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    Simultaneous refinement of the structure of BPTI against NMR data measured in solution and X-ray diffraction data measured in single crystals

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    Authors
    Schiffer, Celia A.
    Huber, Robert
    Wuthrich, Kurt
    van Gunsteren, Wilfred F.
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Document Type
    Journal Article
    Publication Date
    1994-08-26
    Keywords
    Amino Acid Sequence
    Aprotinin
    Crystallography, X-Ray
    Magnetic Resonance Spectroscopy
    Models, Chemical
    Molecular Sequence Data
    Protein Conformation
    Solutions
    Biochemistry, Biophysics, and Structural Biology
    Pharmacology, Toxicology and Environmental Health
    
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    Link to Full Text
    http://dx.doi.org/10.1006/jmbi.1994.1533
    Abstract
    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.
    Source
    J Mol Biol. 1994 Aug 26;241(4):588-99. Link to article on publisher's site
    DOI
    10.1006/jmbi.1994.1533
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/25972
    PubMed ID
    7520085
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1006/jmbi.1994.1533
    Scopus Count
    Collections
    UMass Chan Faculty and Researcher Publications
    Schiffer Lab Publications

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