Table 8. Relative Binding Free Energies From the LIE Method and the Combined OSP + TPF Results in Comparison Against Experimental Findingsa.
| mut at 105 |
P1’ = Ile |
P1’ = Pro |
||||
|---|---|---|---|---|---|---|
| mut | LIE | OSP + TPF | exp | LIE | OSP + TPF | exp |
| Arg | 1.4 | –2.5 | √ | –18.5 | –14.7 | |
| Asn | –12.3 | –14.1 | √ | –20.4 | –16.7 | |
| Asp | 34.0 | 1.1 | –47.1 | 6.9 | ||
| Cys | 5.1 | –13.8 | √ | –11.8 | –12.2 | |
| Gln | –8.9 | –5.5 | √ | –30.9 | 11.8 | |
| Glu | 0.0 | 0.0 | √ | 0.0 | 0.0 | |
| His | –1.2 | –15.6 | √ | –23.2 | –2.4 | |
| Lys | –20.6 | –11.4 | –11.0 | 16.1 | ||
| Met | –0.9 | –6.2 | √ | –24.8 | –12.3 | √ |
| Phe | –6.9 | 1.5 | –29.7 | 5.3 | ||
| Ser | –10.5 | –22.2 | √ | –22.9 | 12.9 | |
| Thr | –10.2 | –11.9 | √ | –19.0 | 11.5 | |
| Trp | –15.8 | –79.5 | √ | –30.5 | –18.2 | |
| Tyr | 2.8 | –9.4 | √ | –20.3 | 9.0 | |
| MAD | 13.3 | 22.0 | ||||
| R | 0.41 | –0.06 | ||||
| at 171 | P1′ = Ile | P1′ = Pro | ||||
| mut | LIE | OSP + TPF | exp | LIE | OSP + TPF | exp |
| Arg | 4.8 | –4.1 | √ | –2.2 | 4.9 | √ |
| Asn | –0.1 | –0.8 | –4.4 | –1.8 | √ | |
| Asp | 4.2 | –10.3 | –0.5 | –3.9 | √ | |
| Cys | 8.8 | 5.4 | √ | 7.1 | 0.7 | √ |
| Gln | –0.2 | –8.4 | 2.4 | –2.1 | √ | |
| Glu | –0.3 | –9.9 | √ | –0.1 | –8.2 | √ |
| His | 0.4 | 2.2 | 3.8 | 3.2 | ||
| Lys | –4.1 | –4.5 | √ | –2.8 | 5.3 | |
| Met | 1.6 | 0.8 | –14.2 | 8.3 | ||
| Phe | –0.1 | 3.0 | 4.2 | 6.7 | ||
| Ser | 3.4 | –3.7 | √ | –2.1 | 6.3 | |
| Thr | –6.7 | –6.6 | 4.6 | 0.2 | ||
| Trp | –1.8 | –1.2 | √ | 0.8 | 3.8 | |
| Tyr | –0.2 | 16.8 | 1.6 | –0.3 | ||
| MAD | 5.5 | 6.0 | ||||
| R | 0.15 | –0.31 | ||||
a
All free energies are reported in kJ/mol for both mutation sites and both P1′ amino acids. MAD: mean average deviation between LIE and OSP + TPF approach; r: Pearson correlation coefficient between LIE and OSP + TPF approach.