1NJQ

NMR structure of the single QALGGH zinc finger domain from Arabidopsis thaliana SUPERMAN protein

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D TOCSY	2mM peptide,2.2mM ZnCl2, 90%H2O;10%D2O	90% H2O/10% D2O		6.4		301
2	2D NOESY	2mM peptide,2.2mM ZnCl2, 90%H2O;10%D2O	90% H2O/10% D2O		6.4		301
3	DQF-COSY	2mM peptide,2.2mM ZnCl2, 90%H2O;10%D2O	90% H2O/10% D2O		6.4		301
4	2D TOCSY	2mM peptide,2.2mM ZnCl2;100%D2O	100% D2O		6.4		301
5	2D NOESY	2mM peptide,2.2mM ZnCl2;100%D2O	100% D2O		6.4		301
6	DQF-COSY	2mM peptide,2.2mM ZnCl2;100%D2O	100% D2O		6.4		301

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

NMR Refinement
Method	Details	Software
torsion angle dynamics and unrestrained energy minimization	Torsion angle dynamics structure calculations contained 338 upper distance constraints and 123 dihedral angle constraints, no hydrogen bonding constraints were used.	VNMR

NMR Ensemble Information
Conformer Selection Criteria	target function
Conformers Calculated Total Number	100
Conformers Submitted Total Number	20
Representative Model	1 (fewest violations)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	processing	VNMR	6.1B	Varian team
2	processing	PROSA	3.7	Guentert, P.
3	data analysis	XEASY	1.3.12	Bartels, C.
4	structure solution	DYANA	1.5	Guentert, P.
5	refinement	OPAL	2.2	Guentert, P.

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.