Skip to main content
. Author manuscript; available in PMC: 2016 Jun 2.
Published in final edited form as: Biochemistry. 2015 May 21;54(21):3360–3369. doi: 10.1021/acs.biochem.5b00174

Table 2.

Interface Residues

electrostatic interactions between chainsa
Glu194 (Oε2) ↔ Arg281 (Nε)
Glu194 (O) ↔ Ser278 (Oγ)
buried residuesa
Ser178 Asn192 Pro271 Phe279
Ile179 Pro193 Tyr272 Arg281
Leu182 Glu194 Asp274 Ala282
Gly183 Ile195 Thr275 Gln285
Arg184 Leu198 Ile276 Asn286
Gln185 Tyr260 Tyr277
Ile189 Asp269 Ser278
a

The application of 2-fold symmetry completes these interactions within the interface.