. 2015 May 20;10(5):e0127081. doi: 10.1371/journal.pone.0127081

Table 4. Ephrin-A5 interactions with EphA3.

Ephrin-A5^L	EphA3^R
Residues not in the GH loopops
A27^SC	H50^SC
V28^SC	H50^SC
A29^BB	H50^SC
Y57^SC	H50^SC , H50 ^SC, E53 ^SC
F97^SC	R160^SC
K98^SC	Y62^SC
W100^SC	S56^SC, P64^SC
R104^SC	I38^SC
P108^BB	I38^SC
N109^BB	I38^SC, L42^SC
F114^SC	S56^SC
S115^BB	E54^BB, I55^SC, S56 ^SC, S56 ^BB
S115^SC	E54^BB
K117^SC	E53 ^SC, I55^SC
Residues in the GH loop
F121 ^SC	P110 ^SC, I 111 ^SC
T122 ^SC	L157 ^SC
T122 ^BB	*R 104* ^SC, F152 ^SC
P123 ^SC	Q69 ^SC, C189 ^BB, V190 ^BB, A191 ^BB
P123 ^BB	*T102* ^SC, T102 ^BB, F152 ^BB, A191 ^SC
F124 ^SC	G57 ^BB, V58 ^BB, Q69 ^SC, R 104 ^SC, F152 ^SC, V193 ^SC
S125 ^SC	F152 ^SC, *I161* ^BB, L162 ^SC, *K163* ^BB
S125 ^BB	T102 ^SC, L157 ^SC
L126 ^SC	R160 ^BB
L126 ^BB	*R160* ^SC
G127 ^BB	*R160* ^SC
F128 ^SC	R160 ^SC
E129 ^SC	*R104* ^SC, L157 ^SC

BB, backbone; SC, side chain.

Modes of interaction are marked as follows: van der Waals interactions in plain text, hydrogen bonds in bold, and salt bridges in bold and underlined.