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Open data
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Basic information
Entry | Database: PDB / ID: 1asx | ||||||
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Title | APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM | ||||||
![]() | THERMOSOME | ||||||
![]() | CHAPERONIN / HSP60 / THERMOSOME / TCP1 / GROEL / THERMOPLASMA ACIDOPHILUM / ATP-BINDING | ||||||
Function / homology | ![]() chaperonin-containing T-complex / ATP-dependent protein folding chaperone / unfolded protein binding / ATP hydrolysis activity / ATP binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Klumpp, M. / Baumeister, W. / Essen, L.-O. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 41.7 KB | Display | ![]() |
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PDB format | ![]() | 29 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.6 KB | Display | ![]() |
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Full document | ![]() | 438.5 KB | Display | |
Data in XML | ![]() | 8.2 KB | Display | |
Data in CIF | ![]() | 9.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1assSC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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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.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-PO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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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: ![]() |
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 % |
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Processing
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Refinement | Method to determine structure: ![]() 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: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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