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Open data
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Basic information
Entry | Database: PDB / ID: 3cru | ||||||
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Title | Structural characterization of an engineered allosteric protein | ||||||
![]() | Glutathione S-transferase class-mu 26 kDa isozyme | ||||||
![]() | TRANSFERASE / protein design / allosteric switch / pH-response | ||||||
Function / homology | ![]() glutathione transferase / glutathione transferase activity / glutathione metabolic process Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Sagermann, M. / Chapleau, R. / DeLorimier, E. / Lei, M. | ||||||
![]() | ![]() Title: Using affinity chromatography to engineer and characterize pH-dependent protein switches. Authors: Sagermann, M. / Chapleau, R.R. / DeLorimier, E. / Lei, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 58.4 KB | Display | ![]() |
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PDB format | ![]() | 42.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 735.4 KB | Display | ![]() |
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Full document | ![]() | 741.5 KB | Display | |
Data in XML | ![]() | 12.2 KB | Display | |
Data in CIF | ![]() | 16 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3crtC ![]() 3d0zC ![]() 1gneS ![]() 3crs 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: 25063.148 Da / Num. of mol.: 1 / Mutation: L50C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-GSH / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 49.97 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 9.5 Details: 20% PEG8000, 50 mM Tris-HCL, 3 mM B-ME., pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 150 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Oct 4, 2007 / Details: Rigaku Varimax HR |
Radiation | Monochromator: Rigaku VariMax HR optics / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→19.507 Å / Num. all: 21386 / Num. obs: 17967 / % possible obs: 84 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 1.99 % / Biso Wilson estimate: 29.96 Å2 / Rmerge(I) obs: 0.61 / Net I/σ(I): 14.87 |
Reflection shell | Resolution: 2.3→3 Å / Redundancy: 1.91 % / Rmerge(I) obs: 0.158 / Mean I/σ(I) obs: 6.2 / Num. unique all: 8979 / % possible all: 76.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDBid: 1GNE with the engineered peptide deleted. Resolution: 2.3→19.507 Å / Isotropic thermal model: Anisotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: last four residues (HPPK) could not be modeled reliably and were omitted from the model.
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.3→19.507 Å
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Refine LS restraints |
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