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- PDB-1flu: HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FOR GLYCINE -
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Open data
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Basic information
Entry | Database: PDB / ID: 1flu | ||||||
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Title | HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FOR GLYCINE | ||||||
![]() | LYSOZYME | ||||||
![]() | HYDROLASE / HEN LYSOZYME / ALANINE SCANNING | ||||||
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 | ![]() | ||||||
![]() | Masumoto, K. / Ueda, T. / Motoshima, H. / Imoto, T. | ||||||
![]() | ![]() Title: Relationship between local structure and stability in hen egg white lysozyme mutant with alanine substituted for glycine Authors: Masumoto, K. / Ueda, T. / Motoshima, H. / Imoto, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 33.3 KB | Display | ![]() |
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PDB format | ![]() | 25.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 354.1 KB | Display | ![]() |
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Full document | ![]() | 354.2 KB | Display | |
Data in XML | ![]() | 3.8 KB | Display | |
Data in CIF | ![]() | 5.7 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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1 |
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Unit cell |
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Components
#1: Protein | Mass: 14345.186 Da / Num. of mol.: 1 / Mutation: G67A 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: 2.08 Å3/Da / Density % sol: 40.96 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 4.7 Details: sodium chloride, sodium acetate, pH 4.7, VAPOR DIFFUSION, HANGING DROP, temperature 295K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS PH range low: 3.2 / PH range high: 2.4 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.785→6 Å / Num. all: 12048 / Num. obs: 10452 / Redundancy: 1.15 % / Rmerge(I) obs: 0.0558 |
Reflection | *PLUS % possible obs: 86.8 % / Num. measured all: 12048 |
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Processing
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Refinement | Resolution: 1.785→6 Å / Cross valid method: THROUGHOUT
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Refinement step | Cycle: LAST / Resolution: 1.785→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | |||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 6 Å / % reflection Rfree: 10 % / Rfactor Rfree: 0.25 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |