Table 2.
Interactions between mini-chaperone and the N-terminal tag
| Mini-chaperone residue | Closest distance of interaction, Å |
|---|---|
| Residues postulated to interact from sdm (9) | |
| Y199 | 17.3 |
| Y203 | 7.5 |
| F204 | 10.9 |
| L234 | 4.3 |
| L237 | 3.8 |
| L259 | 6.4 |
| V263 | 5.4 |
| V264 | 3.5 |
| Residues not found to interact from sdm (9) | |
| I230 | 3.3 |
| E238 | 3.5 |
| Residues not mutated (9) | |
| A241 | 4.3 |
| E257* | 2.7 |
| A260 | 3.6 |
| T261* | 3.1 |
| N265* | 2.7 |
| R268 | 3.8 |
| I270 | 3.6 |
| V271 | 3.7 |
The table comprises all the residues in the apical domain of GroEL (residues 191–376) that have been found by site-directed mutagenesis (sdm) to appear to be involved in the binding of peptide substrates (9) and all those detected in the crystal structure.
*
Hydrogen-bonded interaction.