1ejg

<StructureSection load='1ejg' size='340' side='right' caption='[[1ejg]], [[Resolution|resolution]] 0.54&Aring;' scene=''>

<table><tr><td colspan='2'>[[1ejg]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EJG FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cbn|1cbn]], [[1crn|1crn]], [[1ab1|1ab1]], [[1cnr|1cnr]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ejg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ejg OCA], [http://pdbe.org/1ejg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ejg RCSB], [http://www.ebi.ac.uk/pdbsum/1ejg PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/CRAM_CRAAB CRAM_CRAAB]] The function of this hydrophobic plant seed protein is not known.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ej/1ejg_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ejg" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Blessing, B]]

[[Category: Jelsch, C]]

[[Category: Lamzin, V]]

[[Category: Lecomte, C]]

[[Category: Pichon-Lesme, V]]

[[Category: Teeter, M M]]

[[Category: Valence electron density]]