This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1omt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:49, 17 April 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1omt.gif|left|200px]]
 
-
{{Structure
+
==SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAIN) FROM DOMESTIC TURKEY (298K, PH 4.1) (NMR, 50 STRUCTURES) (STANDARD NOESY ANALYSIS)==
-
|PDB= 1omt |SIZE=350|CAPTION= <scene name='initialview01'>1omt</scene>
+
<StructureSection load='1omt' size='340' side='right'caption='[[1omt]]' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<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>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
|GENE=
+
<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>
-
|DOMAIN=
+
</table>
-
|RELATEDENTRY=
+
== Function ==
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1omt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omt OCA], [http://www.ebi.ac.uk/pdbsum/1omt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1omt RCSB]</span>
+
[https://www.uniprot.org/uniprot/IOVO_MELGA IOVO_MELGA]
-
}}
+
== Evolutionary Conservation ==
-
 
+
[[Image:Consurf_key_small.gif|200px|right]]
-
'''SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAIN) FROM DOMESTIC TURKEY (298K, PH 4.1) (NMR, 50 STRUCTURES) (STANDARD NOESY ANALYSIS)'''
+
Check<jmol>
-
 
+
<jmolCheckbox>
-
 
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/om/1omt_consurf.spt"</scriptWhenChecked>
-
==Overview==
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
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.
+
<text>to colour the structure by Evolutionary Conservation</text>
-
 
+
</jmolCheckbox>
-
==About this Structure==
+
</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].
-
1OMT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMT OCA].
+
<div style="clear:both"></div>
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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://www.ncbi.nlm.nih.gov/pubmed/8563625 8563625]
+
[[Category: Large Structures]]
[[Category: Meleagris gallopavo]]
[[Category: Meleagris gallopavo]]
-
[[Category: Single protein]]
+
[[Category: Choe S]]
-
[[Category: Choe, S.]]
+
[[Category: Hoogstraten CG]]
-
[[Category: Hoogstraten, C G.]]
+
[[Category: Markley JL]]
-
[[Category: Markley, J L.]]
+
[[Category: Westler WM]]
-
[[Category: Westler, W M.]]
+
-
[[Category: bd-noesy]]
+
-
[[Category: cbd-noesy]]
+
-
[[Category: network editing]]
+
-
[[Category: spin diffusion]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:47:27 2008''
+

Current revision

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

PDB ID 1omt

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1omt"
Personal tools