Table 2 NMR and refinement statistics for ribbon BuIA
From: Structure of α-conotoxin BuIA: influences of disulfide connectivity on structural dynamics
NMR distance & dihedral constraints | |
|---|---|
Distance constraints | |
Total NOE | 96 |
Sequential (|i-j| = 1) | 50 |
Medium-range (|i-j| < 4) | 18 |
Long-range (|i-j| > 5) | 12 |
Intra-residual | 16 |
Total dihedral angle restraints | |
Phi | 5 |
chi1 | 1 |
Structure statistics | |
Violations (mean and s.d.) | |
Distance constraints (Å) | 0.05 ± 0.003 |
Dihedral angle constraints (°) | 0.61 ± 0.2 |
Max. dihedral angle violation (°) | 3 |
Max. distance constraint violation (Å) | 0.3 |
Deviations from idealized geometry | |
Bond length (Å) | 0.004 ± 0.00025 |
Bond angles (°) | 0.53 ± 0.02 |
Impropers (°) | 0.35 ± 0.02 |
Average pairwise r.m.s.d.** (Å) | |
Backbone | 0.36 ± 0.12 |
Heavy atoms | 1.1 ± 0.49 |
Ramachandran statistics (%) | |
Most favoured | 55.6 |
Additionally allowed | 44.4 |
Disallowed | 0.0 |