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dc.contributor.authorSchiffer, Celia A.
dc.contributor.authorHuber, Robert
dc.contributor.authorWuthrich, Kurt
dc.contributor.authorvan Gunsteren, Wilfred F.
dc.date2022-08-11T08:08:00.000
dc.date.accessioned2022-08-23T15:38:37Z
dc.date.available2022-08-23T15:38:37Z
dc.date.issued1994-08-26
dc.date.submitted2010-02-05
dc.identifier.citationJ Mol Biol. 1994 Aug 26;241(4):588-99. <a href="http://dx.doi.org/10.1006/jmbi.1994.1533">Link to article on publisher's site</a>
dc.identifier.issn0022-2836 (Print)
dc.identifier.doi10.1006/jmbi.1994.1533
dc.identifier.pmid7520085
dc.identifier.urihttp://hdl.handle.net/20.500.14038/25972
dc.description.abstractThe structure of the bovine pancreatic trypsin inhibitor (BPTI) has been determined to high resolution by both NMR spectroscopy in solution and X-ray diffraction in crystals. The root-mean-square difference calculated between the two structures for the polypeptide backbone is 0.9 A. Several amino acid side-chains, of which all but one are charged or polar, have different conformations. We find that by refining one structure simultaneously against both the NMR and crystallographic data sets, it can accommodate both. Different starting configurations were used, including the X-ray structure 5pti, an NMR conformer, and the X-ray structure in the full unit cell with extra solvent placed in the bulk solvent region. The X-ray structures quickly converged to accommodate the NMR data in addition to the crystallographic data. Starting from an NMR conformer, however, the convergence to accommodate the more abundant X-ray data in addition to the NMR data is much slower.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=7520085&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1006/jmbi.1994.1533
dc.subjectAmino Acid Sequence
dc.subjectAprotinin
dc.subjectCrystallography, X-Ray
dc.subjectMagnetic Resonance Spectroscopy
dc.subjectModels, Chemical
dc.subjectMolecular Sequence Data
dc.subjectProtein Conformation
dc.subjectSolutions
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectPharmacology, Toxicology and Environmental Health
dc.titleSimultaneous refinement of the structure of BPTI against NMR data measured in solution and X-ray diffraction data measured in single crystals
dc.typeJournal Article
dc.source.journaltitleJournal of molecular biology
dc.source.volume241
dc.source.issue4
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/bmp_pp/100
dc.identifier.contextkey1134073
html.description.abstract<p>The structure of the bovine pancreatic trypsin inhibitor (BPTI) has been determined to high resolution by both NMR spectroscopy in solution and X-ray diffraction in crystals. The root-mean-square difference calculated between the two structures for the polypeptide backbone is 0.9 A. Several amino acid side-chains, of which all but one are charged or polar, have different conformations. We find that by refining one structure simultaneously against both the NMR and crystallographic data sets, it can accommodate both. Different starting configurations were used, including the X-ray structure 5pti, an NMR conformer, and the X-ray structure in the full unit cell with extra solvent placed in the bulk solvent region. The X-ray structures quickly converged to accommodate the NMR data in addition to the crystallographic data. Starting from an NMR conformer, however, the convergence to accommodate the more abundant X-ray data in addition to the NMR data is much slower.</p>
dc.identifier.submissionpathbmp_pp/100
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages588-99


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