Accurate Backbone 13 C and 15 N Chemical Shift Tensors in Galectin-3 Determined by MAS NMR and QM/MM: Details of Structure and Environment Matter.,ChemPhysChem

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Accurate Backbone 13 C and 15 N Chemical Shift Tensors in Galectin-3 Determined by MAS NMR and QM/MM: Details of Structure and Environment Matter.
ChemPhysChem ( IF 2.3 ) Pub Date : 2020-06-04 , DOI: 10.1002/cphc.202000249
Jodi Kraus _{1,

2} , Rupal Gupta _{1,

3} , Manman Lu _{1,

2,

4} , Angela M Gronenborn _{2,

4} , Mikael Akke ₅ , Tatyana Polenova _{1,

2}

Affiliation

Chemical shift tensors obtained from solid‐state NMR spectroscopy are very sensitive reporters of structure and dynamics in proteins. While accurate ¹³C and ¹⁵N chemical shift tensors are accessible by magic angle spinning (MAS) NMR, their quantum mechanical calculations remain challenging, particularly for ¹⁵N atoms. Here we compare experimentally determined backbone ¹³C^α and ¹⁵N^H chemical shift tensors by MAS NMR with hybrid quantum mechanics/molecular mechanics/molecular dynamics (MD‐QM/MM) calculations for the carbohydrate‐binding domain of galectin‐3. Excellent agreement between experimental and computed ¹⁵N^H chemical shift anisotropy values was obtained using the Amber ff15ipq force field when solvent dynamics was taken into account in the calculation. Our results establish important benchmark conditions for improving the accuracy of chemical shift calculations in proteins and may aid in the validation of protein structure models derived by MAS NMR.

中文翻译：

通过 MAS NMR 和 QM/MM 测定 Galectin-3 中准确的主链 13 C 和 15 N 化学位移张量：结构和环境问题的详细信息。

从固态核磁共振波谱获得的化学位移张量是蛋白质结构和动力学的非常敏感的报告者。虽然可以通过魔角旋转 (MAS) NMR 获得准确的¹³ C 和¹⁵ N 化学位移张量，但它们的量子力学计算仍然具有挑战性，特别是对于¹⁵ N 原子。在这里，我们将通过 MAS NMR 实验确定的主链¹³ C ^α和¹⁵ N ^H化学位移张量与半乳糖凝集素 3 碳水化合物结合域的混合量子力学/分子力学/分子动力学 (MD-QM/MM) 计算进行比较。当计算中考虑溶剂动力学时，使用 Amber ff15ipq 力场获得了实验值和计算值之间的极好的¹⁵ N ^{H化学位移各向异性值。}我们的结果为提高蛋白质化学位移计算的准确性建立了重要的基准条件，并可能有助于验证由 MAS NMR 得出的蛋白质结构模型。

更新日期：2020-06-04

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