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Yorodumi- PDB-3lz2: STRUCTURE DETERMINATION OF TURKEY EGG WHITE LYSOZYME USING LAUE D... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3lz2 | ||||||
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Title | STRUCTURE DETERMINATION OF TURKEY EGG WHITE LYSOZYME USING LAUE DIFFRACTION | ||||||
Components | TURKEY EGG WHITE LYSOZYME | ||||||
Keywords | HYDROLASE(O-GLYCOSYL) | ||||||
Function / homology | Function and homology information glycosaminoglycan binding / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / defense response to Gram-negative bacterium / killing of cells of another organism / defense response to Gram-positive bacterium / extracellular space / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Meleagris gallopavo (turkey) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Howell, P.L. / Almo, S.C. / Parsons, M.R. / Hajdu, J. / Petsko, G.A. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.B / Year: 1992 Title: Structure determination of turkey egg-white lysozyme using Laue diffraction data. Authors: Howell, P.L. / Almo, S.C. / Parsons, M.R. / Hajdu, J. / Petsko, G.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3lz2.cif.gz | 30.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3lz2.ent.gz | 24.1 KB | Display | PDB format |
PDBx/mmJSON format | 3lz2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3lz2_validation.pdf.gz | 408.5 KB | Display | wwPDB validaton report |
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Full document | 3lz2_full_validation.pdf.gz | 414.5 KB | Display | |
Data in XML | 3lz2_validation.xml.gz | 7.5 KB | Display | |
Data in CIF | 3lz2_validation.cif.gz | 9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lz/3lz2 ftp://data.pdbj.org/pub/pdb/validation_reports/lz/3lz2 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 14228.105 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Meleagris gallopavo (turkey) / References: UniProt: P00703, lysozyme |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 42.95 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 8 / Method: vapor diffusion, sitting drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 5 Å / Num. obs: 2697 / Observed criterion σ(F): 2 / Rmerge(I) obs: 0.074 |
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-Processing
Software |
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Refinement | Rfactor Rwork: 0.2 / Rfactor obs: 0.2 / Highest resolution: 2.5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.5 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.5 Å / Rfactor obs: 0.207 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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