Table 2. The list of predicted messenger residues, along with the domains, conformational states, and supporting experimental evidence.

Residue	Domain	State	Possible structural and functional roles
K245	A	R″	salt-bridge [11], binding of substrate protein [43]
V273	A	R″	binding of substrate protein [43]
G148, A152–S154	I	R″,T	ATPase activity [25],[29], GroES binding ability [29]
D155–T157	I	R″,T	GroEL inter-subunits interactions [38],[39]
V396, L400	I	R″	ATPase activity [25]
A406–E408	I	R″	ATPase activity [29], salt-bridge between inter-subunits [35]
T149–S151	I	T	ATPase activity [25],[29], GroES binding ability [29]
K380, T385	A	T	ATPase activity [29], GroES binding ability [29], folding of substrate protein [29], salt-bridge in T and R state [11],[36], GroEL inter-subunits contacts [32]
A399	A	T	ATP hydrolysis [25]
V411	E	R	GroEL inter-subunits interactions [35]
E460	E	R	folding and releasing of substrate protein [29], GroEL subunits inter-ring contacts [32]
R197	A	R	GroEL inter-subunits contacts [32]
N206	A	R	GroES binding ability [29]
N265, T266	A	R	GroES binding ability [29], folding of substrate protein [29]
I270	A	R	binding of substrate protein [43]
V276	A	R	ATPase activity [29]
F281	A	R	ATPase activity [29], folding of substrate protein [29]
I353	A	R	inter-subunit interaction [10]
S358	A	R	salt-bridge [11], GroEL inter-subunits contacts [32]