1ZNT

18 NMR structures of AcAMP2-Like Peptide with non Natural Fluoroaromatic Residue (AcAMP2F18Pff/Y20Pff) complex with N,N,N-triacetylchitotriose

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D TOCSY	1mM AcAMP2F18Pff/Y20Pff, 12mM chitotriose, 20mM Phosphate buffer; 90% H2O, 10% D2O	90% H2O/10% D2O	100mM NaCl	5.6	ambient	298
2	2D NOESY	1mM AcAMP2F18Pff/Y20Pff, 12mM chitotriose, 20mM Phosphate buffer; 90% H2O, 10% D2O	90% H2O/10% D2O	100mM NaCl	5.6	ambient	298

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	AVANCE	800

NMR Refinement
Method	Details	Software
The structures are based on a total 314 cross peaks, 248 NOE-derived distance restraints, and finally 208 distance constraints and 18 come from cys-cys disulfide were used in the final round of calculation		XwinNMR

NMR Ensemble Information
Conformer Selection Criteria	Fewest restraint violation, secondary lowest energy
Conformers Calculated Total Number	30
Conformers Submitted Total Number	18
Representative Model	1 (fewest violations)

Additional NMR Experimental Information
Details	This structure was determined using standard 2D homonuclear techniques which are NOESY at tm=300 and TOCSY at tm=50 and 70 ms

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	collection	XwinNMR	3.2	Bruker
2	data analysis	XEASY	1.3.13	Wuthrich
3	structure solution	DYANA	1.5	Guentert
4	refinement	Amber	5.0	Kollman

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.