How good is a Homology Model? Comparison of Model and X-ray Structure of the anti-Ampicillin scFV aL2

How good are homology predictions? 1.23Å rms deviation between model and structure (all c-alpha) much of it due to domain orientation. For the individual domains, the rms deviation is approximately twice as large between model and experimental structure than between the two experimental structures derived from crystals grown in the presence of isopropanol and ammoniumsulfate (iso) and in the presence of methanepentanediol and ammoniumsulfate (mpd)

The anti-ampicillin-antibody aL2 (Anke Krebber) has an extremly short CDR3, which had to be free-modelled, since it is shorter than any in the PDB databank. However, since it is so short , its conformation has to be that of a very tight beta turn.