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Solution Structure of Ribosomal Protein L18 of Thermus thermophilus

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_13C-separated_NOESY	0.8 mM L18 U-15N,13C; 50 mM phosphate buffer; 200 mM LiCl	90% H2O/10% D2O	50 mM KH2PO4, 200 mM LiCl	5.9	1 atm	303
2	2D NOESY	0.8 mM L18 U-15N,13C; 50 mM phosphate buffer; 200 mM LiCl	90% H2O/10% D2O	50 mM KH2PO4, 200 mM LiCl	5.9	1 atm	303
3	3D_15N-separated_NOESY	1.3 mM L18 U-15N; 50 mM phosphate buffer; 200 mM LiCl	90% H2O/10% D2O	50 mM KH2PO4, 200 mM LiCl	5.9	1 atm	303

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	AVANCE	600
2	Varian	INOVA	800
3	Bruker	AVANCE	500
4	Bruker	AVANCE	700

NMR Refinement
Method	Details	Software
simulated annealing, torsion angle dynamics	structures are based on 1925 NOE-derived distance restraints, 125 backbone dihedral angle restraints, 12 chi-1 angle restraints, 68 distance restraints from hydrogen bonds	XwinNMR

NMR Ensemble Information
Conformer Selection Criteria	structures with the lowest energy
Conformers Calculated Total Number	50
Conformers Submitted Total Number	27
Representative Model	1 (closest to the average)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	collection	XwinNMR		Bruker
2	processing	NMRPipe		Delaglio
3	data analysis	ANSIG	3.3	Kraulis
4	data analysis	ANSIG	for Windows	Helgstrand
5	structure solution	CNS	1.0	Brunger
6	refinement	CNS	1.0	Brunger

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.