Table 1.

The table contains a list of interacting residues. Based on the dAffinity, dStability, and Predicted ΔΔG was used to understand the impact of each substitution when changed to alanine. The significant substitutions which reduce the binding affinity and stability of the Protein-RNA complex are given in bold.

Index	Residue Position	dAffinity	dStability	Predicted ΔΔG	Outcome
1	D103A	−0.218208126	0.7058154	5.07	Increased affinity
2	E174A	−0.627432562	1.099226294	4.5735	Increased affinity
3	F171A	0.131910418	2.094553371	−8.7225	Reduced affinity
4	G170A	0.799354909	0.041698953	−5.559	Reduced affinity
5	G175A	−0.632812623	0.687884896	6.7065	Increased affinity
6	G178A	−1.332230401	0.668020025	9.135	Increased affinity
7	G60A	−0.655284048	0.079444368	0.4935	Increased affinity
8	H59A	3.80850533	0.429009885	−8.3685	Reduced affinity
9	K102A	1.651298071	0.815469681	1.0365	Increased affinity
10	K169A	1.957372005	−0.315900659	−1.6425	Reduced affinity
11	K61A	2.456900907	−0.43984319	−2.547	Reduced affinity
12	L104A	3.159796329	1.738786997	5.541	Increased affinity
13	P168A	0.064328214	1.125976312	0.3195	Increased affinity
14	R107A	0.831868936	1.887304986	−1.0755	Reduced affinity
15	R177A	6.054382342	0.310284166	4.212	Increased affinity
16	S105A	0.957764581	0.470427697	−1.6065	Reduced affinity
17	S176A	0.304609561	0.649918458	1.368	Increased affinity
18	T57A	0.936589745	1.111603419	−7.2075	Reduced affinity
19	Y172A	6.632200002	2.154790282	−0.438	Reduced affinity

Molecular Dynamics Simulation.