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- PDB-1k3k: Solution Structure of a Bcl-2 Homolog from Kaposi's Sarcoma Virus -

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Entry
Database: PDB / ID: 1k3k
TitleSolution Structure of a Bcl-2 Homolog from Kaposi's Sarcoma Virus
Componentsfunctional anti-apoptotic factor vBCL-2 homolog
KeywordsAPOPTOSIS / Bcl-2 / herpesvirus / solution structure
Function / homologyBcl2-like / Blc2 family / Blc2-like superfamily / Apoptosis regulator proteins, Bcl-2 family / BCL2-like apoptosis inhibitors family profile. / negative regulation by symbiont of host apoptotic process / regulation of apoptotic process / integral component of membrane / ORF 16 / Bcl-2
Function and homology information
Specimen sourceHuman herpesvirus 8
MethodSOLUTION NMR / simulated annealing
AuthorsHuang, Q. / Petros, A.M. / Virgin, H.W. / Fesik, S.W. / Olejniczak, E.T.
CitationJournal: 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.
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Oct 3, 2001 / Release: Apr 10, 2002
RevisionDateData content typeGroupProviderType
1.0Apr 10, 2002Structure modelrepositoryInitial release
1.1Apr 27, 2008Structure modelVersion format compliance
1.2Jul 13, 2011Structure modelVersion format compliance

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Assembly

Deposited unit
A: functional anti-apoptotic factor vBCL-2 homolog


Theoretical massNumber of molelcules
Total (without water)17,7581
Polyers17,7581
Non-polymers00
Water0
NMR ensembles
Datacriteria
Number of conformers (submitted / calculated)1 / 100AVERAGE, MINIMIZED
Representative

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Components

#1: Protein/peptide functional anti-apoptotic factor vBCL-2 homolog


Mass: 17758.215 Da / Num. of mol.: 1 / Mutation: N76D, V117A / Source: (gene. exp.) Human herpesvirus 8 / Genus: Rhadinovirus / Genus (production host): Escherichia / Production host: Escherichia coli (E. coli) / References: UniProt: P90504, UniProt: Q76RI8*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions IDExperiment IDSolution IDType
111HNCA
121HN(CO)CA
131HN(CA)CB
141HN(COCA)CB
151HNCO
161HN(CA)CO
17113C-NOESY
18115N-NOESY

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Sample preparation

DetailsContents: 0.5-1.0 MM PROTEIN, 20 mM2 H-TRIS, 5 mM2 H-dithiothreitol
sample conditionsIonic strength: 20 mM / pH: 7.8 / Pressure: ATMOSPHERIC atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationDiffraction protocol: SINGLE WAVELENGTH / Monochromatic or laue m l: M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strengthSpectrometer ID
Bruker DRXBrukerDRX5001
Bruker DRXBrukerDRX6002
Bruker DRXBrukerDRX8003

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Processing

NMR software
NameClassification
CNXstructure solution
CNXrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: AVERAGE, MINIMIZED / Conformers calculated total number: 100 / Conformers submitted total number: 1

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