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- PDB-1hem: STRUCTURAL AND THERMODYNAMIC ANALYSIS OF COMPENSATING MUTATIONS W... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1hem | |||||||||
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Title | STRUCTURAL AND THERMODYNAMIC ANALYSIS OF COMPENSATING MUTATIONS WITHIN THE CORE OF CHICKEN EGG WHITE LYSOZYME | |||||||||
![]() | 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 | ![]() | |||||||||
![]() | Wilson, K.P. / Malcolm, B.A. / Matthews, B.W. | |||||||||
![]() | ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 37.4 KB | Display | ![]() |
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PDB format | ![]() | 28 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1helC ![]() 1henC ![]() 1heoC ![]() 1hepC ![]() 1heqC ![]() 1herC 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 on special symmetry positions |
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Components
#1: Protein | Mass: 14345.188 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: 40.15 % | |||||||||||||||||||||||||||||||||||
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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: ![]() |
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 |
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Processing
Software |
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Refinement | Rfactor obs: 0.14 / 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: 8336 / Rfactor obs: 0.14 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: t_angle_d / Dev ideal: 2.2 |