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- PDB-2ezz: SOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF... -

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Entry
Database: PDB / ID: 2ezz
TitleSOLUTION STRUCTURE OF HUMAN BARRIER-TO-AUTOINTEGRATION FACTOR BAF NMR, ENSEMBLE OF 20 SIMULATED ANNEALING STRUCTURES
ComponentsBARRIER-TO-AUTOINTEGRATION FACTOR
KeywordsDNA BINDING PROTEIN / DNA-BINDING PROTEIN / INTEGRATION / AIDS / RETROVIRUSES
Function / homology
Function and homology information


negative regulation of protein ADP-ribosylation / Nuclear Envelope Breakdown / mitotic nuclear membrane reassembly / Initiation of Nuclear Envelope (NE) Reformation / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / negative regulation of type I interferon production / negative regulation of viral genome replication / negative regulation of cGAS/STING signaling pathway / 2-LTR circle formation ...negative regulation of protein ADP-ribosylation / Nuclear Envelope Breakdown / mitotic nuclear membrane reassembly / Initiation of Nuclear Envelope (NE) Reformation / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / negative regulation of type I interferon production / negative regulation of viral genome replication / negative regulation of cGAS/STING signaling pathway / 2-LTR circle formation / Vpr-mediated nuclear import of PICs / Integration of provirus / APOBEC3G mediated resistance to HIV-1 infection / chromosome organization / condensed chromosome / negative regulation of innate immune response / response to virus / DNA integration / chromatin organization / nuclear envelope / double-stranded DNA binding / response to oxidative stress / chromatin / protein homodimerization activity / DNA binding / nucleoplasm / identical protein binding / nucleus / cytoplasm / cytosol
Similarity search - Function
Barrier-to-autointegration factor, BAF / Barrier- to-autointegration factor, BAF / Barrier-to-autointegration factor, BAF superfamily / Barrier to autointegration factor / Barrier to autointegration factor / DNA polymerase; domain 1 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Barrier-to-autointegration factor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsClore, G.M. / Cai, M. / Gronenborn, A.M.
CitationJournal: Nat.Struct.Biol. / Year: 1998
Title: Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration.
Authors: Cai, M. / Huang, Y. / Zheng, R. / Wei, S.Q. / Ghirlando, R. / Lee, M.S. / Craigie, R. / Gronenborn, A.M. / Clore, G.M.
History
DepositionJul 26, 1998Processing site: BNL
Revision 1.0Jan 13, 1999Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 2022Group: Database references / Derived calculations / Structure summary
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_keywords
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_keywords.text
Revision 1.4May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: BARRIER-TO-AUTOINTEGRATION FACTOR
B: BARRIER-TO-AUTOINTEGRATION FACTOR


Theoretical massNumber of molelcules
Total (without water)20,1472
Polymers20,1472
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 40
Representative

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Components

#1: Protein BARRIER-TO-AUTOINTEGRATION FACTOR


Mass: 10073.588 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: O75531

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 6.5 / Temperature: 313 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DMX600BrukerDMX6005001
Bruker DMX500BrukerDMX5006002

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Processing

Software
NameVersionClassification
CNSrefinement
X-PLOR3.1model building
X-PLOR3.1refinement
CNSphasing
X-PLOR3.1phasing
NMR software
NameVersionDeveloperClassification
CNSBRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,SIMONSON,WARRENrefinement
CNS MODIFIEDMODIFIEDstructure solution
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformers calculated total number: 40 / Conformers submitted total number: 20

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