+Open data
-Basic information
Entry | Database: PDB / ID: 1g0l | ||||||
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Title | CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152V | ||||||
Components | PROTEIN (LYSOZYME) | ||||||
Keywords | HYDROLASE / O-Glycosyl / Glycosidase / Bacteriolytic Enzyme | ||||||
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: 1.8 Å | ||||||
Authors | Xu, J. / Baase, W.A. / Quillin, M.L. / Matthews, B.W. | ||||||
Citation | Journal: Protein Sci. / Year: 2001 Title: Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. Authors: Xu, J. / Baase, W.A. / Quillin, M.L. / Baldwin, E.P. / 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 | 1g0l.cif.gz | 48.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g0l.ent.gz | 34.1 KB | Display | PDB format |
PDBx/mmJSON format | 1g0l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g0/1g0l ftp://data.pdbj.org/pub/pdb/validation_reports/g0/1g0l | HTTPS FTP |
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-Related structure data
Related structure data | 1g06C 1g07C 1g0gC 1g0jC 1g0kC 1g0mC 1g0pC 1g0qC 1g1vC 1g1wC 1i6sC C: citing same article (ref.) |
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Similar 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: 18626.391 Da / Num. of mol.: 1 / Mutation: C54T; C97A; T152V 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 / Production host: Escherichia coli (E. coli) / References: UniProt: P00720, lysozyme | ||||
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#2: Chemical | #3: Chemical | ChemComp-HED / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.77 Å3/Da / Density % sol: 55.59 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.8 Details: Phosphate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion / Details: Eriksson, A.E., (1993) J. Mol. Biol., 229, 747. / PH range low: 7.1 / PH range high: 6.3 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 300 K |
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Diffraction source | Source: ROTATING ANODE / Type: OTHER / Wavelength: 1.5418 |
Detector | Type: OTHER / Detector: AREA DETECTOR / Date: Sep 7, 1994 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→20 Å / Num. all: 21753 / Num. obs: 21753 / % possible obs: 85.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.1 % / Biso Wilson estimate: 25.5 Å2 / Rmerge(I) obs: 0.029 / Net I/σ(I): 13 |
Reflection shell | Resolution: 1.65→1.78 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.188 / Num. unique all: 2824 / % possible all: 57 |
Reflection | *PLUS Highest resolution: 1.8 Å / % possible obs: 90 % |
-Processing
Software |
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Refinement | Resolution: 1.8→10 Å / σ(F): 0 / σ(I): 2 / Stereochemistry target values: TNT
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Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.8 Å / σ(F): 0 / Rfactor all: 0.154 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: t_angle_deg / Dev ideal: 2 |