Table 1. Input for the structure calculation and characterization of the energy-minimized NMR structures of ePrP(121–231), mPrP(121–231), and two variants of mPrP(121–231).

Quantity*	ePrP	mPrP[S170N,N174T]	mPrP[N174T]	mPrP
NOE upper distance limits	2,254	2,183	2,027	2,264
Dihedral angle constraints	110	110	110	110
Residual target function value, Å2	1.77 ± 0.41	1.67 ± 0.22	1.68 ± 0.32	1.93 ± 0.20
Residual distance constraint violations
No. >0.1 Å	29 ± 4	35 ± 4	26 ± 4	26 ± 4
Maximum, Å	0.13 ± 0.01	0.15 ± 0.01	0.15 ± 0.02	0.15 ± 0.01
Residual dihedral angle constraint violations
No. >2.5°	0	0	0	1 ± 0
Maximum, °	1.3 ± 0.4	1.9 ± 0.7	1.7 ± 0.6	2.6 ± 0.4
amber energies, kcal/mol
Total	–4,821 ± 57	–4,978 ± 80	–4,879 ± 97	–4,911 ± 71
Van der Waals	–320 ± 14	–339 ± 13	–351 ± 15	–306 ± 13
Electrostatic	–5,044 ± 56	–5,598 ± 84	–5,470 ± 89	–5,523 ± 75
rms deviation to the mean coordinates, ņ
N, Cα, and C′ (125–228)	0.57 ± 0.10	0.54 ± 0.07	0.67 ± 0.08	0.60 ± 0.09
All heavy atoms (125–228)	1.01 ± 0.09	0.95 ± 0.07	1.03 ± 0.09	1.00 ± 0.08
N, Cα, and C′ (127–166 and 172–225)	0.53 ± 0.09	0.51 ± 0.06	0.54 ± 0.07	0.46 ± 0.06
All heavy atoms (127–166 and 172–225)	0.96 ± 0.10	0.93 ± 0.08	0.92 ± 0.07	0.88 ± 0.06

^*Except for the top two entries, the average for the 20 conformers with the lowest residual dyana target function values and the standard deviation among them are given

^†The numbers in parentheses identify the polypeptide segments for which the rms deviation was calculated