Literature DB >> 12766419

Rapid and accurate calculation of protein 1H, 13C and 15N chemical shifts.

Stephen Neal1, Alex M Nip, Haiyan Zhang, David S Wishart.   

Abstract

A computer program (SHIFTX) is described which rapidly and accurately calculates the diamagnetic 1H, 13C and 15N chemical shifts of both backbone and sidechain atoms in proteins. The program uses a hybrid predictive approach that employs pre-calculated, empirically derived chemical shift hypersurfaces in combination with classical or semi-classical equations (for ring current, electric field, hydrogen bond and solvent effects) to calculate 1H, 13C and 15N chemical shifts from atomic coordinates. The chemical shift hypersurfaces capture dihedral angle, sidechain orientation, secondary structure and nearest neighbor effects that cannot easily be translated to analytical formulae or predicted via classical means. The chemical shift hypersurfaces were generated using a database of IUPAC-referenced protein chemical shifts--RefDB (Zhang et al., 2003), and a corresponding set of high resolution (<2.1 A) X-ray structures. Data mining techniques were used to extract the largest pairwise contributors (from a list of approximately 20 derived geometric, sequential and structural parameters) to generate the necessary hypersurfaces. SHIFTX is rapid (<1 CPU second for a complete shift calculation of 100 residues) and accurate. Overall, the program was able to attain a correlation coefficient (r) between observed and calculated shifts of 0.911 (1Halpha), 0.980 (13Calpha), 0.996 (13Cbeta), 0.863 (13CO), 0.909 (15N), 0.741 (1HN), and 0.907 (sidechain 1H) with RMS errors of 0.23, 0.98, 1.10, 1.16, 2.43, 0.49, and 0.30 ppm, respectively on test data sets. We further show that the agreement between observed and SHIFTX calculated chemical shifts can be an extremely sensitive measure of the quality of protein structures. Our results suggest that if NMR-derived structures could be refined using heteronuclear chemical shifts calculated by SHIFTX, their precision could approach that of the highest resolution X-ray structures. SHIFTX is freely available as a web server at http://redpoll.pharmacy.ualberta.ca.

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Year:  2003        PMID: 12766419     DOI: 10.1023/a:1023812930288

Source DB:  PubMed          Journal:  J Biomol NMR        ISSN: 0925-2738            Impact factor:   2.835


  38 in total

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2.  RefDB: a database of uniformly referenced protein chemical shifts.

Authors:  Haiyan Zhang; Stephen Neal; David S Wishart
Journal:  J Biomol NMR       Date:  2003-03       Impact factor: 2.835

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Journal:  J Biomol NMR       Date:  1995-09       Impact factor: 2.835

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  217 in total

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Authors:  Yunjun Wang; Godwin Amegbey; David S Wishart
Journal:  J Biomol NMR       Date:  2004-05       Impact factor: 2.835

2.  Predicting 15N chemical shifts in proteins using the preceding residue-specific individual shielding surfaces from phi, psi i-1, and chi 1 torsion angles.

Authors:  Yunjun Wang; Oleg Jardetzky
Journal:  J Biomol NMR       Date:  2004-04       Impact factor: 2.835

3.  Uncovering symmetry-breaking vector and reliability order for assigning secondary structures of proteins from atomic NMR chemical shifts in amino acids.

Authors:  Wookyung Yu; Woonghee Lee; Weontae Lee; Suhkmann Kim; Iksoo Chang
Journal:  J Biomol NMR       Date:  2011-10-30       Impact factor: 2.835

4.  VITAL NMR: using chemical shift derived secondary structure information for a limited set of amino acids to assess homology model accuracy.

Authors:  Michael C Brothers; Anna E Nesbitt; Michael J Hallock; Sanjeewa G Rupasinghe; Ming Tang; Jason Harris; Jerome Baudry; Mary A Schuler; Chad M Rienstra
Journal:  J Biomol NMR       Date:  2011-11-03       Impact factor: 2.835

5.  Resolution-by-proxy: a simple measure for assessing and comparing the overall quality of NMR protein structures.

Authors:  Mark Berjanskii; Jianjun Zhou; Yongjie Liang; Guohui Lin; David S Wishart
Journal:  J Biomol NMR       Date:  2012-06-08       Impact factor: 2.835

Review 6.  Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins.

Authors:  Hazime Saitô; Isao Ando; Ayyalusamy Ramamoorthy
Journal:  Prog Nucl Magn Reson Spectrosc       Date:  2010-05-07       Impact factor: 9.795

7.  Mapping of protein structural ensembles by chemical shifts.

Authors:  Kumaran Baskaran; Konrad Brunner; Claudia E Munte; Hans Robert Kalbitzer
Journal:  J Biomol NMR       Date:  2010-08-01       Impact factor: 2.835

8.  A probabilistic approach for validating protein NMR chemical shift assignments.

Authors:  Bowei Wang; Yunjun Wang; David S Wishart
Journal:  J Biomol NMR       Date:  2010-05-06       Impact factor: 2.835

9.  Arginine kinase: joint crystallographic and NMR RDC analyses link substrate-associated motions to intrinsic flexibility.

Authors:  Xiaogang Niu; Lei Bruschweiler-Li; Omar Davulcu; Jack J Skalicky; Rafael Brüschweiler; Michael S Chapman
Journal:  J Mol Biol       Date:  2010-11-12       Impact factor: 5.469

10.  Application of the random coil index to studying protein flexibility.

Authors:  Mark V Berjanskii; David S Wishart
Journal:  J Biomol NMR       Date:  2007-11-06       Impact factor: 2.835

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