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Yorodumi- PDB-191l: A HELIX INITIATION SIGNAL IN T4 LYSOZYME IDENTIFIED BY POLYALANIN... -
+Open data
-Basic information
Entry | Database: PDB / ID: 191l | ||||||
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Title | A HELIX INITIATION SIGNAL IN T4 LYSOZYME IDENTIFIED BY POLYALANINE MUTAGENESIS | ||||||
Components | LYSOZYME | ||||||
Keywords | HYDROLASE (O-GLYCOSYL) | ||||||
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: 1.95 Å | ||||||
Authors | Zhang, X.-J. / Matthews, B.W. | ||||||
Citation | Journal: Biophys.Chem. / Year: 2002 Title: A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. Authors: Zhang, X.J. / Baase, W.A. / Matthews, B.W. #1: Journal: J.Mol.Biol. / Year: 1987 Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 Angstroms Resolution Authors: Weaver, L.H. / Matthews, B.W. #2: Journal: Biochemistry / Year: 1991 Title: Toward a Simplification of the Protein Folding Problem: A Stabilizing Polyalanine Alpha-Helix Engineered in T4 Lysozyme Authors: Zhang, X.-J. / Baase, W.A. / Matthews, B.W. #3: Journal: J.Mol.Biol. / Year: 1978 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. / Ten Eyck, L.F. / Grainger, C.T. / Matthews, B.W. | ||||||
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 AS REFERENCE 3 ABOVE SHOULD BE CONSULTED FOR THESE SUBTLETIES. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 191l.cif.gz | 47.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb191l.ent.gz | 33.7 KB | Display | PDB format |
PDBx/mmJSON format | 191l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 191l_validation.pdf.gz | 424.6 KB | Display | wwPDB validaton report |
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Full document | 191l_full_validation.pdf.gz | 429.8 KB | Display | |
Data in XML | 191l_validation.xml.gz | 10.3 KB | Display | |
Data in CIF | 191l_validation.cif.gz | 14.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/91/191l ftp://data.pdbj.org/pub/pdb/validation_reports/91/191l | HTTPS FTP |
-Related 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: 18419.250 Da / Num. of mol.: 1 / Mutation: N53A, N55A, V57A, E128A, V131A, N132A 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 / Gene: T4 LYSOZYME GENE / Plasmid: pHN1403 / 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: 2.83 Å3/Da / Density % sol: 56.59 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion / Details: A.E. Eriksson, (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
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.95 Å / % possible obs: 86 % / Rmerge(I) obs: 0.05 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.95→20 Å / Rfactor obs: 0.171 Details: RESIDUES 162 - 164 IN WILD-TYPE AND ALL MUTANT LYSOZYMES THAT CRYSTALIZED IN THE WILD-TYPE CRYSTAL (P32 2 1) CRYSTAL FORM ARE EXTREMELY MOBILE. THUS THE COORDINATES FOR THESE RESIDUES ARE ...Details: RESIDUES 162 - 164 IN WILD-TYPE AND ALL MUTANT LYSOZYMES THAT CRYSTALIZED IN THE WILD-TYPE CRYSTAL (P32 2 1) CRYSTAL FORM ARE EXTREMELY MOBILE. THUS THE COORDINATES FOR THESE RESIDUES ARE VERY UNRELIABLE (IF INCLUDED). RESIDUES 162 - 164 IN WILD-TYPE AND ALL MUTANT LYSOZYMES ARE EXTREMELY MOBILE. THUS THE COORDINATES FOR THESE RESIDUES ARE VERY UNRELIABLE. | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.95→20 Å
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Refine LS restraints |
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