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Open data
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Basic information
Entry | Database: PDB / ID: 1kw7 | ||||||
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Title | METHIONINE CORE MUTANT OF T4 LYSOZYME | ||||||
![]() | LYSOZYME | ||||||
![]() | HYDROLASE / hydrolase (o-glycosyl) / T4 lysozyme / methionine core mutant / protein engineering / protein folding | ||||||
Function / homology | ![]() 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 | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Gassner, N.C. / Baase, W.A. / Mooers, B.H. / Busam, R.D. / Weaver, L.H. / Lindstrom, J.D. / Quillin, M.L. / Matthews, B.W. | ||||||
![]() | ![]() 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. #1: ![]() Title: Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lyzoayme is a rate-limiting step in folding Authors: Gassner, N.C. / Baase, W.A. / Lindstrom, J. / Lu, J. / Dahquist, F.W. / Matthews, B.W. #2: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 48.1 KB | Display | ![]() |
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PDB format | ![]() | 34.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 431.2 KB | Display | ![]() |
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Full document | ![]() | 436.5 KB | Display | |
Data in XML | ![]() | 10.8 KB | Display | |
Data in CIF | ![]() | 14.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ks3C ![]() 1kw5C ![]() 1ky0C ![]() 1ky1C ![]() 1l0jC ![]() 1l0kC ![]() 1lpyC ![]() 1lw9C ![]() 1lwgC ![]() 1lwkC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 18473.254 Da / Num. of mol.: 1 / Mutation: C54T,L84M,L91M,C97A,L99M,L133M Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Chemical | #3: Chemical | ChemComp-HED / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.84 Å3/Da / Density % sol: 56.71 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.9 Details: Na2Po4, NaCl, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Detector: AREA DETECTOR |
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: 1.89→30 Å / Num. all: 16871 / Num. obs: 16871 / % possible obs: 91.21 % / Redundancy: 2.8091 % / Biso Wilson estimate: 28.564 Å2 / Rmerge(I) obs: 0.0453 / Net I/σ(I): 11.99 |
Reflection shell | Resolution: 1.8088→1.893 Å / Redundancy: 1.6977 % / Rmerge(I) obs: 0.1988 / Num. unique all: 2534 / % possible all: 65.34 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 1.89→30 Å
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