Table 2.
NMR and refinement statistics for the low-pH glucagon amyloid fibril.
| Glucagon fibril (PDB 6NZN) | |
|---|---|
| NMR distance and dihedral constraints | |
| Distance constraints | |
| Total NOE | 635 × 2 |
| Inter-residue | 635 × 2 |
| Sequential (|i – j| = 1) | 231 × 2 |
| Medium range (2 ≤ |i – j| ≤ 4) | 119 × 2 |
| Long range (|i – j| ≥ 5) | 0 |
| Intermolecular | 285 × 2 |
| Hydrogen bonds | 27 × 2 |
| Total dihedral-angle restraints | |
| ϕ | 54 × 2 |
| ψ | 54 × 2 |
| Structure statistics | |
| Violations (mean ± s.d.) | |
| Distance constraints (Å) | 0.016 ± 0.001 |
| Dihedral-angle constraints (°) | 0.35 ± 0.03 |
| Max. dihedral-angle violation (°) | 3.9 ± 0.7 |
| Max. distance-constraint violation (Å) | 0.39 ± 0.06 |
| Deviations from idealized geometry | |
| Bond lengths (Å) | 0.00 ± 0.00 |
| Bond angles (°) | 0.49 ± 0.01 |
| Impropers (°) | 0.00 ± 0.00 |
| Average pairwise r.m.s. deviation (Å)a | |
| Heavy | 1.67 |
| Backbone | 0.80 |
a
Pairwise r.m.s.d. was calculated among 10 refined structures.