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Yorodumi- PDB-1bvg: HIV-1 PROTEASE-DMP323 COMPLEX IN SOLUTION, NMR MINIMIZED AVERAGE ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1bvg | ||||||
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Title | HIV-1 PROTEASE-DMP323 COMPLEX IN SOLUTION, NMR MINIMIZED AVERAGE STRUCTURE | ||||||
Components | HIV-1 PROTEASE | ||||||
Keywords | ASPARTYL PROTEASE / AIDS / POLYPROTEIN / HYDROLASE / ENDONUCLEASE / RNA-DIRECTED DNA POLYMERASE | ||||||
Function / homology | Function and homology information integrase activity / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / Minus-strand DNA synthesis / Plus-strand DNA synthesis / Uncoating of the HIV Virion / 2-LTR circle formation / Early Phase of HIV Life Cycle / Vpr-mediated nuclear import of PICs / Integration of provirus ...integrase activity / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / Minus-strand DNA synthesis / Plus-strand DNA synthesis / Uncoating of the HIV Virion / 2-LTR circle formation / Early Phase of HIV Life Cycle / Vpr-mediated nuclear import of PICs / Integration of provirus / APOBEC3G mediated resistance to HIV-1 infection / Binding and entry of HIV virion / viral life cycle / Assembly Of The HIV Virion / HIV-1 retropepsin / : / retroviral ribonuclease H / Budding and maturation of HIV virion / exoribonuclease H / : / exoribonuclease H activity / protein processing / host multivesicular body / RNA-directed DNA polymerase / viral genome integration into host DNA / viral penetration into host nucleus / establishment of integrated proviral latency / RNA-directed DNA polymerase activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / RNA-DNA hybrid ribonuclease activity / peptidase activity / viral nucleocapsid / DNA recombination / Hydrolases; Acting on ester bonds / DNA-directed DNA polymerase / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / symbiont entry into host cell / symbiont-mediated suppression of host gene expression / lipid binding / host cell nucleus / host cell plasma membrane / virion membrane / structural molecule activity / DNA binding / RNA binding / zinc ion binding / membrane / identical protein binding Similarity search - Function | ||||||
Biological species | Human immunodeficiency virus 1 | ||||||
Method | SOLUTION NMR | ||||||
Authors | Yamazaki, T. / Hinck, A.P. / Wang, Y.-X. / Nicholson, L.K. / Torchia, D.A. / Wingfield, P. / Stahl, S.J. / Kaufman, J.D. / Chang, C. / Domaille, P.J. / Lam, P.Y.S. | ||||||
Citation | Journal: Protein Sci. / Year: 1996 Title: Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy. Authors: Yamazaki, T. / Hinck, A.P. / Wang, Y.X. / Nicholson, L.K. / Torchia, D.A. / Wingfield, P. / Stahl, S.J. / Kaufman, J.D. / Chang, C.H. / Domaille, P.J. / Lam, P.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bvg.cif.gz | 77.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bvg.ent.gz | 63.8 KB | Display | PDB format |
PDBx/mmJSON format | 1bvg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bv/1bvg ftp://data.pdbj.org/pub/pdb/validation_reports/bv/1bvg | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10757.664 Da / Num. of mol.: 2 / Mutation: C95A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human immunodeficiency virus 1 / Genus: Lentivirus / Strain: HXB2 / Plasmid: PET11A / Production host: Escherichia coli (E. coli) / References: UniProt: P04585, HIV-1 retropepsin #2: Chemical | ChemComp-DMP / [ | |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR details | Text: THIS ENTRY CONTAINS MINIMIZED AVERAGE STRUCTURE. |
-Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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-Processing
Software |
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NMR software |
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NMR ensemble | Conformer selection criteria: MINIMIZED / Conformers calculated total number: 28 / Conformers submitted total number: 1 |