Table S6.
NOE upper distance limits | 175 |
Angle constraints | 74 |
Residual target function, Å2 | 0.21±0.02 |
Residual NOE violations | |
Total Number >0.1 Å* | 1 |
Maximum Å | 0.23 |
Residual angle violations | |
Total number | 0 |
Atomic pairwise RMSD,# Å | |
Backbone atoms (a.a. 1–11) | 0.22±0.17 |
Heavy atoms (a.a. 1–11) | 0.65±0.15 |
Ramachandran statistics‡ | |
Residues in core regions | 68.8% |
Residues in allowed regions | 25.0% |
Residues in generous regions | 6.3% |
Residues in disallowed regions | 0.0% |
Notes:
Average CYANA1 violations;
evaluated with iCing;4
Procheck-NMR5 analysis (residues 1–11). The final structure calculation included 175 upper limit distance restraints from NOE data (83 intra-residue, 58 short-range, 22 medium-range, and 12 long-range) together with three lower limit distance constraints that were inserted for the disulfide bridge between Cys1 and Cys11. Calculations started from 100 random conformers; the 20 structures with the lowest CYANA target functions were included in the NMR ensemble and additionally inspected with the programs MOLMOL,2 UCSF Chimera,3 and iCing.4 Data are presented as mean ± standard deviation.
Abbreviations: a.a., amino acid; AMC, antimicrobial cyclic peptide; NMR, nuclear magnetic resonance; NOE, Nuclear Overhauser effect; RMSD, root mean square deviation; TFE, 2-2-2 trifluoroethanol-d3; CYANA, Combined Assignment and Dynamics Algorithm for NMR Applications; UCSF, University of California San Francisco.