www.biomedcentral.com

Table 6
List of top ranked residues and the most persistent edges
Rank	Position	Number of edges (at λ = 38)	Most persistent pair position (edges at penalty λ = 140)
1	A117^3.32	41	G90^2.57, E247 ^IC3, F293^7.40, K296^7.43
2	A272^6.55	30	L72^IC1, G114^3.29, S176^EC2, Y178^EC2
3	E113^3.28	29	M44^1.39, L72^IC1, W126^3.41, Q237^IC3, F293^7.40
4	H211^5.46	29	F91^2.58, C140 ^IC2, F148 ^IC2
5	A292^7.39	28	Y29^{EC (N-terminus)}
6	S186^EC2	27	K67^IC1, Q244^IC3, P291^7.38
7	E122^3.37	26	I48^1.43, G90^2.57, E196^EC3, M207^5.42, A269^6.52, F293^7.40, C316^{IC (C-terminus)}
8	G90^2.57	23	A117^3.32, G120^3.35, E122^3.37, M207^5.42, Q237^IC3, A269^6.52, F293^7.40
9	G114^3.29	22	S176^EC2, A272^6.55, Y178^EC2
10	M207^5.42	22	G90^2.57, E122^3.37, C316^{IC (C-terminus)}

Residues in bold are part of the RT binding pocket extracted from the rhodopsin structure (PDB ID: 1U19). The Ballesteros-Weinstein numbering (superscript) is given for comparison with other GPCRs. Only long-range edges are reported i.e. the edges formed with neighboring residues (8 amino acids on either side) are filtered out.

Moitra et al. BMC Biophysics 2012 5:13 doi:10.1186/2046-1682-5-13

Table 6