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Open data
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Basic information
Entry | Database: PDB / ID: 1ks3 | ||||||
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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 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. #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 | ![]() | 47.7 KB | Display | ![]() |
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PDB format | ![]() | 33.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 424.3 KB | Display | ![]() |
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Full document | ![]() | 431.6 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 | ![]() 1kw5C ![]() 1kw7C ![]() 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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Unit cell |
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Components
#1: Protein | Mass: 18437.180 Da / Num. of mol.: 1 / Mutation: C54T,C97A,L118M,L121M 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: 2.83 Å3/Da / Density % sol: 56.56 % |
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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 / Date: Apr 27, 1995 |
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: 2.16→30 Å / Num. all: 16868 / Num. obs: 16868 / % possible obs: 0.9054 % / Redundancy: 2.796 % / Biso Wilson estimate: 26.317 Å2 / Rmerge(I) obs: 0.072 / Net I/σ(I): 7.511 |
Reflection shell | Resolution: 1.8427→1.929 Å / Redundancy: 1.6504 % / Rmerge(I) obs: 0.2694 / Num. unique all: 2360 / % possible all: 65.23 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.16→30 Å
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