5V1E

Suboptimization of a glycine rich peptide allows the combinatorial space exploration for designing novel antimicrobial peptides

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D 1H-1H TOCSY	100 mM dodecylphosphocholine, 5 % D2O, 1 mM peptide, 5 % sodium 2,2-dimethyl-2-silapentane-5-sulfonate, 90 % H2O	90% H2O/10% D2O	0.01	4	1 atm	289	Bruker AVANCE III 500
2	2D 1H-1H NOESY	100 mM dodecylphosphocholine, 5 % D2O, 1 mM peptide, 5 % sodium 2,2-dimethyl-2-silapentane-5-sulfonate, 90 % H2O	90% H2O/10% D2O	0.01	4	1 atm	289	Bruker AVANCE III 500
3	2D 1H-13C HSQC	100 mM dodecylphosphocholine, 5 % D2O, 1 mM peptide, 5 % sodium 2,2-dimethyl-2-silapentane-5-sulfonate, 90 % H2O	90% H2O/10% D2O	0.01	4	1 atm	289	Bruker AVANCE III 500

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	AVANCE III	500

NMR Ensemble Information
Conformer Selection Criteria
Conformers Calculated Total Number
Conformers Submitted Total Number	10

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	data analysis	NMRView		Johnson, One Moon Scientific
2	structure calculation	X-PLOR NIH	2.28	Schwieters, Kuszewski, Tjandra and Clore
3	refinement	X-PLOR NIH	2.28	Schwieters, Kuszewski, Tjandra and Clore
5	processing	NMRDraw		Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
4	processing	NMRPipe		Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
6	geometry optimization	TALOS		Cornilescu, Delaglio and Bax
7	data analysis	QUEEN		Nabuurs, Spronk, Krieger, Maassen, Vriend and Vuister
8	data analysis	MOLMOL		Koradi, Billeter and Wuthrich

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.