M82L

Structure-based Mutation Analysis

SCWRL

scwrl wt energy?

Hydrogen Bonding network

The following figures show the hydrogen bonds between the wildtype residue and its environment compared to the formation of hydrogen bonds when the corresponding residue is mutated.

M82L

Figure 2: Hydrogen Bonds for methionine on pos 82 in the wild type structure

Figure 3: Hydrogen Bonds for leucine on pos 82 in the mutated type structure

Comparing the figures 2 and 3 for the wildtype and the mutated amino acid on position 82, no change in the hydrogen bonding network can be observed. This is due to the similar physiochemical properties of these two amino acids. No atom which could serve as additional hydrogen-bond donor or acceptor was introduced or removed.

Comparison Energies

foldX

wildtype energy	total energy of mutated protein	difference
401.00	437.88	36.88

minimise

wildtype energy	total energy of mutated protein	difference
-2485.452755	-4253.174790	-1767.722015

gromacs

Energy	Average	Err.Est	RMSD	Tot-Drift (kJ/mol)
Bond	2518.71	1700	6337.97	-10023.3
Angle	3642.41	270	638.624	-1479.34
Potential	5.16e+06	5.1e+06	7.47e+07	-3.13e+07