KEY RESOURCES TABLE

REAGENT or RESOURCE	SOURCE	IDENTIFIER
Software and Algorithms
Modeller 9v22	Šali and Blundell, 1993	https://salilab.org/modeller/
CHARMM36 forcefield (July 2017 revision)	Huang et al., 2017	http://mackerell.umaryland.edu/charmm_ff.shtml
Gromacs 2016.4	Abraham et al., 2015	http://manual.gromacs.org/documentation/
OpenBabel 2.4.1	O’Boyle et al., 2011	http://openbabel.org/wiki/Main_Page
PRODRG server	Schüttelkopf and van Aalten, 2004	http://davapc1.bioch.dundee.ac.uk/cgi-bin/prodrg
CGenFF forcefield	Vanommeslaeghe et al., 2009	https://cgenff.umaryland.edu/
Matplotlib	Hunter, 2007	https://matplotlib.org/
MDTraj 1.9.3	McGibbon et al., 2015	http://mdtraj.org/1.9.3/
ProDy 1.10.10	Bakan et al., 2011	http://prody.csb.pitt.edu/
R 3.6.0	R Core Team (2018)	https://www.r-project.org/
Lattice library (R 3.6.0 package)	Sarkar, 2008	https://cran.r-project.org/web/packages/lattice/index.html
Visual Molecular Dynamics 1.9.3 (VMD)	Humphrey et al., 1996	https://www.ks.uiuc.edu/Research/vmd/
Bio3D v. 2.3–4 (R 3.6.0 package)	Grant et al., 2006	http://thegrantlab.org/bio3d/index.php
PyMOL	Delano, 2002	https://pymol.org/2/
nglview module (IPython)	Nguyen et al., 2018	https://github.com/arose/nglview
Deposited Data
Crystal structure of p110alpha H1047R mutant in complex with niSH2 of p85alpha and the drug wortmannin	Mandelker et al., 2009	PDB: 3HHM
Crystal structure of p110alpha in complex with iSH2 of p85alpha and the inhibitor PIK-108	Hon et al., 2012	PDB: 4A55
Crystal Structure of PI3Kalpha in complex with diC4-PIP2	Miller et al., 2014	PDB: 4OVV
Crystal structure of PI3Kgamma bound to ATP	Walker et al., 2000	PDB: 1E8X
Crystal structure of the PI3-kinase p85 N-terminal SH2 domain in complex with c-Kit phosphotyrosyl peptide	Nolte et al., 1996	PDB: 2IUH
Timeseries data for the distance between the ATP PG and di-C4 PIP2 O3’ for PI3Kα WT simulation, first replicate	This paper	Table S3
Timeseries data for the distance between the ATP PG and di-C4 PIP2 O3’ for PI3Kα WT simulation, second replicate	This paper	Table S4
Timeseries data for the distance between the ATP PG and di-C4 PIP2 O3’ for PI3Kα WT simulation, third replicate	This paper	Table S5
Timeseries data for the distance between the ATP PG and di-C4 PIP2 O3’ for PI3Kα simulation without nSH2, first replicate	This paper	Table S6
Timeseries data for the distance between the ATP PG and di-C4 PIP2 O3’ for PI3Kα simulation without nSH2, second replicate	This paper	Table S7
Timeseries data for the distance between the ATP PG and di-C4 PIP2 O3’ for PI3Kα simulation without nSH2, third replicate	This paper	Table S8
Timeseries data for the distance between the ATP PG and di-C4 PIP2 O3’ for PI3Kαsimulation with pY peptide and no active site restraints, first replicate	This paper	Table S9
Timeseries data for the distance between the ATP PG and di-C4 PIP2 O3’ for PI3Kαsimulation with pY peptide and no active site restraints, second replicate	This paper	Table S10
Timeseries data for the distance between the ATP PG and di-C4 PIP2 O3’ for PI3Kαsimulation with pY peptide and active site restraints	This paper	Table S11