Data for: Enhanced Spectral Density Mapping through Combined Multiple-Field Deuterium 13CH2D Methyl Spin Relaxation NMR Spectroscopy

Published: 2 January 2018| Version 1 | DOI: 10.17632/8hr4jb687t.1
Contributors:
Arthur Palmer,
Andrew Hsu,
Shibani Bhattacharya,
Mark Rance

Description

The two files contain the relaxation rate constants and experimental uncertainties in the relaxation rate constants (1 standard deviation) for deuterium relaxation measurements for 13CH2D methyl group isotopomers in E. coli ribonuclease H protein. The data are recorded at 298 K using 400, 500, 800, and 900 MHz NMR spectrometers. The relaxation measurements are R1, R2, RQ, and RAP, that is, the relaxation rate constants for longitudinal magnetization, transverse magnetization, quadrupolar order, and antiphase magnetization, respectively.

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Categories

Nuclear Magnetic Resonance Spectroscopy, Protein Dynamics

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