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- PDB-1srv: THERMUS THERMOPHILUS GROEL (HSP60 CLASS) FRAGMENT (APICAL DOMAIN)... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1srv | ||||||
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Title | THERMUS THERMOPHILUS GROEL (HSP60 CLASS) FRAGMENT (APICAL DOMAIN) COMPRISING RESIDUES 192-336 | ||||||
![]() | PROTEIN (GROEL (HSP60 CLASS)) | ||||||
![]() | CHAPERONE / HSP60 / GROEL / CELL DIVISION / ATP-BINDING / PHOSPHORYLATION | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Walsh, M.A. / Dementieva, I. / Evans, G. / Sanishvili, R. / Joachimiak, A. | ||||||
![]() | ![]() Title: Taking MAD to the extreme: ultrafast protein structure determination. Authors: Walsh, M.A. / Dementieva, I. / Evans, G. / Sanishvili, R. / Joachimiak, A. #1: ![]() Title: A structural model for GroEL-polypeptide recognition. Authors: Buckle, A.M. / Zahn, R. / Fersht, A.R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 41.6 KB | Display | ![]() |
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PDB format | ![]() | 29.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 417.6 KB | Display | ![]() |
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Full document | ![]() | 424.4 KB | Display | |
Data in XML | ![]() | 9.7 KB | Display | |
Data in CIF | ![]() | 12.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 15754.218 Da / Num. of mol.: 1 / Fragment: APICAL DOMAIN, RESIDUES 191 - 376 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48 % Description: MAD DATA WERE COLLECTED AT THE STRUCTURAL BIOLOGY CENTER'S UNDULATOR BEAMLINE 19ID AT THE APS | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 7.5 / Details: pH 7.5, VAPOR DIFFUSION, HANGING DROP | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Nov 15, 1997 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→20 Å / Num. obs: 15546 / % possible obs: 88 % / Observed criterion σ(I): -3 / Redundancy: 3.8 % / Biso Wilson estimate: 30.7 Å2 / Rmerge(I) obs: 0.058 / Net I/σ(I): 17.2 |
Reflection shell | Resolution: 1.7→1.73 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.39 / Mean I/σ(I) obs: 2.2 / % possible all: 46 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 41.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 10 Å / Num. reflection obs: 15676 / σ(F): 0 / % reflection Rfree: 5 % / Rfactor all: 0.193 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 41.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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