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- PDB-1a6s: M-DOMAIN FROM GAG POLYPROTEIN OF ROUS SARCOMA VIRUS, NMR, 20 STRU... -
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Open data
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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 | ||||||
![]() | GAG POLYPROTEIN | ||||||
![]() | VIRAL PROTEIN / CORE PROTEIN / VIRUS STRUCTURE / MEMBRANE BINDING | ||||||
Function / homology | ![]() host cell nucleoplasm / viral procapsid maturation / host cell nucleolus / Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / viral capsid / nucleic acid binding / structural constituent of virion / 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 / nucleic acid binding / structural constituent of virion / aspartic-type endopeptidase activity / host cell plasma membrane / proteolysis / zinc ion binding / membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / distance geometry | ||||||
![]() | 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. | ||||||
![]() | ![]() 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: ![]() 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: ![]() 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: ![]() 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: ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 507.9 KB | Display | ![]() |
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PDB format | ![]() | 423.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 344 KB | Display | ![]() |
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Full document | ![]() | 567.5 KB | Display | |
Data in XML | ![]() | 101.5 KB | Display | |
Data in CIF | ![]() | 131.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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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.) ![]() ![]() ![]() |
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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. |
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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
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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 |