2YSM

Solution structure of the second and third PHD domain from Histone-lysine N-methyltransferase 2C (KMT2C/MLL3)

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-separated_NOESY	0.94mM 13C, 15N-labeled protein; 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 0.05mM ZnCl2+1mM IDA; 90% H2O, 10% D2O	90% H2O/10% D2O	120mM	7.0	ambient	293
2	3D_13C-separated_NOESY	0.94mM 13C, 15N-labeled protein; 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 0.05mM ZnCl2+1mM IDA; 90% H2O, 10% D2O	90% H2O/10% D2O	120mM	7.0	ambient	293

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Varian	INOVA	800
2	Varian	INOVA	900

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)

Additional NMR Experimental Information
Details	spectrometer_id 1 for 3D_15N_separaed_NOESY; spectrometer_id 2 for 3D_13C_separaed_NOESY;

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	collection	VNMR	6.1C	Varian
2	processing	NMRPipe	20030801	Delaglio, F.
3	data analysis	NMRView	5.0.4	Johnson, B.A.
4	data analysis	KUJIRA	0.9820	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 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.