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Yorodumi- PDB-1lwg: Multiple Methionine Substitutions are Tolerated in T4 Lysozyme an... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lwg | ||||||
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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: 1.7 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 | 1lwg.cif.gz | 50.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lwg.ent.gz | 35.2 KB | Display | PDB format |
PDBx/mmJSON format | 1lwg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lwg_validation.pdf.gz | 446.1 KB | Display | wwPDB validaton report |
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Full document | 1lwg_full_validation.pdf.gz | 452.7 KB | Display | |
Data in XML | 1lwg_validation.xml.gz | 11.4 KB | Display | |
Data in CIF | 1lwg_validation.cif.gz | 15.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lw/1lwg ftp://data.pdbj.org/pub/pdb/validation_reports/lw/1lwg | HTTPS FTP |
-Related structure data
Related structure data | 1ks3C 1kw5C 1kw7C 1ky0C 1ky1C 1l0jC 1l0kC 1lpyC 1lw9C 1lwkC 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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2 |
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Unit cell |
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-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 18800.719 Da / Num. of mol.: 1 Mutation: C54T,L84M,V87M,L91M,C97A,L99M,V111M,L118M,L121M,L133M 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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-Non-polymers , 5 types, 152 molecules
#2: Chemical | ChemComp-PO4 / | ||||||
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#3: Chemical | #4: Chemical | ChemComp-K / | #5: Chemical | #6: 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: 2.53 Å3/Da / Density % sol: 51.45 % |
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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: 0.77487 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: 0.77487 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→19.8 Å / Num. all: 21411 / Num. obs: 21345 / % possible obs: 99.4 % / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Biso Wilson estimate: 21.4 Å2 / Rmerge(I) obs: 0.052 / Rsym value: 0.052 / Net I/σ(I): 7.1 |
Reflection shell | Resolution: 1.7→1.79 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.284 / Mean I/σ(I) obs: 2.7 / Num. unique all: 2976 / Rsym value: 0.284 / % possible all: 96.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1L63 Resolution: 1.7→19.8 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: 1.7→19.8 Å
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Refine LS restraints |
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