Table 2.

Energy contributions to binding at the A_2AAR associated with individual amino acid residues in proximity to the co-crystallized ligand in the binding site. Bold font refers to residues that form an H-bond with the ribose moiety.

Residue	Minimized docked pose A (toward H250), 4		Minimized docked pose B (toward T88), 4		Minimized docked pose, 14
	Tot En	vdW	Tot En	vdW	Tot En	vdW
V84	−7.26	−6.63	−8.65	−7.19	−10.03	−9.26
L85	−6.22	−6.74	−6.51	−6.64	−17.21	−15.61
T88	−10.18	−6.51	−28.40	−4.62	−29.98	−5.95
F168	−30.17	−30.45	−30.91	−30.93	−30.77	−30.60
E169	−46.96	−3.40	−46.15	−3.75	−45.86	−3.39
M177	−10.99	−9.26	−9.31	−8.55	−10.11	−10.83
W246	−9.66	−7.11	−8.69	−6.28	−11.58	−9.99
L249	−13.31	−15.38	−13.86	−15.25	−14.55	−15.35
H250	−27.87	−1.81	−5.16	−4.41	−36.64	−4.60
N253	−43.30	−3.08	−42.14	−3.58	−44.03	−3.98
M270	−7.07	−5.27	−6.84	−5.16	−7.23	−5.36
I274	−17.35	−14.54	−16.86	−14.28	−17.77	−14.64
S277	−30.83	−2.61	−28.44	−3.21	−33.07	−1.81
H278	−18.31	−4.54	−18.70	−4.35	−17.13	−4.93