Table 1.
NMR Structural Statistics.
| Blade II in interface | Blade IV in interface | |
|---|---|---|
| PDB accession code | 6CM1 | 6CLZ |
| RMSD deviations a | ||
| Avg. RMSD (Å) for backbone atoms | 1.18 ± 0.28 | 1.27 ± 0.26 |
| Distance restraints | ||
| Lipid - protein methyl PREs, explicit | 3*7 | 3*4 |
| Lipid - amide shifts, broadenings, ambiguous | 11 | 3 |
| Restraint violations > 10% | ||
| Protein-lipid PREs | V380–10doxyl: 15±3%, 3.1±0.6A |
0 |
| Protein-lipid ambiguous residues | 0 | 0 |
| Structural quality | ||
| Procheck G-factor (all dihedrals) | −0.55 | −0.53 |
| Molprobity score b | 1.11 | 1.10 |
| Most favored Ramachadran plot residues (%)c | 84.7 | 85.3 |
| Allowed Ramachandran plot residues (%)c | 11.0 | 12.3 |
| Buried surface area (Å2)d | ||
| 1225 ± 90 | 1423 ± 68 | |
| CH3 groups with PREs from 5-doxyl DPCCe | ||
| 357δ, 380γ, 389γ 395δ, 442γ |
473γ, 493γ | |
| CH3 groups with PREs from 10-doxyl DPCCe | ||
| 357δ, 380γ, 389γ | 473γ, 493γ | |
| Amide groups perturbed by nanodiscs | ||
| 330 f, 342, 377, 379, 386, 387 f, 396, 422, 428 | 459, 489, 499 | |
a
calculated from the ensemble of 15 lowest energy structures
b
Combines the clash score, rotamers, and Ramachandran evaluation into a single score
c
From Procheck-NMR
d
Average buried surface area from the ensemble of 15 structures
e
Leu methyl groups are denoted δ and Val methyl groups γ
f
amide NMR peak undergoes both a shift and broadening