1YQA

Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-separated_NOESY	1mM GII-L U-15N,13C; 100mM phosphate buffer; 1mM EDTA; 1-2mM DTT	90% H2O/10% D2O	100mM phosphate	7.0	1 atm	288
2	3D_13C-separated_NOESY	1mM GII-L U-15N,13C; 100mM phosphate buffer; 1mM EDTA; 1-2mM DTT	90% H2O/10% D2O	100mM phosphate	7.0	1 atm	288

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

NMR Refinement
Method	Details	Software
see journal citation		XwinNMR

NMR Ensemble Information
Conformer Selection Criteria	structures with the lowest energy
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
2	processing	Azara	2.7
3	data analysis	Analysis	1.0	Boucher, W. & Stevens, T.J.
4	structure solution	ARIA	1.1.2
5	structure solution	CNS	1.1
6	refinement	CNS	1.1

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.