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- PDB-1b22: RAD51 (N-TERMINAL DOMAIN) -

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Basic information

Entry
Database: PDB / ID: 1b22
TitleRAD51 (N-TERMINAL DOMAIN)
ComponentsDNA REPAIR PROTEIN RAD51
KeywordsDNA BINDING PROTEIN / DNA BINDING / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics
Function / homology
Function and homology information


response to glucoside / mitotic recombination-dependent replication fork processing / cellular response to camptothecin / DNA recombinase assembly / chromosome organization involved in meiotic cell cycle / telomere maintenance via telomere lengthening / mitotic recombination / telomere maintenance via recombination / positive regulation of DNA ligation / strand invasion ...response to glucoside / mitotic recombination-dependent replication fork processing / cellular response to camptothecin / DNA recombinase assembly / chromosome organization involved in meiotic cell cycle / telomere maintenance via telomere lengthening / mitotic recombination / telomere maintenance via recombination / positive regulation of DNA ligation / strand invasion / replication-born double-strand break repair via sister chromatid exchange / cellular response to cisplatin / lateral element / cellular response to hydroxyurea / DNA strand exchange activity / single-stranded DNA helicase activity / Homologous DNA Pairing and Strand Exchange / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / reciprocal meiotic recombination / Resolution of D-loop Structures through Holliday Junction Intermediates / replication fork processing / condensed chromosome / HDR through Single Strand Annealing (SSA) / DNA unwinding involved in DNA replication / regulation of double-strand break repair via homologous recombination / Presynaptic phase of homologous DNA pairing and strand exchange / Transcriptional Regulation by E2F6 / response to X-ray / interstrand cross-link repair / DNA polymerase binding / ATP-dependent activity, acting on DNA / nuclear chromosome / condensed nuclear chromosome / meiotic cell cycle / regulation of protein phosphorylation / double-strand break repair via homologous recombination / microtubule organizing center / HDR through Homologous Recombination (HRR) / cellular response to ionizing radiation / PML body / Meiotic recombination / cellular response to gamma radiation / response to toxic substance / single-stranded DNA binding / site of double-strand break / double-stranded DNA binding / chromosome, telomeric region / DNA recombination / protein C-terminus binding / mitochondrial matrix / DNA repair / chromatin / cellular response to DNA damage stimulus / response to xenobiotic stimulus => GO:0009410 / chromatin binding / perinuclear region of cytoplasm / enzyme binding / protein-containing complex / mitochondrion / nucleoplasm / ATP binding / identical protein binding / nucleus / cytoplasm
Similarity search - Function
DNA recombination/repair protein Rad51 / DNA recombination and repair protein, RecA-like / Rad51/DMC1/RadA / Rad51 / DNA recombination and repair protein Rad51-like, C-terminal / Helix-hairpin-helix domain / DNA recombination and repair protein RecA, monomer-monomer interface / RecA family profile 2. / DNA recombination and repair protein RecA-like, ATP-binding domain / RecA family profile 1. ...DNA recombination/repair protein Rad51 / DNA recombination and repair protein, RecA-like / Rad51/DMC1/RadA / Rad51 / DNA recombination and repair protein Rad51-like, C-terminal / Helix-hairpin-helix domain / DNA recombination and repair protein RecA, monomer-monomer interface / RecA family profile 2. / DNA recombination and repair protein RecA-like, ATP-binding domain / RecA family profile 1. / DNA repair Rad51/transcription factor NusA, alpha-helical / 5' to 3' exonuclease, C-terminal subdomain / DNA polymerase; domain 1 / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
DNA repair protein RAD51 homolog 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / RANDOM SIMULATED ANNEALING
AuthorsAihara, H. / Ito, Y. / Kurumizaka, H. / Yokoyama, S. / Shibata, T. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)
CitationJournal: J.Mol.Biol. / Year: 1999
Title: The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR.
Authors: Aihara, H. / Ito, Y. / Kurumizaka, H. / Yokoyama, S. / Shibata, T.
History
DepositionDec 4, 1998Deposition site: BNL / Processing site: RCSB
Revision 1.0Dec 3, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: DNA REPAIR PROTEIN RAD51


Theoretical massNumber of molelcules
Total (without water)12,5471
Polymers12,5471
Non-polymers00
Water0
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)30 / 140LEAST TARGET FUNCTION VALUES
Representative

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Components

#1: Protein DNA REPAIR PROTEIN RAD51 /


Mass: 12547.283 Da / Num. of mol.: 1 / Fragment: N-TERMINAL DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: PET3A / Gene (production host): RAD51(1-114) / Production host: Escherichia coli (E. coli) / Strain (production host): JM109(DE3) / References: UniProt: Q06609

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111DOUBLE
121TRIPLE RESONANCE EXPERIMENTS
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED HUMAN RAD51(1-114).

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Sample preparation

Sample conditionsIonic strength: 100mM NACL / pH: 6.5 / Pressure: 1 atm / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DRX600 / Manufacturer: Bruker / Model: DRX600 / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.851BRUNGERrefinement
X-PLORstructure solution
RefinementMethod: RANDOM SIMULATED ANNEALING / Software ordinal: 1 / Details: SIMULATED ANNEALING REFINEMENT
NMR ensembleConformer selection criteria: LEAST TARGET FUNCTION VALUES / Conformers calculated total number: 140 / Conformers submitted total number: 30

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