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. 2006 Jun;80(12):6093–6105. doi: 10.1128/JVI.00205-06

TABLE 6.

Hydrogen bonding and salt bridge distances between Fab 2219 and different V3 peptides and intrapeptide hydrogen bonds within each V3 peptidea

Atom Residues in peptides and peptide atom Distance (Å)
MN UG1033 UR29
Fab atom
AsnL31OD1 R/R/QP315NH2 2.14 2.28
AsnL31OD1 G/G/RP312NH1 2.35
TyrL32N I/L/IP309O 2.93 2.77 3.02
TyrH32OH R/R/KP304NZ 3.31
TrpH33NE1 K/K/KP305O 2.77 2.78 2.82
TyrH52OH K/T/TP303NZ 3.18
AspH54OD1 K/K/KP305NZ 2.68 2.75 2.91
AspH56OD2 K/K/KP305NZ 2.62 2.45 2.76
GluH100OE1 H/H/KP308NZ 2.76
SerH100bO H/H/KP308NZ 2.35
GluH100O R/R/KP304NH1 2.87 2.81
GluH100O R/R/KP304NH2 3.47 3.17
GlyH100cN K/T/TP303O 3.30 2.83
GlyH100cN K/T/TP303OG1 3.25
GlyH100cO R/R/KP304NH1 3.04 2.86
AlaH100dN R/S/SP306O 2.79 2.76 2.82
AlaH100dO H/H/KP308N 3.02 2.91 3.08
Peptide atom
I/I/IP307N F/F/FP317O 2.81 2.87 2.97
I/L/IP309N R/R/QP315O 3.12 3.30
G/G/RP312N R/R/QP315O 3.47 3.47
R/R/QP315N G/G/RP312O 3.04 3.27 3.29
F/F/FP317N I/I/IP307O 2.90 2.92 2.90
R/R/KP304N K/T/TP303OG1 2.15 2.25
R/S/SP306OG K/T/TP303O 3.42
I/L/IP309N R/R/QP315OE1 3.10
a

Hydrogen bonds were evaluated with HBPLUS (55) and Contacsym (67, 68). The corresponding peptide residues for the three structures (MN, UG1033, and UR29) are shown separated by slashes. The atom making the hydrogen bond is shown, although this atom may not exist in the alternate residues.