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- PDB-1kxy: ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPO... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1kxy | ||||||
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Title | ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE AND CHARGED SIDE CHAINS | ||||||
![]() | LYSOZYME | ||||||
![]() | HYDROLASE / GLYCOSIDASE / ELECTROSTATIC INTERACTION / HELIX / HEN LYSOZYME / STABILITY | ||||||
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 | ![]() | ||||||
![]() | Motoshima, H. / Ohmura, T. / Ueda, T. / Imoto, T. | ||||||
![]() | ![]() Title: Analysis of the stabilization of hen lysozyme by helix macrodipole and charged side chain interaction. Authors: Motoshima, H. / Mine, S. / Masumoto, K. / Abe, Y. / Iwashita, H. / Hashimoto, Y. / Chijiiwa, Y. / Ueda, T. / 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 | ![]() | 33.8 KB | Display | ![]() |
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PDB format | ![]() | 25.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 406.5 KB | Display | ![]() |
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Full document | ![]() | 407.6 KB | Display | |
Data in XML | ![]() | 7.6 KB | Display | |
Data in CIF | ![]() | 9.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1kxwC ![]() 1kxxC ![]() 1rfpSC S: Starting model for refinement C: citing same article ( |
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Similar 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: 14330.176 Da / Num. of mol.: 1 / Mutation: D18N 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: 40.93 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 4.7 / Details: 50 MM ACETATE AT PH 4.7 CONTAINING 0.9 M NACL | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / pH: 5.5 | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Jul 1, 1996 |
Radiation | Monochromator: DOUBLE CRYSTAL SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.79→100 Å / Num. obs: 10402 / % possible obs: 86.4 % / Observed criterion σ(I): 1 / Rmerge(I) obs: 0.0774 |
Reflection shell | Resolution: 1.79→1.8 Å / Rmerge(I) obs: 0.258 / % possible all: 56.1 |
Reflection | *PLUS Highest resolution: 1.95 Å / Num. obs: 8613 / % possible obs: 93.8 % / Rmerge(I) obs: 0.047 |
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Processing
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Refinement | Starting model: PDB ENTRY 1RFP Resolution: 1.79→6 Å / Data cutoff low absF: 1 / σ(F): 1
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Refinement step | Cycle: LAST / Resolution: 1.79→6 Å
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Xplor file |
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Software | *PLUS Name: ![]() | |||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.95 Å / Rfactor obs: 0.168 / Rfactor Rwork: 0.168 | |||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||
Refine LS restraints | *PLUS
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