Biomolecular NMR Assignments

, Volume 13, Issue 1, pp 115–119 | Cite as

Sequential backbone resonance assignment of AT-rich interaction domain of human BAF200

  • Abhishek Bastiray
  • Malyasree Giri
  • Mahavir SinghEmail author


BAF200 is a subunit of PBAF chromatin remodeling complex that contains an N-terminal AT-rich interaction domain (ARID). ARID domain in general has been shown to bind to the AT-rich DNA sequences. The human BAF200 ARID (~ 110 residues) has the potential to bind the DNA sequences with high affinity, however, the structure and the exact contribution of hBAF200 ARID in PBAF functions as well its DNA binding specificities have not been established. In this study, we have expressed and purified the hBAF200 ARID for NMR studies. We report the complete backbone 1H, 13C, and 15N chemical shift assignment and secondary structure of hBAF200 ARID domain.


SWI/SNF complex hBAF200 ARID NMR Backbone assignment 



Authors would like to acknowledge Department of Science and Technology and Department of Biotechnology, India for the NMR facilities at the Indian Institute of Science. This work is supported by funding from Ramalingaswami Fellowship from Department of Biotechnology (DBT), India; and Early Career Award from Department of Science and Technology (DST), India [BT/RLF/Re-entry/23/2013; ECR/2015/000023 to M.S.]; and IISc-DBT Partnership program. M.G. would like to acknowledge Department of Science and Technology for the INSPIRE fellowship. Authors thank Prof. Siddhartha P. Sarma for help with NMR data acquisition.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.


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Copyright information

© Springer Nature B.V. 2018

Authors and Affiliations

  1. 1.Molecular Biophysics UnitIndian Institute of ScienceBengaluruIndia
  2. 2.Undergraduate DepartmentIndian Institute of ScienceBengaluruIndia
  3. 3.NMR Research CentreIndian Institute of ScienceBengaluruIndia

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