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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.