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Open data
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Basic information
Entry | Database: PDB / ID: 1cv3 | ||||||
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Title | T4 LYSOZYME MUTANT L121M | ||||||
![]() | LYSOZYME | ||||||
![]() | HYDROLASE / HYDROLASE (O-GLYCOSYL) / T4 LYSOZYME / METHIONINE CORE MUTANT / PROTEIN ENGINEERING / PROTEIN FOLDING | ||||||
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 | ![]() | ||||||
![]() | 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: A test of the "jigsaw-puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme Authors: Gassner, N.C. / Baase, W.A. / Matthews, B.W. #2: ![]() 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 | ![]() | 47.8 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 ![]() 1cv4C ![]() 1cv5C ![]() 1cv6C ![]() 1cvkC ![]() 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: 18646.400 Da / Num. of mol.: 1 / Mutation: C54T, C97A, L121M 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: 2.79 Å3/Da / Density % sol: 55.86 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop Details: NA2PO4, NACL, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||||||||||||||||||||
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 | 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: 1.7→30 Å / Num. all: 19501 / Num. obs: 19501 / % possible obs: 88.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.6 % / Biso Wilson estimate: 28.8 Å2 / Rmerge(I) obs: 0.036 / Net I/σ(I): 12.2 |
Reflection shell | Resolution: 1.74→1.87 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.22 / % possible all: 64 |
Reflection shell | *PLUS % possible obs: 64 % |
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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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