2cti: Difference between revisions
New page: left|200px<br /><applet load="2cti" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cti" /> '''DETERMINATION OF THE COMPLETE THREE-DIMENSIO... |
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'''DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF THE TRYPSIN INHIBITOR FROM SQUASH SEEDS IN AQUEOUS SOLUTION BY NUCLEAR MAGNETIC RESONANCE AND A COMBINATION OF DISTANCE GEOMETRY AND DYNAMICAL SIMULATED ANNEALING'''<br /> | '''DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF THE TRYPSIN INHIBITOR FROM SQUASH SEEDS IN AQUEOUS SOLUTION BY NUCLEAR MAGNETIC RESONANCE AND A COMBINATION OF DISTANCE GEOMETRY AND DYNAMICAL SIMULATED ANNEALING'''<br /> | ||
==Overview== | ==Overview== | ||
The complete three-dimensional structure of the trypsin inhibitor from | The complete three-dimensional structure of the trypsin inhibitor from seeds of the squash Cucurbita maxima in aqueous solution was determined on the basis of 324 interproton distance constraints, 80 non-nuclear Overhauser effect distances, and 22 hydrogen-bonding constraints, supplemented by 27 phi backbone angle constraints derived from nuclear magnetic resonance measurements. The nuclear magnetic resonance input data were converted to the distance constraints in a semiquantitative manner after a sequence specific assignment of 1H spectra was obtained using two-dimensional nuclear magnetic resonance techniques. Stereospecific assignments were obtained for 17 of the 48 prochiral centers of the squash trypsin inhibitor using the floating chirality assignment introduced at the dynamical simulated annealing stage of the calculations. A total of 34 structures calculated by a hybrid distance geometry-dynamical simulated annealing method exhibit well-defined positions for both backbone and side-chain atoms. The average atomic root-mean-square difference between the individual structures and the minimized mean structure is 0.35(+/- 0.08) A for the backbone atoms and 0.89(+/- 0.17) A for all heavy atoms. The precision of the structure determination is discussed and correlated to the experimental input data. | ||
==About this Structure== | ==About this Structure== | ||
2CTI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cucurbita_maxima Cucurbita maxima]. Full crystallographic information is available from [http:// | 2CTI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cucurbita_maxima Cucurbita maxima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CTI OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Gondol, D.]] | [[Category: Gondol, D.]] | ||
[[Category: Holak, T | [[Category: Holak, T A.]] | ||
[[Category: Otlewski, J.]] | [[Category: Otlewski, J.]] | ||
[[Category: Wilusz, T.]] | [[Category: Wilusz, T.]] | ||
[[Category: proteinase inhibitor (trypsin)]] | [[Category: proteinase inhibitor (trypsin)]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:52:15 2008'' | ||
Revision as of 17:52, 21 February 2008
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DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF THE TRYPSIN INHIBITOR FROM SQUASH SEEDS IN AQUEOUS SOLUTION BY NUCLEAR MAGNETIC RESONANCE AND A COMBINATION OF DISTANCE GEOMETRY AND DYNAMICAL SIMULATED ANNEALING
OverviewOverview
The complete three-dimensional structure of the trypsin inhibitor from seeds of the squash Cucurbita maxima in aqueous solution was determined on the basis of 324 interproton distance constraints, 80 non-nuclear Overhauser effect distances, and 22 hydrogen-bonding constraints, supplemented by 27 phi backbone angle constraints derived from nuclear magnetic resonance measurements. The nuclear magnetic resonance input data were converted to the distance constraints in a semiquantitative manner after a sequence specific assignment of 1H spectra was obtained using two-dimensional nuclear magnetic resonance techniques. Stereospecific assignments were obtained for 17 of the 48 prochiral centers of the squash trypsin inhibitor using the floating chirality assignment introduced at the dynamical simulated annealing stage of the calculations. A total of 34 structures calculated by a hybrid distance geometry-dynamical simulated annealing method exhibit well-defined positions for both backbone and side-chain atoms. The average atomic root-mean-square difference between the individual structures and the minimized mean structure is 0.35(+/- 0.08) A for the backbone atoms and 0.89(+/- 0.17) A for all heavy atoms. The precision of the structure determination is discussed and correlated to the experimental input data.
About this StructureAbout this Structure
2CTI is a Single protein structure of sequence from Cucurbita maxima. Full crystallographic information is available from OCA.
ReferenceReference
Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamical simulated annealing., Holak TA, Gondol D, Otlewski J, Wilusz T, J Mol Biol. 1989 Dec 5;210(3):635-48. PMID:2614837
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