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Open data
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Basic information
Entry | Database: PDB / ID: 1qug | ||||||
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Title | E108V MUTANT OF T4 LYSOZYME | ||||||
![]() | PROTEIN (LYSOZYME) | ||||||
![]() | HYDROLASE | ||||||
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 | ![]() | ||||||
![]() | Wray, J. / Baase, W.A. / Lindstrom, J.D. / Poteete, A.R. / Matthews, B.W. | ||||||
![]() | ![]() Title: Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. Authors: Wray, J.W. / Baase, W.A. / Lindstrom, J.D. / Weaver, L.H. / Poteete, A.R. / Matthews, B.W. #1: ![]() Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7A Resolution Authors: Weaver, L.H. / Matthews, B.W. #2: ![]() Title: Second-site Revertants of an Inactive T4 Lysozyme Mutant Restore Activity Structuring the Active Site Cleft Authors: Poteete, A.R. / Sun, D.P. / Nicholson, 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 | ![]() | 46.9 KB | Display | ![]() |
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PDB format | ![]() | 33 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 430.2 KB | Display | ![]() |
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Full document | ![]() | 435.7 KB | Display | |
Data in XML | ![]() | 10.3 KB | Display | |
Data in CIF | ![]() | 13.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 18371.121 Da / Num. of mol.: 1 / Mutation: C54T, C97A, E108V Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-CL / |
#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: 56.62 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 7.1 / PH range high: 6.3 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() |
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Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→20 Å / Num. all: 44381 / Num. obs: 16431 / % possible obs: 97 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.7 % / Rmerge(I) obs: 0.088 / Net I/σ(I): 5.6 |
Reflection shell | Resolution: 1.9→2.05 Å / Redundancy: 1.5 % / Rmerge(I) obs: 0.23 / Num. unique all: 3200 / % possible all: 96 |
Reflection | *PLUS Num. obs: 16430 / % possible obs: 93 % |
Reflection shell | *PLUS % possible obs: 96 % |
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Processing
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Refinement | Resolution: 1.9→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: TNT
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Refinement step | Cycle: LAST / Resolution: 1.9→20 Å
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Refine LS restraints |
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