Virtual Molecule: P0 Myelin Glycoprotein. I. Homology Modeling and Prediction of the Secondary and Tertiary Structure - Molecules: Nucleation, Aggregation and Crystallization - page 242

Fig. 2. BLAST results from searching the PDP database for the sequence template of the
P0 protein. The best hit was 1NEU chain A. “Query” is an analyzed sequence of P0 pro-
tein; “Sbjct,” subject sequence, is the sequence found in database by BLAST. Identity
between target (query) and template (subject) was 97% and E value 2 × 10 −71 (an E value
close to zero means that both sequences are homologs). The sequence between “Query”
and “Sbjct” means consensus sequence (full agreement) of this alignment; similar residues
are depicted as “+” and different residues by “ ” (space).
Fig. 3. The ribbon/wire model of the P0_Ex subunit of human P0 protein constructed
using the homology modeling method. The structure of the 25 Ser … 33 Ile loop (in red) is pre-
dicted using the loop database of the Swiss-Model — in the 1NEU model there is no infor-
mation about the structure of this loop. The ending of the C-terminus is colored orange,
and the ending of the N-terminus is colored blue. The 28 Trp residue is shown as a stick
model (right). The disulfide bridge between 21 Cys … 98 Cys is visible in the central part of
the model.