Table 3.
Scanning for affinity enhancing mutations at the E6AP – UbcH7 interface.
| Mutation | ΔΔG°bind | ΔΔG° chain A | ΔΔG° chain B | # neighbors | ΔΔG°h-bond |
|---|---|---|---|---|---|
| D:A92F | −2.7 | 0 | 9 | 13 | 0 |
| D:K9W | −1.8 | 0 | 1.6 | 12 | 0.2 |
| A:D641F | −1.8 | 1.9 | 0 | 16 | 0.1 |
| A:D641Y | −1.7 | 1.2 | 0 | 16 | 0.1 |
| A:D641W | −1.7 | 2.1 | 0 | 16 | 0.1 |
| D:A98W | −1.7 | 0 | −0.1 | 15 | 0 |
| D:N31W | −1.6 | 0 | 3.1 | 14 | 0 |
| D:L33W | −1.5 | 0 | 3.2 | 22 | 0 |
| D:A92Y | −1.5 | 0 | 7.3 | 13 | 0 |
| D:A92W | −1.4 | 0 | 6 | 13 | 0 |
| D:L33F | −1.1 | 0 | 0.2 | 22 | 0 |
| D:A98F | −1.1 | 0 | 1.3 | 15 | 0 |
| D:A98V | −1.1 | 0 | 2 | 15 | 0 |
| D:R6W | −1.1 | 0 | 3.8 | 18 | 0.1 |
| D:A98Y | −1 | 0 | 0.7 | 15 | 0 |
| A:L639Y | −0.9 | 14.4 | 0 | 23 | 0 |
| D:K64L | −0.7 | 0 | −1 | 19 | 0 |
| A:M653W | −0.7 | −5.8 | 0 | 24 | 0 |
| D:N31M | −0.6 | 0 | 1.7 | 14 | 0 |
| A:Q637W | −0.6 | −1.9 | 0 | 20 | 0 |
| D:P62I | −0.6 | 0 | 7.7 | 26 | 0 |
| A:D641V | −0.6 | 0.9 | 0 | 16 | 0.1 |
| D:R6Y | −0.6 | 0 | 5 | 18 | 0.1 |
| A:S660W | −0.6 | 13.8 | 0 | 17 | 0 |
| D:F63W | −0.6 | 0 | 0.2 | 23 | 0 |
| D:N31I | −0.5 | 0 | 0 | 14 | 0 |
| A:T656I | −0.5 | 2.9 | 0 | 20 | 0 |
| D:E60I | −0.5 | 0 | −2.3 | 20 | 0.1 |
| D:P58W | −0.5 | 0 | 4 | 18 | 0 |
| D:A92M | −0.5 | 0 | 5 | 13 | 0 |
| A:T662M | −0.5 | −3.4 | 0 | 15 | 0.1 |
Mutations selected for experimental study are highlighted in orange. Mutations highlighted in gray were not considered for experimental study because were predicted to destabilize the monomer.
a
Predicted change in binding energy (kcal/mol) with the Rosetta Energy function.
b
Predicted change in folding energy (kcal/mol) of the isolated chain.
c
Number of residues in the complex within 10Å of the mutation.
d
Predicted change in hydrogen bond energy across the interface.