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PDBsum entry 1tur
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Serine proteinase inhibitor
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PDB id
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1tur
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Contents |
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* Residue conservation analysis
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J Mol Biol
242:203-214
(1994)
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PubMed id:
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Solution structure of turkey ovomucoid third domain as determined from nuclear magnetic resonance data.
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A.M.Krezel,
P.Darba,
A.D.Robertson,
J.Fejzo,
S.Macura,
J.L.Markley.
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ABSTRACT
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The solution structure of the 56 amino acid residue turkey ovomucoid third
domain was determined by n.m.r. methods. Of the 661 distance constraints used in
the calculations, 120 were determined by quadratic approximation of the
cross-relaxation rates. The remaining constraints were crudely estimated from a
more standard analysis of NOESY spectra. Additionally, 29 torsion angle
constraints, 17 hydrogen bonds, and three disulfide bridges were used in the
structure calculations. Stereospecific assignments were accomplished for 24
beta-methylene groups and six isopropyl methyl groups (43% chiral assignments).
The addition of more accurate distance constraints to the distance
geometry/simulated annealing approach resulted in a significant reduction in the
dispersion of calculated backbone torsion angles and root-mean-square deviations
between structures. Detailed comparisons have been made between the n.m.r.
structures of OMTKY3 and published X-ray structures of the same protein and of
closely related avian ovomucoid third domains. The refinement with more accurate
distance constraints reduced differences between families of the n.m.r. and the
X-ray structures.
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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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N.Powers,
and
J.H.Jensen
(2006).
Chemically accurate protein structures: validation of protein NMR structures by comparison of measured and predicted pKa values.
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J Biomol NMR,
35,
39-51.
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K.A.Newton,
S.J.Pitteri,
M.Laskowski,
and
S.A.McLuckey
(2004).
Effects of single amino acid substitution on the collision-induced dissociation of intact protein ions: Turkey ovomucoid third domain.
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J Proteome Res,
3,
1033-1041.
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T.Cierpicki,
J.Bania,
and
J.Otlewski
(2000).
NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.
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Protein Sci,
9,
976-984.
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PDB code:
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W.R.Forsyth,
and
A.D.Robertson
(2000).
Insensitivity of perturbed carboxyl pK(a) values in the ovomucoid third domain to charge replacement at a neighboring residue.
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Biochemistry,
39,
8067-8072.
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J.J.Havranek,
and
P.B.Harbury
(1999).
Tanford-Kirkwood electrostatics for protein modeling.
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Proc Natl Acad Sci U S A,
96,
11145-11150.
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J.Liu,
Y.Gong,
O.Prakash,
L.Wen,
I.Lee,
J.K.Huang,
and
R.Krishnamoorthi
(1998).
NMR studies of internal dynamics of serine proteinase protein inhibitors: Binding region mobilities of intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor (CMTI)-III of the squash family and comparison with those of counterparts of CMTI-V of the potato I family.
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Protein Sci,
7,
132-141.
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W.R.Forsyth,
M.K.Gilson,
J.Antosiewicz,
O.R.Jaren,
and
A.D.Robertson
(1998).
Theoretical and experimental analysis of ionization equilibria in ovomucoid third domain.
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Biochemistry,
37,
8643-8652.
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J.Antosiewicz,
J.A.McCammon,
and
M.K.Gilson
(1996).
The determinants of pKas in proteins.
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Biochemistry,
35,
7819-7833.
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J.Liu,
O.Prakash,
Y.Huang,
L.Wen,
J.J.Wen,
J.K.Huang,
and
R.Krishnamoorthi
(1996).
Internal mobility of reactive-site-hydrolyzed recombinant Cucurbita maxima trypsin inhibitor-V characterized by NMR spectroscopy: evidence for differential stabilization of newly formed C- and N-termini.
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Biochemistry,
35,
12503-12510.
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L.Swint-Kruse,
and
A.D.Robertson
(1996).
Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain.
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Biochemistry,
35,
171-180.
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C.G.Hoogstraten,
S.Choe,
W.M.Westler,
and
J.L.Markley
(1995).
Comparison of the accuracy of protein solution structures derived from conventional and network-edited NOESY data.
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Protein Sci,
4,
2289-2299.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
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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