Table S5.

Structure statistics for the AMC NMR conformers in H₂O/D₂O (90/10)

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.