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Open data
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Basic information
Entry | Database: PDB / ID: 1g0q | ||||||
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Title | CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT V149I | ||||||
![]() | PROTEIN (LYSOZYME) | ||||||
![]() | HYDROLASE / O-Glycosyl / Glycosidase / Bacteriolytic Enzyme | ||||||
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 | ![]() | ||||||
![]() | Xu, J. / Baase, W.A. / Quillin, M.L. / Matthews, B.W. | ||||||
![]() | ![]() Title: Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. Authors: Xu, J. / Baase, W.A. / Quillin, M.L. / Baldwin, E.P. / 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 | ![]() | 47.9 KB | Display | ![]() |
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PDB format | ![]() | 33.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 426.7 KB | Display | ![]() |
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Full document | ![]() | 430.2 KB | Display | |
Data in XML | ![]() | 10.9 KB | Display | |
Data in CIF | ![]() | 15 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1g06C ![]() 1g07C ![]() 1g0gC ![]() 1g0jC ![]() 1g0kC ![]() 1g0lC ![]() 1g0mC ![]() 1g0pC ![]() 1g1vC ![]() 1g1wC ![]() 1i6sC 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: 18642.391 Da / Num. of mol.: 1 / Mutation: C54T; C97A; V149I 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: 2.75 Å3/Da / Density % sol: 55.21 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.8 Details: Phosphate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS 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: 300 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Apr 25, 1994 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→10 Å / Num. all: 18113 / Num. obs: 18113 / % possible obs: 90 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2 % / Biso Wilson estimate: 25 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 12 |
Reflection shell | Resolution: 1.8→2 Å / Redundancy: 1.5 % / Rmerge(I) obs: 0.112 / % possible all: 60 |
Reflection | *PLUS Rmerge(I) obs: 0.05 |
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Processing
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Refinement | Resolution: 1.8→10 Å / σ(F): 0 / σ(I): 2 / Stereochemistry target values: TNT
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Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Version: 5E / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.8 Å / σ(F): 0 / Rfactor all: 0.15 / Rfactor Rwork: 0.15 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: t_angle_deg / Dev ideal: 1.9 |