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Yorodumi- PDB-1lsa: THE INFLUENCE OF TEMPERATURE ON LYSOZYME CRYSTALS. STRUCTURE AND ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lsa | ||||||
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Title | THE INFLUENCE OF TEMPERATURE ON LYSOZYME CRYSTALS. STRUCTURE AND DYNAMICS OF PROTEIN AND WATER | ||||||
Components | HEN EGG WHITE LYSOZYME | ||||||
Keywords | HYDROLASE(O-GLYCOSYL) | ||||||
Function / homology | Function and homology information Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / killing of cells of another organism / defense response to Gram-negative bacterium / defense response to Gram-positive bacterium / defense response to bacterium ...Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / killing of cells of another organism / defense response to Gram-negative bacterium / defense response to Gram-positive bacterium / defense response to bacterium / endoplasmic reticulum / extracellular space / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.7 Å | ||||||
Authors | Kurinov, I. / Harrison, R.W. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 1995 Title: The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water. Authors: Kurinov, I.V. / Harrison, R.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lsa.cif.gz | 44.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lsa.ent.gz | 35.8 KB | Display | PDB format |
PDBx/mmJSON format | 1lsa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ls/1lsa ftp://data.pdbj.org/pub/pdb/validation_reports/ls/1lsa | HTTPS FTP |
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-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: 14331.160 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / References: UniProt: P00698, lysozyme |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.93 Å3/Da / Density % sol: 36.13 % | ||||||||||||||||||
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Crystal grow | *PLUS pH: 4.7 / 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 |
Reflection | *PLUS Highest resolution: 1.7 Å / Num. all: 25732 / Num. obs: 9792 / % possible obs: 75.3 % / Rmerge(I) obs: 0.0788 |
-Processing
Software |
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Refinement | Resolution: 1.7→6 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 1.7→6 Å
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Software | *PLUS Name: X-PLOR / Classification: refinement | |||||||||||||||
Refinement | *PLUS Rfactor obs: 0.209 | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS
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