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Open data
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Basic information
Entry | Database: PDB / ID: 206l | ||||||
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Title | PHAGE T4 LYSOZYME | ||||||
![]() | LYSOZYME | ||||||
![]() | HYDROLASE (O-GLYCOSYL) / HYDROLASE / O-GLYCOSYL | ||||||
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 | ![]() ![]() | ||||||
![]() | Blaber, M. / Matthews, B.W. | ||||||
![]() | ![]() Title: Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. Authors: Blaber, M. / Lindstrom, J.D. / Gassner, N. / Xu, J. / Heinz, D.W. / 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 | ![]() | 46.8 KB | Display | ![]() |
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PDB format | ![]() | 33.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 423.2 KB | Display | ![]() |
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Full document | ![]() | 425.3 KB | Display | |
Data in XML | ![]() | 9.9 KB | Display | |
Data in CIF | ![]() | 13.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 118lC ![]() 119lC ![]() 120lC ![]() 122lC ![]() 123lC ![]() 125lC ![]() 126lC ![]() 127lC ![]() 128lC ![]() 221lC ![]() 224lC ![]() 3lzmS S: Starting model for refinement 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: 18644.363 Da / Num. of mol.: 1 / Mutation: A42S, C54T, C97A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Chemical | #3: Chemical | ChemComp-BME / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.79 Å3/Da / Density % sol: 55.97 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.7 / Details: pH 6.7 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6.9 / Method: batch method / Details: Matthew, B.W., (1973) J. Mol. Biol., 78, 575. / PH range low: 7.3 / PH range high: 6.7 | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Jan 1, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 18840 / % possible obs: 82 % / Observed criterion σ(I): 3 / Rmerge(I) obs: 0.034 |
Reflection | *PLUS Highest resolution: 1.75 Å |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3LZM Resolution: 1.75→20 Å / σ(F): 3 / Stereochemistry target values: TNT /
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Solvent computation | Solvent model: TNT / Bsol: 509 Å2 / ksol: 1 e/Å3 | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.75→20 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.17 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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