Table 1. Hydrogen-Bonding and Electrostatic Interactions for the Tryptophan-Binding Site in the Wild-Type Full Complex PrnA.
| residue 1 | atom 1 | residue 2 | atom 2 | % of the simulation time <3.5 Å | average distance in MD (Å) | distance in crystal structure (Å) |
|---|---|---|---|---|---|---|
| H395 | NE2 | E346 | OE2 | 53 | 3.5 | 2.5 |
| E346 | OE1 | HYP | O | 91 | 3.0 | 3.5 |
| E346 | OE2 | HYP | O | 90 | 3.1 | 5.2 |
| G104 | N | Trp-S | O | 82 | 3.0 | 6.0 |
| G104 | N | Trp-S | carboxylate | 81 | 3.1 | 8.0 |
| Y443 | OH | Trp-S | amino | 95 | 3.1 | 3.1 |
| F454 | O | Trp-S | amino | 69 | 3.4 | 2.8 |
| H395 | NE2 | E346 | carboxylate | n/a | 3.7 | 4.5 |
| E346 | carboxylate | HYP | H | n/a | 2.5 | 4.6 |
| K79 | NZ | HYP | O1 | n/a | 6.7 | 3.2 |
| E450 | carboxylate | Trp-S | N | n/a | 4.2 | 3.8 |
| K57 | NZ | E450 | CD | n/a | 5.8 | 10.3 |