[English] 日本語
Yorodumi- PDB-1l77: DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PA... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1l77 | ||||||
---|---|---|---|---|---|---|---|
Title | DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME | ||||||
Components | T4 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: 2.05 Å | ||||||
Authors | Hurley, J.H. / Matthews, B.W. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1992 Title: Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. Authors: Hurley, J.H. / Baase, W.A. / Matthews, B.W. | ||||||
History |
| ||||||
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 J.MOL.BIOL., V. 118, P. 81, 1978 BE CONSULTED FOR THESE SUBTLETIES. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1l77.cif.gz | 47.1 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1l77.ent.gz | 33.2 KB | Display | PDB format |
PDBx/mmJSON format | 1l77.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1l77_validation.pdf.gz | 431.5 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1l77_full_validation.pdf.gz | 436.7 KB | Display | |
Data in XML | 1l77_validation.xml.gz | 10.1 KB | Display | |
Data in CIF | 1l77_validation.cif.gz | 13.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l7/1l77 ftp://data.pdbj.org/pub/pdb/validation_reports/l7/1l77 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 18610.324 Da / Num. of mol.: 1 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 / Plasmid: M13 / References: UniProt: P00720, lysozyme | ||||
---|---|---|---|---|---|
#2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 55.73 % |
---|---|
Crystal grow | *PLUS Method: other / Details: Matthews, B.W., (1973) J. Mol. Biol., 78, 575. |
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.05 Å / Rmerge(I) obs: 0.068 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.05→6 Å Details: RESIDUES 162 - 164 IN WILD-TYPE AND ALL MUTANT LYSOZYMES ARE EXTREMELY MOBILE. THUS THE COORDINATES FOR THESE RESIDUES ARE VERY UNRELIABLE. THIS ENTRY DOES NOT INCLUDE RESIDUES 163 AND 164.
| ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.05→6 Å
| ||||||||||||||||||||||||||||||
Refine LS restraints |
|