+Open data
-Basic information
Entry | Database: PDB / ID: 1roc | ||||||
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Title | Crystal structure of the histone deposition protein Asf1 | ||||||
Components | Anti-silencing protein 1 | ||||||
Keywords | REPLICATION / CHAPERONE / beta-sandwich | ||||||
Function / homology | Function and homology information Formation of Senescence-Associated Heterochromatin Foci (SAHF) / : / H3 histone acetyltransferase complex / acetyltransferase activator activity / DNA replication-dependent chromatin assembly / nucleosome disassembly / : / silent mating-type cassette heterochromatin formation / subtelomeric heterochromatin formation / negative regulation of DNA damage checkpoint ...Formation of Senescence-Associated Heterochromatin Foci (SAHF) / : / H3 histone acetyltransferase complex / acetyltransferase activator activity / DNA replication-dependent chromatin assembly / nucleosome disassembly / : / silent mating-type cassette heterochromatin formation / subtelomeric heterochromatin formation / negative regulation of DNA damage checkpoint / regulation of DNA repair / positive regulation of transcription elongation by RNA polymerase II / regulation of protein phosphorylation / nucleosome assembly / chromatin organization / histone binding / regulation of gene expression / chromosome, telomeric region / regulation of transcription by RNA polymerase II / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.5 Å | ||||||
Authors | Daganzo, S.M. / Erzberger, J.P. / Lam, W.M. / Skordalakes, E. / Zhang, R. / Franco, A.A. / Brill, S.J. / Adams, P.D. / Berger, J.M. / Kaufman, P.D. | ||||||
Citation | Journal: Curr.Biol. / Year: 2003 Title: Structure and function of the conserved core of histone deposition protein Asf1. Authors: Daganzo, S.M. / Erzberger, J.P. / Lam, W.M. / Skordalakes, E. / Zhang, R. / Franco, A.A. / Brill, S.J. / Adams, P.D. / Berger, J.M. / Kaufman, P.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1roc.cif.gz | 46.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1roc.ent.gz | 32.9 KB | Display | PDB format |
PDBx/mmJSON format | 1roc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ro/1roc ftp://data.pdbj.org/pub/pdb/validation_reports/ro/1roc | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 17499.730 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: ASF1, YJL115W, J0755 / Plasmid: pSV271 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 RIL / References: UniProt: P32447 | ||
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#2: Chemical | ChemComp-BR / #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.89 Å3/Da / Density % sol: 34.82 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG 3350, sodium bromide, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 200 K | |||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 0.956, 0.920 | |||||||||
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 30, 2003 | |||||||||
Radiation | Monochromator: Double Crystal Si (111) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 1.4→50 Å / Num. all: 25672 / Num. obs: 23670 / % possible obs: 92.2 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.3 % / Rsym value: 0.06 / Net I/σ(I): 18.8 | |||||||||
Reflection shell | Resolution: 1.4→1.46 Å / Redundancy: 1.5 % / Mean I/σ(I) obs: 1.9 / Rsym value: 0.34 / % possible all: 48 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.5→30 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.926 / SU B: 1.685 / SU ML: 0.063 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 2.6 / ESU R: 0.095 / ESU R Free: 0.1 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.847 Å2
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Refinement step | Cycle: LAST / Resolution: 1.5→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.5→1.539 Å / Total num. of bins used: 20 /
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Refinement TLS params. | Method: refined / Origin x: 61.9243 Å / Origin y: 9.4668 Å / Origin z: 7.3717 Å
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Refinement | *PLUS Highest resolution: 1.5 Å / Lowest resolution: 30 Å / Num. reflection Rfree: 1082 / Rfactor Rwork: 0.1977 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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