Table 3.

Structure features of MuML RT and mutation.

Domain	Region	Function	Mutations
			Deleterious	Ambiguous	Advantageous
Palm	1–23	dispensable			E5K
	D150, D224, D225	polymerase catalytically essential residues
	Y222-V223-D224-D225	conserved YXDD moiety	Y222A/S, V223F	Y222F	V223A/H/M
	D153, F155, F156, Q190, V223	dNTP binding pocket	Q190, V223F		F115Y, Q190F, V223A/H/M
	I125-F155, L220-E233, K257-E275	surface interacting with a template	T147, V148, L149, D150, L151, K152, C157, R159, H161, K152, A154S, D153A, F155W, F156	F155	P130S, L139P, Q221R
Fingers	S60-Q84, N95-D124, F156-C157, Q190-N194	surface interacting with the template	Y64A, D114A, R116A, E117, N119	Y64W, R116M, K152R, T197A	M66L, S67R, E69K, Q84A, T197A
	L188-P189-Q190-G191	contributing to the positioning of the incoming dNTP
	K103, R110, D153, A154, F155, Q190	equivalent to the dTTP binding residues of HIV-1 RT	K103, R110
Thumb	F303-L304	consecutive surface hydrophobic residues
	L280-T287, R301-L333, A354-L359	located on the surface interacting with a template			E286R, T287A, R301L, E302K/R, A307V, F309A/N, M320L, W313F, T330E/P, L333Q
	267–274	primer grip
	295–318	minor groove binding track			R301L, E302K/R, A307V, F309A/N
Connection	P360-K373, Y394-A436, S453-A462	surface interacting with a template			N454K
	L432-V433-I434-L435-A436	five consecutive hydrophobic residues	L435K		V433K/R, L435G/K/M/R
RNAse H	475–502	RNAse H domain flexibility, essential for viral propagation			A502V
	D524, E562, D583, D653	RNAse H catalytically active residues			D524A/E/G/N, E562D/Q, D583N, D623A/D/H/N/V
	V402-G403-W404, S557-A558-Q559-R560, Y586, T590	RNAse H primer grip	V402-G403-W404, S557-A558-Q559-R560, Y586, T590		Y586A
	L529, A558, Q559, R585, H638	participating in contacts with a template			H638G