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Quantum chemical 13C(alpha) chemical shift calculations for protein NMR structure determination, refinement, and validation.

Vila JA, Aramini JM, Rossi P, Kuzin A, Su M, Seetharaman J, Xiao R, Tong L, Montelione GT, Scheraga HA,
Proceedings of the National Academy of Sciences of the United States of America (2008) 105:14389-94 PublishedPSI:Phase 2  
Northeast Structural Genomics Consortium

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A recently determined set of 20 NMR-derived conformations of a 48-residue all-alpha-helical protein, (PDB ID code 2JVD), is validated here by comparing the observed (13)C(alpha) chemical shifts with those computed at the density functional level of theory. ...
Crystallography, X-Ray Protein Structure, Tertiary Hydrogen Bonding Models, Molecular Bacterial Proteins Nuclear Magnetic Resonance, Biomolecular Carbon Isotopes Bacillus subtilis Reproducibility of Results Torsion, Mechanical 
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Quantum-Mechanics-Derived 13Cα Chemical Shifts for Protein Structure Validation
Quantum-mechanics-derived 13Cα chemical shifts for protein structure validation