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Yorodumi- PDB-3g0v: Crystal structure of the C-terminal domain from the Rous Sarcoma ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3g0v | ||||||
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Title | Crystal structure of the C-terminal domain from the Rous Sarcoma Virus capsid protein: mutant D179A | ||||||
Components | Gag polyproteinGroup-specific antigen | ||||||
Keywords | VIRAL PROTEIN / ALPHA-HELICAL BUNDLE / CAPSID PROTEIN / VIRION / RETROVIRUS | ||||||
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 | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Kingston, R.L. | ||||||
Citation | Journal: Structure / Year: 2009 Title: Proton-linked dimerization of a retroviral capsid protein initiates capsid assembly Authors: Bailey, G.D. / Hyun, J.K. / Mitra, A.K. / Kingston, R.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3g0v.cif.gz | 28.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3g0v.ent.gz | 17.9 KB | Display | PDB format |
PDBx/mmJSON format | 3g0v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g0/3g0v ftp://data.pdbj.org/pub/pdb/validation_reports/g0/3g0v | HTTPS FTP |
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-Related structure data
Related structure data | 3g1gC 3g1iC 3g21C 3g26C 3g28SC 3g29C C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 8430.626 Da / Num. of mol.: 1 / Fragment: C-terminal domain, UNP residues 389-465 / Mutation: D179A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rous sarcoma virus / Strain: Prague C Strain / Gene: gag / Plasmid: pTYB11 / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta 2 (DE3) References: UniProt: P03322, Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases |
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#2: Chemical | ChemComp-NO3 / |
#3: 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: 2.69 Å3/Da / Density % sol: 54.29 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 4.3 Details: 0.2M Succinic acid/KOH, pH4.3, 24% PEG8000, 1M Sodium Nitrate, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.54178 Å |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Oct 21, 2008 / Details: Rigaku Varimax HF confocal optics |
Radiation | Monochromator: Rigaku Varimax HF confocal optics / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 2→38 Å / Num. all: 6413 / Num. obs: 6413 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 10.7 % / Rmerge(I) obs: 0.078 / Net I/σ(I): 9.2 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 10.5 % / Rmerge(I) obs: 0.333 / Mean I/σ(I) obs: 2.8 / Num. unique all: 630 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3G28 Resolution: 2→38 Å / Cor.coef. Fo:Fc: 0.942 / Cor.coef. Fo:Fc free: 0.923 / SU B: 3.499 / SU ML: 0.097 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.174 / ESU R Free: 0.153 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.479 Å2
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Refinement step | Cycle: LAST / Resolution: 2→38 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.004→2.056 Å / Total num. of bins used: 20
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