2KWJ

Solution structures of the double PHD fingers of human transcriptional protein DPF3 bound to a histone peptide containing acetylation at lysine 14

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D 1H-15N NOESY	100 mM potassium phosphate, 2 mM DTT	100% D2O		6.5	ambient	298
2	3D 1H-13C NOESY	100 mM potassium phosphate, 2 mM DTT	100% D2O		6.5	ambient	298
3	3D_13C-Edited_13C/15N-filtered NOEST	100 mM potassium phosphate, 2 mM DTT	100% D2O		6.5	ambient	298
4	3D HNCACB	100 mM potassium phosphate, 2 mM DTT	100% D2O		6.5	ambient	298
5	3D HN(COCA)CB	100 mM potassium phosphate, 2 mM DTT	100% D2O		6.5	ambient	298

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	AVANCE	900
2	Bruker	AVANCE	800
3	Bruker	AVANCE	600
4	Bruker	DRX	500

NMR Refinement
Method	Details	Software
DGSA-distance geometry simulated annealing, torsion angle dynamics		ARIA

NMR Ensemble Information
Conformer Selection Criteria	structures with the lowest energy
Conformers Calculated Total Number	200
Conformers Submitted Total Number	20
Representative Model	1 (lowest energy)

Additional NMR Experimental Information
Details	The structures were determined using triple-resonance NMR spectroscopy

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	refinement	ARIA	2.2	Linge, O'Donoghue and Nilges
2	processing	NMRPipe	2.3	Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
3	data analysis	NMRView	5.04	Johnson, One Moon Scientific
4	structure solution	CNS	1.2	Brunger, Adams, Clore, Gros, Nilges and Read

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.