1IFW

SOLUTION STRUCTURE OF C-TERMINAL DOMAIN OF POLY(A) BINDING PROTEIN FROM SACCHAROMYCES CEREVISIAE

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D_NOESY	3mM protein, 50mM phosphate buffer, 0.1M NaCl, 1mM NaN3	90% H2O/10% D2O	0.2	6.3	ambient	303
2	2D_NOESY	3mM protein, 50mM phosphate buffer, 0.1M NaCl, 1mM NaN3	100% D2O	0.2	6.3	ambient	303
3	3D_15N-separated_NOESY	3mM protein U-15N, 50mM phosphate buffer, 0.1M NaCl, 1mM NaN3	90% H2O/10% D2O	0.2	6.3	ambient	303
4	3D_13C-separated_NOESY	3mM protein U-15N,13C, 50mM phosphate buffer, 0.1M NaCl, 1mM NaN3	100% D2O	0.2	6.3	ambient	303

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	DRX	500
2	Varian	UNITYPLUS	750

NMR Refinement
Method	Details	Software
simulated annealing	The structures are based on 972 NOE distance constraints, 69 dihedral angles constraints and 40 hydrogen bonds.	XwinNMR

NMR Ensemble Information
Conformer Selection Criteria	structures with the lowest energy
Conformers Calculated Total Number	200
Conformers Submitted Total Number	30
Representative Model	1 (lowest energy)

Additional NMR Experimental Information
Details	The structure was determined using standard triple-resonance and homonuclear techniques. The N-terminal sequence GPLGS is a cloning artifact.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	collection	XwinNMR	2.1	Bruker
2	processing	Gifa	4.31	Delsuc
3	data analysis	XEASY	1.3.13	Wuthrich
4	structure solution	CNS	0.9	Brunger
5	structure solution	ARIA	0.9	Nilges
6	refinement	CNS	0.9	Brunger

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.