Table 1.

Collection of the input for the structure calculation and characterization of the energy-minimized NMR structures of the polypeptide segment 121–230 in different human PrP constructs

Quantity*	hPrP(23–230)	hPrP(90–230)	hPrP(121–230)
NOE upper distance limits	1,732	1,705	1,752
Dihedral angle constraints	429	453	436
Residual target function value, Å2	0.25 ± 0.06	0.34 ± 0.08	0.39 ± 0.05
Residual distance constraint violations
Number ≥ 0.1, Å	0.3 ± 0.5	0.7 ± 0.9	0.1 ± 0.3
Maximum, Å	0.10 ± 0.01	0.11 ± 0.01	0.10 ± 0.00
Residual dihedral angle constraint violations
Number ≥ 2.0 degrees	1.8 ± 1.0	1.5 ± 1.0	5.6 ± 2.0
Maximum, degrees	2.9 ± 0.8	3.0 ± 1.2	3.7 ± 0.9
amber energies, kcal/mol
Total	−4824 ± 85	−4533 ± 79	−4698 ± 83
Van der Waals	−352 ± 16	−315 ± 15	−325 ± 16
Electrostatic	−5398 ± 84	−5164 ± 71	−5283 ± 67
rms deviation from ideal geometry
Bond lengths, Å	0.0084 ± 0.0002	0.0089 ± 0.0002	0.0084 ± 0.0003
Bond angles, degrees	2.25 ± 0.04	2.41 ± 0.04	2.29 ± 0.04
rms deviation to the averaged coordinates, Å
N, Cα, C′ (125–228)	0.65 ± 0.10	0.79 ± 0.11	0.81 ± 0.11
All heavy atoms (125–228)	1.06 ± 0.09	1.27 ± 0.10	1.26 ± 0.13
N, Cα, C′ of regular secondary structures†	0.51 ± 0.12	0.60 ± 0.12	0.68 ± 0.13

^*Except for the top two entries, the data characterize the group of 20 conformers that is used to represent the NMR structure; the mean value and the standard deviation are given. 

^† Secondary structure elements are formed by residues 128–131 (β-strand 1), 144–154 (α-helix 1), 161–164 (β-strand 2), 173–194 (α-helix 2), and 200–228 (α-helix 3).