Table S6.

Structure statistics for AMC NMR ensemble of structures in TFE/H₂O (80/20)

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.