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PDBsum entry 1fdl
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Complex (antibody-antigen)
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PDB id
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1fdl
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Contents |
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214 a.a.
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218 a.a.
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129 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystallographic refinement of the three-Dimensional structure of the fabd1.3-Lysozyme complex at 2.5-A resolution.
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Authors
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T.O.Fischmann,
G.A.Bentley,
T.N.Bhat,
G.Boulot,
R.A.Mariuzza,
S.E.Phillips,
D.Tello,
R.J.Poljak.
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Ref.
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J Biol Chem, 1991,
266,
12915-12920.
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PubMed id
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Abstract
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The three-dimensional crystal structure of the complex between the Fab from the
monoclonal anti-lysozyme antibody D1.3 and the antigen, hen egg white lysozyme,
has been refined by crystallographic techniques using x-ray intensity data to
2.5-A resolution. The antibody contacts the antigen with residues from all its
complementarity determining regions. Antigen residues 18-27 and 117-125 form a
discontinuous antigenic determinant making hydrogen bonds and van der Waals
interactions with the antibody. Water molecules at or near the antigen-antibody
interface mediate some contacts between antigen and antibody. The fine
specificity of antibody D1.3, which does not bind (K alpha less than 10(5) M-1)
avian lysozymes where Gln121 in the amino acid sequence is occupied by His, can
be explained on the basis of the refined model.
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