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Yorodumi- PDB-1a6s: M-DOMAIN FROM GAG POLYPROTEIN OF ROUS SARCOMA VIRUS, NMR, 20 STRU... -
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-Basic information
Entry | Database: PDB / ID: 1a6s | ||||||
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Title | M-DOMAIN FROM GAG POLYPROTEIN OF ROUS SARCOMA VIRUS, NMR, 20 STRUCTURES | ||||||
Components | GAG POLYPROTEINGroup-specific antigen | ||||||
Keywords | VIRAL PROTEIN / CORE PROTEIN / VIRUS STRUCTURE / MEMBRANE BINDING | ||||||
Function / homology | Function and homology information host cell nucleoplasm / viral procapsid maturation / host cell nucleolus / Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / viral capsid / structural constituent of virion / nucleic acid binding / aspartic-type endopeptidase activity / host cell plasma membrane / proteolysis ...host cell nucleoplasm / viral procapsid maturation / host cell nucleolus / Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / viral capsid / structural constituent of virion / nucleic acid binding / aspartic-type endopeptidase activity / host cell plasma membrane / proteolysis / zinc ion binding / membrane Similarity search - Function | ||||||
Biological species | Rous sarcoma virus - Prague C | ||||||
Method | SOLUTION NMR / distance geometry | ||||||
Authors | Mcdonnell, J.M. / Fushman, D. / Cahill, S.M. / Zhou, W. / Wolven, A. / Wilson, C.B. / Nelle, T.D. / Resh, M.D. / Wills, J. / Cowburn, D. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1998 Title: Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus Authors: McDonnell, J.M. / Fushman, D. / Cahill, S.M. / Zhou, W. / Wolven, A. / Wilson, C.B. / Nelle, T.D. / Resh, M.D. / Wills, J. / Cowburn, D. #1: Journal: J.Virol. / Year: 1996 Title: A Large Region within the Rous Sarcoma Virus Matrix Protein is Dispensable for Budding and Infectivity Authors: Nelle, T.D. / Wills, J.W. #2: Journal: J.Mol.Biol. / Year: 1996 Title: Three-Dimensional Structure of the Htlv-II Matrix Protein and Comparative Analysis of Matrix Proteins from the Different Classes of Pathogenic Human Retroviruses Authors: Christensen, A.M. / Massiah, M.A. / Turner, B.G. / Sundquist, W.I. / Summers, M.F. #3: Journal: Embo J. / Year: 1996 Title: The Solution Structure of the Bovine Leukaemia Virus Matrix Protein and Similarity with Lentiviral Matrix Proteins Authors: Matthews, S. / Mikhailov, M. / Burny, A. / Roy, P. #4: Journal: Nature / Year: 1995 Title: Crystal Structure of Siv Matrix Antigen and Implications for Virus Assembly Authors: Rao, Z. / Belyaev, A.S. / Fry, E. / Roy, P. / Jones, I.M. / Stuart, D.I. #5: Journal: J.Mol.Biol. / Year: 1994 Title: Three-Dimensional Structure of the Human Immunodeficiency Virus Type 1 Matrix Protein Authors: Massiah, M.A. / Starich, M.R. / Paschall, C. / Summers, M.F. / Christensen, A.M. / Sundquist, W.I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1a6s.cif.gz | 504.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a6s.ent.gz | 437.9 KB | Display | PDB format |
PDBx/mmJSON format | 1a6s.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a6/1a6s ftp://data.pdbj.org/pub/pdb/validation_reports/a6/1a6s | 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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NMR ensembles |
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-Components
#1: Protein | Mass: 9179.745 Da / Num. of mol.: 1 / Fragment: M-DOMAIN / Mutation: M1G Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rous sarcoma virus - Prague C / Genus: Alpharetrovirus / Species: Rous sarcoma virus / Strain: PRAGUE C / Cell line: BL21 / Gene: GAG / Plasmid: PATV-8 / Species (production host): Escherichia coli / Gene (production host): GAG / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P03322 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: COORDINATES WERE CALCULATED FROM SOLUTION NMR DATA USING THE PROGRAM DYANA. |
-Sample preparation
Details | Contents: H20 |
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Sample conditions | Ionic strength: 100 mM / pH: 6.0 / Pressure: 1 atm / Temperature: 308 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DMX500 / Manufacturer: Bruker / Model: DMX500 / Field strength: 500 MHz |
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-Processing
Software |
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NMR software |
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Refinement | Method: distance geometry / Software ordinal: 1 Details: STRUCTURES WERE CALCULATED USING THE DISTANCE GEOMETRY PROGRAM DYANA. NO FURTHER REFINEMENT WAS PERFORMED. AN ANALYSIS OF THE QUALITY OF STRUCTURES PRODUCED WAS CARRIED OUT USING PROCHECK-NMR. | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 1000 / Conformers submitted total number: 20 |