Investigation of allosteric coupling in human β2-adrenergic receptor in the presence of intracellular loop 3

BMC Structural Biology

Table 2 Restraint distances in all seven MD runs and their corresponding values in experimentally reported active and inactive states

		Distances in crystallographic structures (Å)		Bond Restraints (Å)
Residue pair	Exper.^b (Å)	Inactive (PDB id: 2RH1)	Active (PDB id: 3SN6)	rstr1	rstr2	rstr3	rstr4	rstr5
Ser203O^γa-Asp113C^γa	8.0–10.0	11.2	10.3	17	8	17	17	8
Ser204O^γ-Asp113C^γ	8.0–10.0	14.2	12.4	14	10	14	14	10
Ser207O^γ-Asp113C^γ	8.0–10.0	11.5	10.4	11.7	8	11.7	11.7	8
Ser207C^α-Asp113C^α	N/A	12.2	12.0	-	-	-	17	-
Asn293C^β1-Asp113C^β	8.0–10.0	13.6	14.0	14	15	14	14	8
Phe289C^β-Asp113C^β	8.0–8.4	11.7	12.3	13	12	13	13	8
Asn312 C^β-Asp113C^β	8.0–8.4	9.1	8.6	10	9	10	10	8
Phe289C^β-Asn312C^β	8.0–8.4	5.5	5.5	5.5	5.5	5.5	5.5	8

^aγ Oxygen, and β and γ Carbon atoms of the side chains were taken into consideration
^bThese are the distance ranges observed previously in various experimental studies [28–33]

ISSN: 1472-6807