+Open data
-Basic information
Entry | Database: PDB / ID: 1ass | ||||||
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Title | APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM | ||||||
Components | THERMOSOME | ||||||
Keywords | CHAPERONIN / HSP60 / THERMOSOME / TCP1 / GROEL / THERMOPLASMA ACIDOPHILUM / ATP-BINDING | ||||||
Function / homology | Function and homology information ATP-dependent protein folding chaperone / unfolded protein binding / ATP hydrolysis activity / ATP binding Similarity search - Function | ||||||
Biological species | Thermoplasma acidophilum (acidophilic) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 2.3 Å | ||||||
Authors | Klumpp, M. / Baumeister, W. / Essen, L.-O. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1997 Title: Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin. Authors: Klumpp, M. / Baumeister, W. / Essen, L.O. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ass.cif.gz | 42.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ass.ent.gz | 30 KB | Display | PDB format |
PDBx/mmJSON format | 1ass.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/as/1ass ftp://data.pdbj.org/pub/pdb/validation_reports/as/1ass | 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
#1: Protein | Mass: 17822.625 Da / Num. of mol.: 1 Fragment: ALPHA-SUBUNIT, APICAL DOMAIN, SUBSTRATE-BINDING DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermoplasma acidophilum (acidophilic) / Cell line: BL21 / Cellular location: CYTOPLASM / Gene: THSA / Plasmid: PRSET6A / Species (production host): Escherichia coli / Gene (production host): THSA / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P48424 | ||
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#2: Chemical | ChemComp-NA / | ||
#3: Chemical | #4: 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: 4.27 Å3/Da / Density % sol: 70 % | ||||||||||||||||||||
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Crystal grow | pH: 3.5 / Details: pH 3.5 | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 30 ℃ / pH: 3.8 / Method: vapor diffusion | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: MPG/DESY, HAMBURG / Beamline: BW6 / Wavelength: 1.05 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 14, 1997 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.05 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→18 Å / Num. obs: 10935 / % possible obs: 96.3 % / Observed criterion σ(I): -3 / Redundancy: 4 % / Biso Wilson estimate: 57.4 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 24.3 |
Reflection shell | Highest resolution: 2.3 Å / Rmerge(I) obs: 0.256 / Mean I/σ(I) obs: 7 / % possible all: 95.5 |
Reflection | *PLUS Num. measured all: 44064 |
Reflection shell | *PLUS % possible obs: 95.5 % |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.3→10 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: RFREE / σ(F): 0
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Displacement parameters | Biso mean: 60 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.33→2.4 Å / % reflection obs: 95.5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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