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Yorodumi- PDB-151l: CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 L... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 151l | ||||||
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| Title | CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME | ||||||
Components | T4 LYSOZYME | ||||||
Keywords | HYDROLASE(O-GLYCOSYL) | ||||||
| Function / homology | Function and homology informationviral 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: 2.2 Å | ||||||
Authors | Zhang, X.-J. / Matthews, B.W. | ||||||
Citation | Journal: Protein Sci. / Year: 1994Title: Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme. Authors: Zhang, X.J. / Matthews, B.W. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 151l.cif.gz | 44.2 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb151l.ent.gz | 31.3 KB | Display | PDB format |
| PDBx/mmJSON format | 151l.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 151l_validation.pdf.gz | 423.4 KB | Display | wwPDB validaton report |
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| Full document | 151l_full_validation.pdf.gz | 441.5 KB | Display | |
| Data in XML | 151l_validation.xml.gz | 11.4 KB | Display | |
| Data in CIF | 151l_validation.cif.gz | 14.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/51/151l ftp://data.pdbj.org/pub/pdb/validation_reports/51/151l | HTTPS FTP |
-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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| Components on special symmetry positions |
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Components
| #1: Protein | Mass: 18532.301 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 |
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| #2: Chemical | ChemComp-PO4 / |
| #3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.51 % |
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| Crystal grow | *PLUS pH: 6.9 / Method: unknown |
| Components of the solutions | *PLUS Conc.: 2.2 M / Common name: phosphate |
-Data collection
| Radiation | Scattering type: x-ray |
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| Radiation wavelength | Relative weight: 1 |
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Processing
| Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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| Refinement | Resolution: 2.2→20 Å / σ(F): 0 /
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| Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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| Refine LS restraints |
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| Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
| Refinement | *PLUS Rfactor obs: 0.187 | ||||||||||||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
| Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
| Refine LS restraints | *PLUS Type: t_angle_d / Dev ideal: 2.67 |
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Enterobacteria phage T4 (virus)
X-RAY DIFFRACTION
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