Table S5.
NOE upper distance limits | 125 |
Angle constraints | 71 |
Residual target function, Å2 | 0.17±0.02 |
Residual NOE violations | |
Total Number >0.1 Å* | 1 |
Maximum Å | 0.24 |
Residual angle violations | |
Total number | 0 |
Atomic pairwise RMSD,# Å | |
Backbone atoms (a.a. 1–11) | 0.92±0.30 |
Heavy atoms (a.a. 1–11) | 1.52±0.45 |
Ramachandran statistics‡ | |
Residues in core regions | 40.6% |
Residues in allowed regions | 57.5% |
Residues in generous regions | 1.9% |
Residues in disallowed regions | 0.0% |
Notes:
Average CYANA1 violations;
evaluated with iCing;2
Procheck-NMR5 analysis (residues 1–11). Structures were generated from 125 NOE upper distance limits (52 intra-residue, 62 sequential, 8 medium-range, and 3 long-range); three upper and three lower distance limits were enforced for the disulfide bridge. Structure calculations initiated from 100 random conformers; in the end, the 20 structures with the lowest CYANA1 target functions and showing largest agreement with the experimental restraints were considered representative and, thus, incorporated in the NMR ensemble. These structures were additionally analyzed with the molecular graphic programs MOLMOL4 and UCSF Chimera5 and validated with iCing.2 Data are presented as mean ± standard deviation.
Abbreviations: a.a., amino acid; AMC, antimicrobial cyclic peptide; D2O, deuterium oxide; NMR, nuclear magnetic resonance; NOE, Nuclear Overhauser effect; RMSD, root mean square deviation; CYANA, Combined Assignment and Dynamics Algorithm for NMR Applications; UCSF, University of California San Francisco.