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Yorodumi- PDB-1lwk: Multiple Methionine Substitutions are Tolerated in T4 Lysozyme an... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lwk | ||||||
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Title | Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects on Folding and Stability | ||||||
Components | Lysozyme | ||||||
Keywords | HYDROLASE / hydrolase (o-glycosyl) / T4 lysozyme / methionine core mutant / protein engineering / protein folding | ||||||
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 / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Gassner, N.C. / Baase, W.A. / Mooers, B.H.M. / Busam, R.D. / Weaver, L.H. / Lindstrom, J.D. / Quillin, M.L. / Matthews, B.M. | ||||||
Citation | Journal: Biophys.Chem. / Year: 2003 Title: Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability. Authors: Gassner, N.C. / Baase, W.A. / Mooers, B.H. / Busam, R.D. / Weaver, L.H. / Lindstrom, J.D. / Quillin, M.L. / 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 | 1lwk.cif.gz | 44.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lwk.ent.gz | 34.7 KB | Display | PDB format |
PDBx/mmJSON format | 1lwk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lwk_validation.pdf.gz | 428.2 KB | Display | wwPDB validaton report |
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Full document | 1lwk_full_validation.pdf.gz | 443.6 KB | Display | |
Data in XML | 1lwk_validation.xml.gz | 11.6 KB | Display | |
Data in CIF | 1lwk_validation.cif.gz | 15.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lw/1lwk ftp://data.pdbj.org/pub/pdb/validation_reports/lw/1lwk | HTTPS FTP |
-Related structure data
Related structure data | 1ks3C 1kw5C 1kw7C 1ky0C 1ky1C 1l0jC 1l0kC 1lpyC 1lw9C 1lwgC 1l63S C: citing same article (ref.) S: Starting model for refinement |
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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: 19541.418 Da / Num. of mol.: 1 Mutation: C54T,L84MSE,V87MSE,L91MSE,C97A,L99MSE,G110R,V111MSE,L118MSE,L121MSE,L133MSE,F153MSE 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: 2.46 Å3/Da / Density % sol: 49.92 % |
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Crystal grow | Method: vapor diffusion, hanging drop / Details: VAPOR DIFFUSION, HANGING DROP |
-Data collection
Diffraction | Mean temperature: 173 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-1 / Wavelength: 0.82653 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 10, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.82653 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→60 Å / Num. all: 11728 / Num. obs: 11279 / % possible obs: 99.2 % / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 2.1→2.18 Å / % possible all: 99.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1L63 Resolution: 2.1→60 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber Details: Residues ASN 163 and LEU 164 are missing in the electron density.
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.1→60 Å
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Refine LS restraints |
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