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Open data
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Basic information
Entry | Database: PDB / ID: 1qso | ||||||
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Title | Histone Acetyltransferase HPA2 from Saccharomyces Cerevisiae | ||||||
![]() | HPA2 HISTONE ACETYLTRANSFERASE | ||||||
![]() | TRANSFERASE / TETRAMER / HISTONE ACETYLTRANSFERASE | ||||||
Function / homology | ![]() polyamine acetylation / Hpa2 acetyltransferase complex / spermidine acetylation / spermidine binding / diamine N-acetyltransferase activity / N-acetyltransferase activity / protein acetylation / histone acetyltransferase activity / histone acetyltransferase / identical protein binding ...polyamine acetylation / Hpa2 acetyltransferase complex / spermidine acetylation / spermidine binding / diamine N-acetyltransferase activity / N-acetyltransferase activity / protein acetylation / histone acetyltransferase activity / histone acetyltransferase / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Angus-Hill, M.L. / Dutnall, R.N. / Tafrov, S.T. / Sterngalnz, R. / Ramakrishnan, V. | ||||||
![]() | ![]() Title: Crystal structure of the histone acetyltransferase Hpa2: A tetrameric member of the Gcn5-related N-acetyltransferase superfamily. Authors: Angus-Hill, M.L. / Dutnall, R.N. / Tafrov, S.T. / Sternglanz, R. / Ramakrishnan, V. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 128.3 KB | Display | ![]() |
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PDB format | ![]() | 103.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 434.4 KB | Display | ![]() |
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Full document | ![]() | 449.3 KB | Display | |
Data in XML | ![]() | 22.9 KB | Display | |
Data in CIF | ![]() | 30.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 17590.830 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: PET13A / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.37 Å3/Da / Density % sol: 63.47 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8 Details: PEG 4000, TRIS.CL, CALCIUM ACETATE, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 55 % | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: BRANDEIS / Detector: CCD / Date: Jan 1, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.93 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→20 Å / Num. all: 168213 / % possible obs: 99.7 % / Observed criterion σ(I): -3 / Redundancy: 4 % / Biso Wilson estimate: 73.3 Å2 / Rmerge(I) obs: 0.084 / Net I/σ(I): 6.5 |
Reflection shell | Resolution: 2.9→3.13 Å / Redundancy: 4 % / Rmerge(I) obs: 0.231 / % possible all: 99.9 |
Reflection | *PLUS Num. obs: 21539 / Num. measured all: 168213 |
Reflection shell | *PLUS Mean I/σ(I) obs: 3.2 |
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Processing
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Refinement | Rfactor Rfree error: 0.005 / Highest resolution: 2.9 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Details: BULK SOLVENT MODEL USED
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Displacement parameters | Biso mean: 24.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Highest resolution: 2.9 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.9→3.08 Å / Rfactor Rfree error: 0.014 / Total num. of bins used: 6
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 20 Å / σ(F): 0 / % reflection Rfree: 9.9 % / Rfactor obs: 0.19 / Rfactor Rwork: 0.19 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 24.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.296 / % reflection Rfree: 9.6 % / Rfactor Rwork: 0.245 |