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Yorodumi- PDB-3aab: Small heat shock protein hsp14.0 with the mutations of I120F and ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3aab | ||||||
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Title | Small heat shock protein hsp14.0 with the mutations of I120F and I122F in the form I crystal | ||||||
Components | Putative uncharacterized protein ST1653 | ||||||
Keywords | CHAPERONE / alpha-crystallin domain | ||||||
Function / homology | Function and homology information : / Immunoglobulin-like - #790 / Hsp20/alpha crystallin family / Small heat shock protein (sHSP) domain profile. / Alpha crystallin/Hsp20 domain / HSP20-like chaperone / Immunoglobulin-like / Sandwich / Mainly Beta Similarity search - Domain/homology | ||||||
Biological species | Sulfolobus tokodaii (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 1.851 Å | ||||||
Authors | Takeda, K. / Hayashi, T. / Abe, T. / Hirano, Y. / Hanazono, Y. / Yohda, M. / Miki, K. | ||||||
Citation | Journal: J.Struct.Biol. / Year: 2011 Title: Dimer structure and conformational variability in the N-terminal region of an archaeal small heat shock protein, StHsp14.0 Authors: Takeda, K. / Hayashi, T. / Abe, T. / Hirano, Y. / Hanazono, Y. / Yohda, M. / Miki, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3aab.cif.gz | 60.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3aab.ent.gz | 44.7 KB | Display | PDB format |
PDBx/mmJSON format | 3aab.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/aa/3aab ftp://data.pdbj.org/pub/pdb/validation_reports/aa/3aab | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 14132.262 Da / Num. of mol.: 2 / Mutation: I120F, I122F Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sulfolobus tokodaii (archaea) / Strain: 7 / Gene: ST1653 / Plasmid: pET23a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q970D9 #2: Chemical | #3: Chemical | ChemComp-IPA / | #4: 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: 2.1 Å3/Da / Density % sol: 41.35 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 5% isopropanol, 10mM magnesium chloride, 50 mM Tris-HCl, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 290K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL38B1 / Wavelength: 1 Å |
Detector | Type: RIGAKU JUPITER 210 / Detector: CCD / Date: May 21, 2007 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→50 Å / Num. obs: 20341 / % possible obs: 96.8 % / Observed criterion σ(I): 0 / Redundancy: 5.7 % / Biso Wilson estimate: 31.078 Å2 / Rsym value: 0.039 / Net I/σ(I): 37.1 |
Reflection shell | Resolution: 1.85→1.92 Å / Redundancy: 3.3 % / Mean I/σ(I) obs: 3 / Num. unique all: 1909 / Rsym value: 0.285 / % possible all: 92.3 |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS / Resolution: 1.851→37.778 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.813 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / Stereochemistry target values: ML
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Solvent computation | Bsol: 83.41 Å2 / ksol: 0.296 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 32.43 Å2 / Biso mean: 10.718 Å2 / Biso min: 2.15 Å2
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Refinement step | Cycle: LAST / Resolution: 1.851→37.778 Å
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Refine LS restraints |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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