Table 2.
Details of the intermolecular interactions between Mtb β1 domain residues and Mtb CarD. See also Figure S4.
| RNAP β1 | CarD | Distance (Å) | Interaction type |
|---|---|---|---|
| Thr138 | Asn52 | 2.8 | H-bond and van der Waals |
| Pro49 | 3.5 | van der Waals | |
| Val56 | 3.9 | van der Waals | |
| Gly139 | Pro49 | 3.5 | van der Waals |
| Arg47 | 3.5 | van der Waals | |
| Glu140 | Arg47 | 3.4 | van der Waals |
| Val48 | 3.8 | van der Waals | |
| Tyr11 | 2.4 | H-bond and van der Waals | |
| Val56 | 3.6 | van der Waals | |
| Ile141 | Arg47 | 2.8 | H-bond and van der Waals |
| Thr45 | 3.4 | van der Waals | |
| Val46 | 3.2 | van der Waals, hydrophobic | |
| Arg25 | 3.9 | van der Waals | |
| Lys142 | Thr45 | 3.3 | van der Waals |
| His14 | 2.9 | H-bond and van der Waals | |
| Ser143 | Thr45 | 2.8 | H-bond and van der Waals |
| Leu44 | 3.6 | van der Waals | |
| Gln144 | Leu44 | 3.8 | van der Waals |
| Asp43 | 3.8 | van der Waals | |
| Gly42 | 3.0 | H-bond and van der Waals | |
| Glu404 | His14 | 3.8 | van der Waals |
| His13 | 3.4 | van der Waals | |
| Ala405 | His13 | 3.7 | van der Waals |
| His14 | 3.7 | van der Waals | |
| Thr407 | His14 | 3.3 | van der Waals |