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Open data
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Basic information
| Entry | Database: PDB / ID: 3vl1 | ||||||
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| Title | Crystal structure of yeast Rpn14 | ||||||
Components | 26S proteasome regulatory subunit RPN14 | ||||||
Keywords | CHAPERONE / Beta-Propeller / Rpt6 | ||||||
| Function / homology | Function and homology informationproteasome regulatory particle assembly / protein folding chaperone / proteasome complex / ubiquitin-dependent protein catabolic process / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å | ||||||
Authors | Kim, S. / Nishide, A. / Saeki, Y. / Takagi, K. / Tanaka, K. / Kato, K. / Mizushima, T. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.F / Year: 2012Title: New crystal structure of the proteasome-dedicated chaperone Rpn14 at 1.6 A resolution Authors: Kim, S. / Nishide, A. / Saeki, Y. / Takagi, K. / Tanaka, K. / Kato, K. / Mizushima, T. | ||||||
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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 | 3vl1.cif.gz | 360.2 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb3vl1.ent.gz | 295.2 KB | Display | PDB format |
| PDBx/mmJSON format | 3vl1.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 3vl1_validation.pdf.gz | 432.2 KB | Display | wwPDB validaton report |
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| Full document | 3vl1_full_validation.pdf.gz | 452.8 KB | Display | |
| Data in XML | 3vl1_validation.xml.gz | 36.5 KB | Display | |
| Data in CIF | 3vl1_validation.cif.gz | 52.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vl/3vl1 ftp://data.pdbj.org/pub/pdb/validation_reports/vl/3vl1 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 3acpS S: Starting model for refinement |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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| 2 | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 46657.926 Da / Num. of mol.: 2 / Mutation: E384A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: RPN14 / Plasmid: pET28 / Production host: ![]() #2: 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: 1.92 Å3/Da / Density % sol: 36.02 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: 0.1M NaCitrate pH4.5, 0.2M MgCl2, 10%(w/v) PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL44XU / Wavelength: 0.9 Å |
| Detector | Type: RAYONIX MX225HE / Detector: CCD / Date: Nov 25, 2009 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
| Reflection | Resolution: 1.6→50 Å / Num. obs: 90359 / % possible obs: 97.2 % / Observed criterion σ(I): -3 / Redundancy: 3.9 % / Rmerge(I) obs: 0.048 / Net I/σ(I): 19.5 |
| Reflection shell | Resolution: 1.6→1.62 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.528 / % possible all: 97.2 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 3ACP Resolution: 1.6→24.47 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.939 / SU B: 5.725 / SU ML: 0.089 / Cross valid method: THROUGHOUT / ESU R Free: 0.111 / Stereochemistry target values: MAXIMUM LIKELIHOOD / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 28.67 Å2
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| Refinement step | Cycle: LAST / Resolution: 1.6→24.47 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 1.597→1.638 Å / Total num. of bins used: 20
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