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. 2014 Aug 13;289(41):28539–28553. doi: 10.1074/jbc.M114.600031

TABLE 3.

Van Der Waals interactions between SH2 domain and Nef residues in the Nef·Hck32 complex

SH2 domain and Nef residues making Van Der Waals interactions with distances of 3.8–5.5 Å are shown. Hck SH2 domain residues are numbered as per the c-Src crystal structure (PDB code 2SRC). Nef residues are numbered as per the Nef·SH3 crystal structure (PDB code 1EFN). Note that residues in the PDB file from the Nef·Hck32 complex presented in this paper are numbered as per the Nef-SF2 sequence; due to an internal insertion, the Nef-SF2 residues are offset by +4 relative to the Nef-NL43 sequence numbering used in the table.

Complex A SH2 domain residues Complex B Nef residues
Ser-154 (side/main chain) Leu-76 (side chain)
Glu-178 (main chain) Gln-73 (side chain)
Glu-178 (side chain) Tyr-115 (side chain)
Thr-179 (side chain) Gln-73 (side/main chain)
Thr-179 (side chain) Val-74 (main chain)
Thr-179 (side chain) Pro-75 (side chain)
Thr-179 (side chain) Leu-76 (main chain)

Complex A SH2 domain residues Complex A Nef residues

Lys-151 (main chain) Pro-69 (side chain)
Gly-152 (main chain) Pro-69 (side chain)
Ile-153 (side/main chain) Pro-69 (side chain)
Ile-153 (side chain) Phe-68 (main chain)

Complex B SH2 domain residues Complex A Nef residues

Asn-209 (side/main chain) Phe-121 (side chain)
Asn-209 (side/main chain) Asp-123 (side chain)
Pro-216 (main chain) Pro-78 (side chain)
Arg-217 (main chain) Pro-78 (side chain)
Ser-218 (main chain) Leu-76 (main chain)
Thr-219 (side/main chain) Leu-76 (side/main chain)
Phe-220 (main chain) Leu-76 (side chain)
Ser-221 (side/main chain) Leu-76 (side chain)
Ser-221 (side chain) Tyr-115 (side chain)

Complex B SH2 domain residues Complex B Nef residues

Asp-208 (main chain) Phe-68 (side chain)
Asn-209 (main chain) Phe-68 (side/main chain)
Gly-210 (main chain) Phe-68 (side chain)
Ser-221 (side/main chain) Pro-69 (side chain)