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| Cα atom of the BC-CT residue and the closest Cα atom in the B-chain α-helix | Distances in the crystal structure 2G4M [Å] | Average distances from MD simulations where insulin is in the closed state [Å] |
|---|---|---|
| F24(Cα)–L15(Cα) | 6.7 | 7.0±0.4 |
| F25(Cα)–L15(Cα) | 8.5 | 9.4±0.5 |
| Y26(Cα)–V12(Cα) | 7.2 | 8.1±0.9 |
| T27(Cα)–V12(Cα) | 10.2 | 10.5±1.1 |
| P28(Cα)–G8(Cα) | 9.1 | 9.8±2.1 |
| L29(Cα)–G8(Cα) | 12.2 | 12.3±2.4 |
| T30(Cα)–G8(Cα) | 14.5 | 13.8±2.7 |
