Table 2.

Comparison of the extent of LBD closure in wild-type and T686 mutant protomers

	Wild type					T686A		T686S
	Glu			Quis		Glu	Quis	Glu
	A	B	C	A	B	A	A	A	B	C	D
wtApo(A)	19.1	21.1	20.9	20.4	21.3	22.5	22.0	22.7	21.7	6.9	8.7a
	(5.2)	(6.3)	(6.3)	(5.6)	(5.8)	(6.4)	(6.3)	(6.7)	(6.3)	(2.2)	(2.7)
wtApo(B)	11.6	17.9	17.9	17.6	18.5	19.6	18.9	20.1	18.8	4.2	5.3a
	(3.4)	(4.2)	(4.4)	(3.8)	(4.0)	(4.3)	(4.3)	(5.0)	(5.0)	(0.7)	(2.0)

Angles of rotation (in degrees) and the linear displacement (in angstroms) of the linker residue G630 for glutamate- and quisqualate-bound GluR2-wt and T686 mutant protomers. For each cell in the table, the displacement values are in parentheses. Values are referenced to protomers A and B in the published wild-type GluR2–S1S2J apo structure (Armstrong and Gouaux, 2000). The wild-type glutamate- and quisqualate-bound structures were published previously (Armstrong and Gouaux, 2000; Jin et al., 2002). Rotation angles were measured with the analysis program DynDom (http://www.sys.uea.ac.uk/dyndom/). Protomers C and D in the T686S structure did not contain detectable electron density for bound glutamate.

^aFor protomer D, residues 640–700 had poor electron density and were excluded before the rotation angle was measured.