Table 1.
Number of hydrogen bonds and heavy-atom contacts between each drug and the protein (cut-off 4 Å). Average and standard deviations for each system were obtained over the whole triplicate simulation sampling (300 ns). The number of contacts using a larger cut-off distance of 5 Å is shown in Table S1, and follow the same trend.
| a) drug positively and E65 negatively charged | |||||
|---|---|---|---|---|---|
| Number of hydrogen bonds |
Number of contacts |
||||
| BDQ | TBAJ-876 | BDQ | TBAJ-876 | ||
| Lagging | 1.4 ± 0.6 | 1.4 ± 0.5 | Lagging | 26.3 ± 4.2 | 32.2 ± 4.0 |
| Leading | 1.2 ± 0.5 | 1.1 ± 0.4 | Leading | 31.4 ± 4.9 | 35.4 ± 4.7 |
| c-ring | 1.2 ± 0.5 | 1.3 ± 0.5 | c-ring | 22.1 ± 3.5 | 23.0 ± 3.3 |
| b) drug and E65 neutral | |||||
| Number of hydrogen bonds | Number of contacts | ||||
| BDQ | TBAJ-876 | BDQ | TBAJ-876 | ||
| Lagging | 1.0 ± 0.2 | 0.9 ± 0.3 | Lagging | 25.0 ± 3.8 | 28.1 ± 3.9 |
| Leading | 0.9 ± 0.3 | 1.0 ± 0.3 | Leading | 32.1 ± 3.8 | 32.7 ± 5.5 |
| c-ring | 0.8 ± 0.4 | 0.8 ± 0.4 | c-ring | 19.2 ± 3.4 | 19.8 ± 3.9 |