2FK4

Solution structure of the C-terminal zinc binding domain of the HPV16 E6 oncoprotein

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-separated_NOESY	1.0 mM E6C U-15N; 20 mM TRIS-HCl, 50 mM NaCl, 1mM DTT	90% H2O/10% D2O	50 mM	6.8	ambient	288
2	2D NOESY	1.0 mM E6C, 20 mM TRIS-HCl, 50 mM NaCl, 1mM DTT	90% H2O/10% D2O	50 mM	6.8	ambient	288

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	DRX	600
2	Bruker	DRX	500

NMR Refinement
Method	Details	Software
simulated annealing, protocol refine.inp	NOE distance restraints were split in two sets. One set involved residues that were identified as beeing affected by conformational exchange by relaxation dispersion experiments. These distances were assigned an additional 1A to the upper distance limit. Reported close contacts are due to conformational heterogeneities in the set of NOES. The dynamical properties of this protein have been described in depth in the J. Biomol. NMR reference cited above.	X-PLOR

NMR Ensemble Information
Conformer Selection Criteria	structures with the lowest energy
Conformers Calculated Total Number	20
Conformers Submitted Total Number	10
Representative Model	1 (fewest violations)

Additional NMR Experimental Information
Details	This structure was determined using standard 2D homonuclear and 3D 15N heteronuclear techniques.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	structure solution	X-PLOR	NIH	Brunger
2	data analysis	XEASY	1.0	Bartels
3	processing	XwinNMR	2.6	Bruker
4	refinement	X-PLOR	NIH	Brunger

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.