2K1L

NMR structures of dimeric transmembrane domain of the receptor tyrosine kinase EphA1 in lipid bicelles at pH 6.3

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D 1H-15N HSQC	3 mM 15N, 13C EphA1_TM 15N, 96 mM 2H DHPC, 24 mM 2H DMPC, 1.5 mM NaN3, 1 mM EDTA, 10 mM phosphate buffer	95% H2O/5% D2O		6.3		313
2	2D 1H-13C HSQC	3 mM 15N, 13C EphA1_TM 15N, 13C, 96 mM 2H DHPC, 24 mM 2H DMPC, 1.5 mM NaN3, 1 mM EDTA, 10 mM phosphate buffer	100% D2O		6.3		313
3	3D 1H-15N NOESY	3 mM 15N, 13C EphA1_TM 15N, 96 mM 2H DHPC, 24 mM 2H DMPC, 1.5 mM NaN3, 1 mM EDTA, 10 mM phosphate buffer	95% H2O/5% D2O		6.3		313
4	3D 1H-13C NOESY	3 mM 15N, 13C EphA1_TM 15N, 13C, 96 mM 2H DHPC, 24 mM 2H DMPC, 1.5 mM NaN3, 1 mM EDTA, 10 mM phosphate buffer	100% D2O		6.3		313
5	13C F1-filtered/F3-edited-NOESY	1.5 mM 15N, 13C EphA1_TM 15N,13C, 96 mM 2H DHPC, 24 mM 2H DMPC, 1.5 mM NaN3, 1 mM EDTA, 10 mM phosphate buffer, 1.5 mM EphA1_TM	100% D2O		6.3		313
6	15N-T1	3 mM 15N, 13C EphA1_TM 15N, 96 mM 2H DHPC, 24 mM 2H DMPC, 1.5 mM NaN3, 1 mM EDTA, 10 mM phosphate buffer	95% H2O/5% D2O		6.3		313
7	15N-T2	3 mM 15N, 13C EphA1_TM 15N, 96 mM 2H DHPC, 24 mM 2H DMPC, 1.5 mM NaN3, 1 mM EDTA, 10 mM phosphate buffer	95% H2O/5% D2O		6.3		313
8	15N-NOE	3 mM 15N, 13C EphA1_TM 15N, 96 mM 2H DHPC, 24 mM 2H DMPC, 1.5 mM NaN3, 1 mM EDTA, 10 mM phosphate buffer	95% H2O/5% D2O		6.3		313

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Varian	UNITY	600

NMR Refinement
Method	Details	Software
simulated annealing		NMRPipe

NMR Ensemble Information
Conformer Selection Criteria	target function
Conformers Calculated Total Number	100
Conformers Submitted Total Number	12
Representative Model	1 (fewest violations)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	processing	NMRPipe		Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
2	chemical shift assignment	CARA	1.5.5, 1.8	Keller and Wuthrich
3	structure solution	CYANA	2.1	Guntert, Mumenthaler and Wuthrich
4	refinement	CYANA	2.1	Guntert, Mumenthaler and Wuthrich

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.