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

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

   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
Ser203Oγa-Asp113Cγa 8.0–10.0 11.2 10.3 17 8 17 17 8
Ser204Oγ-Asp113Cγ 8.0–10.0 14.2 12.4 14 10 14 14 10
Ser207Oγ-Asp113Cγ 8.0–10.0 11.5 10.4 11.7 8 11.7 11.7 8
Ser207Cα-Asp113Cα N/A 12.2 12.0 - - - 17 -
Asn293Cβ1-Asp113Cβ 8.0–10.0 13.6 14.0 14 15 14 14 8
Phe289Cβ-Asp113Cβ 8.0–8.4 11.7 12.3 13 12 13 13 8
Asn312 Cβ-Asp113Cβ 8.0–8.4 9.1 8.6 10 9 10 10 8
Phe289Cβ-Asn312Cβ 8.0–8.4 5.5 5.5 5.5 5.5 5.5 5.5 8
  1. aγ Oxygen, and β and γ Carbon atoms of the side chains were taken into consideration
  2. bThese are the distance ranges observed previously in various experimental studies [2833]