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PDBsum entry 1rjv
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Metal binding protein
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PDB id
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1rjv
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Contents |
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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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Paramagnetism-Based refinement strategy for the solution structure of human alpha-Parvalbumin.
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Authors
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I.Baig,
I.Bertini,
C.Del bianco,
Y.K.Gupta,
Y.M.Lee,
C.Luchinat,
A.Quattrone.
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Ref.
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Biochemistry, 2004,
43,
5562-5573.
[DOI no: ]
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PubMed id
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Abstract
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In the frame of a research aimed at the detailed structural characterization of
human calcium-binding proteins of the EF-hand family, the solution structure of
human alpha-parvalbumin has been solved by NMR and refined with the help of
substitution of the Ca(2+) ion in the EF site with the paramagnetic Dy(3+) ion.
A simple (1)H-(15)N HSQC spectrum allowed the NH assignments based on the
properties of Dy(3+). This allowed us to exploit pseudocontact shifts and
residual dipolar couplings for solution structure refinement. The backbone and
heavy atom RMSD are 0.55 +/- 0.08 and 1.02 +/- 0.08 A, respectively, and
decrease to 0.39 +/- 0.05 and 0.90 +/- 0.06 A upon refinement with
paramagnetism-based restraints. The RMSD for the metal itself in the EF site in
the refined structure is 0.26 +/- 0.12 A. Backbone NH R(1), R(2), and NOE
measured at two temperatures show the protein to be relatively rigid. The NH
orientations are well determined by the paramagnetism-based restraints. This
allows us to detect small but significant local structural differences with the
orthologue protein from rat, whose X-ray structure is available at 2.0 A
resolution. All differences are related to local changes in the amino acidic
composition.
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