Table 2.
Effects of in silico mutations of selected important residues of FP2 on the E64-FP2 binding Gibbs free energy change.
| Binding ΔG* (kJ/mol) | Mutation Binding ΔΔG (kJ/mol) | A: Rank/Order Based on ΔΔG | B: Rank/Order Based on Fig. 4b | C: Combined Rank (C = A + B) | |
|---|---|---|---|---|---|
| Wild Type | −12.2 ± 1.1 | — | — | — | — |
| D234A | −0.4 ± 0.5 | 11.8 ± 0.9 | 2 | 1 | 3 |
| N173L | −0.7 ± 1.0 | 11.5 ± 1.0 | 4 | 2 | 6 |
| W43F | −1.3 ± 0.2 | 10.9 ± 0.2 | 7 | 3 | 10 |
| H174F | −0.5 ± 0.7 | 11.7 ± 0.7 | 3 | 10 | 13 |
| N38A | −0.8 ± 1.1 | 11.4 ± 1.1 | 6 | 7 | 13 |
| L172A | −1.4 ± 0.8 | 10.8 ± 1.0 | 8 | 5 | 13 |
| W43A | −2.5 ± 1.2 | 9.7 ± 1.1 | 10 | 3 | 13 |
| D234L | −3.3 ± 0.7 | 8.9 ± 0.7 | 12 | 1 | 13 |
| N38L | −3.1 ± 0.8 | 9.1 ± 0.8 | 11 | 7 | 18 |
| N173A | −6.1 ± 0.6 | 6.1 ± 0.9 | 19 | 2 | 21 |
| G40A | −3.3 ± 0.9 | 8.9 ± 1.0 | 13 | 9 | 22 |
| D170L | −0.7 ± 1.0 | 11.5 ± 1.0 | 5 | 19 | 24 |
| H174A | −3.9 ± 1.2 | 8.3 ± 1.1 | 14 | 10 | 24 |
| S41A | −0.2 ± 0.3 | 12.0 ± 0.8 | 1 | 25 | 26 |
| G82A | −6.2 ± 1.6 | 6.0 ± 1.4 | 21 | 6 | 27 |
| L84A | −8.1 ± 0.7 | 4.1 ± 0.9 | 23 | 4 | 27 |
| D170A | −2.0 ± 0.9 | 10.2 ± 1.0 | 9 | 19 | 28 |
| W206A | −3.9 ± 1.2 | 8.3 ± 1.1 | 15 | 16 | 31 |
| N81A | −6.2 ± 1.5 | 6.0 ± 1.3 | 20 | 11 | 31 |
| N77A | −4.3 ± 1.1 | 7.9 ± 1.1 | 17 | 18 | 35 |
| N81L | −8.6 ± 2.1 | 3.7 ± 2.1 | 24 | 11 | 35 |
| G83A | −7.4 ± 2.6 | 4.8 ± 2.0 | 22 | 15 | 37 |
| S149A | −4.0 ± 0.5 | 8.2 ± 0.8 | 16 | 23 | 39 |
| N86A | −4.4 ± 1.1 | 7.8 ± 1.1 | 18 | 21 | 39 |
*Each of the binding ΔG was obtained from ABMD as described in the methods section. In silico mutations to non-Alanine residues (e.g. N173L and D234L) are show in italics.