Table 2.

Propensity of polar residues forming sidechain hydrogen bonds to mainchain atoms in various architectural contexts.

	Propensity of polar residues forming sidechain hydrogen bonds to mainchain atoms
Amino Acid	Within helix N-termini		Within helix C-termini		Within edge strands		From edge strands		Within central strands		From central strands		Within 310 helices		Within β-hairpins		Within polyproline helices		Within coil regions
	Con	All	Con	All	Con	All	Con	All	Con	All	Con	All	Con	All	Con	All	Con	All	Con	All
Arg	1.05	0.46	14.38	6.44	3.17	3.29	1.71	3.25	0.34	1.73	3.07	3.42	3.02	3.52	1.48	2.69	6.11	3.70	2.48	3.52
Asn	1.30	2.88	1.14	1.84	3.12	3.20	3.20	2.00	2.44	2.44	3.06	2.30	1.58	2.41	1.13	3.05	2.54	2.43	1.85	2.57
Asp	4.84	3.04	0.61	0.54	2.65	1.20	2.27	2.06	0.97	1.44	2.42	1.46	3.04	2.28	6.37	2.97	1.74	1.43	5.20	2.52
Cys	9.86	2.20	4.52	1.40	3.83	2.66	0.93	2.22	5.09	4.06	0.39	2.53	8.99	2.59	4.51	1.70	1.55	0.84	5.94	1.97
Gln	0.11	1.22	0.44	1.80	2.33	2.98	6.19	2.23	4.87	1.86	1.67	2.10	0.96	1.69	1.04	1.80	1.55	3.06	0.52	1.96
Glu	1.94	1.40	0.00	0.06	0.00	0.82	0.00	0.64	0.57	0.48	2.35	0.78	0.81	0.79	0.08	0.93	0.80	1.19	0.90	0.99
His	2.37	1.13	0.89	2.50	0.97	2.24	4.08	2.14	0.82	2.08	1.81	2.22	1.45	2.62	1.90	1.89	4.71	2.38	2.66	2.08
Lys	0.00	0.13	0.60	1.99	0.00	1.05	0.00	0.88	1.25	0.51	0.00	1.12	0.15	1.18	0.00	0.67	0.40	1.00	0.13	0.97
Ser	1.53	3.43	0.65	2.15	0.47	1.92	2.61	2.01	2.32	3.22	2.46	1.75	1.09	2.01	3.58	2.23	0.76	2.03	0.90	1.95
Thr	1.53	3.64	0.70	2.05	2.91	1.81	0.68	2.25	3.43	3.29	0.48	2.37	0.65	1.88	0.75	2.23	0.62	1.88	1.19	1.81
Trp	0.81	0.23	0.36	1.28	2.06	1.31	6.53	2.01	1.84	1.83	1.84	1.83	3.41	1.23	3.88	1.40	2.93	1.25	3.58	1.30
Tyr	1.06	0.68	0.56	1.23	4.04	1.77	0.30	2.37	1.03	1.26	3.14	2.37	4.20	1.37	0.07	0.91	3.12	1.84	1.60	1.39

Columns headed "Col" display the propensities of conserved buried polar residues.

Columns headed "All" display the propensities of all polar residues forming the indicated interaction (regardless of solvent accessibility or conservation).