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Yorodumi- PDB-149l: CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 L... -
+Open data
-Basic information
Entry | Database: PDB / ID: 149l | ||||||
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Title | CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME | ||||||
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: 2.6 Å | ||||||
Authors | Wilson, K. / Matthews, B.W. | ||||||
Citation | Journal: Protein Sci. / Year: 1994 Title: Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme. Authors: Zhang, X.J. / Matthews, B.W. #1: Journal: Nature / Year: 1988 Title: Hydrophobic Stabilization in T4 Lysozyme Determined Directly by Multiple Substitutions of Ile 3 Authors: Matsumura, M. / Becktel, W.J. / Matthews, B.W. #2: Journal: J.Biol.Chem. / Year: 1989 Title: Structural Studies of Mutants of T4 Lysozyme that Alter Hydrophobic Stabilization Authors: Matsumura, M. / Wozniak, J.A. / Sun, D. / 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 | 149l.cif.gz | 43.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb149l.ent.gz | 31.3 KB | Display | PDB format |
PDBx/mmJSON format | 149l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 149l_validation.pdf.gz | 413.2 KB | Display | wwPDB validaton report |
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Full document | 149l_full_validation.pdf.gz | 422.4 KB | Display | |
Data in XML | 149l_validation.xml.gz | 10 KB | Display | |
Data in CIF | 149l_validation.cif.gz | 12.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/49/149l ftp://data.pdbj.org/pub/pdb/validation_reports/49/149l | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 18662.467 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: 2.56 Å3/Da / Density % sol: 51.89 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.8 / Method: unknown | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.6→10 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.6→10 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 10 Å / Num. reflection all: 5904 / σ(F): 0 / Rfactor all: 0.192 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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