1H, 13C, 15N backbone chemical shift assignments of the extended ARID domain in human AT-rich interactive domain protein 5a (Arid5a)

Figures

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  Fig. 1. Constructs of Arid5a used in this study. a Sequence of Arid5a 37-183 numbered according to Uniprot entry Q03989. Non-native amino acids “GAMA” at the N-terminus are colored in gray. Red, orange and turquoise coloring of sequence corresponds to constructs in b Scheme of the four Arid5a constructs used in this study with their ARID core domain and extending IDRs (black lines). Respective molecular weights are shown on the right. c Overlay of 1H, 15N-HSQC spectra of the four Arid5a constructs. The spectrum of 37–183 is shifted slightly to the right for better visibility. Spectra are colored according to b. d Shift distance plots for the ARID between residues 49-152 of the three extended constructs (color-coded as in b) versus the core-construct (49-152). CSPs have been calculated in CCPNMR Analysis 2.5.2 (Vranken et al. 2005) with default settings

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  Fig. 2. 1H, 15N-HSQC-spectra of the 15N-labelled Arid5a 49-152 (a) and 37-183 (b) ARID domain constructs at 0.33 and 0.35 mM concentration, respectively, in 20 mM Bis-Tris pH 6.5, 150 mM NaCl, 2 mM TCEP, 0.02% NaN3, 5% (v/v) D2O collected at 298 K on a 600 MHz Bruker Avance III HD spectrometer equipped with a triple-resonance QCl cryogenic probe. Straight lines indicate side chain amide pairs. Tryptophan side chain amides are indicated with ε. Zoom-ins of spectral regions in boxes 1 and 2 are shown for clarity

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  Fig. 3. Display of {1H}-15 N heteronuclear NOE values (a) and combined Cα/Cβ carbon secondary chemical shift (SCS) values of Arid5a 37-183 plotted against the primary protein sequence as described by (Metzler et al. 1993) (b). a hetNOE values are shown with errors as derived from the program CCPNMR Analysis 2.5.2 (Vranken et al. 2005). Pentagons indicate prolines, and triangles indicate unassigned amino acid amides. b SCS for Arid5a ARID are shown with their interpreted secondary structure (shown above). α-helices are marked H1-H6 and indicated by gray bars above the SCS values and primary sequence. Loops L1 and L2 are shown for orientation