+Open data
-Basic information
Entry | Database: PDB / ID: 1ctw | ||||||
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Title | T4 LYSOZYME MUTANT I78A | ||||||
Components | LYSOZYME | ||||||
Keywords | HYDROLASE / HYDROLASE (O-GLYCOSYL) / T4 LYSOZYME / CAVITY 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 / Resolution: 2.1 Å | ||||||
Authors | Gassner, N.C. / Baase, W.A. / Lindstrom, J.D. / Lu, J. / Matthews, B.W. | ||||||
Citation | Journal: Biochemistry / Year: 1999 Title: Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Authors: Gassner, N.C. / Baase, W.A. / Lindstrom, J.D. / Lu, J. / Dahlquist, F.W. / Matthews, B.W. #1: Journal: Protein Sci. / Year: 1998 Title: The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect Authors: Xu, J. / Baase, W.A. / Baldwin, E. / Matthews, B.W. #2: Journal: J.Mol.Biol. / Year: 1987 Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 A Resolution Authors: Weaver, L.H. / 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 | 1ctw.cif.gz | 47 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ctw.ent.gz | 33 KB | Display | PDB format |
PDBx/mmJSON format | 1ctw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ct/1ctw ftp://data.pdbj.org/pub/pdb/validation_reports/ct/1ctw | HTTPS FTP |
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-Related structure data
Related structure data | 1cu0C 1cu2C 1cu3C 1cu5C 1cu6C 1cupC 1cuqC 1cv0C 1cv1C 1cv3C 1cv4C 1cv5C 1cv6C 1cvkC 1qsqC 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: 18586.283 Da / Num. of mol.: 1 / Mutation: C54T, I78A, C97A 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 | ChemComp-CL / |
#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: 2.84 Å3/Da / Density % sol: 56.61 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.6 Details: NA2PO4, NACL, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.7 / 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: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Jan 1, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.05→30 Å / Num. all: 11183 / Num. obs: 11183 / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.1 % / Rmerge(I) obs: 0.088 / Net I/σ(I): 7.1 |
Reflection shell | Resolution: 2.05→2.1 Å / Redundancy: 6.9 % / Rmerge(I) obs: 0.51 |
Reflection | *PLUS % possible obs: 83 % |
-Processing
Software |
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Refinement | Resolution: 2.1→30 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: TNT PROTGEO
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Refinement step | Cycle: LAST / Resolution: 2.1→30 Å
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Refine LS restraints |
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