Table II.

Restraints Used in CS-Rosetta Calculations for Residues 111–141 of Amyloid Fibrils of the Y145X Stop Mutant of the Human Prion Protein

Restraints	Type	Upper distance limits	No. of restraints
Chemical shifts	Experimentala		510
	GS-linkerb		224
	Total		734
Distance restraints	Interstrand H-bondsc	O–HN 1.8 Å/O–N 2.7 Å	176
	Intra β-strand Hα(i)–HN(i+1)d	2.5 Å	85
	Interstrand polymer	4.8 Å/9.6 Å/19.2 Åe	714
	Total		975

^aTaken from Ref.29.

^bRandom coil values for N, CA, C of Gly and N, CA, C, CB for Ser.

^cH-bond restraints enforce a parallel, in register alignment in agreement with solid-state NMR data for fibrils of the Y145X stop mutant of the human prion protein.³¹

^dResidues ¹¹²MAGA¹¹⁵, ¹²⁰AVVG¹²³, ¹²⁸YMLGSAMSR¹³⁶, ¹³⁸IIHF¹⁴¹ are in a β-strand conformation according to fragments selected by CS-Rosetta (Supporting Information Fig. S1).

^eUpper distance limits for strands i+1, i+2, and i+3 along the fibril axis enforcing the cross-β structure of the fibrils.