Table 3.
NMR structural statistics for trpzip peptides
Parameter | trpzip1 | trpzip2 | trpzip4 |
---|---|---|---|
rmsd from experimental distance restraints (Å) | 0.005 ± 0.001 | 0.004 ± 0.003 | 0.003 ± 0.001 |
(number of restraints) | (77) | (84) | (117) |
rmsd from experimental dihedral restraints (°) | 0.14 ± 0.09 | 0.16 ± 0.09 | 0.33 ± 0.08 |
(number of restraints) | (15) | (15) | (21) |
Maximum distance violation (Å) | 0.03 ± 0.00 | 0.04 ± 0.03 | 0.03 ± 0.01 |
Maximum dihedral violation (°) | 0.5 ± 0.3 | 0.6 ± 0.3 | 1.1 ± 0.3 |
Ramachandran geometry (% in most favored region)* | 71 ± 10 | 85 ± 10 | 82 ± 4 |
Backbone (N,Cα,C) rmsd from mean coordinates (Å) | 0.40 ± 0.07 | 0.41 ± 0.09 | 0.29 ± 0.06 |
(residues used for rmsd calculation) | (2–11) | (2–11) | (43–54) |
Resonance assignments and coupling constants for trpzip1, trpzip2, and trpzip4 are available in Tables 4–6.
Ramachandran geometry was evaluated by using the program procheck (31); remainder of the residues for all structures are in the allowed regions of φ, ψ space, with none in the disallowed or generously allowed regions.