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Table 9 Comparison of edges reported in SCA and GMRC studies with GREMLIN

From: A minimal ligand binding pocket within a network of correlated mutations identified by multiple sequence and structural analysis of G protein coupled receptors

GREMLIN SCA [12] GMRC [14]
Residues involved in edges with K296 (at λ = 38) Residues that are statistically coupled to K296 perturbation Statistically coupled residues in amine + peptide + rhodopsin model
M44, L72, N73, G90, T93, G114, A117, G121, W175, Y178, C185, D190, S202, H211, A269, P291, A292, F293 I54, T58, N73, N78, F91, T92, T93, E113, A117, G121, E122, I123, L125, V129, E134, Y136, F148, A164, F212, I213, I219, M257, F261, W265, Y268, F293 , F294, A295, S298, A299, N302 , F313, M317 L57 – A82, F313 – R314, I305 – Y306, N302 – I304, C264 – A299
   Note: None of the above residues have any edges in GREMLIN (at λ =38)
  1. Short range edges are italicized while bold residues are common edges between SCA and GREMLIN. Edges from GRMC are not shared by SCA or GREMLIN.