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. 2001 May 1;98(10):5578–5583. doi: 10.1073/pnas.091100898

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. 

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