Table 2. Structural statistics for myosin VI1050–1131.
| Protein | |
|---|---|
| NMR distance and dihedral constraints | |
| Distance constraints | |
| Total NOE | 1846 |
| Intraresidue | 483 |
| Inter-residue | |
| Sequential (|i – j| = 1) | 537 |
| Medium range (2 ≤ |i – j| ≤ 4) | 566 |
| Long range (|i – j| ≥ 5) | 260 |
| Intermolecular | |
| Hydrogen bonds | 42 |
| Total dihedral-angle restraints | |
| ϕ | 51 |
| ψ | 51 |
| Structure statistics | |
| Violations (mean ± s.d.) | |
| Distance constraints (Å) | 0.0077±0.0010 |
| Dihedral-angle constraints (°) | 0.12±0.041 |
| Max. dihedral-angle violation (°) | 1.13 |
| Max. distance-constraint violation (Å) | 0.22 |
| Deviations from idealized geometry | |
| Bond lengths (Å) | 0.0016±0.000073 |
| Bond angles (°) | 0.39±0.0042 |
| Impropers (°) | 0.23±0.0067 |
| Average pairwise r.m.s. deviation (Å)a | |
| Heavy | 0.68±0.06 |
| Backbone | 0.18±0.05 |
a
Values were calculated for residues T1054-R1068 and Y1084-S1126 from the twenty lowest energy structures.