Table 4.

Accuracy of Predicting Coil ³J_HN‐Hα Values for Disordered Peptides and Proteins

Protein	N a	RMS deviationsb [Hz]
		<3J>	3Jna	3JANN	<(3Jna+3JANN)/2>	3JSearle
Aβ(1–40)	30	0.45	0.38	0.37	0.37	0.42
α‐synuclein	111	0.39	0.29	0.29	0.29	0.50
Protease	64	0.44	0.38	0.42	0.38	0.43
Integrase‐N	44	0.47	0.41	0.36	0.37	0.58
Ubiquitinc	65	0.45	0.41	0.38	0.38	0.42
GGXGGd	18	0.43	0.43	0.28	0.31	0.37
All	332	0.43	0.37	0.36	0.35	0.47

^aNumber of experimental ³J _HN‐Hα couplings for each test set; for N‐terminally acetylated α‐synuclein, the first six residues have partial helical character and were excluded; temperature correction48 was applied to experimental data if not measured at 20°C, including a +0.16 Hz correction for Aβ (measured at 4°C) and a −0.10 Hz correction for denatured ubiquitin data (measured at 30°C); pressure correction of +0.08 Hz/kbar49 is applied to the experimental data not acquired at 1 bar, including a +0.20 Hz correction for both pressure‐denatured HIV‐1 Protease and the N‐terminal DNA‐binding domain of HIV‐1 Integrase (both collected at 2500 bar).

^bRMSD between experimental and predicted ³J _HN‐Hα coupling constants; <³J> is the difference relative to the average ³J _HN–Hα value calculated using Eq. (2) for residues of type X in the newly generated coil library, ³J_na is calculated relative to <³J> plus the neighbor adjustments of Table 3; ³J_ANN is the RMSD relative to values predicted by the ANN‐based Eq. (4). ³J_ANN values for each of the 8000 triplets are also available at https://spin.niddk.nih.gov/bax/nmrserver/rc_3Jhnha/ann_results.txt; ³J_Searle is the RMSD relative to the neighbor‐corrected coil values of Searle and co‐workers.15

^cFrom Peti et al.50

^dFrom Shi and Kallenbach.33