2MOL

3D NMR structure of the cytoplasmic rhodanese domain of the full-length inner membrane protein YgaP from Escherichia coli

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D 1H-15N HSQC	0.5 mM [U-100% 13C; U-100% 15N; U-80% 2H] YgaP	95% H2O/5% D2O
2	3D HNCA	0.5 mM [U-100% 13C; U-100% 15N; U-80% 2H] YgaP	95% H2O/5% D2O
3	3D HN(CO)CA	0.5 mM [U-100% 13C; U-100% 15N; U-80% 2H] YgaP	95% H2O/5% D2O
4	3D 1H-15N NOESY	0.5 mM [U-100% 13C; U-100% 15N] YgaP	95% H2O/5% D2O	0	7.0	ambient	303
5	3D 1H-13C NOESY	0.5 mM [U-100% 13C; U-100% 15N] YgaP	95% H2O/5% D2O	0	7.0	ambient	303
6	3D 1H-15N NOESY	0.5 mM [U-100% 13C; U-100% 15N; U-80% 2H] YgaP	95% H2O/5% D2O

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	AVANCE	700

NMR Refinement
Method	Details	Software
simulated annealing		CYANA

NMR Ensemble Information
Conformer Selection Criteria	target function
Conformers Calculated Total Number	100
Conformers Submitted Total Number	10
Representative Model	1 (fewest violations)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	structure solution	CYANA		Guntert, Mumenthaler and Wuthrich
2	chemical shift assignment	XEASY		Bartels et al.
3	refinement	CYANA		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.