Foot-and-mouth disease virus / Genus: Aphthovirus / Strain: STRAIN BFS, 1860 / References: UniProt: Q84771 |
#3: Protein | Mass: 23860.830 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Foot-and-mouth disease virus / Genus: Aphthovirus / Strain: STRAIN BFS, 1860 / References: UniProt: Q84771 |
#4: Protein | Mass: 8778.129 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Foot-and-mouth disease virus / Genus: Aphthovirus / Strain: STRAIN BFS, 1860 / References: UniProt: P87677 |
Compound details | ATTACHMENT OF FOOT AND MOUTH DISEASE VIRUS (FMDV) TO ITS CELLULAR RECEPTOR INVOLVES A LONG AND ...ATTACHMENT |
Sequence details | SEQUENCE ADVISORY NOTICE: DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. SWISS-PROT ENTRY NAME: ...SEQUENCE ADVISORY NOTICE: DIFFERENCE |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||
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Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
-Processing
Software |
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Refinement | Rfactor Rwork: 0.208 / Rfactor obs: 0.208 / Highest resolution: 2.6 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.6 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.6 Å / Rfactor obs: 0.208 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.7 |