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- PDB-1l16: STRUCTURAL ANALYSIS OF THE TEMPERATURE-SENSITIVE MUTANT OF BACTER... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1l16 | |||||||||
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Title | STRUCTURAL ANALYSIS OF THE TEMPERATURE-SENSITIVE MUTANT OF BACTERIOPHAGE T4 LYSOZYME, GLYCINE 156 (RIGHT ARROW) ASPARTIC ACID | |||||||||
![]() | T4 LYSOZYME | |||||||||
![]() | 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 | ![]() | |||||||||
![]() | Gray, T.M. / Matthews, B.W. | |||||||||
![]() | ![]() Title: Structural analysis of the temperature-sensitive mutant of bacteriophage T4 lysozyme, glycine 156----aspartic acid. Authors: Gray, T.M. / Matthews, B.W. #1: ![]() Title: Contributions of Hydrogen Bonds of Thr 157 to the Thermodynamic Stability of Phage T4 Lysozyme Authors: Alber, T. / Dao-Pin, S. / Wilson, K. / Wozniak, J.A. / Cook, S.P. / Matthews, B.W. #2: ![]() Title: Structural Studies of Mutants of the Lysozyme of Bacteriophage T4. The Temperature-Sensitive Mutant Protein Thr157 (Right Arrow) Ile Authors: Gruetter, M.G. / Gray, T.M. / Weaver, L.H. / Alber, T. / Wilson, K. / Matthews, B.W. #3: ![]() Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 Angstroms Resolution Authors: Weaver, L.H. / Matthews, B.W. #4: ![]() Title: Temperature-Sensitive Mutations of Bacteriophage T4 Lysozyme Occur at Sites with Low Mobility and Low Solvent Accessibility in the Folded Protein Authors: Alber, T. / Dao-Pin, S. / Nye, J.A. / Muchmore, D.C. / Matthews, B.W. #5: ![]() Title: Common Precursor of Lysozymes of Hen Egg-White and Bacteriophage T4 Authors: Matthews, B.W. / Gruetter, M.G. / Anderson, W.F. / Remington, S.J. #6: ![]() Title: Crystallographic Determination of the Mode of Binding of Oligosaccharides to T4 Bacteriophage Lysozyme. Implications for the Mechanism of Catalysis Authors: Anderson, W.F. / Gruetter, M.G. / Remington, S.J. / Weaver, L.H. / Matthews, B.W. #7: ![]() Title: Relation between Hen Egg White Lysozyme and Bacteriophage T4 Lysozyme. Evolutionary Implications Authors: Matthews, B.W. / Remington, S.J. / Gruetter, M.G. / Anderson, W.F. #8: ![]() Title: Structure of the Lysozyme from Bacteriophage T4, an Electron Density Map at 2.4 Angstroms Resolution Authors: Remington, S.J. / Anderson, W.F. / Owen, J. / Teneyck, L.F. / Grainger, C.T. / Matthews, B.W. #9: ![]() Title: Atomic Coordinates for T4 Phage Lysozyme Authors: Remington, S.J. / Teneyck, L.F. / Matthews, B.W. #10: ![]() Title: Comparison of the Predicted and Observed Secondary Structure of T4 Phage Lysozyme Authors: Matthews, B.W. #11: ![]() Title: The Three Dimensional Structure of the Lysozyme from Bacteriophage T4 Authors: Matthews, B.W. / Remington, S.J. #12: ![]() Title: Crystallographic Data for Lysozyme from Bacteriophage T4 Authors: Matthews, B.W. / Dahlquist, F.W. / Maynard, A.Y. | |||||||||
History |
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Remark 700 | SHEET THERE ARE SEVERAL SUBTLE ASPECTS OF THE SECONDARY STRUCTURE OF THIS MOLECULE WHICH CANNOT ...SHEET THERE ARE SEVERAL SUBTLE ASPECTS OF THE SECONDARY STRUCTURE OF THIS MOLECULE WHICH CANNOT CONVENIENTLY BE REPRESENTED IN THE HELIX AND SHEET RECORDS BELOW. THESE ASPECTS INFLUENCE THE REPRESENTATION OF HELIX 6 AND STRAND 3 OF SHEET *S1*. THE PAPER CITED IN REFERENCE 8 ABOVE SHOULD BE CONSULTED FOR THESE SUBTLETIES. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 48.3 KB | Display | ![]() |
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PDB format | ![]() | 34 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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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: 18720.504 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 55.79 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.7 / Method: batch methodDetails: taken from Remington, S.J. et al (1978). J. Mol. Biol., 81-98. | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Ambient pressure: 101 kPa / Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: OSCILLATION CAMERA / Detector: FILM / Details: Kodak No-Screen X-ray film |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray / Wavelength: 1.5418 Å |
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.7 Å / Num. obs: 15606 / Rmerge(I) obs: 0.052 |
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Processing
Software |
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Refinement | Resolution: 1.7→6 Å / Rfactor obs: 0.177 | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→6 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.177 / Highest resolution: 1.7 Å / Lowest resolution: 6 Å / Num. reflection obs: 15606 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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