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Yorodumi- PDB-189l: ENHANCEMENT OF PROTEIN STABILITY BY THE COMBINATION OF POINT MUTA... -
+Open data
-Basic information
Entry | Database: PDB / ID: 189l | ||||||
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Title | ENHANCEMENT OF PROTEIN STABILITY BY THE COMBINATION OF POINT MUTATIONS IN T4 LYSOZYME IS ADDITIVE | ||||||
Components | T4 LYSOZYME | ||||||
Keywords | HYDROLASE (O-GLYCOSYL) | ||||||
Function / homology | Function and homology information 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 | Enterobacteria phage T4 (virus) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Zhang, X.-J. / Matthews, B.W. | ||||||
Citation | Journal: Protein Eng. / Year: 1995 Title: Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. Authors: Zhang, X.J. / Baase, W.A. / Shoichet, B.K. / Wilson, K.P. / Matthews, B.W. #1: Journal: J.Mol.Biol. / Year: 1987 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 189l.cif.gz | 44.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb189l.ent.gz | 31.5 KB | Display | PDB format |
PDBx/mmJSON format | 189l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 189l_validation.pdf.gz | 408.1 KB | Display | wwPDB validaton report |
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Full document | 189l_full_validation.pdf.gz | 423.6 KB | Display | |
Data in XML | 189l_validation.xml.gz | 10.8 KB | Display | |
Data in CIF | 189l_validation.cif.gz | 13.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/89/189l ftp://data.pdbj.org/pub/pdb/validation_reports/89/189l | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 18718.486 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage T4 (virus) / Genus: T4-like viruses / Species: Enterobacteria phage T4 sensu lato / Plasmid: M13 / References: UniProt: P00720, lysozyme |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.48 Å3/Da / Density % sol: 50.35 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.7 / Method: unknown | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Ambient pressure: 101 kPa / Mean temperature: 298 K |
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Diffraction source | Source: rotating-anode X-ray tube / Type: RIGAKU RU200 / Target: Cu |
Detector | Type: AREA DETECTOR / Detector: AREA DETECTOR / Details: Xuong-Hamlin |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray / Wavelength: 1.5418 Å |
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.5 Å / Num. obs: 6024 / % possible obs: 88 % / Rmerge(I) obs: 0.046 |
-Processing
Software |
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Refinement | Resolution: 2.5→20 Å /
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Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
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Refinement | *PLUS Rfactor obs: 0.2 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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