1R4G

Solution structure of the Sendai virus protein X C-subdomain

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-separated_NOESY	1.2-1.5mM 15N/13C Protein X, 50mM potassium phosphate buffer, 0.5M NaCl, 10mM DTT, antiprotease cocktail	90% H2O/10% D2O	0.5M NaCl	6	ambient	298
2	3D_13C-separated_NOESY	1.2-1.5mM 15N/13C Protein X, 50mM potassium phosphate buffer, 0.5M NaCl, 10mM DTT, antiprotease cocktail	90% H2O/10% D2O	0.5M NaCl	6	ambient	298
3	3D HNCO type experiments	1mM 15N/13C Protein X, 5% C12/E6/hexanol, 50mM potassium phosphate buffer, 0.5M NaCl, 10mM DTT	90% H2O/10% D2O

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Varian	INOVA	800
2	Varian	INOVA	600

NMR Refinement
Method	Details	Software
simulated annealing		Discover

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

Additional NMR Experimental Information
Details	Sample 2 was used to measure the three different types of residual dipolar couplings used for structure refinement.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	structure solution	Discover	2.98	Accelrys, Inc.
2	refinement	SCULPTOR		hus & blackledge

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.