Table 1 NMR and refinement statistics for the final 20 ensemble structures of Pvfp-5β.
From: Solution structure of recombinant Pvfp-5β reveals insights into mussel adhesion
NMR distance and dihedral constraints | |
Distance constraints | |
Total NOE | 1696 |
Intra-residue | 544 |
Inter-residue | 1152 |
Sequential (|i – j| = 1) | 621 |
Medium-range (|i – j| < 4) | 164 |
Long-range (|i – j| > 5) | 367 |
Intermolecular | 0 |
Hydrogen bonds | 9 |
Total dihedral angle restraints | 112 |
ϕ | 56 |
ψ | 56 |
Structure statistics | |
Violations (mean and s.d.) | |
Distance constraints >1 Å | 1 |
Dihedral angle constraints >5° | 0 |
Deviations from idealized geometry | |
Bond lengths (Å) | 0,004 Å |
Bond angles (°) | 0,6 ° |
Impropers (°) | n/a |
Average pairwise r.m.s. deviation (Å) | 20 structures |
Backbone of structured regionsa | 1.09 ± 0.29 Å |
Heavy of structured regions | 1.52 ± 0.37 Å |
Backbone of all residues | 1.42 ± 0.50 Å |
Heavy of all residues | 1.71 ± 0.49 Å |
