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HuCal VH6 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: Ser->Gly pos. Phi angle
H58: Thr->Ile(or Val) hydrophilic residue buried in hydrophobic core
H76: Ser->Gly pos. Phi Angle
H103: Val->Thr
exposed hydrophobic residue
4/4/20: V84S, M87S,I89S (++) %sol. (Lars), but: no data on how it would affect FAB format
Caution:
Lateral interaction with Leu H144 and Pro H10 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
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 6

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

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