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- PDB-1lwg: Multiple Methionine Substitutions are Tolerated in T4 Lysozyme an... -
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Open data
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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 | ||||||
![]() | 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.M. / Busam, R.D. / Weaver, L.H. / Lindstrom, J.D. / Quillin, M.L. / Matthews, B.M. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 50.3 KB | Display | ![]() |
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PDB format | ![]() | 35.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 446.1 KB | Display | ![]() |
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Full document | ![]() | 452.7 KB | Display | |
Data in XML | ![]() | 11.4 KB | Display | |
Data in CIF | ![]() | 15.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ks3C ![]() 1kw5C ![]() 1kw7C ![]() 1ky0C ![]() 1ky1C ![]() 1l0jC ![]() 1l0kC ![]() 1lpyC ![]() 1lw9C ![]() 1lwkC ![]() 1l63S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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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.) ![]() ![]() ![]() |
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-Non-polymers , 5 types, 152 molecules ![](data/chem/img/PO4.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/K.gif)
![](data/chem/img/HED.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/K.gif)
![](data/chem/img/HED.gif)
![](data/chem/img/HOH.gif)
#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: ![]() |
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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: ![]() ![]() ![]() |
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 |
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Processing
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Refinement | Method to determine structure: ![]() 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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