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- PDB-1lsc: THE INFLUENCE OF TEMPERATURE ON LYSOZYME CRYSTALS. STRUCTURE AND ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1lsc | ||||||
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Title | THE INFLUENCE OF TEMPERATURE ON LYSOZYME CRYSTALS. STRUCTURE AND DYNAMICS OF PROTEIN AND WATER | ||||||
![]() | HEN EGG WHITE LYSOZYME | ||||||
![]() | HYDROLASE(O-GLYCOSYL) | ||||||
Function / homology | ![]() Lactose synthesis / Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / 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 ...Lactose synthesis / Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / 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 / defense response to bacterium / endoplasmic reticulum / extracellular space / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Kurinov, I. / Harrison, R.W. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 47 KB | Display | ![]() |
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PDB format | ![]() | 34 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 366.9 KB | Display | ![]() |
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Full document | ![]() | 372.4 KB | Display | |
Data in XML | ![]() | 4.5 KB | Display | |
Data in CIF | ![]() | 6.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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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.) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.06 Å3/Da / Density % sol: 40.36 % | ||||||||||||||||||
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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: 34846 / Num. obs: 12186 / % possible obs: 83.1 % / Rmerge(I) obs: 0.0931 |
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Processing
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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: ![]() | |||||||||||||||
Refinement | *PLUS Rfactor obs: 0.195 | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS
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