Experiment: 2JS3

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D 1H-15N HSQC	0.5 mM [U-100% 13C; U-100% 15N] protein	90% H2O/10% D2O	300	7.0	ambient	298
2	3D HNCACB	0.5 mM [U-100% 13C; U-100% 15N] protein	90% H2O/10% D2O	300	7.0	ambient	298
3	3D CBCA(CO)NH	0.5 mM [U-100% 13C; U-100% 15N] protein	90% H2O/10% D2O	300	7.0	ambient	298
4	3D HNCO	0.5 mM [U-100% 13C; U-100% 15N] protein	90% H2O/10% D2O	300	7.0	ambient	298
5	3D simNOESY	0.5 mM [U-100% 13C; U-100% 15N] protein	90% H2O/10% D2O	300	7.0	ambient	298
6	3D filtered NOESY	0.5 mM [U-50% 13C; U-50% 15N] protein	90% H2O/10% D2O	300	7.0	ambient	298
7	3D HCCH-COSY	0.5 mM [U-100% 13C; U-100% 15N] protein	90% H2O/10% D2O	300	7.0	ambient	298

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Varian	INOVA	750
2	Varian	INOVA	600
3	Bruker	DRX	800

NMR Refinement
Method	Details	Software
simulated annealing		AutoAssign

NMR Ensemble Information
Conformer Selection Criteria	structures with the least restraint violations
Conformers Calculated Total Number	100
Conformers Submitted Total Number	20
Representative Model	1 (lowest energy)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	chemical shift assignment	AutoAssign		Zimmerman, Moseley, Kulikowski and Montelione
2	processing	NMRPipe		Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
3	collection	VNMR		Varian
4	refinement	CYANA		Guntert, Mumenthaler and Wuthrich
5	refinement	CNS		Brunger, Adams, Clore, Gros, Nilges and Read
6	structure solution	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.