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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== | ||
<StructureSection load='2cti' size='340' side='right'caption='[[2cti]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2cti]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cucurbita_maxima Cucurbita maxima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CTI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CTI FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 5 models</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cti OCA], [https://pdbe.org/2cti PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cti RCSB], [https://www.ebi.ac.uk/pdbsum/2cti PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cti ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ITR1_CUCMA ITR1_CUCMA] Inhibits trypsin. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | 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. | ||
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<ref>PMID:2614837</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2cti" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cucurbita maxima]] | [[Category: Cucurbita maxima]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Gondol | [[Category: Gondol D]] | ||
[[Category: Holak | [[Category: Holak TA]] | ||
[[Category: Otlewski | [[Category: Otlewski J]] | ||
[[Category: Wilusz | [[Category: Wilusz T]] | ||
Latest revision as of 10:53, 30 October 2024
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 ANNEALINGDETERMINATION 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
Structural highlights
FunctionITR1_CUCMA Inhibits trypsin. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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