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Yorodumi- PDB-150l: CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 L... -
+Open data
-Basic information
Entry | Database: PDB / ID: 150l | ||||||
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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: 2.2 Å | ||||||
Authors | Faber, H.R. / 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: 1990 Title: A Mutant T4 Lysozyme Displays Five Different Crystal Conformations Authors: Faber, H.R. / 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 | 150l.cif.gz | 137.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb150l.ent.gz | 109.7 KB | Display | PDB format |
PDBx/mmJSON format | 150l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 150l_validation.pdf.gz | 441.1 KB | Display | wwPDB validaton report |
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Full document | 150l_full_validation.pdf.gz | 484.4 KB | Display | |
Data in XML | 150l_validation.xml.gz | 30.9 KB | Display | |
Data in CIF | 150l_validation.cif.gz | 42.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/50/150l ftp://data.pdbj.org/pub/pdb/validation_reports/50/150l | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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4 |
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Unit cell |
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-Components
#1: Protein | Mass: 18644.430 Da / Num. of mol.: 4 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 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.69 Å3/Da / Density % sol: 54.24 % |
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Crystal grow | *PLUS Method: unknown / PH range low: 7.1 / PH range high: 6.7 |
Components of the solutions | *PLUS Conc.: 2.0 M / Common name: phosphate |
-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: 2.2→6 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.2→6 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.21 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: t_angle_d / Dev ideal: 2.69 |