2MBB
Solution Structure of the human Polymerase iota UBM1-Ubiquitin Complex
Summary for 2MBB
| Entry DOI | 10.2210/pdb2mbb/pdb |
| NMR Information | BMRB: 19394 |
| Descriptor | Immunoglobulin G-binding protein G/DNA polymerase iota fusion protein, Polyubiquitin-B (2 entities in total) |
| Functional Keywords | polymerase iota, ubm, ubm1, ubiquitin, transferase, signaling protein |
| Biological source | Streptococcus sp. 'group G', Homo sapiens More |
| Cellular location | Nucleus: Q9UNA4 Ubiquitin: Cytoplasm (By similarity): P0CG47 |
| Total number of polymer chains | 2 |
| Total formula weight | 20796.27 |
| Authors | |
| Primary citation | Wang, S.,Zhou, P. Sparsely-sampled, high-resolution 4-D omit spectra for detection and assignment of intermolecular NOEs of protein complexes. J.Biomol.Nmr, 59:51-56, 2014 Cited by PubMed Abstract: Unambiguous detection and assignment of intermolecular NOEs are essential for structure determination of protein complexes by NMR. Such information has traditionally been obtained with 3-D half-filtered experiments, where scalar coupling-based purging of intramolecular signals allows for selective detection of intermolecular NOEs. However, due to the large variation of (1)JHC scalar couplings and limited chemical shift dispersion in the indirect proton dimension, it is difficult to obtain reliable and complete assignments of interfacial NOEs. Here, we demonstrate a strategy that combines selective labeling and high-resolution 4-D NOE spectroscopy with sparse sampling for reliable identification and assignment of intermolecular NOEs. Spectral subtraction of component-labeled complexes from a uniformly-labeled protein complex yields an "omit" spectrum containing positive intermolecular NOEs with little signal degeneracy. Such a strategy can be broadly applied to unbiased detection, assignment and presentation of intermolecular NOEs of protein complexes. PubMed: 24789524DOI: 10.1007/s10858-014-9834-2 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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