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- PDB-197l: THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-R... -
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Open data
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Basic information
Entry | Database: PDB / ID: 197l | ||||||
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Title | THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME | ||||||
![]() | LYSOZYME![]() | ||||||
![]() | HYDROLASE (O-GLYCOSYL) / CAVITIES / CORE-PACKING / ![]() | ||||||
Function / homology | ![]() viral release from host cell by cytolysis / peptidoglycan catabolic process / cell wall macromolecule catabolic process / ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Baldwin, E. / Xu, J. / Hajiseyedjavadi, O. / Matthews, B.W. | ||||||
![]() | ![]() Title: Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. Authors: Baldwin, E. / Xu, J. / Hajiseyedjavadi, O. / Baase, W.A. / Matthews, B.W. #1: ![]() Title: Construction and Functional Selection of a T4 Lysozyme Gene Library Randomly Mutagenized at Five Specific Sites Authors: Baldwin, E. / Xu, J. / Hajiseyedjavadi, O. #2: ![]() Title: The Role of Backbone Flexibility in the Accommodation of Variants that Repack the Core of T4 Lysozyme Authors: Baldwin, E.P. / Hajiseyedjavadi, O. / Baase, W.A. / Matthews, B.W. #3: ![]() Title: Control of Enzyme Activity by an Engineered Disulfide Bond Authors: Matsumura, M. / Matthews, B.W. #4: ![]() Title: Expression and Nitrogen-15 Labeling of Proteins for Proton and Nitrogen-15 Nuclear Magnetic Resonance Authors: Muchmore, D.C. / Mcintosh, L.P. / Russell, C.B. / Anderson, D.E. / Dahlquist, F.W. #5: ![]() Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 Angstroms Resolution Authors: Weaver, L.H. / Matthews, B.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 46.6 KB | Display | ![]() |
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PDB format | ![]() | 33.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 18612.385 Da / Num. of mol.: 1 / Mutation: C54T, C97A, A129M, F153A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Description: MUTANT GENE WAS DERIVED FROM SITE-DIRECTED MUTAGENESIS OF THE GENE FOR CYS-FREE WILDTYPE T4 LYSOZYME IN M13 USING THE METHOD OF KUNKEL AND THE VECTOR SYSTEM DESCRIBED IN REFERENCE 3 BELOW Variant: CYS-FREE WILDTYPE T4 / Plasmid: M13 / Production host: ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | ![]() #3: Chemical | ![]() #4: Water | ChemComp-HOH / | ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 55.42 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | pH: 6.7 / Details: pH 6.7 | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: batch method | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR |
Radiation | Monochromator: GRAPHITE / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Rmerge(I) obs: 0.042 |
Reflection | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 5 Å / Num. obs: 10369 / % possible obs: 87 % / Rmerge(I) obs: 0.042 |
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Processing
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Refinement | Resolution: 2.1→5 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.1→5 Å
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Refine LS restraints |
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