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HuCal VH 2 Problem Spots

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CDRs VH
positive Phi angles
cis/trans Pro residues
H-Bonds
V/C interf. VH
Core residues VH
Dimer interf. VH Haptens
Dimer interf. VH Oligom.
Dimer interf. VH Proteins
Antigen interf. VH Haptens
Antigen interf. VH Oligom.
Antigen interf. VH Proteins
Randomized residues VH
Arg H108 - Asp H137
H12: Leu->Asp
exposed hydrophobic residue
4/4/20: H12 Leu-> Asn (+), H12 Leu -> Asp (++) %sol (L.Nieba)
4D5Flu: Ser selected from (L S D N F Y P H I T V A) (S.Jung)
No data on how it would affect FAB format
H16: Thr->Gly (Ser) positive Phi angle
H47: Pro->Ala
mcpc: Pro in this position has negative effect on folding yield (A.Knappik,)
H51: Ala->Gly conserved Gly
H56: Ala->Gly positive Phi Angle
H76: Thr->Gly positive Phi Angle
H97 Asp->Arg,
H99: Val->Glu
exposed hydrophobic residue,
peripheral contribution to charge cluster (usually H97 Arg, H99 Glu)
H144: Leu->Thr
exposed hydrophobic residue
4D5Flu: Ser not conterselected from LS (S.Jung)
Caution:
Lateral interaction with Val H103 may have a stabilizing effect, which would be lost upon substitution with a small hydrophilic residue
No data on how it would affect FAB format

HuCal Structure Display VH 2

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AAAAA Homepage Zürich University Dept. of Biochemistry Plückthun Group Annemarie Honegger

Last Modified by A.Honegger Tuesday, March 25, 2008