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Open data
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Basic information
| Entry | Database: PDB / ID: 3v46 | ||||||
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| Title | Crystal Structure of Yeast Cdc73 C-Terminal Domain | ||||||
Components | Cell division control protein 73 | ||||||
Keywords | TRANSCRIPTION / Ras-like fold / non-GTP binding / Protein Interaction Surface / Transcription Elongation Factor | ||||||
| Function / homology | Function and homology informationpositive regulation of transcription elongation by RNA polymerase I / regulation of transcription-coupled nucleotide-excision repair / RNA polymerase II C-terminal domain phosphoserine binding / Cdc73/Paf1 complex / negative regulation of DNA recombination / mRNA 3'-end processing / RNA polymerase II complex binding / transcription elongation by RNA polymerase I / transcription elongation by RNA polymerase II / positive regulation of transcription elongation by RNA polymerase II ...positive regulation of transcription elongation by RNA polymerase I / regulation of transcription-coupled nucleotide-excision repair / RNA polymerase II C-terminal domain phosphoserine binding / Cdc73/Paf1 complex / negative regulation of DNA recombination / mRNA 3'-end processing / RNA polymerase II complex binding / transcription elongation by RNA polymerase I / transcription elongation by RNA polymerase II / positive regulation of transcription elongation by RNA polymerase II / euchromatin / chromatin binding / nucleus Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.549 Å | ||||||
Authors | Amrich, C.G. / VanDemark, A.P. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2012Title: Cdc73 subunit of Paf1 complex contains C-terminal Ras-like domain that promotes association of Paf1 complex with chromatin. Authors: Amrich, C.G. / Davis, C.P. / Rogal, W.P. / Shirra, M.K. / Heroux, A. / Gardner, R.G. / Arndt, K.M. / VanDemark, A.P. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 3v46.cif.gz | 133.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb3v46.ent.gz | 102.9 KB | Display | PDB format |
| PDBx/mmJSON format | 3v46.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 3v46_validation.pdf.gz | 419.7 KB | Display | wwPDB validaton report |
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| Full document | 3v46_full_validation.pdf.gz | 421.3 KB | Display | |
| Data in XML | 3v46_validation.xml.gz | 9.5 KB | Display | |
| Data in CIF | 3v46_validation.cif.gz | 13.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v4/3v46 ftp://data.pdbj.org/pub/pdb/validation_reports/v4/3v46 | HTTPS FTP |
-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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| Components on special symmetry positions |
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Components
| #1: Protein | Mass: 20065.814 Da / Num. of mol.: 1 / Fragment: C-Terminal Domain residues 230-393 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: CDC73, YLR418C / Plasmid: pET151 / Production host: ![]() |
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| #2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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Sample preparation
| Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.68 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 8 Details: PEG 8000, pH 8.0, VAPOR DIFFUSION, temperature 293K |
-Data collection
| Diffraction |
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| Diffraction source |
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| Detector |
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| Radiation |
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| Radiation wavelength |
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| Reflection | Redundancy: 12.3 % / Av σ(I) over netI: 58.1 / Number: 230812 / Rmerge(I) obs: 0.064 / Χ2: 0.87 / D res high: 1.78 Å / D res low: 50 Å / Num. obs: 18777 / % possible obs: 99.9 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Diffraction reflection shell |
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| Reflection | Resolution: 1.549→50 Å / Num. all: 28216 / Num. obs: 28111 / % possible obs: 99.3 % / Observed criterion σ(F): 3 / Observed criterion σ(I): 2 / Redundancy: 7.1 % / Biso Wilson estimate: 30.5 Å2 / Rmerge(I) obs: 0.054 / Χ2: 2.038 / Net I/σ(I): 17.5 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection shell |
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-Phasing
| Phasing | Method: SAD | ||||||||||||||||||||||||||||
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| Phasing MAD set site |
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Processing
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| Refinement | Resolution: 1.549→37.706 Å / Occupancy max: 1 / Occupancy min: 0.45 / FOM work R set: 0.8784 / SU ML: 0.16 / σ(F): 0.18 / Phase error: 18.18 / Stereochemistry target values: ML
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 40.378 Å2 / ksol: 0.4 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso max: 78.97 Å2 / Biso mean: 31.8662 Å2 / Biso min: 11.58 Å2
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| Refinement step | Cycle: LAST / Resolution: 1.549→37.706 Å
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| Refine LS restraints |
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| LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 10
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