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New page: left|200px<br /><applet load="1ejg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ejg, resolution 0.54Å" /> '''CRAMBIN AT ULTRA-HIG... |
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== | ==CRAMBIN AT ULTRA-HIGH RESOLUTION: VALENCE ELECTRON DENSITY.== | ||
The charge density distribution of a protein has been refined | <StructureSection load='1ejg' size='340' side='right'caption='[[1ejg]], [[Resolution|resolution]] 0.54Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ejg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EJG FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.54Å</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=1ejg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ejg OCA], [https://pdbe.org/1ejg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ejg RCSB], [https://www.ebi.ac.uk/pdbsum/1ejg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ejg ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CRAM_CRAAB CRAM_CRAAB] The function of this hydrophobic plant seed protein is not known. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ej/1ejg_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1ejg ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The charge density distribution of a protein has been refined experimentally. Diffraction data for a crambin crystal were measured to ultra-high resolution (0.54 A) at low temperature by using short-wavelength synchrotron radiation. The crystal structure was refined with a model for charged, nonspherical, multipolar atoms to accurately describe the molecular electron density distribution. The refined parameters agree within 25% with our transferable electron density library derived from accurate single crystal diffraction analyses of several amino acids and small peptides. The resulting electron density maps of redistributed valence electrons (deformation maps) compare quantitatively well with a high-level quantum mechanical calculation performed on a monopeptide. This study provides validation for experimentally derived parameters and a window into charge density analysis of biological macromolecules. | |||
Accurate protein crystallography at ultra-high resolution: valence electron distribution in crambin.,Jelsch C, Teeter MM, Lamzin V, Pichon-Pesme V, Blessing RH, Lecomte C Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3171-6. PMID:10737790<ref>PMID:10737790</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ejg" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Crambe hispanica subsp. abyssinica]] | [[Category: Crambe hispanica subsp. abyssinica]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Blessing | [[Category: Blessing B]] | ||
[[Category: Jelsch | [[Category: Jelsch C]] | ||
[[Category: Lamzin | [[Category: Lamzin V]] | ||
[[Category: Lecomte | [[Category: Lecomte C]] | ||
[[Category: Pichon-Lesme | [[Category: Pichon-Lesme V]] | ||
[[Category: Teeter | [[Category: Teeter MM]] | ||
Latest revision as of 09:34, 30 October 2024
CRAMBIN AT ULTRA-HIGH RESOLUTION: VALENCE ELECTRON DENSITY.CRAMBIN AT ULTRA-HIGH RESOLUTION: VALENCE ELECTRON DENSITY.
Structural highlights
FunctionCRAM_CRAAB The function of this hydrophobic plant seed protein is not known. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe charge density distribution of a protein has been refined experimentally. Diffraction data for a crambin crystal were measured to ultra-high resolution (0.54 A) at low temperature by using short-wavelength synchrotron radiation. The crystal structure was refined with a model for charged, nonspherical, multipolar atoms to accurately describe the molecular electron density distribution. The refined parameters agree within 25% with our transferable electron density library derived from accurate single crystal diffraction analyses of several amino acids and small peptides. The resulting electron density maps of redistributed valence electrons (deformation maps) compare quantitatively well with a high-level quantum mechanical calculation performed on a monopeptide. This study provides validation for experimentally derived parameters and a window into charge density analysis of biological macromolecules. Accurate protein crystallography at ultra-high resolution: valence electron distribution in crambin.,Jelsch C, Teeter MM, Lamzin V, Pichon-Pesme V, Blessing RH, Lecomte C Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3171-6. PMID:10737790[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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