Protein structure determination from pseudocontact shifts using ROSETTA.
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David Baker | Thomas Huber | Gottfried Otting | D. Baker | R. Vernon | G. Otting | T. Huber | C. Schmitz | Christophe Schmitz | Robert Vernon
[1] R. Schaaper,et al. Nuclear Magnetic Resonance Solution Structure of the Escherichia coli DNA Polymerase III θ Subunit , 2005 .
[2] Thomas Huber,et al. DOTA-amide lanthanide tag for reliable generation of pseudocontact shifts in protein NMR spectra. , 2011, Bioconjugate chemistry.
[3] N. Dixon,et al. Structure determination of protein-ligand complexes by transferred paramagnetic shifts. , 2006, Journal of the American Chemical Society.
[4] K. Wüthrich. NMR of proteins and nucleic acids , 1988 .
[5] Oliver F. Lange,et al. Structure prediction for CASP8 with all‐atom refinement using Rosetta , 2009, Proteins.
[6] Guido Pintacuda,et al. Lanthanide labeling offers fast NMR approach to 3D structure determinations of protein-protein complexes. , 2006, Journal of the American Chemical Society.
[7] N. Dixon,et al. Efficient χ-tensor determination and NH assignment of paramagnetic proteins , 2006, Journal of biomolecular NMR.
[8] F. Richards,et al. NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteriation. , 1988, Biochemistry.
[9] Hilla Peretz,et al. Ju n 20 03 Schrödinger ’ s Cat : The rules of engagement , 2003 .
[10] Ivano Bertini,et al. Magnetic susceptibility in paramagnetic NMR , 2002 .
[11] G. Otting,et al. 4,4'-dithiobisdipicolinic acid: a small and convenient lanthanide binding tag for protein NMR spectroscopy. , 2011, Chemistry.
[12] V. Gaponenko,et al. Improving the Accuracy of NMR Structures of Large Proteins Using Pseudocontact Shifts as Long-Range Restraints , 2004, Journal of biomolecular NMR.
[13] P. Keizers,et al. A solution model of the complex formed by adrenodoxin and adrenodoxin reductase determined by paramagnetic NMR spectroscopy. , 2010, Biochemistry.
[14] Guido Pintacuda,et al. NMR structure determination of protein-ligand complexes by lanthanide labeling. , 2007, Accounts of chemical research.
[15] G. Otting,et al. [Ln(DPA)(3)](3-) is a convenient paramagnetic shift reagent for protein NMR studies. , 2009, Journal of the American Chemical Society.
[16] M. Piccioli,et al. Assignment Strategy for Fast Relaxing Signals: Complete Aminoacid Identification in Thulium Substituted Calbindin D9K , 2006, Journal of biomolecular NMR.
[17] Oliver F. Lange,et al. Consistent blind protein structure generation from NMR chemical shift data , 2008, Proceedings of the National Academy of Sciences.
[18] K. Ogura,et al. Two-point anchoring of a lanthanide-binding peptide to a target protein enhances the paramagnetic anisotropic effect , 2009, Journal of biomolecular NMR.
[19] G. Otting,et al. 3-Mercapto-2,6-pyridinedicarboxylic acid: a small lanthanide-binding tag for protein studies by NMR spectroscopy. , 2010, Chemistry.
[20] J. Hus,et al. De novo determination of protein structure by NMR using orientational and long-range order restraints. , 2000, Journal of molecular biology.
[21] M. Ubbink,et al. The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics. , 1998, Structure.
[22] I. Bertini,et al. Paramagnetism-based versus classical constraints: An analysis of the solution structure of Ca Ln calbindin D9k , 2001, Journal of biomolecular NMR.
[23] T. Darden,et al. Model for the catalytic domain of the proofreading epsilon subunit of Escherichia coli DNA polymerase III based on NMR structural data. , 2002, Biochemistry.
[24] Ad Bax,et al. Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase , 1998 .
[25] H. Gray,et al. Pseudocontact shifts as constraints for energy minimization and molecular dynamics calculations on solution structures of paramagnetic metalloproteins , 1997, Proteins.
[26] David Baker,et al. Improved beta‐protein structure prediction by multilevel optimization of nonlocal strand pairings and local backbone conformation , 2006, Proteins.
[27] A. Bax,et al. Protein backbone angle restraints from searching a database for chemical shift and sequence homology , 1999, Journal of biomolecular NMR.
[28] P. Keizers,et al. Paramagnetic tagging for protein structure and dynamics analysis. , 2011, Progress in nuclear magnetic resonance spectroscopy.
[29] Thomas Szyperski,et al. NMR Structure Determination for Larger Proteins Using Backbone-Only Data , 2010, Science.
[30] P. Bradley,et al. High-resolution structure prediction and the crystallographic phase problem , 2007, Nature.
[31] H. Dyson,et al. Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxin , 1991, FEBS letters.
[32] C Venclovas,et al. Processing and analysis of CASP3 protein structure predictions , 1999, Proteins.
[33] Andrea Giachetti,et al. Paramagnetism-Based Restraints for Xplor-NIH , 2004, Journal of biomolecular NMR.
[34] G. Otting,et al. A dipicolinic acid tag for rigid lanthanide tagging of proteins and paramagnetic NMR spectroscopy. , 2008, Journal of the American Chemical Society.
[35] P. Bradley,et al. Toward High-Resolution de Novo Structure Prediction for Small Proteins , 2005, Science.
[36] G. Otting,et al. Paramagnetic labelling of proteins and oligonucleotides for NMR , 2010, Journal of biomolecular NMR.
[37] I. Bertini,et al. Accurate solution structures of proteins from X-ray data and a minimal set of NMR data: calmodulin-peptide complexes as examples. , 2009, Journal of the American Chemical Society.
[38] Antonio Rosato,et al. CASD-NMR: critical assessment of automated structure determination by NMR , 2009, Nature Methods.
[39] J. Prestegard,et al. Structure determination of a Galectin‐3–carbohydrate complex using paramagnetism‐based NMR constraints , 2008, Protein science : a publication of the Protein Society.
[40] G. Otting,et al. Numbat: an interactive software tool for fitting Δχ-tensors to molecular coordinates using pseudocontact shifts , 2008, Journal of biomolecular NMR.
[41] David J Wilton,et al. Pressure‐induced changes in the solution structure of the GB1 domain of protein G , 2007, Proteins.
[42] L. Banci,et al. NMR structures of paramagnetic metalloproteins , 2005, Quarterly Reviews of Biophysics.
[43] R J Read,et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. , 1998, Acta crystallographica. Section D, Biological crystallography.
[44] C. D. Barry,et al. Quantitative Determination of Mononucleotide Conformations in Solution using Lanthanide Ion Shift and Broadening NMR Probes , 1971, Nature.
[45] Cristina Del Bianco,et al. Paramagnetism-based refinement strategy for the solution structure of human alpha-parvalbumin. , 2004, Biochemistry.
[46] C Kooperberg,et al. Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions. , 1997, Journal of molecular biology.
[47] Ivano Bertini,et al. Experimentally exploring the conformational space sampled by domain reorientation in calmodulin. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[48] K. Wüthrich,et al. PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics , 1998, Journal of biomolecular NMR.
[49] I. Bertini,et al. Efficiency of paramagnetism-based constraints to determine the spatial arrangement of α-helical secondary structure elements , 2002, Journal of biomolecular NMR.