2MWP

Solution structure of 53BP1 tandem Tudor domains in complex with a p53K382me2 peptide

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D 1H-15N HSQC	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	90% H2O/10% D2O	25	7.5	ambient	298
2	2D 1H-15N HSQC	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	90% H2O/10% D2O	25	7.5	ambient	298
3	2D 1H-13C HSQC aliphatic	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	100% D2O	25	7.5	ambient	298
4	2D 1H-13C HSQC aromatic	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	100% D2O	25	7.5	ambient	298
5	2D 1H-13C HSQC	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM 53BP1-Tudor, 0.5 mM [U-100% 13C; U-100% 15N] p53Kc382me2	100% D2O	25	7.5	ambient	298
6	2D 1H-13C HSQC	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM p53K382me2	100% D2O	25	7.5	ambient	298
7	2D 1H-13C HSQC	25 mM sodium phosphate, 1.5 mM sodium azide, 0.5 mM [U-100% 13C; U-100% 15N] p53Kc382me2	100% D2O	25	7.5	ambient	298
8	3D HNCA	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	90% H2O/10% D2O	25	7.5	ambient	298
9	3D HNCACB	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	90% H2O/10% D2O	25	7.5	ambient	298
10	3D CBCA(CO)NH	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	90% H2O/10% D2O	25	7.5	ambient	298
11	3D HNCO	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	90% H2O/10% D2O	25	7.5	ambient	298
12	3D HN(CA)CO	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	90% H2O/10% D2O	25	7.5	ambient	298
13	3D HBHA(CO)NH	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	90% H2O/10% D2O	25	7.5	ambient	298
14	3D C(CO)NH	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	90% H2O/10% D2O	25	7.5	ambient	298
15	3D H(CCO)NH	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	90% H2O/10% D2O	25	7.5	ambient	298
16	3D HCCH-TOCSY	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	100% D2O	25	7.5	ambient	298
17	3D 1H-15N TOCSY	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	90% H2O/10% D2O	25	7.5	ambient	298
18	2D (HB)CB(CGCD)HD	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	100% D2O	25	7.5	ambient	298
19	3D 1H-15N NOESY	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	90% H2O/10% D2O	25	7.5	ambient	298
20	3D 1H-13C NOESY aliphatic	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	90% H2O/10% D2O	25	7.5	ambient	298
21	2D 1H-13C HSQC aromatic	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	90% H2O/10% D2O	25	7.5	ambient	298
22	3D Filtered(13C/15N)-Edited (13C)	25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2	100% D2O	25	7.5	ambient	298

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	Avance III	700

NMR Refinement
Method	Details	Software
simulated annealing		xwinnmr

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)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	collection	xwinnmr		Bruker Biospin
2	processing	NMRPipe		Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
3	data analysis	NMRPipe		Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
4	data analysis	NMRView		Johnson, One Moon Scientific
5	chemical shift assignment	SANE		Duggan, Legge, Dyson & Wright
6	data analysis	TALOS		Cornilescu, Delaglio and Bax
7	chemical shift assignment	CYANA		Guntert, Mumenthaler and Wuthrich
8	structure solution	CYANA		Guntert, Mumenthaler and Wuthrich
9	structure solution	AMBER		Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, and Kollman
10	refinement	AMBER		Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, and Kollman
11	data analysis	ProcheckNMR		Laskowski and MacArthur

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.

Prepare Data

Validate Data

Deposit Data

Help and Resources

2MWP

Solution structure of 53BP1 tandem Tudor domains in complex with a p53K382me2 peptide