+Open data
-Basic information
Entry | Database: PDB / ID: 256l | ||||||
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Title | BACTERIOPHAGE T4 LYSOZYME | ||||||
Components | LYSOZYME | ||||||
Keywords | HYDROLASE / LYSOZYME | ||||||
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 / DIFFERENCE FOURIER / Resolution: 1.8 Å | ||||||
Authors | Faber, H.R. / Matthews, B.W. | ||||||
Citation | 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 | 256l.cif.gz | 46.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb256l.ent.gz | 32.8 KB | Display | PDB format |
PDBx/mmJSON format | 256l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/56/256l ftp://data.pdbj.org/pub/pdb/validation_reports/56/256l | HTTPS FTP |
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-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: 18644.430 Da / Num. of mol.: 1 / Mutation: M6I 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 / 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: 2.82 Å3/Da / Density % sol: 56 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.7 / Method: batch method / Details: Remington, S.J., (1978) J.Mol.Biol., 118, 81. | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
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Detector | Type: FILM / Detector: FILM / Date: 1990 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / Num. obs: 13645 / % possible obs: 65 % / Rmerge(I) obs: 0.052 |
-Processing
Software |
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Refinement | Method to determine structure: DIFFERENCE FOURIER Starting model: WT T4LYS Resolution: 1.8→30 Å
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Solvent computation | Bsol: 375.4 Å2 / ksol: 0.906 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→30 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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