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1omt

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(New page: 200px<br /><applet load="1omt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1omt" /> '''SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAI...)
Current revision (05:49, 17 April 2024) (edit) (undo)
 
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[[Image:1omt.gif|left|200px]]<br /><applet load="1omt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1omt" />
 
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'''SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAIN) FROM DOMESTIC TURKEY (298K, PH 4.1) (NMR, 50 STRUCTURES) (STANDARD NOESY ANALYSIS)'''<br />
 
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==Overview==
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==SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAIN) FROM DOMESTIC TURKEY (298K, PH 4.1) (NMR, 50 STRUCTURES) (STANDARD NOESY ANALYSIS)==
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Network-editing experiments are variants of the basic NOESY experiment, that allow more accurate direct measurement of interproton distances in, macromolecules by defeating specific spin-diffusion pathways. Two, network-editing approaches, block-decoupled NOESY and, complementary-block-decoupled-NOESY, were applied as three-dimensional, heteronuclear-edited experiments to distance measurement in a small, protein, turkey ovomucoid third domain (OMTKY3). Two-hundred and twelve of, the original 655 distance constraints observed in this molecule (Krezel AM, et al., 1994, J Mol Biol 242:203-214) were improved by their replacement, by distances derived from network-edited spectra, and distance, geometry/simulated annealing solution structure calculations were, performed from both the unimproved and improved distance sets. The, resulting two families of structures were found to differ significantly, the most important differences being the hinge angle of a beta-turn and an, expansion of the sampled conformation space in the region of the, reactive-site loop. The structures calculated from network-editing data, are interpreted as a more accurate model of the solution conformation of, OMTKY3.
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<StructureSection load='1omt' size='340' side='right'caption='[[1omt]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1omt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OMT FirstGlance]. <br>
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1OMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OMT OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1omt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omt OCA], [https://pdbe.org/1omt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1omt RCSB], [https://www.ebi.ac.uk/pdbsum/1omt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1omt ProSAT]</span></td></tr>
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==Reference==
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</table>
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Comparison of the accuracy of protein solution structures derived from conventional and network-edited NOESY data., Hoogstraten CG, Choe S, Westler WM, Markley JL, Protein Sci. 1995 Nov;4(11):2289-99. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8563625 8563625]
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== Function ==
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[https://www.uniprot.org/uniprot/IOVO_MELGA IOVO_MELGA]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/om/1omt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1omt ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Meleagris gallopavo]]
[[Category: Meleagris gallopavo]]
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[[Category: Single protein]]
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[[Category: Choe S]]
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[[Category: Choe, S.]]
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[[Category: Hoogstraten CG]]
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[[Category: Hoogstraten, C.G.]]
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[[Category: Markley JL]]
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[[Category: Markley, J.L.]]
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[[Category: Westler WM]]
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[[Category: Westler, W.M.]]
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[[Category: bd-noesy]]
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[[Category: cbd-noesy]]
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[[Category: network editing]]
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[[Category: spin diffusion]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:00:52 2007''
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Current revision

SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAIN) FROM DOMESTIC TURKEY (298K, PH 4.1) (NMR, 50 STRUCTURES) (STANDARD NOESY ANALYSIS)

PDB ID 1omt

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