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PDBsum entry 1pvb
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Calcium binding protein
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PDB id
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1pvb
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Contents |
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* Residue conservation analysis
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DOI no:
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Acta Crystallogr D Biol Crystallogr
52:165-169
(1996)
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PubMed id:
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X-ray structure of a new crystal form of pike 4.10 beta parvalbumin.
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J.P.Declercq,
B.Tinant,
J.Parello.
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ABSTRACT
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A new crystal form of pike (pI 4.10) parvalbumin has been crystallized in
presence of EDTA at pH 8.0. The crystals are orthorhombic, space group
P2(1)2(1)2(1), with a = 51.84, b = 49.95, c = 34.96 A. Diffractometer data were
collected to 1.75 A. The structure was solved by molecular replacement and
in the range
8.0-1.75 A. In spite of the presence of EDTA, calcium ions are present in both
primary binding sites. As compared to the previously reported structures, the
main differences concern the conformation of the N-terminal residues and the
packing in the unit cell.
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Selected figure(s)
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Figure 5.
Fig. 5. Superposition of the Ca atoms of pike (p/4.10) parvalbumin
crystallized in the presence of EDTA (this study, thick lines) and in
the absence of EDTA [1PAL, Declercq
et al.
(1991), thin lines].
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Figure 5.
Fig. 5. Superposition of the Ca atoms of pike (p/4.10) parvalbumin
crystallized in the presence of EDTA (this study, thick lines) and in
the absence of EDTA [1PAL, Declercq
et al.
(1991), thin lines].
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1996,
52,
165-169)
copyright 1996.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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S.E.Permyakov,
A.G.Bakunts,
A.I.Denesyuk,
E.L.Knyazeva,
V.N.Uversky,
and
E.A.Permyakov
(2008).
Apo-parvalbumin as an intrinsically disordered protein.
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Proteins,
72,
822-836.
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J.M.Zanotti,
M.C.Bellissent-Funel,
and
J.Parello
(1999).
Hydration-coupled dynamics in proteins studied by neutron scattering and NMR: the case of the typical EF-hand calcium-binding parvalbumin.
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Biophys J,
76,
2390-2411.
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J.P.Declercq,
C.Evrard,
V.Lamzin,
and
J.Parello
(1999).
Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 A) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core.
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Protein Sci,
8,
2194-2204.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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