1pit: Difference between revisions

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-[[Image:1pit.gif|left|200px]]<br /><applet load="1pit" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1pit" />
-'''DETERMINATION OF A HIGH-QUALITY NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF THE BOVINE PANCREATIC TRYPSIN INHIBITOR AND COMPARISON WITH THREE CRYSTAL STRUCTURES'''<br />
-==Overview==
+==DETERMINATION OF A HIGH-QUALITY NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF THE BOVINE PANCREATIC TRYPSIN INHIBITOR AND COMPARISON WITH THREE CRYSTAL STRUCTURES==
-A high-quality three-dimensional structure of the bovine pancreatic, trypsin inhibitor (BPTI) in aqueous solution was determined by 1H nuclear, magnetic resonance (n.m.r.) spectroscopy and compared to the three, available high-resolution X-ray crystal structures. A newly collected, input of 642 distance constraints derived from nuclear Overhauser effects, and 115 dihedral angle constraints was used for the structure calculations, with the program DIANA, followed by restrained energy minimization with, the program AMBER. The BPTI solution structure is represented by a group, of 20 conformers with an average root-mean-square deviation (RMSD), relative to the mean solution structure of 0.43 A for backbone atoms and, 0.92 A for all heavy atoms of residues 2 to 56. The pairwise RMSD values, of the three crystal structures relative to the mean solution structure, are 0.76 to 0.85 A for the backbone atoms and 1.24 to 1.33 A for all heavy, atoms of residues 2 to 56. Small local differences in backbone atom, positions between the solution structure and the X-ray structures near, residues 9, 25 to 27, 46 to 48 and 52 to 58, and conformational, differences for individual amino acid side-chains were analyzed for, possible correlations with intermolecular protein-protein contacts in the, crystal lattices, using the pairwise RMSD values among the three crystal, structures as a reference.
+<StructureSection load='1pit' size='340' side='right'caption='[[1pit]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1pit]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PIT FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1pit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pit OCA], [https://pdbe.org/1pit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pit RCSB], [https://www.ebi.ac.uk/pdbsum/1pit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pit ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/BPT1_BOVIN BPT1_BOVIN] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.
+== 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/pi/1pit_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=1pit ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A high-quality three-dimensional structure of the bovine pancreatic trypsin inhibitor (BPTI) in aqueous solution was determined by 1H nuclear magnetic resonance (n.m.r.) spectroscopy and compared to the three available high-resolution X-ray crystal structures. A newly collected input of 642 distance constraints derived from nuclear Overhauser effects and 115 dihedral angle constraints was used for the structure calculations with the program DIANA, followed by restrained energy minimization with the program AMBER. The BPTI solution structure is represented by a group of 20 conformers with an average root-mean-square deviation (RMSD) relative to the mean solution structure of 0.43 A for backbone atoms and 0.92 A for all heavy atoms of residues 2 to 56. The pairwise RMSD values of the three crystal structures relative to the mean solution structure are 0.76 to 0.85 A for the backbone atoms and 1.24 to 1.33 A for all heavy atoms of residues 2 to 56. Small local differences in backbone atom positions between the solution structure and the X-ray structures near residues 9, 25 to 27, 46 to 48 and 52 to 58, and conformational differences for individual amino acid side-chains were analyzed for possible correlations with intermolecular protein-protein contacts in the crystal lattices, using the pairwise RMSD values among the three crystal structures as a reference.
-==About this Structure==
+Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures.,Berndt KD, Guntert P, Orbons LP, Wuthrich K J Mol Biol. 1992 Oct 5;227(3):757-75. PMID:1383552<ref>PMID:1383552</ref>
-PIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PIT OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures., Berndt KD, Guntert P, Orbons LP, Wuthrich K, J Mol Biol. 1992 Oct 5;227(3):757-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1383552 1383552]
+</div>
+<div class="pdbe-citations 1pit" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[BPTI 3D structures|BPTI 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Bos taurus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Berndt, K.D.]]
+[[Category: Berndt KD]]
-[[Category: Guntert, P.]]
+[[Category: Guntert P]]
-[[Category: Orbons, L.P.M.]]
+[[Category: Orbons LPM]]
-[[Category: Wuthrich, K.]]
+[[Category: Wuthrich K]]
-[[Category: proteinase inhibitor(trypsin)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:50:56 2007''