. 2022 Jan 18;13(1):e03604-21. doi: 10.1128/mbio.03604-21

TABLE 1.

Selected human GPCRs and their QTY-designed variants

UniProt accession no.^a	Wild type^b			QTY designed^b			R_ACT^c	R_SC^d
UniProt accession no.^a	MW (kDa)	pI	H_Y	MW (kDa)	pI	H_Y	R_ACT^c	R_SC^d
P41595	54.30	9.22	0.2672	54.76	9.10	−0.7305	0.5484	0.0291
P29274	44.71	8.33	0.4607	45.15	8.29	−0.7072	0.5060	0.1068
P07550	46.46	6.59	0.1700	46.65	6.59	−0.8764	0.4731	0.0630
P51681	40.52	9.20	0.5466	41.05	9.07	−0.9218	0.5576	0.0483
P61073	39.75	8.46	0.3994	40.05	8.40	−0.9113	0.5608	0.0568
P35462	44.22	9.20	0.3190	44.71	9.12	−0.7351	0.4902	0.0750
P41143	40.37	9.20	0.5384	40.75	9.11	−0.6878	0.4629	0.0538
P47871	51.26	9.01	0.0785	51.93	8.90	−0.9388	0.5094	0.0929
P35367	55.78	9.33	−0.0859	56.20	9.24	−0.9675	0.5067	0.0924
P41145	42.65	7.92	0.4816	42.85	7.88	−0.7465	0.5241	0.0500
P41146	40.69	8.73	0.6511	41.14	8.67	−0.4883	0.4720	0.0243
Q9H244	39.44	9.59	0.3512	39.85	9.38	−0.9786	0.5490	0.0263
P21453	42.81	9.58	0.4408	43.38	9.44	−0.9009	0.5506	0.0314
P28222	43.57	8.95	0.3421	43.99	8.88	−0.8378	0.4938	0.0590
Q99835	83.68	8.70	−0.0599	84.17	8.66	−0.5953	0.5102	0.1329

All 15 selected GPCRs have been well investigated in previous research, and their related structure data can be retrieved from the PDB.

MW, pI, and H_Y indicate molecular weight in kilodaltons, isoelectric point, and hydrophobicity, respectively, which were calculated using ProPAS (8).

R_ACT estimates the changing rate of amino acid sequence in TM regions, calculated by dividing the numbers of changed amino acids by the summarized length of all the TM regions.

R_SC shows the changing rate of secondary structure, which was calculated by dividing the number of positions related to structure changing by the whole length of the protein sequence.