2EL5

Solution structure of the 18th zf-C2H2 domain from human Zinc finger protein 268

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_13C-separated_NOESY	1.08mM 13C, 15N-labeled protein; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 50uM ZnCl2; 1mM IDA; 90% H2O, 10% D2O	90% H2O/10% D2O	120mM	7.0	ambient	298
2	3D_15N-separated_NOESY	1.08mM 13C, 15N-labeled protein; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 50uM ZnCl2; 1mM IDA; 90% H2O, 10% D2O	90% H2O/10% D2O	120mM	7.0	ambient	298

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

NMR Refinement
Method	Details	Software
torsion angle dynamics		VNMR

NMR Ensemble Information
Conformer Selection Criteria	structures with the least restraint violations, structures with the lowest energy, target function
Conformers Calculated Total Number	100
Conformers Submitted Total Number	20
Representative Model	1 (lowest energy)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	collection	VNMR	6.1C	Varian
2	processing	NMRPipe	20031121	Delaglio, F.
3	data analysis	NMRView	5.0.4	Johnson, B.A.
4	data analysis	KUJIRA	0.9817	Kobayashi, N.
5	structure solution	CYANA	2.0.17	Guntert, P.
6	refinement	CYANA	2.0.17	Guntert, 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.