TABLE 2.

Comparison of parallel PCM dimers in their Pr states

	Agp1 (5I5L)a	DrBphP (4Q0J)	RpBphP2 (4R6L)
Superpositioning of PAS-GAF monomers (upper right) and dimers (lower left)
Agp1 (5I5L)		1.27b (270)c	1.38 (277)/1.29 (261)d
DrBphP (4Q0J)	2.87 (536)		1.47 (276)/1.16 (258)
RpBphP2 (4R6L)	2.28 (536)	2.72 (521)
Angles formed between the C-terminal helical segments of the GAF domains within a dimer
Agp1 (5I5L)	42° (289–304)e
DrBphP (4Q0J)	50° (299–314)
RpBphP2 (4R6L)	47° (294–309)
Surface area (Å2) buried at the dimer interface
Agp1 (5I5L)	1193
DrBphP (4Q0J)	1350
RpBphP2 (4R6L)	1313

^a PDB code is shown in parentheses.

^b r.m.s.d. values are in Å.

^c Number of Cα atoms used in structural alignment is shown in parentheses.

^d Data shown are with first (chain A) and second copy (chain B) of the polypeptide chain.

^e Range of residues used to define the helix axis is shown in parentheses.