+Open data
-Basic information
Entry | Database: PDB / ID: 2ynn | ||||||
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Title | yeast betaprime COP 1-304 with KTKTN motif | ||||||
Components |
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Keywords | PROTEIN TRANSPORT / PEPTIDE BINDING PROTEIN / MEMBRANE TRAFFICKING / COPI-MEDIATED TRAFFICKING / DILYSINE MOTIFS | ||||||
Function / homology | Function and homology information COPI vesicle coat / COPI-dependent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / late endosome to vacuole transport via multivesicular body sorting pathway / intracellular mRNA localization / intra-Golgi vesicle-mediated transport / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / endoplasmic reticulum to Golgi vesicle-mediated transport / ubiquitin binding / intracellular protein transport ...COPI vesicle coat / COPI-dependent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / late endosome to vacuole transport via multivesicular body sorting pathway / intracellular mRNA localization / intra-Golgi vesicle-mediated transport / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / endoplasmic reticulum to Golgi vesicle-mediated transport / ubiquitin binding / intracellular protein transport / Golgi membrane / structural molecule activity Similarity search - Function | ||||||
Biological species | SACCHAROMYCES CEREVISIAE (brewer's yeast) SYNTHETIC CONSTRUCT (others) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.782 Å | ||||||
Authors | Jackson, L.P. / Lewis, M. / Kent, H.M. / Edeling, M.A. / Evans, P.R. / Duden, R. / Owen, D.J. | ||||||
Citation | Journal: Dev.Cell / Year: 2012 Title: Molecular Basis for Recognition of Dilysine Trafficking Motifs by Copi. Authors: Jackson, L.P. / Lewis, M. / Kent, H.M. / Edeling, M.A. / Evans, P.R. / Duden, R. / Owen, D.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ynn.cif.gz | 80.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ynn.ent.gz | 60.8 KB | Display | PDB format |
PDBx/mmJSON format | 2ynn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ynn_validation.pdf.gz | 436.9 KB | Display | wwPDB validaton report |
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Full document | 2ynn_full_validation.pdf.gz | 438.1 KB | Display | |
Data in XML | 2ynn_validation.xml.gz | 15 KB | Display | |
Data in CIF | 2ynn_validation.cif.gz | 21.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yn/2ynn ftp://data.pdbj.org/pub/pdb/validation_reports/yn/2ynn | HTTPS FTP |
-Related structure data
Related structure data | 2ynoSC 2ynpC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-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: 34651.953 Da / Num. of mol.: 1 / Fragment: WD40-REPEAT DOMAIN, RESIDUES 1-304 Source method: isolated from a genetically manipulated source Details: IN COMPLEX WITH KXKXX MOTIF Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Plasmid: PMWGST / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYSS / References: UniProt: P41811 | ||||
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#2: Protein/peptide | Mass: 944.106 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others) | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Has protein modification | Y | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 44 % / Description: NONE |
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Crystal grow | Details: 0.1M HEPES PH 7.5, 0.5M AMMONIUM SULFATE, 30% V/V MPD |
-Data collection
Diffraction | Mean temperature: 77 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.917 |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Jul 2, 2011 |
Radiation | Monochromator: SINGLE BOUNCE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.917 Å / Relative weight: 1 |
Reflection | Resolution: 1.73→56 Å / Num. obs: 54637 / % possible obs: 100 % / Observed criterion σ(I): 2 / Redundancy: 2 % / Biso Wilson estimate: 14.12 Å2 / Rmerge(I) obs: 0.13 / Net I/σ(I): 8.7 |
Reflection shell | Resolution: 1.73→1.77 Å / Redundancy: 6.3 % / Rmerge(I) obs: 0.66 / Mean I/σ(I) obs: 2.7 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2YNO Resolution: 1.782→55.928 Å / SU ML: 0.33 / σ(F): 1.35 / Phase error: 16.49 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.73 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 41.27 Å2 / ksol: 0.4 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 14.1 Å2
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Refinement step | Cycle: LAST / Resolution: 1.782→55.928 Å
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Refine LS restraints |
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LS refinement shell |
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