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Open data
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Basic information
Entry | Database: PDB / ID: 1e0r | ||||||
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Title | Beta-apical domain of thermosome | ||||||
![]() | THERMOSOME | ||||||
![]() | CHAPERONIN / HSP60 / THERMOSOME / TCP1 / GROEL / THERMOPLASMA ACIDOPHILUM | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Bosch, G. / Baumeister, W. / Essen, L.-O. | ||||||
![]() | ![]() Title: Crystal Structure of the Beta-Apical Domain from Thermosome Reveals Structural Plasticity in Protrusion Region Authors: Bosch, G. / Baumeister, W. / Essen, L.-O. #1: ![]() 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. #2: ![]() 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 | ![]() | 42 KB | Display | ![]() |
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PDB format | ![]() | 28.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 419.6 KB | Display | ![]() |
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Full document | ![]() | 423.1 KB | Display | |
Data in XML | ![]() | 8.1 KB | Display | |
Data in CIF | ![]() | 9.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1assS S: Starting model for refinement |
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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: 17763.393 Da / Num. of mol.: 1 / Fragment: SUBSTRATE-BINDING DOMAIN / Mutation: YES Source method: isolated from a genetically manipulated source Details: LYS 364 IS FOLLOWED BY ASN 365 AND HEXAHISTIDINE TAIL Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||
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Compound details | CHAIN B ENGINEEREDSequence details | HIS: HISTIDINE TAG FROM HIS 368 - HIS 372 NOT SEEN IN ELECTRON DENSITY | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.83 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 9.1 / Details: pH 9.10 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop / pH: 9.1 | ||||||||||||||||||||||||||||||
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: Jun 15, 1998 / Details: MIRROR |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.99 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→25 Å / Num. obs: 5170 / % possible obs: 97.8 % / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Biso Wilson estimate: 95 Å2 / Rmerge(I) obs: 0.041 / Net I/σ(I): 27 |
Reflection shell | Resolution: 2.8→2.87 Å / Rmerge(I) obs: 0.393 / Mean I/σ(I) obs: 3.3 / % possible all: 96.8 |
Reflection | *PLUS Num. measured all: 19163 |
Reflection shell | *PLUS % possible obs: 96.8 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1ASS WITHOUT I245-K274 Resolution: 2.8→15 Å / Data cutoff high absF: 10000 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 35.8 Å2 / ksol: 0.293 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 76 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.9 Å / Total num. of bins used: 10 /
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Xplor file | Serial no: 1 / Param file: PROTEIN.PARAM / Topol file: PROTEIN.TOP | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 5135 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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