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- PDB-6cw4: HADDOCK structure of the Rous sarcoma virus matrix protein (M-dom... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6cw4 | ||||||
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Title | HADDOCK structure of the Rous sarcoma virus matrix protein (M-domain) in complex with inositol 1,3,5-trisphosphate | ||||||
![]() | Matrix protein p19 | ||||||
![]() | VIRAL PROTEIN / RSV / ASV / Gag / I(1 / 3 / 5)P3 | ||||||
Function / homology | ![]() Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / ribonuclease H / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / RNA stem-loop binding / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases ...Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / ribonuclease H / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / RNA stem-loop binding / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / viral nucleocapsid / DNA recombination / DNA-directed DNA polymerase / Hydrolases; Acting on ester bonds / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / symbiont entry into host cell / proteolysis / DNA binding / zinc ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Vlach, J. / Saad, J.S. | ||||||
![]() | ![]() Title: Structural basis for targeting avian sarcoma virus Gag polyprotein to the plasma membrane for virus assembly. Authors: Vlach, J. / Eastep, G.N. / Ghanam, R.H. / Watanabe, S.M. / Carter, C.A. / Saad, J.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 575.1 KB | Display | ![]() |
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PDB format | ![]() | 487.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 894.3 KB | Display | ![]() |
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Full document | ![]() | 991.7 KB | Display | |
Data in XML | ![]() | 48.5 KB | Display | |
Data in CIF | ![]() | 77 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6ccjC ![]() 6ce5C ![]() 6cusC ![]() 6cv8C C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 9209.771 Da / Num. of mol.: 1 / Fragment: residues 1-87 / Mutation: M1S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-FGV / ( |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Sample state: isotropic / Type: 2D 1H-15N ![]() |
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Sample preparation
Details | Type: solution Contents: 100 uM [U-98% 15N] Matrix protein, 50 mM sodium phosphate, 2 mM TCEP, 1.6 mM IP3, 95% H2O/5% D2O Label: s1 / Solvent system: 95% H2O/5% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 100 M / Label: cond1 / pH: 6 / Pressure: 1 atm / Temperature: 305 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE II / Manufacturer: Bruker / Model: AVANCE II / Field strength: 700 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 4 | |||||||||||||||
NMR representative | Selection criteria: medoid | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |