Wild-type: GLU
Position: 346
Mutant: LYS
Chain: A
ΔΔG ENCoM: -0.139 kcal/mol (Destabilizing)
ΔΔG mCSM: -0.371 kcal/mol (Destabilizing)
ΔΔG SDM: -0.160 kcal/mol (Destabilizing)
ΔΔG DUET: -0.203 kcal/mol (Destabilizing)
ΔΔSVib ENCoM: 0.174 kcal.mol-1.K-1 (Increase of molecule flexibility)
Amino acids colored according to the vibrational entropy change upon mutation. BLUE represents a rigidification of the structure and RED a gain in flexibility
Bond Type | Color |
---|---|
Hydrogen bonds | |
Water mediated hydrogen bonds | |
Weak hydrogen bonds | |
Water mediated weak hydrogen bonds | |
Halogen bonds | |
Ionic interactions | |
Metal complex interactions | |
Aromatic contacts | |
Hydrophobic contacts | |
Carbonyl contacts |
Wild-type and mutant residues are colored in light-green and are also represented as sticks alongside with the surrounding residues which are involved on any type of interactions.
Wild-type and Mutant sequence were extracted from their respective 3D structures and then aligned. The results of normal mode data for each of the sequences are displayed below.
Type of secondary structure on each region of the sequence is added to the top and bottom margins of the plot (helices black and strands gray)
Atomic Fluctuation provides the amplitude of the absolute atomic motion.
Calculations performed over the first 10 non-trivial modes of the molecule.
The magnitute of the fluctuation is represented by thin to thick tube colored blue (low), white (moderate) and red (high).
Deformation energy provides a measure for the amount of local flexibility in the protein.
Calculations performed over the first 10 non-trivial modes of the molecule.
The magnitute of the deformation is represented by thin to thick tube colored blue (low), white (moderate) and red (high).