. Author manuscript; available in PMC: 2010 Oct 14.

Published in final edited form as: Structure. 2009 Oct 14;17(10):1356–1367. doi: 10.1016/j.str.2009.08.014

Table 1.

Summary of two-state exchange parameters for individual and groups of residues in substrate-free arginine kinase.

			Individual Fits			Collective Fits
	Residue	2°	k_ex [s⁻¹]	p_B (%)	\|Δω\| [ppm]	k_ex [s⁻¹]	p_B (%)	\|Δω\| [ppm]
NTD HINGE	D88	α4	3200 ± 240	0.3 ± 0.1	1.9 ± 0.3	1930 ± 350	0.4 ± 0.1	3.2 ± 0.3
	H90	α4	1020 ± 480	0.4 ± 0.1	4.5 ± 0.5			4.4 ± 0.6
	G92	L4	1560 ± 760	0.3 ± 0.1	5.1 ± 0.6			3.4 ± 0.4

NTD-CTD INTERFACE	D71	L3	*	*	*	800 ± 100	1.1 ± 0.1	1.1 ± 0.1
	F136	L6
	N137	L6	1150 ± 160	1.9 ± 0.7	0.9 ± 0.6			1.7 ± 0.2
	F270	L11	2830 ± 230	0.9 ± 0.8	2.3 ± 0.5			2.4 ± 0.4
	C271	L11	*	*	*			0.9 ± 0.3
	N274	L11	1100 ± 710	0.6 ± 0.1	3.6 ± 0.7			1.6 ± 0.2
	G276	L11	1930 ± 340	1.4 ± 0.4	3.0 ± 0.6			3.8 ± 0.5
	G332	L14	1330 ± 320	1.5 ± 2.1	1.5 ± 1.0			1.5 ± 0.1

DYNAMIC DOMAIN 1 AND HINGE	R126	β1	690 ± 220	0.3 ± 0.1	2.9 ± 0.3	790 ± 70	0.4 ± 0.1	2.2 ± 0.3
	C127	β1	940 ± 550	0.2 ± 0.1	3.7 ± 0.6			1.9 ± 2.3
	R129	β1	950 ± 450	0.3 ± 0.1	5.6 ± 0.4			5.6 ± 0.2
	V220	β4	2360 ± 210	1.0 ± 0.1	1.3 ± 0.1			2.7 ± 3.0
	V222	β4	*	*	*			1.7 ± 0.6
	R229	β5	360 ± 350	0.3 ± 0.2	2.5 ± 0.4			1.7 ± 0.1
	Q234	β5	*	*	*			1.0 ± 1.0

SUBSTRATE BINDING LOOP L8	I182	α7	700 ± 420	0.5 ± 0.2	4.5 ± 0.4	790 ± 60	2.6 ± 0.6	0.8 ± 0.4
	D183	α7	*	*	*			*
	D184	α7	2730 ± 1760	0.5 ± 1.3	3.1 ± 4.5			0.6 ± 0.3
	H185	α7	1810 ± 650	0.3 ± 0.1	5.1 ± 0.6			0.8 ± 0.4
	E190	L8	990 ± 70	4.5 ± 0.6	1.6 ± 0.1			2.4 ± 0.8
	G191	L8	*	*	*			*
	D192	L8	760 ± 90	1.7 ± 0.4	1.3 ± 0.2			1.0 ± 0.2
	R193	L8	1470 ± 390	0.5 ± 0.1	4.4 ± 0.4			1.0 ± 0.5
	T197	L8	3660 ± 1360	0.5 ± 0.1	6.8 ± 1.3			1.1 ± 0.9
	A198	L8	4190 ± 1160	0.0 ± 1.2	2.6 ± 1.6			*
	A200	L8	1610 ± 440	0.7 ± 0.1	4.6 ± 0.5			1.3 ± 0.7
	C201	L8	510 ± 230	1.3 ± 0.1	1.9 ± 0.3			1.2 ± 0.1
	R202	L8	1300 ± 220	0.0 ± 0.0	0.8 ± 0.1			0.8 ± 0.6
	T206	L8	570 ± 50	2.6 ± 0.2	1.7 ± 0.1			1.7 ± 0.2
	G207	L8	1350 ± 140	0.0 ± 0.0	0.8 ± 0.1			0.7 ± 0.3
	R208	L8	920 ± 180	0.6 ± 0.1	3.8 ± 0.2			1.1 ± 0.1
	G209	β3	1450 ± 380	0.7 ± 0.2	3.3 ± 0.6			1.1 ± 0.2

Secondary structure of each residue is denoted with 2° as observed in the substrate-free crystal structure of arginine kinase. In all cases, fitting was performed assuming a two-state exchange model, where k_ex is the sum of forward and reverse rate constants, p_B is the relative population of the higher energy state, and Δω is the chemical shift difference between the two states. Asterisks denote residues for which fitting did not converge.