Protein science : a publication of the Protein Society
Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping.

LEHHHHHH are at the C-terminal as part of His-Tag

Solution Nmr Structure Of Ser13 From Staphylococcus Epidermidis. Northeast Structural Genomics Consortium Target Ser13

hypothetical protein SEB_01149 [Staphylococcus epidermidis PM221]

conserved hypothetical protein [Staphylococcus epidermidis ATCC 12228]

conserved hypothetical protein [Staphylococcus epidermidis RP62A]

hypothetical protein DP17_90 [Staphylococcus epidermidis]

scaffolding protein [Staphylococcus epidermidis]

Scaffold protein Nfu/NifU N terminal domain protein [Staphylococcus epidermidis W23144]

hypothetical protein SE1124 [Staphylococcus epidermidis ATCC 12228]

MULTISPECIES: hypothetical protein [Bacteria]

hypothetical protein [Staphylococcus epidermidis]

The oligomeric states of the SeR13 were verified by pulsed-field-gradient diffusion, dynamic light scattering, sedimentation equilibrium, and concentration dependent studies. The results indicated that the SeR13 self-associates weakly at protein concentration below 1 mM. Using the residual dipolar couplings as well as chemical shift perturbations on dilution, we constructed dimeric models for SeR13. Possible inter-subunit NOEs were identified based on these models. In cases where corresponding NOEs were observed, they were eliminated as constraints and the protein structure recalculated. The absence of structural variation and the failure to observed other predicted inter-subunit NOEs validated use of all NOEs as intra-subunit constraints.
Chemical Shift assignment of SeR13 from Staphylococcus Epidermidis, North East Structural Genomics Consortium Target SeR13

Northeast Structural Genomics Consortium

Negative Charged Poly Acrylamide Compressed Gel

Schwieters, Kuszewski, Tjandra and Clore

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax