Table 3. ProteinANS interactions (3.2) in all 28 copies of Hyp-1 at the internal sites 1, 2 and 3 with the frequency in parentheses.

Residues highlighted in bold form hydrogen bonds to the sulfonate group of ANS (note that Arg27 at site 1 always interacts with ANS via hydrogen bonding, while other residues in bold show a variable pattern of hydrogen-bonding/hydrophobic/no interactions at the remaining binding sites).

Binding site (No. of chains occupied by ANS in this binding site)	Residues involved in contact to ANS (No. of chains with this interaction)
1 (23)	Arg27 (22), Gln35 (5), Leu31 (2), Val91 (1), Glu132 (1), Gly136 (1), Lys139 (1), ANS at site 7 (2)
2 (24)	Tyr144 (23), Lys8 (12), Leu19 (6), Ile116 (6), Glu10 (5), Tyr141 (3), Leu23 (2), Arg27 (1), Tyr84 (1)
3 (13)	Tyr150 (11), Lys33 (9), Val30 (3), Val147 (3), Phe158 (3), Val157 (2), Leu151 (1)