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Biological Magnetic Resonance Data BankA Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules |
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| Entry ID | Data summary | Entry Title | Citation Title(s) | Authors |
|---|---|---|---|---|
| 19047 | Chemical Shifts: 2 sets |
Solution Structure of the Bacillus cereus Metallo-Beta-Lactamase BcII |
1: Complete 1H, 15N and 13C resonance assignments of Bacillus cereus metallo-beta-lactamase and its complex with the inhibitor R-thiomandelic acid 2: Complete 1H, 15N and 13C Resonance Assignments of the 25 kDa Bacillus cereus Metallo-Beta-Lactamase BcII and its Complex with the Broad Spectrum Inhibitor R-Thiomandelic Acid 
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Andreas Ioannis Karsisiotis, Christian F Damblon, Gordon C Roberts |
| 16163 | Chemical Shifts: 1 set |
NMR structure of the N-terminal domain of kindlin1 |
The structure of the N-terminus of kindlin-1: a domain important for alphaiibbeta3 integrin activation.
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Benjamin T Goult, Bipin Patel, David A Calderwood, David R Critchley, David S Harburger, Gordon C Roberts, Iain D Campbell, Igor L Barsukov, Mohamed Bouaouina, Neil Bate, Nicholas J Anthis |
| 15457 | Chemical Shifts: 1 set |
NMR Structure of the Talin Rod domain, 1655-1822 |
The Structure of an Interdomain Complex That Regulates Talin Activity
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Alexandre R Gingras, Benjamin T Goult, Bipin Patel, David R Critchley, Gordon C Roberts, Iain D Campbell, Igor L Barsukov, Kate L Wegener, Neil Bate, Nicholas J Anthis |
| 15411 | Chemical Shifts: 1 set |
NMR structure of the talin C-terminal actin binding site |
NMR assignment of the C-terminal actin-binding domain of talin
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Alexandre R Gingras, Benjamin T Goult, David R Critchley, Gordon CK Roberts, Igor L Barsukov, Neil Bate |
| 6285 | Chemical Shifts: 1 set |
15N, 13C, 1H NMR assignment of a 14kDa construct of the focal adhesion protein Talin |
A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head
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A R Gingras, B Patel, D R Critchley, E Papagrigoriou, Gordon C Roberts, Ian J Fillingham, Ian L Barsukov, J Emsley |
| 5750 | Chemical Shifts: 1 set |
1H, 13C, and 15N Chemical Shift Assignments for the extracellular domain of BR3 |
BAFF/BLyS Receptor 3 Comprises a Minimal TNF Receptor-like Module that Encodes a Highly Focused Ligand-binding Site
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Andrea G Cochran, Borlan Pan, JianPing Yin, Melissa A Starovasnik, Minhong Yan, Nathaniel C Gordon, Robert F Kelley, Sarah G Hymowitz, Vishva M Dixit, Wayne J Fairbrother |