1RJA

Solution Structure and Backbone Dynamics of the Nonreceptor Tyrosine Kinase PTK6/Brk SH2 Domain

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-separated_NOESY	1mM SH2 domain U-15N; 50mM phospahte buffer NA; 90% H2O, 10% D2O	90% H2O/10% D2O	0.15	6.5	1 atm	298
2	3D_13C-separated_NOESY	1mM SH2 domain U-15N, 13C; 50mM phospahte buffer NA; 90% H2O, 10% D2O	90% H2O/10% D2O	0.15	6.5	1 atm	298
3	3D_13C-separated_NOESY	1mM SH2 domain U-15N, 13C; 50mM phospahte buffer NA; 100% D2O	100% D2O	0.15	6.5	1 atm	298
4	3D_13C-separated_NOESY	1mM SH2 domain U-13C; 50mM phospahte buffer NA; 100% D2O	100% D2O	0.15	6.5	1 atm	298

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	DRX	500
2	Bruker	DRX	600
3	Varian	INOVA	500

NMR Refinement
Method	Details	Software
distance geometry, simulated annealing		XwinNMR

NMR Ensemble Information
Conformer Selection Criteria	structures with the lowest energy
Conformers Calculated Total Number	50
Conformers Submitted Total Number	21
Representative Model	1 (minimized average structure)

Additional NMR Experimental Information
Details	This structure was determined using triple-resonance NMR

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	data analysis	XwinNMR	2.6	Bruker Gmb.
2	processing	NMRPipe	1.8	Delaglio, F.
3	data analysis	Sparky	3.106	Goddard, T.D.
4	refinement	CNS	1.0
5	structure solution	Insight II	98	MSI

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.