+Open data
-Basic information
Entry | Database: PDB / ID: 1asx | ||||||
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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 / MOLECULAR REPLACEMENT / Resolution: 2.8 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 | 1asx.cif.gz | 41.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1asx.ent.gz | 29 KB | Display | PDB format |
PDBx/mmJSON format | 1asx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/as/1asx ftp://data.pdbj.org/pub/pdb/validation_reports/as/1asx | HTTPS FTP |
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-Related structure data
Related structure data | 1assSC S: Starting model for refinement C: citing same article (ref.) |
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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: 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-PO4 / |
#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: 3.63 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: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 1, 1997 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→19 Å / Num. obs: 6335 / % possible obs: 94.8 % / Observed criterion σ(I): -3 / Redundancy: 2.7 % / Biso Wilson estimate: 39.9 Å2 / Rmerge(I) obs: 0.064 / Net I/σ(I): 20.6 |
Reflection shell | Highest resolution: 2.8 Å / Rmerge(I) obs: 0.145 / Mean I/σ(I) obs: 6.9 / % possible all: 71.8 |
Reflection | *PLUS Num. measured all: 17354 |
Reflection shell | *PLUS % possible obs: 71.8 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: GLOBULAR DOMAIN PORTION OF CRYSTAL FORM A (PDB ENTRY 1ASS) Resolution: 2.8→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: 36 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.8→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.9 Å / % reflection obs: 71.8 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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