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Yorodumi- PDB-1k3k: Solution Structure of a Bcl-2 Homolog from Kaposi's Sarcoma Virus -
+Open data
-Basic information
Entry | Database: PDB / ID: 1k3k | ||||||
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Title | Solution Structure of a Bcl-2 Homolog from Kaposi's Sarcoma Virus | ||||||
Components | functional anti-apoptotic factor vBCL-2 homolog | ||||||
Keywords | APOPTOSIS / Bcl-2 / herpesvirus / solution structure | ||||||
Function / homology | Function and homology information symbiont-mediated suppression of host apoptosis / regulation of apoptotic process / membrane => GO:0016020 / membrane Similarity search - Function | ||||||
Biological species | Human herpesvirus 8 | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Huang, Q. / Petros, A.M. / Virgin, H.W. / Fesik, S.W. / Olejniczak, E.T. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2002 Title: Solution structure of a Bcl-2 homolog from Kaposi sarcoma virus. Authors: Huang, Q. / Petros, A.M. / Virgin, H.W. / Fesik, S.W. / Olejniczak, E.T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1k3k.cif.gz | 55.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1k3k.ent.gz | 45.9 KB | Display | PDB format |
PDBx/mmJSON format | 1k3k.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k3/1k3k ftp://data.pdbj.org/pub/pdb/validation_reports/k3/1k3k | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 17758.215 Da / Num. of mol.: 1 / Mutation: N76D, V117A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human herpesvirus 8 / Genus: Rhadinovirus / Production host: Escherichia coli (E. coli) / References: UniProt: P90504, UniProt: Q76RI8*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.5-1.0 MM PROTEIN, 20 mM2 H-TRIS, 5 mM2 H-dithiothreitol |
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Sample conditions | Ionic strength: 20 mM / pH: 7.8 / Pressure: ATMOSPHERIC atm / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | ||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||
NMR ensemble | Conformer selection criteria: AVERAGE, MINIMIZED / Conformers calculated total number: 100 / Conformers submitted total number: 1 |