+Open data
-Basic information
Entry | Database: PDB / ID: 1cu3 | ||||||
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Title | T4 LYSOZYME MUTANT V87M | ||||||
Components | LYSOZYME | ||||||
Keywords | HYDROLASE / HYDROLASE (O-GLYCOSYL) / T4 LYSOZYME / METHIONINE CORE MUTANT / PROTEIN ENGINEERING / PROTEIN FOLDING | ||||||
Function / homology | Function and homology information 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 | Enterobacteria phage T4 (virus) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.12 Å | ||||||
Authors | Gassner, N.C. / Baase, W.A. / Lindstrom, J.D. / Lu, J. / Matthews, B.W. | ||||||
Citation | Journal: Biochemistry / Year: 1999 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: Journal: Proc.Natl.Acad.Sci.USA / Year: 1996 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: Journal: J.Mol.Biol. / Year: 1987 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cu3.cif.gz | 47.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cu3.ent.gz | 33.8 KB | Display | PDB format |
PDBx/mmJSON format | 1cu3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1cu3_validation.pdf.gz | 408.9 KB | Display | wwPDB validaton report |
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Full document | 1cu3_full_validation.pdf.gz | 413.6 KB | Display | |
Data in XML | 1cu3_validation.xml.gz | 6.4 KB | Display | |
Data in CIF | 1cu3_validation.cif.gz | 8.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cu/1cu3 ftp://data.pdbj.org/pub/pdb/validation_reports/cu/1cu3 | HTTPS FTP |
-Related structure data
Related structure data | 1ctwC 1cu0C 1cu2C 1cu5C 1cu6C 1cupC 1cuqC 1cv0C 1cv1C 1cv3C 1cv4C 1cv5C 1cv6C 1cvkC 1qsqC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 18660.428 Da / Num. of mol.: 1 / Mutation: C54T, V87M, C97A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage T4 (virus) / Genus: T4-like viruses / Species: Enterobacteria phage T4 sensu lato / Production host: Escherichia coli (E. coli) / References: UniProt: P00720, lysozyme | ||||
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#2: Chemical | #3: Chemical | ChemComp-HED / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 55.5 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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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 source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
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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: 1.74→30 Å / Num. all: 17681 / Num. obs: 17681 / % possible obs: 85.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 26.9 Å2 / Rmerge(I) obs: 0.059 / Net I/σ(I): 8.1 |
-Processing
Software |
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Refinement | Resolution: 2.12→30 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: TNT PROTGEO
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Refinement step | Cycle: LAST / Resolution: 2.12→30 Å
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Refine LS restraints |
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