The crystal structure of the Fab of McPC603, a phosphocholine-binding mouse
myeloma protein, has been refined at 2.7 A resolution by a combination of
restrained least-squares refinement and molecular modeling. The overall
structure remains as previously reported, with an elbow bend angle between the
variable and constant modules of 133 degrees. Some adjustments have been made in
the structure of the loops as a result of the refinement. The hypervariable
loops are all visible in the electron density map with the exception of three
residues in the first hypervariable loop of the light chain. A sulfate ion
occupies the site of binding of the phosphate moiety of phosphocholine.