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. Author manuscript; available in PMC: 2020 Jul 12.
Published in final edited form as: J Mol Biol. 2019 May 22;431(15):2729–2746. doi: 10.1016/j.jmb.2019.05.026

Table 2.

Substitutions used for crosslinking and BTH assays

Protein Substitution Residue tested for interaction Distance (Å) between residues (CA)a
Hsp90Ec K354C DnaK E209C
DnaK D211C		 10.6
7.8
Hsp90Ec Q358C DnaK G328C
DnaK D45C		 10.1
60.8
Hsp90Ec E584C DnaK G328C 73.0
DnaK E209C Hsp90Ec K354C 10.6
DnaK D211C Hsp90Ec K354C
Hsp90Ec Q358C		 7.8
13.4
DnaK G328C Hsp90Ec Q358C
Hsp90Ec E584C		 10.1
73.0
DnaK D45C Hsp90Ec Q358C 60.8
Hsp82 P281C Ssa1 T219C 9.1
Hsp82 E402C Ssa1 K322C
Ssa1 K323C		 10.7
11.6
Hsp82 E409C Ssa1 K322C
Ssa1 K323C
Ssa1 T219C		 10.7
13.3
23.4
Hsp82 E635C Ssa1 T219C 86.0
Ssa1 T219C Hsp82 P281C
Hsp82 E409C
Hsp82 E635C		 9.1
23.4
86.0
Ssa1 K322C Hsp82 E402C
Hsp82 E409C		 10.7
10.7
Ssa1 L323C Hsp82 E402C
Hsp82 E409C		 11.6
13.3
a

Distances between carbon α atoms for residues indicated are determined using the docked models of Hsp90Ec and DnaK (Fig. 1a) [32] or Hsp82 and Ssa1 (Fig. 4a) [33].