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HuCal VLl 2 Problem Spots

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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
L9: Ala->Pro

conserved Proline
In a lambda-like length of the "kink" reagion, L8 Pro/ L9 Pro wins out over all other sequence combinations, although a kappa-like length (no gap in L7) combined with L8 cis-Pro performs even better (S.Spada, SIP)

L10: Ser Positive Phi angle, usually Ser
L47 His->Lys?
Charge interactions
Rei: L47 Thr-> Lys stabilizes (-5.3kJ/mol)
charge interaction with Asp L103, but repiulsive interaction with L50 Lys
L58: Asp Positive Phi angle
L67: Val Positive Phi angle
L148: Leu->Thr
exposed hydrophobic residue, no stabilizing lateral contacts. Effects on FAB?

HuCal Structure Display VLl 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