+Open data
-Basic information
Entry | Database: PDB / ID: 2z2r | ||||||
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Title | Nucleosome assembly proteins I (NAP-1, 74-365) | ||||||
Components | Nucleosome assembly protein | ||||||
Keywords | CHAPERONE / Nucleosome Assembly Protein 1 (NAP1) / Histone chaperone | ||||||
Function / homology | Function and homology information protein localization to cell division site after cytokinesis / Gin4 complex / cellular bud neck septin collar / budding cell bud growth / : / septin ring assembly / septum digestion after cytokinesis / nucleosome disassembly / NLS-bearing protein import into nucleus / cell division site ...protein localization to cell division site after cytokinesis / Gin4 complex / cellular bud neck septin collar / budding cell bud growth / : / septin ring assembly / septum digestion after cytokinesis / nucleosome disassembly / NLS-bearing protein import into nucleus / cell division site / enzyme activator activity / positive regulation of microtubule polymerization / cyclin binding / positive regulation of transcription elongation by RNA polymerase II / ribosomal small subunit biogenesis / nucleosome assembly / unfolded protein binding / histone binding / chromatin binding / chromatin / DNA binding / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å | ||||||
Authors | Park, Y.J. / Luger, K. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2008 Title: A beta-hairpin comprising the nuclear localization sequence sustains the self-associated states of nucleosome assembly protein 1 Authors: Park, Y.J. / McBryant, S.J. / Luger, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2z2r.cif.gz | 110.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2z2r.ent.gz | 87.2 KB | Display | PDB format |
PDBx/mmJSON format | 2z2r.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z2/2z2r ftp://data.pdbj.org/pub/pdb/validation_reports/z2/2z2r | HTTPS FTP |
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-Related structure data
Related structure data | 2ayuS S: Starting model for refinement |
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Similar 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: 33879.812 Da / Num. of mol.: 2 / Fragment: residues 74-365 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: NAP1 / Plasmid: pet28a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21DE3 / References: UniProt: P25293 |
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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: 4.23 Å3/Da / Density % sol: 70.9 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 40% MPD, 0.1M sodium citrate, 0.2M ammonium acetate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 1.1 Å |
Detector | Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→50 Å / Num. all: 19761 / Num. obs: 17067 / % possible obs: 86.4 % / Redundancy: 5 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 14 |
Reflection shell | Highest resolution: 3.2 Å / Redundancy: 5 % / Rmerge(I) obs: 0.38 / Mean I/σ(I) obs: 3.5 / Num. unique all: 17067 / % possible all: 92 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2ayu Resolution: 3.2→50 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0
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Refinement step | Cycle: LAST / Resolution: 3.2→50 Å
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Refine LS restraints |
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