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Complete ¹H, ¹³C, ¹⁵N resonance assignments and secondary structure of the Vpr binding region of hHR23A (residues 223-363).

ABSTRACT: Comprehensive resonance assignments and delineation of the secondary structure elements of the C-terminal Vpr-binding region of hHR23A, residues 223-363, were achieved by triple-resonance NMR experiments on uniformly ¹³C,¹⁵N-labeled protein. Assignments are 100% and > 95% complete for backbone and side-chain resonances, respectively. This data constitutes important complementary information for our ongoing structure determination of the Vpr-hHR23A(223-363) complex. At high concentrations, severe line-broadening was observed for several residues in the ¹H-¹⁵N HSQC spectrum, most likely resulting from inter-molecular interactions.

SUBMITTER: Byeon IL

PROVIDER: S-EPMC7047585 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature

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Complete 1H, 13C, 15N resonance assignments and secondary structure of the Vpr binding region of hHR23A (residues 223-363).

Byeon In-Ja L IL Jung Jinwon J Byeon Chang H CH DeLucia Maria M Ahn Jinwoo J Gronenborn Angela M AM

Biomolecular NMR assignments 20190828 1

Comprehensive resonance assignments and delineation of the secondary structure elements of the C-terminal Vpr-binding region of hHR23A, residues 223-363, were achieved by triple-resonance NMR experiments on uniformly 13C,15N-labeled protein. Assignments are 100% and > 95% complete for backbone and side-chain resonances, respectively. This data constitutes important complementary information for our ongoing structure determination of the Vpr-hHR23A(223-363) complex. At high ...[more]

PMID: 31463759

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