2KJR

Solution NMR structure of the N-terminal Ubiquitin-like Domain from Tubulin-binding Cofactor B, CG11242, from Drosophila melanogaster. Northeast Structural Genomics Consortium Target FR629A (residues 8-92)

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D 1H-15N HSQC	50 mM MES, 50 mM arginine, 10 mM DTT, 0.02 % sodium azide, 1.1 mM [U-100% 13C; U-100% 15N] protein, 50 uM DSS	95% H2O/5% D2O	50	6.0	ambient	273
2	2D 1H-13C HSQC	50 mM MES, 50 mM arginine, 10 mM DTT, 0.02 % sodium azide, 1.1 mM [U-100% 13C; U-100% 15N] protein, 50 uM DSS	95% H2O/5% D2O	50	6.0	ambient	273
3	3D 1H-15N NOESY	50 mM MES, 50 mM arginine, 10 mM DTT, 0.02 % sodium azide, 1.1 mM [U-100% 13C; U-100% 15N] protein, 50 uM DSS	95% H2O/5% D2O	50	6.0	ambient	273
4	3D 1H-13C NOESY	50 mM MES, 50 mM arginine, 10 mM DTT, 0.02 % sodium azide, 1.1 mM [U-100% 13C; U-100% 15N] protein, 50 uM DSS	95% H2O/5% D2O	50	6.0	ambient	273
5	3D HNCO	50 mM MES, 50 mM arginine, 10 mM DTT, 0.02 % sodium azide, 1.1 mM [U-100% 13C; U-100% 15N] protein, 50 uM DSS	95% H2O/5% D2O	50	6.0	ambient	273
6	3D HNCA	50 mM MES, 50 mM arginine, 10 mM DTT, 0.02 % sodium azide, 1.1 mM [U-100% 13C; U-100% 15N] protein, 50 uM DSS	95% H2O/5% D2O	50	6.0	ambient	273
7	3D CBCA(CO)NH	50 mM MES, 50 mM arginine, 10 mM DTT, 0.02 % sodium azide, 1.1 mM [U-100% 13C; U-100% 15N] protein, 50 uM DSS	95% H2O/5% D2O	50	6.0	ambient	273
8	3D HNCACB	50 mM MES, 50 mM arginine, 10 mM DTT, 0.02 % sodium azide, 1.1 mM [U-100% 13C; U-100% 15N] protein, 50 uM DSS	95% H2O/5% D2O	50	6.0	ambient	273
9	3D C(CO)NH	50 mM MES, 50 mM arginine, 10 mM DTT, 0.02 % sodium azide, 1.1 mM [U-100% 13C; U-100% 15N] protein, 50 uM DSS	95% H2O/5% D2O	50	6.0	ambient	273
10	3D HBHA(CO)NH	50 mM MES, 50 mM arginine, 10 mM DTT, 0.02 % sodium azide, 1.1 mM [U-100% 13C; U-100% 15N] protein, 50 uM DSS	95% H2O/5% D2O	50	6.0	ambient	273
11	3D HCCH-TOCSY	50 mM MES, 50 mM arginine, 10 mM DTT, 0.02 % sodium azide, 1.1 mM [U-100% 13C; U-100% 15N] protein, 50 uM DSS	95% H2O/5% D2O	50	6.0	ambient	273
12	3D HCCH-TOCSY	50 mM MES, 50 mM arginine, 10 mM DTT, 0.02 % sodium azide, 1.1 mM [U-100% 13C; U-100% 15N] protein, 50 uM DSS	95% H2O/5% D2O	50	6.0	ambient	273
13	2D 1H-13C HSQC	50 mM MES, 50 mM arginine, 10 mM DTT, 0.02 % sodium azide, 1.0 mM [U-5% 13C; U-100% 15N] protein, 50 uM DSS	95% H2O/5% D2O	50	6.0	ambient	273

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Varian	INOVA	500
2	Bruker	AVANCE III	850

NMR Refinement
Method	Details	Software
simulated annealing	NIH-Xplor-2.20 refinement with hydrogen bond PMF, radius of gyration, rama, IVM module.	NMRPipe

NMR Ensemble Information
Conformer Selection Criteria	structures with the lowest energy
Conformers Calculated Total Number	125
Conformers Submitted Total Number	20
Representative Model	1 (closest to the average)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	processing	NMRPipe	2008	Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
2	collection	VNMR	6.1C	Varian
3	collection	TopSpin	2.1.3	Bruker Biospin
4	data analysis	AutoStructure	2.2.1	Huang, Tejero, Powers and Montelione
5	structure solution	X-PLOR NIH	2.20	Schwieters, Kuszewski, Tjandra and Clore
6	data analysis	Sparky	3.113	Goddard
7	structure validation	PSVS	1.3	Bhattacharya and Montelione
8	chemical shift assignment	AutoAssign	2.3.0	Zimmerman, Moseley, Kulikowski and Montelione
9	data analysis	PdbStat	5.1	(PDBStat) R. Tejero, G.T. Montelione
10	refinement	X-PLOR NIH	2.20	Schwieters, Kuszewski, Tjandra and Clore

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.