Table 1.
Structural statistics for the NMR conformers of τC14
| Parameter | Value |
|---|---|
| Number of assigned NOE cross-peaks | 2500 |
| Number of non-redundant NOE upper-distance limits | 1891 |
| Number of scalar coupling constants (Hα–Hβ)a | 64 |
| Number of dihedral-angle restraints | 241 |
| Intra-protein AMBER energy (kcal/mol) | −5388 ± 321 |
| Maximum NOE-restraint violations (Å) | 0.09 ± 0.00 |
| Maximum dihedral-angle restraint violations (°) | 2.0 ± 0.5 |
| r.m.s.d. to the mean for N, Cα and C′ (Å)b | 0.55 ± 0.14 |
| r.m.s.d. to the mean for all heavy atoms (Å)b | 0.99 ± 0.11 |
| Ramachandran plot appearancec | |
| Most favored regions (%) | 90.2 |
| Additionally allowed regions (%) | 9.5 |
| Generously allowed regions (%) | 0.3 |
| Disallowed regions (%) | 0.0 |
aStereo-specific resonance assignments were obtained for 49 pairs of CβH2, one pair of CγH2 and two pairs of CδH2 protons. bFor residues 509–609. cFrom PROCHECK-NMR (34).