## 3 Results
### Hydrophobicity Characteristic--Dimers
\begin{table}
\begin{tabular}{c c c c c c c c c c c} \hline \hline  & \multicolumn{3}{c}{**Residues**} & \multicolumn{3}{c}{**RD**} & \multicolumn{3}{c}{**TvH**} & \multicolumn{3}{c}{**OvT**} & \multicolumn{3}{c}{**OvH**} \\ \cline{2-11}
**Fragment** & \multicolumn{1}{c}{**FdI**} & \multicolumn{1}{c}{**FdII**} & \multicolumn{1}{c}{**FdII**} & \multicolumn{1}{c}{**FdII**} & \multicolumn{1}{c}{**FdII**} & \multicolumn{1}{c}{**FdII**} & \multicolumn{1}{c}{**FdII**} & \multicolumn{1}{c}{**FdII**} & \multicolumn{1}{c}{**FdII**} & \multicolumn{1}{c}{**FdII**} \\ \hline monomer & chain A & chain A & 0.56 & 0.58 & 0.16 & 0.25 & 0.53 & 0.31 & 0.75 & 0.87 \\ strand A.1 & 3–6 & 1–4 & **0.43** & **0.32** & 0.72 & 0.56 & 0.46 & 0.75 & 0.86 & 0.96 \\ strand A.2 & 59–62 & 55–58 & **0.25** & **0.19** & 0.91 & 0.92 & 0.91 & 1.00 & 0.76 & 0.93 \\ sheet A & strand A.1 + A.2 & strand A.1 + A.2 & **0.37** & **0.38** & 0.70 & 0.35 & 0.57 & 0.58 & 0.77 & 0.87 \\ strand B.1 & 25–27 & 22–24 & **0.19** & 0.52 & 0.18 & \(-\)0.52 & 0.95 & 0.00 & 0.49 & 0.85 \\ strand B.2 & 34–36 & 31–33 & 0.97 & **0.19** & 0.97 & 0.99 & \(-\)0.73 & 0.89 & \(-\)0.88 & 0.94 \\ sheet B & strand B.1 + B.2 & strand B.1 + B.2 & **0.35** & 0.50 & 0.42 & 0.11 & 0.80 & 0.35 & 0.45 & 0.87 \\ all sheets & sheet A + B & sheet A + B & **0.33** & **0.38** & 0.55 & 0.31 & 0.71 & 0.64 & 0.71 & 0.83 \\ no sheets &!(sheet A + B) &!(sheet A + B) & 0.59 & 0.57 & 0.10 & 0.14 & 0.50 & 0.20 & 0.76 & 0.88 \\ helix 1 & 15–21 & 13–17 & **0.27** & **0.26** & 0.59 & 0.74 & 0.80 & 0.83 & 0.88 & 0.95 \\ helix 2 & 43–54 & 41–49 & 0.64 & **0.19** & \(-\)0.09 & 0.81 & 0.01 & 0.86 & 0.92 & 0.92 \\ all helices & helix 1 + 2 & helix 1 + 2 & 0.54 & **0.19** & 0.20 & 0.78 & 0.35 & 0.86 & 0.90 & 0.94 \\ no helices &!(helix 1 + 2) &!(helix 1 + 2) & 0.57 & 0.55 & 0.16 & 0.24 & 0.59 & 0.39 & 0.69 & 0.85 \\ P-P & FdII(P-P) & FdII(P-P) & **0.29** & **0.28** & 0.90 & 0.50 & 0.95 & 0.82 & 0.97 & 0.89 \\ no P-P &!(FdI(P-P)) &!(FdII(P-P)) & 0.54 & 0.57 & 0.27 & 0.30 & 0.51 & 0.34 & 0.78 & 0.86 \\ P-L & FdII(P-L) &!(FdII(P-L)) & 0.77 & 0.65 & \(-\)0.28 & \(-\)0.03 & 0.06 & 0.30 & 0.81 & 0.69 \\ no P-L &!(FdI(P-L)) &!(FdII(P-L)) & **0.41** & 0.57 & 0.35 & 0.34 & 0.73 & 0.36 & 0.68 & 0.88 \\ catalytic & 11,14,17,54 & 8,14,50 & 0.76 & 0.68 & n/a & n/a & 0.84 & 0.38 & n/a & n/a \\ no catalytic &!(11,14,17,54) &!(8,14,50) & 0.52 & 0.58 & 0.23 & 0.27 & 0.60 & 0.35 & 0.72 & 0.86 \\ S-S bond & n/a & 18–42 & n/a & 0.51 & n/a & 0.33 & n/a & 0.42 & n/a & 0.91 \\ no S-S bond & n/a &!(18–42) & n/a & 0.53 & n/a & 0.35 & n/a & 0.34 & n/a & 0.83 \\ \hline \hline \end{tabular}
\end{table} 
Table 3: Hydrophobicity status of monomers of FdI (1 FXR) and FdII (1 FXD) seen as parts of dimers (3D Gauss capsule fit to the dimer) and their selected fragments. See description of Table 3 for more information how to interpret this table. The \(RD\) statuses of residues engaged in ligand binding appear to be much higher than 0.5 in both FdI and FdII complex. This is the consequence of a conformation where binding pockets are oriented away from the center. Their theoretical hydrophobicity must decrease, while their \(O\) is unchanged and high due to present cysteines. Because of more elongated dimer structure, this phenomenon is stronger in FdI (\(RD\) 0.77 vs. 0.65). Figure 5 shows how differently complex formations of FdI and FdII affects the \(T\) and \(O\) distributions in monomers seen as part of FOD drop fit to the dimers. O can be influenced only by the interactions between the chains, which is why it does not change much when compared with data from Figure 4. \(T\) however may change drastically, and in this case it, actually, is the reason behind the many \(RD\) values above 0.5 in Table 3.  
Different dimer conformation between FdI and FdII is signaled by a low (0.41) \(T\) vs. \(T\) correlation coefficient (Figure S5).