Table 2 Structural comparison between the open, “C1”, “C2” and partially closed “pC” structures

State	PDB code	R.m.s deviation based on C-half superimposition (Å)		R.m.s deviation based on N-half superimposition (Å)		Opening angle (°)
		N-half	α13	C-half	α13
C1	8WXW	N.A.^a	N.A.	N.A.	N.A.	1.0
C1	3S5H	0.67	0.76	0.68	0.53	2.3
C1	3S5I	0.59	0.71	0.55	0.56	2.2
C1	3S5M	0.55	0.71	0.55	0.50	2.3
C1	7DI7	0.50	0.28	0.48	0.27	2.2
C1	7DIA	0.53	0.28	0.36	0.24	1.6
C1	7DIJ	0.39	0.46	0.31	0.37	1.2
C1	7VPE	0.37	0.37	0.30	0.26	1.6
C1	8HO4	0.64	0.44	0.67	0.36	2.1
C1	8HO5	0.49	0.27	0.28	0.24	2.0
C2	8WXZ	1.60	0.55	1.76	0.53	−3.4
C2	3S5K	1.44	0.76	1.49	0.68	N.A.^b
pC	8WYX	1.97	0.71	2.30	0.85	5.2
pC	8WYT	1.97	0.71	2.30	0.85	5.2
open	8WYY	19.0	4.29	17.3	1.53	32.5
open	8WYU	18.9	4.17	17.2	1.44	32.8

^aFLN-α peptide complex (this work, PDB code: 8WXW) was used as the reference for superposition.
^bK217 of PDB 3S5K is disordered.
R.m.s deviations were calculated for the N- or C-half Cα atoms between different conformations. Smaller yet noticeable changes in hinge helix α13 are also presented. Opening angles between the N-halves and C-halves are quantified by measuring the K217–E516–P1069 angle. A negative angle value denotes an opening between the two half domains in the opposite direction.

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