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. 2009 Jul 1;106(28):11713–11718. doi: 10.1073/pnas.0903228106

Table 1.

The binding interactions between the residues of the PCTD and the residues of the dimeric N protein binding site

Interaction P residues Atoms N residues (subunits 1 and 2) Atoms
Hydrophobic LEU214 Side chain THR361(1) Side chain
H bond GLN215 NE2 ASP359(1) OD1
H bond GLN215 OE1 SER360(1) N
Hydrophobic LEU217 Side chain LEU364(1) Side chain
Hydrophobic ILE219 Side chain LEU364(1) Side chain
H bond SER233 O THR365(2) OG1
H bond VAL234 O LEU364(2) N
Hydrophobic GLY235 CA LEU364(2) Side chain
H bond ARG251 NH1, NH2 THR365(2) OG
H bond LYS253 NZ ASN367(1) ND2
H bond Lys254 NZ ASP384(1) OD2
H bond Lys254 NZ ASP384(1) O
H bond Lys254 O ASN386(1) ND2
Hydrophobic LEU255 Side chain THR366(1) Side chain
H bond TYR256 OH ASP358(2) O
H bond TYR256 N ASP384(1) OD1
H bond ASN257 ND2 ASP359(2) OD1
H bond ASN257 ND2 ASP359(2) OD2
H bond ASN257 ND2 LYS354(2) NZ
H bond ASN257 ND2 GLU383(1) OE2
H bond ASN257 OD1 ASP359(2) OD1
H bond ASN257 OD1 ASP359(2) OD2
H bond ASN257 OD1 SER360(2) OG
H bond ASN257 OD1 ASP384(1) OD1
H bond ASN257 N ASP384(1) OD1
H bond GLN258 N ASP384(1) OD1
H bond ARG260 NH1 ASP358(2) OD1
Hydrophobic VAL261 Side chain VAL367(1) Side chain
H bond LYS262 NZ GLU377(1) OE2
H bond TYR263 OH GLY362(1) N

The numbers 1 and 2 shown in parentheses adjacent to N protein residue names and numbers refer to molecule 1 or 2, respectively, of the N dimer. The list of residues was compiled with the aid of the Protein Interfaces, Surfaces, and Assemblies (PISA) server (42) and visual inspection with COOT (36).