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Yorodumi- PDB-5lcm: STRUCTURE OF the RAD14 DNA-binding domain IN COMPLEX WITH N2-acet... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5lcm | ||||||
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Title | STRUCTURE OF the RAD14 DNA-binding domain IN COMPLEX WITH N2-acetylaminonaphtyl- GUANINE CONTAINING DNA | ||||||
Components |
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Keywords | DNA BINDING PROTEIN / Nucleotide excision repair DNA damage recognition | ||||||
Function / homology | Function and homology information nucleotide-excision repair involved in interstrand cross-link repair / nucleotide-excision repair factor 1 complex / nucleotide-excision repair, DNA damage recognition / UV-damage excision repair / Dual incision in TC-NER / base-excision repair / damaged DNA binding / zinc ion binding / nucleus Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.9 Å | ||||||
Authors | Schneider, S. / Ebert, C. / Simon, N. / Carell, T. | ||||||
Funding support | Germany, 1items
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Citation | Journal: Chembiochem / Year: 2017 Title: Structural Insights into the Recognition of N(2) -Aryl- and C8-Aryl DNA Lesions by the Repair Protein XPA/Rad14. Authors: Ebert, C. / Simon, N. / Schneider, S. / Carell, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5lcm.cif.gz | 165.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5lcm.ent.gz | 140.4 KB | Display | PDB format |
PDBx/mmJSON format | 5lcm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lc/5lcm ftp://data.pdbj.org/pub/pdb/validation_reports/lc/5lcm | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 14224.176 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) Gene: RAD14, YMR201C, YM8325.02C / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: P28519 #2: DNA chain | | Mass: 4672.143 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Saccharomyces cerevisiae (brewer's yeast) #3: DNA chain | | Mass: 4674.046 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Saccharomyces cerevisiae (brewer's yeast) #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 49.68 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion Details: 0.2M Ammonium nitrate 40% (v/v) 2-methyl-1,3,-propanediol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID30B / Wavelength: 0.9726 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: May 4, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9726 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→49.2 Å / Num. obs: 28349 / % possible obs: 99 % / Redundancy: 4.5 % / CC1/2: 0.99 / Rmerge(I) obs: 0.148 / Net I/σ(I): 6.2 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.8 / Mean I/σ(I) obs: 1.1 / % possible all: 99 |
-Processing
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Refinement | Resolution: 1.9→49.2 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.927 / SU B: 11.824 / SU ML: 0.177 / Cross valid method: THROUGHOUT / ESU R: 0.212 / ESU R Free: 0.179 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.009 Å2
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Refinement step | Cycle: 1 / Resolution: 1.9→49.2 Å
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