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Yorodumi- PDB-175l: PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 175l | ||||||
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Title | PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF 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: 2.1 Å | ||||||
Authors | Baldwin, E. / Matthews, B.W. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1995 Title: Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme. Authors: Zhang, X.J. / Wozniak, J.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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 175l.cif.gz | 74.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb175l.ent.gz | 56.9 KB | Display | PDB format |
PDBx/mmJSON format | 175l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 175l_validation.pdf.gz | 422.9 KB | Display | wwPDB validaton report |
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Full document | 175l_full_validation.pdf.gz | 435.1 KB | Display | |
Data in XML | 175l_validation.xml.gz | 15.3 KB | Display | |
Data in CIF | 175l_validation.cif.gz | 20.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/75/175l ftp://data.pdbj.org/pub/pdb/validation_reports/75/175l | HTTPS FTP |
-Related structure data
Related structure data | 167lC 168lC 169lC 170lC 171lC 172lC 173lC 174lC 176lC 177lC 178lC 180lC 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 18542.246 Da / Num. of mol.: 2 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: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 49.94 % | ||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 49 % | ||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8.6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||
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 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Highest resolution: 2.1 Å /
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Refinement step | Cycle: LAST / Highest resolution: 2.1 Å
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Refine LS restraints |
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