Table 1. Stabilizing Point Mutations Discovered in PjTA.

mutation	location	origin	ΔΔGfold (kJ/mol)a	ΔTmapp (°C)b
P9A	surface	Rosetta	–4.3	2
P9K	surface	Rosetta	–7.4	1.5
E38K	surface	Rosetta	–9.9	1.5
E38Q	surface	Rosetta	–5.5	2
A60V	interface	consensus		4
E74I	surface, interface	FoldX, Rosetta	–7.8, −11.2	5.5
N78K	surface, interface	Rosetta	–4.1	1
F86W	interface	Rosetta	–12.9	4
S87D	interface	FoldX	–3.0	7
S87H	interface	Rosetta	–15.1	1
S87N	interface	FoldX, Rosetta	–4.1, −9.9	1.5
S87Q	interface	FolX, Rosetta	–3.8, −4.8	1
K89A	interface	Rosetta	–4.4	2
K89F	interface	FoldX, Rosetta	–6.2, −19.0	6
K89L	interface	FoldX	–7.4	4.5
K89M	interface	FoldX	–3.7	3.5
K89W	interface	Rosetta	–15.9	3.5
K89Y	interface	Rosetta	–16.6	4
S94A	interface	Rosetta	–9.4	8
S110Q	surface	FoldX, Rosetta	–3.8, −4.7	1
M128F	interface	FoldX, Rosetta	–5.0, −15.5	4.5
P139 K	surface	Rosetta	–3.2	1
N149G	surface	FoldX	–3.0	2.5
I154D	interface	Rosetta	–3.2	4
I154N	interface	Rosetta	–7.0	3.5
I154V	interface	Rosetta, consensus	–10.3	9
L227V	surface	consensus		1
L319F	interface	FoldX, Rosetta	–6.9, −4.9	4
A393R	surface	FoldX	–3.9	1.5
M419I	surface	Rosetta	–6.2	1
M419L	surface	Rosetta	–4.2	1.5

^aThe ΔΔG^fold energies are calculated by FoldX and/or the Rosetta Row 3 protocol; values are per monomer.

^bThe ΔT_m^app value of wild-type PjTA (WT) is 62 °C.