Table 6.
RD values calculated for the ABCD complex, for AB and CD subcomplexes, for a single chain and for individual domains (CH1, CH2) of dystrophin (1DXX), as well as for selected secondary structural folds. “FOD DOMAIN” represents fragments contributed by two chains (A,B) which form a coherent domain with its own FOD-compliant hydrophobic core.
| Dystrophin1DXX | ||
|---|---|---|
| Chain Fragment | RD | |
| Complex–Tetramer | ABCD | 0.815 |
| Complex–Dimer | AB/CD | 0.754/0.752 |
| Chain | A/C | 0.839/0.758 |
| Chain | B/D | 0.761/0.762 |
| Domain 1 CH1 | 9–121 | 0.458 |
| CH1 Modified | 9–118 | 0.462 |
| Helix K18N | 13–32 | 0.424 |
| Actin binding | 17–26 | 0.341 |
| Loop | 33–46 | 0.466 |
| Helix L54R | 47–59 | 0.596 |
| Loop | 60–68 | 0.562 |
| Helix | 69–87 | 0.536 |
| Loop | 88–94 | 0.212 |
| Helix-Actin binding | 95–101 | 0.299 |
| Helix-Actin binding | 103–119 | 0.343 |
| Domain 2 CH2 Modified |
122–246 135–241 |
0.510 0.336 |
| 134–246 | 0.432 | |
| Helix | 135–149 | 0.309 |
| Loop | 150–159 | 0.215 |
| HelixD165V | 160–164 | 0.358 |
| Helix D165V, A168D, L172H | 166–177 | 0.321 |
| Helix | 178–181 | 0.299 |
| Helix | 182–188 | 0.195 |
| Helix | 191–206 | 0.455 |
| Loop | 207–213 | 0.492 |
| Helix | 214–219 | 0.134 |
| Loop | 220–223 | 0.865 |
| Helix Y231N | 224–237 | 0.325 |
| β | 242–246 | 0.224 |
| Fod Domain | ||
| A (Helix119-134 + A (β242–246)) + B (Helix119–134 + B (β242–246)) | 0.239 | |
| C (Helix119-134 + C (β42–246)) + D (Helix119–134 + D (β242–246)) | 0.245 |