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Yorodumi- PDB-2lsj: Solution structure of the mouse Rev1 CTD in complex with the Rev1... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2lsj | ||||||
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Title | Solution structure of the mouse Rev1 CTD in complex with the Rev1-interacting Region (RIR)of Pol Kappa | ||||||
Components |
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Keywords | PROTEIN BINDING/PROTEIN BINDING / Rev1 / RIR / Pol Kappa / Translesion Synthesis / TLS / CTD / PROTEIN BINDING-PROTEIN BINDING complex | ||||||
Function / homology | Function and homology information Gap-filling DNA repair synthesis and ligation in GG-NER / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / HDR through Homologous Recombination (HRR) / Termination of translesion DNA synthesis / Dual Incision in GG-NER / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / deoxycytidyl transferase activity ...Gap-filling DNA repair synthesis and ligation in GG-NER / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / HDR through Homologous Recombination (HRR) / Termination of translesion DNA synthesis / Dual Incision in GG-NER / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / deoxycytidyl transferase activity / nucleotide-excision repair, DNA gap filling / error-free translesion synthesis / site of DNA damage / error-prone translesion synthesis / response to UV / cellular response to UV / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / DNA replication / damaged DNA binding / molecular adaptor activity / DNA-directed DNA polymerase / DNA-directed DNA polymerase activity / nuclear body / DNA repair / DNA damage response / nucleus / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Liu, J. / Wojtaszek, J. / Zhou, P. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2012 Title: Multifaceted recognition of vertebrate Rev1 by translesion polymerases zeta and kappa. Authors: Wojtaszek, J. / Liu, J. / D'Souza, S. / Wang, S. / Xue, Y. / Walker, G.C. / Zhou, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lsj.cif.gz | 706.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2lsj.ent.gz | 590.2 KB | Display | PDB format |
PDBx/mmJSON format | 2lsj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2lsj_validation.pdf.gz | 504.6 KB | Display | wwPDB validaton report |
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Full document | 2lsj_full_validation.pdf.gz | 785.5 KB | Display | |
Data in XML | 2lsj_validation.xml.gz | 42.4 KB | Display | |
Data in CIF | 2lsj_validation.cif.gz | 66.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ls/2lsj ftp://data.pdbj.org/pub/pdb/validation_reports/ls/2lsj | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 13271.145 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Rev1, Rev1l / Plasmid: pMAL-C2 / Production host: Escherichia coli (E. coli) References: UniProt: Q920Q2, Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases |
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#2: Protein/peptide | Mass: 2992.351 Da / Num. of mol.: 1 / Fragment: Rev1-interacting Region (RIR) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: pET15b / Production host: Escherichia coli (E. coli) / References: UniProt: Q9QUG2 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0.1 / pH: 7.0 / Pressure: ambient / Temperature: 310 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |