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Open data
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Basic information
Entry | Database: PDB / ID: 1a6e | ||||||
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Title | THERMOSOME-MG-ADP-ALF3 COMPLEX | ||||||
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![]() | CHAPERONIN / THERMOPLASMA ACIDOPHILUM / GROUP II CHAPERONIN / CCT / TRIC / PROTEIN FOLDING / ATPASE / TRANSITION STATE COMPLEX / ATP HYDROLYSIS | ||||||
Function / homology | ![]() ATP-dependent protein folding chaperone / unfolded protein binding / ATP hydrolysis activity / ATP binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Ditzel, L. / Loewe, J. / Stock, D. / Stetter, K.-O. / Huber, H. / Huber, R. / Steinbacher, S. | ||||||
![]() | ![]() Title: Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Authors: Ditzel, L. / Lowe, J. / Stock, D. / Stetter, K.O. / Huber, H. / Huber, R. / Steinbacher, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 240.6 KB | Display | ![]() |
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PDB format | ![]() | 191.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 517.4 KB | Display | ![]() |
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Full document | ![]() | 581.1 KB | Display | |
Data in XML | ![]() | 25.3 KB | Display | |
Data in CIF | ![]() | 37.2 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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Unit cell |
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Components
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 58323.816 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Protein | Mass: 58552.629 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Non-polymers , 4 types, 8 molecules 






#3: Chemical | #4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.3 Å3/Da / Density % sol: 63 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.6 / Details: pH 5.6 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, sitting dropDetails: 0.005ml of drop solution was mixed with 0.0025 ml of precipitant | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 15, 1997 / Details: MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→15 Å / Num. obs: 22043 / % possible obs: 92 % / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Rsym value: 0.113 / Net I/σ(I): 6.2 |
Reflection shell | Resolution: 3.2→3.28 Å / Redundancy: 1.7 % / Mean I/σ(I) obs: 1.6 / Rsym value: 0.458 / % possible all: 61.4 |
Reflection | *PLUS Rmerge(I) obs: 0.113 |
Reflection shell | *PLUS % possible obs: 61.4 % / Rmerge(I) obs: 0.458 |
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Processing
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Refinement | Method to determine structure: DIFFERENCE FOURIER SYNTHESIS / Resolution: 3.2→8 Å / Data cutoff high absF: 100000000 / Data cutoff low absF: 0.1 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 38.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.2→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.2→3.34 Å / Total num. of bins used: 8
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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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LS refinement shell | *PLUS Rfactor obs: 0.262 |