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Yorodumi- PDB-1hen: STRUCTURAL AND THERMODYNAMIC ANALYSIS OF COMPENSATING MUTATIONS W... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1hen | ||||||
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Title | STRUCTURAL AND THERMODYNAMIC ANALYSIS OF COMPENSATING MUTATIONS WITHIN THE CORE OF CHICKEN EGG WHITE LYSOZYME | ||||||
Components | HEN EGG WHITE LYSOZYME | ||||||
Keywords | HYDROLASE(O-GLYCOSYL) | ||||||
Function / homology | Function and homology information Lactose synthesis / 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 ...Lactose synthesis / 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: 1.8 Å | ||||||
Authors | Wilson, K.P. / Malcolm, B.A. / Matthews, B.W. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1992 Title: Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme. Authors: Wilson, K.P. / Malcolm, B.A. / Matthews, B.W. #1: Journal: Nature / Year: 1990 Title: Ancestral Lysozymes Reconstructed, Neutrality Tested, and Thermostability Linked to Hydrocarbon Packing Authors: Malcolm, B.A. / Wilson, K.P. / Matthews, B.W. / Kirsch, J.F. / Wilson, A.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hen.cif.gz | 37.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hen.ent.gz | 28.1 KB | Display | PDB format |
PDBx/mmJSON format | 1hen.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/he/1hen ftp://data.pdbj.org/pub/pdb/validation_reports/he/1hen | HTTPS FTP |
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-Related structure data
Related structure data | 1helC 1hemC 1heoC 1hepC 1heqC 1herC C: citing same article (ref.) |
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Similar 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) / Organ: EGG / 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: 2.05 Å3/Da / Density % sol: 39.89 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 4.4 / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Ambient pressure: 101 kPa / Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: ELLIOTT GX-21 / Target: Cu / Voltage: 40 kV |
Detector | Type: OSCILLATION CAMERA / Detector: FILM / Details: Kodak No-Screen X-ray film |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray / Wavelength: 1.5418 Å |
Radiation wavelength | Relative weight: 1 |
-Processing
Software |
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Refinement | Rfactor obs: 0.152 / Highest resolution: 1.8 Å | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.8 Å / Num. reflection obs: 10080 / Rfactor obs: 0.152 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: t_angle_d / Dev ideal: 2.4 |