Raw data for the figures of manuscript entitled Inherent backbone dynamics fine tune the functional plasticity of Tudor domains. A study by Ashish A. Kawale and Björn M. Burmann. Tudor domains are crucial for mediating a diversity of protein-protein or protein-DNA interactions involved in nucleic acid metabolism. Using solution NMR spectroscopy, here we assess the comprehensive understanding of the dynamical properties of the respective Tudor domains from four different bacterial (E. coli) proteins UvrD, Mfd, RfaH, NusG involved in different aspects of bacterial transcription regulation, like transcription antitermination, transcription–translation coupling, and the coupling of transcription to the nucleotide excision repair DNA repair pathway. These proteins are compared to the canonical Tudor domain fold from human SMN protein as a proxy. The detailed analysis of the protein backbone dynamics via longitudinal (R1), transverse (R2) relaxation rates along with 15N rotating-frame relaxation (R1) and steady state heteronuclear 15N1H}-NOE values of the backbone amide resonances and subsequent analysis by the Lipari-Szabo model-free approach, revealed subtle differences in the motions of the amide-bond vector on the pico- to nanosecond time scale. Our comparative approach revealed the usefulness of dynamics on these fast time scales to discern on a first glance different functionalities for Tudor domains exhibiting promiscuous binding and even more enhanced for a metamorphic Tudor domain included in the study. Our results highlight the importance of the dynamic properties of the Tudor domain in regards to its functional details. Details regarding data collection and processing are provided in detail in the respective manuscript's methods section.