2ARF

Solution structure of the Wilson ATPase N-domain in the presence of ATP

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-separated_NOESY	0.75 mM Wilson ATPase N-domain U-15N, U-13C, 50 mM sodium phosphate, pH 6.0, 5 mM DTT, 50 mM NaN3, 5 mM ATP, 95% H2O, 5% D2O	95% H2O/5% D2O	50 mM sodium phosphate	6.0	ambient	300
2	3D_13C-separated_NOESY	0.75 mM Wilson ATPase N-domain U-15N, U-13C, 50 mM sodium phosphate, pH 6.0, 5 mM DTT, 50 mM NaN3, 5 mM ATP, 95% H2O, 5% D2O	95% H2O/5% D2O	50 mM sodium phosphate	6.0	ambient	300
3	4D_13C/15N-separated_NOESY	0.75 mM Wilson ATPase N-domain U-15N, U-13C, 50 mM sodium phosphate, pH 6.0, 5 mM DTT, 50 mM NaN3, 5 mM ATP, 95% H2O, 5% D2O	95% H2O/5% D2O	50 mM sodium phosphate	6.0	ambient	300

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	DMX	750
2	Bruker	AVANCE	600

NMR Refinement
Method	Details	Software
torsion angle dynamics, simulated annealing		XwinNMR

NMR Ensemble Information
Conformer Selection Criteria	target function
Conformers Calculated Total Number	100
Conformers Submitted Total Number	10
Representative Model	1 (lowest energy)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	collection	XwinNMR	3.5	Bruker Inc
2	data analysis	Felix	2000	Molecular Simulations Inc
3	structure solution	CYANA	1.0	Guntert
4	refinement	CYANA	1.0	Guntert

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.