Table 1.
Protein | |
NMR distance and dihedral constraints | |
Total NOE | 2,591 |
Intraresidue | 312 |
Interresidue | |
Sequential (|i – j| = 1) | 573 |
Medium range (|i – j| < 4) | 561 |
Long range (|i – j| > 5) | 27 |
Intermolecular | 659 |
Ambiguous NOEs restraints (i.e., either intra- or intermolecular couplings) | 382 |
Hydrogen bonds | 104 |
NMR total dihedral angle restraints | 164 |
ϕ | 82 |
ψ | 82 |
Structure statistics | |
Violations (mean and SD) | |
Distance constraints (Å) | 0.004 ± 0.000 |
Dihedral angle constraints (°) | 0.099 ± 0.017 |
Deviations from idealized geometry | |
Bond lengths (Å) | 0.001 ± 0.000 |
Bond angles (°) | 0.331 ± 0.004 |
Impropers (°) | 0.154 ± 0.010 |
Average pairwise rmsd* (Å) | |
Well-ordered residues (Myo 10 anti-CC883–925) | |
Heavy | 1.272 |
Backbone | 0.67 |
*Pairwise rmsd was calculated among 20 refined structures.