Table 1.
Side Chain Dihedral Angle Values for Interface Residues from the Thr Zipper Crystal Structure (Χ 1 xtal), the HS Prediction (Χ 1 pred), and from MD Simulations (Χ 1 MD)
| Residue | Χ 1 xtal (°) | Χ 1 pred (°) | Χ 1 MD (°) | ||
|---|---|---|---|---|---|
| 60° (%) | 180° (%) | 300° (%) | |||
| Thr 17 | 281 | 276 | 1 | 53 | 46 |
| Ser 92 | 67 | 66 | 92.1 | 1.5 | 4.4 |
| Ile 100 | 292 | 295 | 0 | 0 | 99.5 |
| Thr 102 | 52 | 69 | 98.2 | 0 | 0 |
| Thr 104 | 67 | 301 | 2.0 | 29.3 | 67.3 |
| Thr 119 | 67 | 303 | 2.7 | 60.4 | 32.5 |
| Thr 121 | 302 | 301 | 3.8 | 0 | 94.6 |
| Thr 123 | 66 | 71 | 98.3 | 0 | 0 |
Each value is averaged over all four monomers. For Χ 1 MD, we report the fraction of the simulation spent in each rotameric bin with width 30° centered around 60°, 180°, and 300°. See the Supporting Information for the Χ 1 side chain dihedral angle data for each individual monomer.