Experiment: 1RWS

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	soft HNCA-E.COSY	1 mM 1016054 U-15N, 16% 13C; 50 mM phosphate buffer; 200 mM KCl; 90% H2O, 10% D2O	90% H2O/10% D2O	200 mM KCl	5.5	ambient	298
2	modified HNCO	1 mM 1016054 U-15N, 16% 13C; 50 mM phosphate buffer; 200 mM KCl; 90% H2O, 10% D2O	90% H2O/10% D2O	200 mM KCl	5.5	ambient	298
3	15N coupled HSQC	1 mM 1016054 U-15N, 16% 13C; 50 mM phosphate buffer; 200 mM KCl; 90% H2O, 10% D2O	90% H2O/10% D2O	200 mM KCl	5.5	ambient	298
4	3D_15N-separated_NOESY	1 mM 1016054 U-15N, 16% 13C; 50 mM phosphate buffer; 200 mM KCl; 90% H2O, 10% D2O	90% H2O/10% D2O	200 mM KCl	5.5	ambient	298
5	3D_15N-separated_TOCSY	1 mM 1016054 U-15N, 16% 13C; 50 mM phosphate buffer; 200 mM KCl; 90% H2O, 10% D2O	90% H2O/10% D2O	200 mM KCl	5.5	ambient	298
6	soft HNCA-E.COSY	0.5 mM 1016054 U-15N, 16% 13C; 50 mM phosphate buffer; 100 mM KCl; PEG bicelles (C12E5-hexanol in 0.98 ratio); 90% H2O, 10% D2O	PEG bicelles (C12E5-hexanol in 0.98 ratio); 90% H2O, 10% D2O	100 mM KCl	6	ambient	300
7	modified HNCO	0.5 mM 1016054 U-15N, 16% 13C; 50 mM phosphate buffer; 100 mM KCl; PEG bicelles (C12E5-hexanol in 0.98 ratio); 90% H2O, 10% D2O	PEG bicelles (C12E5-hexanol in 0.98 ratio); 90% H2O, 10% D2O	100 mM KCl	6	ambient	300
8	15N coupled HSQC	0.5 mM 1016054 U-15N, 16% 13C; 50 mM phosphate buffer; 100 mM KCl; PEG bicelles (C12E5-hexanol in 0.98 ratio); 90% H2O, 10% D2O	PEG bicelles (C12E5-hexanol in 0.98 ratio); 90% H2O, 10% D2O	100 mM KCl	6	ambient	300
9	soft HNCA-E.COSY	0.5 mM 1016054 U-15N, 16% 13C; 50 mM phosphate buffer; 100 mM KCl; PEG-CTAB (27:1)bicelles (C12E5-hexanol in 0.87 ratio); 90% H2O, 10% D2O	PEG-CTAB (27:1)bicelles (C12E5-hexanol in 0.87 ratio); 90% H2O, 10% D2O	100 mM KCl	6	ambient	293
10	15N coupled HSQC	0.5 mM 1016054 U-15N, 16% 13C; 50 mM phosphate buffer; 100 mM KCl; PEG-CTAB (27:1)bicelles (C12E5-hexanol in 0.87 ratio); 90% H2O, 10% D2O	PEG-CTAB (27:1)bicelles (C12E5-hexanol in 0.87 ratio); 90% H2O, 10% D2O	100 mM KCl	6	ambient	293

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Varian	INOVA	800
2	Varian	INOVA	600

NMR Refinement
Method	Details	Software
RDC directed fragment assembly	RDCs were used in the initial assembly of four fragments. RDCs from two media were used to set relative orientations of the fragments. Translational relationships of fragments were dictated by sequence connectivities and long-range NOEs. The assembled structure was minimized using a molecular force field and RDC error function. A total of 486 restraints were used: 380 residual dipolar coupling restraints, 85 NOE restraints (of which 64 were sequential, 11 short-range and 10 long-range), and 21 dihedral restraints. All sidechain atoms beyond CB are missing.	NMRPipe

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

Additional NMR Experimental Information
Details	This structure was determined using predominantly residual dipolar couplings from backbone atom pairs. It is a backbone structure modeled as an Ala-Gly-Pro polypeptide.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	data analysis	NMRPipe	5.0.4	F. DeLaglio, S. Grzesiek, G. Vuister, G. Zhu, J. Pfeifer and A. Bax
2	structure solution	REDcRAFT	1.0	H. Valafar, J. Prestegard
3	refinement	XPLOR-NIH	2.9.1	Schwieters, Kuszewski, Tjandra, Clore
4	data analysis	REDCAT	1.0	H. Valafar, J. Prestegard

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.