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HuCal VLl 1 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
L3: Val->Ser
exposed hydrophobic side chain, no stabilizing contacts.
L47: Leu->Lys
exposed hydrophobic residue
Rei: L47 Thr-> Lys stabilizes (-5.3kJ/mol)
would enable charge interaction with Asp L103
L50: Thr->Gly positive Phi Angle
L58: Asp positive Phi Angle
L67: Asn positive Phi Angle
L148: Leu->Thr
exposed hydrophobic residue, no stabilizing lateral contacts. Effects on FAB?

HuCal Structure Display VLl 1

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

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