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. Author manuscript; available in PMC: 2014 Jun 4.
Published in final edited form as: Structure. 2013 May 16;21(6):963–974. doi: 10.1016/j.str.2013.04.009

Table 4.

The surface areas and the changes in the surface areas upon ligand binding. The accessible surface areas were calculated without including any hetero atoms and using the same residue range. The Apo homodimer was made from the open conformation monomer of Ade-SeMTAN crystal structure. When the surface areas of liganded dimers were compared to the artificially created Apo dimer, it was noticed that having BuT-DADMe-ImmA in both active sites causes the dimer shrink

Bound ligand Surface of
monomer-A
(Å2)		 Surface of
monomer-B
(Å2)		 Interface
area (Å2)		 Surface of
dimer (Å2)		 Decrease in
the surface
area (%)
Apo1 10368 10367 2567 18168 -
Adenine2 10368 9721 2694 17394 4.3
MT-DADMe-ImmA3 9870 9927 2863 16934 6.8
Homocys-DADMe-ImmA3 9814 9914 2810 16917 6.9
DiEGT-DADMe-ImmA3 9715 9952 2796 16871 7.1
BuT-DADMe-ImmA3 9667 9681 2813 16534 9.0
1

Both monomers are in the open conformation.

2

One monomer is in the open conformation and the other one is in the closed conformation.

3

Both monomers are in the closed conformation.