1OO3

P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_13C-separated_NOESY	1.5mM P395S-15N,13C, 0.1M KCl	90% H2O/10% D2O	0.1M KCl	6.8	ambient	303
2	3D_15N-separated_NOESY	1.5mM P395S-15N,13C, 0.1M KCl	90% H2O/10% D2O	0.1M KCl	6.8	ambient	303
3	HNCA-J	1.5mM P395S-15N,13C, 0.1M KCl	90% H2O/10% D2O	0.1M KCl	6.8	ambient	303
4	HN(CO)CA	1.5mM P395S-15N,13C, 0.1M KCl	90% H2O/10% D2O	0.1M KCl	6.8	ambient	303
5	HCC(CO)NH	1.5mM P395S-15N,13C, 0.1M KCl	90% H2O/10% D2O	0.1M KCl	6.8	ambient	303
6	CC(CO)NH	1.5mM P395S-15N,13C, 0.1M KCl	90% H2O/10% D2O	0.1M KCl	6.8	ambient	303

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	AMX	500
2	Bruker	DMX	600
3	Bruker	DRX	800

NMR Refinement
Method	Details	Software
distance geometry, simulated annealing	1113 NOE-derived, distance constraints, 85 dihedral angle restraints	DYANA

NMR Ensemble Information
Conformer Selection Criteria
Conformers Calculated Total Number
Conformers Submitted Total Number	1
Representative Model	(minimized average structure)

Additional NMR Experimental Information
Details	The structure was determined using triple-resonance NMR spectroscopy.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	structure solution	DYANA	1.5	Guentert
2	collection	XwinNMR	2.5	BRUKER
3	refinement	Discover	97.0	MSI Inc.
4	data analysis	Pronto3D	19990506	Kjaer
5	structure solution	TALOS	1999.019.15.47	Cornilescu, Bax
6	data analysis	nmr2st	1.1	Pristovsek

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.