1i6m

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(New page: 200px<br /><applet load="1i6m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i6m, resolution 1.72&Aring;" /> '''1.7 HIGH RESOLUTION ...)
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[[Image:1i6m.jpg|left|200px]]<br /><applet load="1i6m" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1i6m, resolution 1.72&Aring;" />
 
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'''1.7 HIGH RESOLUTION EXPERIMENTAL PHASES FOR TRYPTOPHANYL-TRNA SYNTHETASE COMPLEXED WITH TRYPTOPHANYL-5'AMP'''<br />
 
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==Overview==
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==1.7 HIGH RESOLUTION EXPERIMENTAL PHASES FOR TRYPTOPHANYL-TRNA SYNTHETASE COMPLEXED WITH TRYPTOPHANYL-5'AMP==
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Native data, anomalous data at three wavelengths and an independent, peak-wavelength data set for SeMet-substituted protein have been collected, from cryoprotected crystals of the TrpRS-adenylate product (TAM) complex, to a resolution limit of 1.7 A. Independent phase sets were developed, using SHARP and improved by solvent flipping with SOLOMON using molecular, envelopes derived from experimental densities for, respectively, peak-wavelength SAD data from four different crystals, MAD data and their, M(S)IRAS combinations with native data. Hendrickson-Lattman, phase-probability coefficients from each phase set were used in BUSTER to, drive maximum-likelihood refinements of well defined parts of the, previously refined room-temperature 2.9 A structure. Maximum-entropy, completion followed by manual rebuilding was then used to generate a model, for the missing segments, bound ligand and solvent molecules., Surprisingly, peak-wavelength SAD experiments produced the smallest phase, errors relative to the refined structures. Selenomethionylated models, deviate from one another by 0.25 A and from the native model by 0.38 A, but all have r.m.s. deviations of approximately 1.0 A from the 2.9 A, model. Difference Fourier calculations between amplitudes from the 300 K, experiment and the new amplitudes at 100 K using 1.7 A model phases show, no significant structural changes arising from temperature variation or, addition of cryoprotectant. The main differences between low- and, high-resolution structures arise from correcting side-chain rotamers in, the core of the protein as well as on the surface. These changes improve, various structure-validation criteria.
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<StructureSection load='1i6m' size='340' side='right'caption='[[1i6m]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1i6m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I6M FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TYM:TRYPTOPHANYL-5AMP'>TYM</scene></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=1i6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i6m OCA], [https://pdbe.org/1i6m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i6m RCSB], [https://www.ebi.ac.uk/pdbsum/1i6m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i6m ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYW_GEOSE SYW_GEOSE]
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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/i6/1i6m_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=1i6m ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1I6M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with SO4, NH4, TYM and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Tryptophan--tRNA_ligase Tryptophan--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.2 6.1.1.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I6M OCA].
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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High-resolution experimental phases for tryptophanyl-tRNA synthetase (TrpRS) complexed with tryptophanyl-5'AMP., Retailleau P, Yin Y, Hu M, Roach J, Bricogne G, Vonrhein C, Roversi P, Blanc E, Sweet RM, Carter CW Jr, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1595-608. Epub, 2001 Oct 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11679724 11679724]
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Tryptophan--tRNA ligase]]
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[[Category: Carter CW]]
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[[Category: Carter, C.W.]]
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[[Category: Retailleau P]]
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[[Category: Retailleau, P.]]
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[[Category: GOL]]
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[[Category: NH4]]
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[[Category: SO4]]
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[[Category: TYM]]
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[[Category: aars]]
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[[Category: class i trna synthetase]]
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[[Category: induced fit]]
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[[Category: trprs]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:06:01 2007''
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Current revision

1.7 HIGH RESOLUTION EXPERIMENTAL PHASES FOR TRYPTOPHANYL-TRNA SYNTHETASE COMPLEXED WITH TRYPTOPHANYL-5'AMP

PDB ID 1i6m

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