+Open data
-Basic information
Entry | Database: PDB / ID: 3l64 | ||||||
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Title | T4 Lysozyme S44E/WT* | ||||||
Components | Lysozyme | ||||||
Keywords | HYDROLASE / hydrolase (O-glycosyl) / Antimicrobial / Bacteriolytic enzyme / Glycosidase | ||||||
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 / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Blaber, M. / Zhang, X.-J. / Lindstrom, J.D. / Pepiot, S.D. / Baase, W.A. / Matthews, B.W. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1994 Title: Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. Authors: Blaber, M. / Zhang, X.J. / Lindstrom, J.D. / Pepiot, S.D. / Baase, W.A. / 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 | 3l64.cif.gz | 47 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3l64.ent.gz | 33 KB | Display | PDB format |
PDBx/mmJSON format | 3l64.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l6/3l64 ftp://data.pdbj.org/pub/pdb/validation_reports/l6/3l64 | HTTPS FTP |
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-Related structure data
Related structure data | 1dyaC 1dybC 1dycC 1dydC 1dyeC 1dyfC 1dygC 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 18670.398 Da / Num. of mol.: 1 / Mutation: S44E, C54T, C97A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage T4 (virus) / Gene: E / Production host: Escherichia coli (E. coli) / References: UniProt: P00720, lysozyme | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.8 % |
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Crystal grow | Method: vapor diffusion, hanging drop Details: 10 Ul of protein solution (20 mg/ml) mixed with 10 Ul of well solution, typically 2.0 M-phosphate (pH 6.3 to 7.1), 0.25 M-NaCl and 6 Ul of 2-hydroxyethyl disulfide/ml (i.e. oxidized beta- ...Details: 10 Ul of protein solution (20 mg/ml) mixed with 10 Ul of well solution, typically 2.0 M-phosphate (pH 6.3 to 7.1), 0.25 M-NaCl and 6 Ul of 2-hydroxyethyl disulfide/ml (i.e. oxidized beta-mercaptoethanol). The drop was then equilibrated over 1 ml of well solution using a Limbro plate, VAPOR DIFFUSION, HANGING DROP |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Type: Multiwire Area Detector / Detector: Xuong-Hamlin / Date: 1993 |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→22.9 Å / Num. all: 14841 / Num. obs: 13554 / % possible obs: 91 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 22 Å2 / Rmerge(I) obs: 0.047 |
Reflection shell | Resolution: 1.9→1.97 Å / Num. unique all: 882 / % possible all: 65 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.9→6 Å / Isotropic thermal model: isotropic / σ(F): 0 / σ(I): 0 / Stereochemistry target values: TNT Protgeo.dat
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.9→6 Å
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Refine LS restraints |
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