2JO0

The solution structure of the monomeric species of the C terminal domain of the CA protein of HIV-1

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D NOESY	1 mM [U-15N] protein, 100 mM potassium phosphate, 0.00001 mM TSP	90% H2O/10% D2O	0.1	7	ambient	293
2	2D TOCSY	1 mM [U-15N] protein, 100 mM potassium phosphate, 0.00001 mM TSP	90% H2O/10% D2O	0.1	7	ambient	293
3	2D 1H-15N HSQC	1 mM [U-15N] protein, 100 mM potassium phosphate, 0.00001 mM TSP	90% H2O/10% D2O	0.1	7	ambient	293
4	3D 1H-15N NOESY	1 mM [U-15N] protein, 100 mM potassium phosphate, 0.00001 mM TSP	90% H2O/10% D2O	0.1	7	ambient	293
5	3D 1H-15N TOCSY	1 mM [U-15N] protein, 100 mM potassium phosphate, 0.00001 mM TSP	90% H2O/10% D2O	0.1	7	ambient	293

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	DRX	500

NMR Refinement
Method	Details	Software
molecular dynamics		CYANA

NMR Ensemble Information
Conformer Selection Criteria	structures with the lowest energy
Conformers Calculated Total Number	50
Conformers Submitted Total Number	30
Representative Model	1 (lowest energy)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	structure solution	CYANA	2.1	P Guntert, C Mumenthaler and K Wuthrich
2	chemical shift assignment	Sparky	3.0	T Goddard
3	peak picking	Sparky	3.0	T Goddard
4	refinement	Amber	8	DA Case, TA Darden, TE Cheatham, III, CL Simmerling, J Wang, RE Duke,
5	collection	XwinNMR		Bruker Biospin

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.