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HuCal VLl 3 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
L53 Val-> Thr
exposed hydrophobic residue:
in 4T5: Thr->Lys improved production
in contrast to other VL and VK, no acidic residue in close contact
L58: Asp->Gly positive Phi Angle
L67: Asp >Gly positive Phi Angle
L96: Thr->Leu, Val buried hydrophilic residue
L148: Leu->Thr
exposed hydrophobic residue, no stabilizing lateral contacts. Effects on FAB?

HuCal Structure Display VLl 3

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

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