|Comparison of edges reported in SCA and GMRC studies with GREMLIN|
|GREMLIN||SCA ||GMRC |
|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)|
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.
Moitra et al.
Moitra et al. BMC Biophysics 2012 5:13 doi:10.1186/2046-1682-5-13