Table 2.

Structural features of the different lipases variants in aqueous conditions.

Enzyme	T a(K)	RMSD (nm)	Radius of Gyration (nm)	Secondary Structure (# of Residues)	SASA (nm)
					SCb	Main chain + H
RML	298	0.15 ± 0.03	1.71 ± 0.01	176 ± 5	100 ± 1	16.6 ± 0.2
	348	0.26 ± 0.01	1.71 ± 0.01	172 ± 4	100 ± 1	17.0 ± 0.1
	368	0.29 ± 0.03	1.72 ± 0.01	167 ± 3	100 ± 1	17.3 ± 0.1
cRML60	298	0.14 ± 0.02	1.70 ± 0.01	182 ± 8	121 ± 7	14.5 ± 2.2
	348	0.22 ± 0.01	1.71 ± 0.01	172 ± 3	121 ± 6	15.2 ± 2.3
	368	0.27 ± 0.03	1.72 ± 0.01	170 ± 2	122 ± 7	15.2 ± 2.3
cRML60-S2	298	0.15 ± 0.02	1.72 ± 0.01	176 ± 2	121 ± 4	14.4 ± 0.7
	348	0.20 ± 0.02	1.73 ± 0.02	174 ± 7	126 ± 4	15.1 ± 1.1
	368	0.25 ± 0.03	1.74 ± 0.01	169 ± 2	128 ± 2	15.9 ± 0.6
cRML60-S7	298	0.12 ± 0.01	1.70 ± 0.01	183 ± 1	123 ± 1	14.0 ± 0.5
	348	0.21 ± 0.01	1.72 ± 0.01	173 ± 3	126 ± 1	15.3 ± 1.4
	368	0.21 ± 0.01	1.72 ± 0.01	174 ± 6	126 ± 3	15.5 ± 2.8

The results presented are the average of three replicates from the last 100 ns of 500 ns of MD simulations.

^aT = Temperature; ^bSC = side chain.