. 2016 Dec 12;5:e21422. doi: 10.7554/eLife.21422

Table 5.

Square matrix of all possible pair-wise structural superpositions. Superpositions were calculated using the nine independently refined DesKC:DesR-REC pairs, taken from the 1.5 complexes in the phosphatase asymmetric unit (named STAB1, STAB2 and STAB3) and the 2 complexes present in the ASU of each of the three different phosphotransferase structures (named as E₁₈₈[1–6]). Below the main diagonal the structurally invariant region of DesK DHp domains (residues 190–234_(HK)) were superposed, whereas above the diagonal, the DesR REC domains (residues 1–129_(RR)) were superposed instead. Resulting root mean squared deviations (in Å) were calculated, for both matrix halves, between all Cα atoms of the REC domains (residues 1–129_(RR)) after superposition, as indicated in each individual matrix cell. Font colors highlight the two different alignment procedures performed. The significant differences between corresponding blue- and red-colored values, indicate that the REC domains do not change within, but rather ‘slip’ with respect to the kinase DHp domain.

DOI: http://dx.doi.org/10.7554/eLife.21422.011

	STAB1	STAB2	STAB3	E₁₈₈1	E₁₈₈2	E₁₈₈3	E₁₈₈4	E₁₈₈5	E₁₈₈6
STAB1		0.229	0.158	0.414	0.349	0.442	0.361	0.344	0.343
STAB2	0.826		0.188	0.496	0.459	0.512	0.334	0.343	0.333
STAB3	1.362	1.917		0.393	0.343	0.414	0.292	0.287	0.277
E₁₈₈1	1.168	1.133	1.682		0.275	0.146	0.305	0.301	0.301
E₁₈₈2	0.909	1.140	1.224	0.584		0.301	0.351	0.309	0.341
E₁₈₈3	1.085	1.110	1.530	0.233	0.459		0.346	0.315	0.313
E₁₈₈4	1.548	1.140	2.453	0.893	1.316	1.040		0.175	0.117
E₁₈₈5	1.295	0.978	2.096	0.593	0.969	0.716	0.449		0.140
E₁₈₈6	1.424	1.058	2.300	0.770	1.182	0.905	0.193	0.306