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Open data
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Basic information
Entry | Database: PDB / ID: 1cvk | ||||||
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Title | T4 LYSOZYME MUTANT L118A | ||||||
![]() | LYSOZYME![]() | ||||||
![]() | ![]() ![]() ![]() | ||||||
Function / homology | ![]() viral release from host cell by cytolysis / peptidoglycan catabolic process / cell wall macromolecule catabolic process / ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Gassner, N.C. / Baase, W.A. / Lindstrom, J. / Lu, J. / Matthews, B.W. | ||||||
![]() | ![]() Title: Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Authors: Gassner, N.C. / Baase, W.A. / Lindstrom, J.D. / Lu, J. / Dahlquist, F.W. / Matthews, B.W. #1: ![]() Title: The Response of T4 Lysozyme to Large-to-Small Substitutions Within the Core and its Relation to the Hydrophobic Effect Authors: Xu, J. / Baase, W.A. / Baldwin, E. / Matthews, B.W. #2: ![]() Title: Alanine Scanning Mutagenesis of the Alpha-Helix 115-123 of Phage T4 Lysozyme: Effects on Structure, Stability and the Binding of Solvent Authors: Blaber, M. / Baase, W.A. / Gassner, N. / Matthews, B.W. #3: ![]() Title: Response of a Protein Structure to Cavity-Creating Mutations and its Relationship to the Hydrophobic Effect Authors: Eriksson, A.E. / Baase, W.A. / Zhang, X.-J. / Heinz, D.W. / Blaber, M. / Baldwin, E.P. / Matthews, B.W. #4: ![]() Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 A Resolution Authors: Weaver, L.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 | ![]() | 47.7 KB | Display | ![]() |
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PDB format | ![]() | 33.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1ctwC ![]() 1cu0C ![]() 1cu2C ![]() 1cu3C ![]() 1cu5C ![]() 1cu6C ![]() 1cupC ![]() 1cuqC ![]() 1cv0C ![]() 1cv1C ![]() 1cv3C ![]() 1cv4C ![]() 1cv5C ![]() 1cv6C ![]() 1qsqC 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: 18586.283 Da / Num. of mol.: 1 / Mutation: C54T, C97A, L118A 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: 2.8 Å3/Da / Density % sol: 56.15 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Temperature: 277 K / Method: vapor diffusion, hanging drop / Details: NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.7 / 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: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: KODAK / Detector: FILM |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.8→30 Å / Num. all: 16392 / Num. obs: 16392 / % possible obs: 92.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 1.26 % / Rmerge(I) obs: 0.06 |
Reflection | *PLUS |
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Processing
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Refinement | Resolution: 1.8→30 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: TNT PROTGEO
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Refinement step | Cycle: LAST / Resolution: 1.8→30 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.8 Å / Rfactor Rwork![]() | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: t_angle_deg / Dev ideal: 2 |