1S6N

NMR Structure of Domain III of the West Nile Virus Envelope Protein, Strain 385-99

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-SEPARATED_NOESY	0.7MM WND3 PROTEIN, 50MM K2HPO4, 100MM NACL, 10MM NAN3, 0.1MM EDTA		50mM PHOSPHATE, 100mM NACL, 10mM NAN3	6.8	AMBIENT	298
2	3D_ 13C-SEPARATED_NOESY	0.7MM WND3 PROTEIN, 50MM K2HPO4, 100MM NACL, 10MM NAN3, 0.1MM EDTA		50mM PHOSPHATE, 100mM NACL, 10mM NAN3	6.8	AMBIENT	298

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Varian	UNITYPLUS	750
2	Varian	UNITYPLUS	600

NMR Ensemble Information
Conformer Selection Criteria	structures with the least restraint violations
Conformers Calculated Total Number	100
Conformers Submitted Total Number	15
Representative Model	1 (n/a)

Additional NMR Experimental Information
Details	CHEMICAL SHIFTS WERE DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	refinement	AMBER	6	PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON, SEIBEL,SINGH,WEINER,KOLLMAN
2	structure solution	VNMR	6.1B
3	structure solution	SANE	1.0
4	structure solution	FELIX	98
5	structure solution	AMBER	6

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.