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Yorodumi- PDB-1hvo: ZINC-AND SEQUENCE-DEPENDENT BINDING TO NUCLEIC ACIDS BY THE N-TER... -
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Basic information
| Entry | Database: PDB / ID: 1hvo | ||||||
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| Title | ZINC-AND SEQUENCE-DEPENDENT BINDING TO NUCLEIC ACIDS BY THE N-TERMINAL ZINC FINGER DOMAIN OF THE HIV-1 NUCLEOCAPSID PROTEIN: NMR STRUCTURE OF THE COMPLEX WITH THE PSI-SITE ANALOG, D/ACGCC | ||||||
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Keywords | Viral protein/DNA / DNA / ZINC FINGER DOMAIN / HIV-1 NUCLEOCAPSID PROTEIN / PSI-SITE ANALOG / Viral protein-DNA COMPLEX | ||||||
| Function / homology | Function and homology informationviral budding via host ESCRT complex / host multivesicular body / viral nucleocapsid / viral translational frameshifting / host cell nucleus / host cell plasma membrane / virion membrane / structural molecule activity / RNA binding / zinc ion binding / membrane Similarity search - Function | ||||||
| Biological species | ![]() Human immunodeficiency virus 1 | ||||||
| Method | SOLUTION NMR / simulated annealing | ||||||
Authors | South, T.L. / Summers, M.F. | ||||||
Citation | Journal: Protein Sci. / Year: 1993Title: Zinc- and sequence-dependent binding to nucleic acids by the N-terminal zinc finger of the HIV-1 nucleocapsid protein: NMR structure of the complex with the Psi-site analog, dACGCC. Authors: South, T.L. / Summers, M.F. #1: Journal: Protein Sci. / Year: 1992Title: Nucleocapsid Zinc Fingers Detected in Retroviruses: Exafs Studies of Intact Viruses and the Solution-State Structure of the Nucleocapsid Protein from HIV-1 Authors: Summers, M.F. / Henderson, L.E. / Chance, M.R. / Bess Junior, J.W. / South, T.L. / Blake, P.R. / Sagi, I. / Perez-Alvarado, G. / Sowder III, R.C. / Hare, D.R. / Arthur, L.O. #2: Journal: Biochemistry / Year: 1991Title: The C-Terminal Retroviral-Type Zinc Finger Domain from the HIV-1 Nucleocapsid Protein is Structurally Similar to the N-Terminal Zinc Finger Domain Authors: South, T.L. / Blake, P.R. / Hare, D.R. / Summers, M.F. #3: Journal: Biochemistry / Year: 1990Title: The Nucleocapsid Protein Isolated from HIV-I Particles Binds Zinc and Form Retroviral-Type Zinc Fingers Authors: South, T.L. / Blake, P.R. / Sowder, R. / Arthur, L.O. / Henderson, L.E. / Summers, M.F. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1hvo.cif.gz | 134 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1hvo.ent.gz | 108.9 KB | Display | PDB format |
| PDBx/mmJSON format | 1hvo.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1hvo_validation.pdf.gz | 357.4 KB | Display | wwPDB validaton report |
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| Full document | 1hvo_full_validation.pdf.gz | 493.7 KB | Display | |
| Data in XML | 1hvo_validation.xml.gz | 12.5 KB | Display | |
| Data in CIF | 1hvo_validation.cif.gz | 20.8 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hv/1hvo ftp://data.pdbj.org/pub/pdb/validation_reports/hv/1hvo | HTTPS FTP |
-Related 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: DNA chain | Mass: 1465.001 Da / Num. of mol.: 1 / Source method: obtained synthetically / Keywords: DEOXYRIBONUCLEIC ACID |
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| #2: Protein/peptide | Mass: 2011.379 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Human immunodeficiency virus 1 / Genus: Lentivirus / Keywords: POLYPEPTIDE / References: UniProt: Q70622 |
| #3: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR |
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| NMR details | Text: THE AVERAGE PAIRWISE RMDS'S FOR THE 40 DG/SA STRUCTURES (C,CA,N ATOMS OF RESIDUES A1-L51) IS 0.42 (0.07) ANGSTROMS. THE AVERAGE RMS DEVIATION FOR THE 40 DG/SA STRUCTURES RELATIVE TO THE MEAN ...Text: THE AVERAGE PAIRWISE RMDS'S FOR THE 40 DG/SA STRUCTURES (C,CA,N ATOMS OF RESIDUES A1-L51) IS 0.42 (0.07) ANGSTROMS. THE AVERAGE RMS DEVIATION FOR THE 40 DG/SA STRUCTURES RELATIVE TO THE MEAN COORDINATES (C,CA,N ATOMS OF RESIDUES A1-L51) IS 0.29 (0.07) ANGSTROMS. |
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Sample preparation
| Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
| NMR software | Name: DSPACE / Classification: refinement |
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| Refinement | Method: simulated annealing / Software ordinal: 1 Details: THE INTERNAL CONFORMATION OF THE OLIGODEOXYRIBONUCLEOTIDE, D(ACGCC), WAS HELD FIXED IN AN IDEALIZED A-HELICAL CONFORMATION. THE A-HELIX STRUCTURE WAS GENERATED WITH QUANTA. SIMULATED ...Details: THE INTERNAL CONFORMATION OF THE OLIGODEOXYRIBONUCLEOTIDE, D(ACGCC), WAS HELD FIXED IN AN IDEALIZED A-HELICAL CONFORMATION. THE A-HELIX STRUCTURE WAS GENERATED WITH QUANTA. SIMULATED ANNEALING WAS PERFORMED IN A MANNER THAT ALLOWED ATOMS OF THE ZINC FINGER ONLY TO MOVE DURING REFINEMENT. |
| NMR ensemble | Conformers submitted total number: 15 |
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