. Author manuscript; available in PMC: 2009 Sep 5.

Published in final edited form as: J Mol Biol. 2008 Jun 14;381(3):509–518. doi: 10.1016/j.jmb.2008.06.019

Table 3.

Packing analysis

Interface	Symmetry operator	Buried Surface area/monomer(Å²) (% Buried surface area)	Major interactions & Interacting residues
Interface 1	−y,x−y+1,z−1/3	740.4 (12.3)	Electrostatic: Arg 77- Glu 60^’ Glu80/Glu76– Lys 2^’ Glu 80/76(-CO-) – Arg 40^’ His54/70(-NH-) – Glu 17^’ Ser55(-NH-) – Cys15 (-CO-) Hydrophobic: Ile 71, Val 39, Phe 19^’
Interface 2	x−y+1,x+1,z−1/6	456.8 (7.5)	Electrostatic: Glu72/w46/81(-CO-)/82(-CO-) – Arg 93^’ Ser83/(-NH-)84– Asp 21^’ Glu 72 – Tyr 46^’ Hydrophobic Leu 68, Leu 75, Ile 74 Phe 51^’, Ile 44^’
Interface 3	−x,−y+1,z−1/2	309.1 (5.14)	Electrostatic: 29 (-NH-) – 73 (-CO-)^’ 27(-CO-) – 77 (-NH-)^’ Ser 26 – His 78^’ 26 (-CO-) – Arg 77^’
Interface 4	x−y,x,z−1/6	190.9 (3.17)	Water-mediated

^’

Represents residues from symmetry related protomer; -CO- and -NH- represent main chain carbonyl and amide groups respectively.