1BT7

THE SOLUTION NMR STRUCTURE OF THE N-TERMINAL PROTEASE DOMAIN OF THE HEPATITIS C VIRUS (HCV) NS3-PROTEIN, FROM BK STRAIN, 20 STRUCTURES

SOLUTION NMR

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	AMX	500
2	Varian	DMX	600
3	Varian	UNITYPLUS	800
4	Varian	DMX	800

NMR Refinement
Method	Details	Software
DG-SA HYBRID	REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. R.M.S. DEVIATIONS FROM EXPERIMENTAL RESTRAINTS: DISTANCE (ANGSTROMS) : 0.076 +/- 0.003 DIHEDRAL (DEGREES) : 1.331 +/- 0.148 IDEALIZED GEOMETRY BONDS (ANGSTROMS): 0.005 +/- 0.0006 ANGLES (DEGREES) : 0.761 +/- 0.032 IMPROPERS (DEGREES) : 0.543 +/- 0.017	X-PLOR

NMR Ensemble Information
Conformer Selection Criteria	LEAST RESTRAINT VIOLATIONS/MINIMUM ENERGY
Conformers Calculated Total Number	60
Conformers Submitted Total Number	20

Additional NMR Experimental Information
Details	THE STRUCTURE WAS DETERMINED USING N15, N15/C13, N15/C13/2H, AND 15N SELECTIVELY LABELED SAMPLES, WITH TRIPLE RESONANCE EXPERIMENTS

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	refinement	X-PLOR	3.851	BRUNGER
2	structure solution	NMRPipe
3	structure solution	NMRView

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.