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CDRs VL

positive Phi angles

cis/trans Pro residues

H-Bonds

V/C interf. VL

Core residues VL

Dimer interf. VL Haptens

Dimer interf. VL Oligom.

Dimer interf. VL Proteins

Antigen interf. VL Haptens

Antigen interf. VL Oligom.

Antigen interf. VL Proteins

Randomized residues VL lambda

Randomized residues VL kappa

exposed hydrophobic side chain, , potentially stabilizing lateral interaction with Pro L98, Phe 101 and Ile L147

In Rei, L15 Ala->Leu was found to be strongly stabilizing(-7.0kJ/mol), L15 Ala->Pro somewhat less so (-4.5kJ/mol), therefore a stabilizing effect of Pro->Leu could be expected.

Leu->Glu was found to have a negative effect in 4/4/20. If stability is a problem, Val->Ile

No data on how this will affect FAB format

exposed hydrophobic side chain,

no experimental evidence

exposed hydrophobic side chain
4T5: Leu->Ala pos. effect on production 4D5Flu: Phe selected over ASTIV, Hag: L101 Leu->Gln strongly selected. Two different side chain conformations observed in the PDB: either pointing outwards and fully exposed (as modelled in VK3) or packing underneath Ile L147 and Val L15 (as modelled in VK1. If stability is the main problem for VK1), Phe should be retained. If the stability is good, but folding yields leave to be desired, substitution of Phe by Ala or Gln might be an option.
No data on how this will affect FAB format

exposed hydrophobic side chain, potentially stabilizing lateral interaction with Val L15 and Pro L98

No data on how this will affect FAB format