Chemical shifts and structural restraints for Saccharomyces cerevisiae Est3 protein

Proceedings of the National Academy of Sciences of the United States of America
Structure of Est3 reveals a bimodal surface with differential roles in telomere replication.

Residues 1-12 were deleted from S. cerevisiae Est3 protein sequence. First serine was part of the cleaved affinity tag.

Structure Of Saccharomyces Cerevisiae Est3 Protein

K7_Est3p [Saccharomyces cerevisiae Kyokai no. 7]

telomerase subunit EST3 [Saccharomyces cerevisiae S288c]

RecName: Full=Telomere replication protein EST3; AltName: Full=Ever shorter telomeres protein 3

TPA: telomerase subunit EST3 [Saccharomyces cerevisiae S288c]

The structure was calculated by a combination of NOE and Residual dipolar coupling

Protein was 2H,15N,13C labeled. Sample concentration was 280 uM.
Protein was 15N labeled. Sample concentration was 140 uM.
Protein was selectively protonated for Ile, Leu, Val methyl protons in 2H,15N,13C labelled background. Sample concentration was 280 uM.
Accelerated Technologies Center for Gene to 3D Structure
Constraints list generation for structure solution
Schwieters, Kuszewski, Tjandra and Clore
Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax