Staphylococcal protein A: Unfolding pathways, unfolded states, and differences between the B and E domains -- Data Supplement - Supplemental Table 2 -- Proceedings of the National Academy of Sciences

Supplementary material for Alonso and Daggett (2000) Proc. Natl. Acad. Sci. USA 97 (1), 133-138.

Table 2. Properties of protein A transition states

Simulation	Time*, ps	<R_g>^†, Å	<SASA>^‡, Å²	<Cont>^§ Nat, %	<Cont>^§ Tot, %	H1		H2		H3
Simulation	Time*, ps	<R_g>^†, Å	<SASA>^‡, Å²	<Cont>^§ Nat, %	<Cont>^§ Tot, %	% a (f, y)	HB	% a (f, y)	HB	% a (f, y)	HB
E1(498)	240	11.1	4,800	76	85	95	8/9	91	11/11	82	11/12
E2(498)	660	12.0	5,200	70	80	83	7/9	84	10/11	84	10/12
B1(498)	240	12.4	5,700	64	81	6	2/8	72	6/8	86	11/12
B2(498)	1200	12.4	5,500	63	78	80	7/8	45	2/8	76	11/12

*The transition state ensembles span the 5 ps before the given time.

^†Radius of gyration, see Table 1. ^‡Solvent-accessible surface area [Hubbard, S. J. & Thornton, J. M. (1993) NACCESS (Dept. Biochem. and Mol. Biol., University College, London)]. ^§Percentage of native and total extent of native heavy atom contacts (distances less than 5.4 Å for aliphatic carbons and 4.6 Å for all others) with respect to NMR structure. ^¶Helix properties for H1, H2, and H3 relative to the secondary structure in the starting structures (see Fig. 1). %a(f, y) is the percentage of helix based on repeating (f, y) angles [Daggett, V., Kuntz, I. D. & Kollman, P. A. (1991) Biopolymers 31, 1115-1134]. HB is the number of intact helical hydrogen bonds (r_{donor-acceptor} £ 2.6 Å more than 25% of the time). The number of native hydrogen bonds is given after the slash.