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- PDB-219l: PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETIO... -
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Open data
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Basic information
Entry | Database: PDB / ID: 219l | ||||||
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Title | PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME | ||||||
![]() | T4 LYSOZYME | ||||||
![]() | HYDROLASE (O-GLYCOSYL) / GLYCOSIDASE / BACTERIOLYTIC ENZYME | ||||||
Function / homology | ![]() viral release from host cell by cytolysis / peptidoglycan catabolic process / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / host cell cytoplasm / defense response to bacterium Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Vetter, I.R. / Baase, W.A. / Heinz, D.W. / Xiong, J.-P. / Snow, S. / Matthews, B.W. | ||||||
![]() | ![]() Title: Protein structural plasticity exemplified by insertion and deletion mutants in T4 lysozyme. Authors: Vetter, I.R. / Baase, W.A. / Heinz, D.W. / Xiong, J.P. / Snow, S. / Matthews, B.W. #1: ![]() Title: How Amino-Acid Insertions are Allowed in an Alpha-Helix of T4 Lysozyme Authors: Heinz, D.W. / Baase, W.A. / Dahlquist, F.W. / Matthews, B.W. #2: ![]() Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 A 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 | ![]() | 47.6 KB | Display | ![]() |
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PDB format | ![]() | 33.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 425.8 KB | Display | ![]() |
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Full document | ![]() | 430.6 KB | Display | |
Data in XML | ![]() | 10.4 KB | Display | |
Data in CIF | ![]() | 14.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 209lC ![]() 210lC ![]() 211lC ![]() 212lC ![]() 213lC ![]() 214lC ![]() 215lC ![]() 218lC 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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Unit cell |
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Components
#1: Protein | Mass: 18628.363 Da / Num. of mol.: 1 / Mutation: C54T, C97A, INS(L164-AAAA) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-HED / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.83 Å3/Da / Density % sol: 48.3 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Details: MUTANT WAS CRYSTALLIZED FROM PHOSPHATE IN CONTRAST TO L1 64AAA_PEG WHICH WAS CRYSTALLIZED FROM PEG. | |||||||||||||||||||||||||||||||||||
Crystal | *PLUS | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.1 / Method: other | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Oct 16, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.66→26.23 Å / Num. obs: 21597 / % possible obs: 87.9 % / Observed criterion σ(I): 0 / Redundancy: 2.9 % / Rmerge(I) obs: 0.0684 |
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Processing
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Refinement | Resolution: 1.66→26.23 Å / σ(F): 0 Details: RESIDUES 162 - 164 IN WILD-TYPE AND ALL MUTANT LYSOZYMES ARE EXTREMELY MOBILE. THUS THE COORDINATES FOR THESE RESIDUES ARE VERY UNRELIABLE. THIS ENTRY DOES NOT INCLUDE RESIDUES 165 - 168. ...Details: RESIDUES 162 - 164 IN WILD-TYPE AND ALL MUTANT LYSOZYMES ARE EXTREMELY MOBILE. THUS THE COORDINATES FOR THESE RESIDUES ARE VERY UNRELIABLE. THIS ENTRY DOES NOT INCLUDE RESIDUES 165 - 168. THIS MUTANT WAS CRYSTALLIZED FROM PHOSPHATE, AS COMPARED TO ENTRY 212L WHICH IS THE SAME MUTANT, BUT CRYSTALLIZED FROM PEG.
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Refinement step | Cycle: LAST / Resolution: 1.66→26.23 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.175 | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: t_plane_restr / Dev ideal: 0.018 / Weight: 3 |