BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

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Entry ID Data summary Entry Title Citation Title Authors
34552 Chemical Shifts: 1 set
Spectral_peak_list: 3 sets
Structure-function analyses of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation to the cell division site Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation Download bibtex for citation iamge Adam Colyer, Adam F Cunningham, Alvin Ck C Teo, Amanda E Rossiter, Christopher Icke, David I Roper, Dema Alodaini, Douglas F Browning, Douglas G Ward, Emily Ca C Goodall, Eva Heinz, Faye C Morris, Gabriela Boelter, Ian R Henderson, Jack Alfred A Bryant, Kara A Staunton, Manuel Banzhaf, Mark Jeeves, Michael Overduin, Peter J Wotherspoon, Pooja Sridhar, Riyaz Maderbocus, Shu-Sin S Chng, Timothy J Knowles, Timothy J Wells, Trevor Lithgow, Vassiliy N Bavro, Yanina R Sevastsyanovich, Zhi-Soon S Chong
19760 Chemical Shifts: 1 set
PlpA plays a central role in lipid homeostasis in Gram-negative bacterial outer membranes Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation Download bibtex for citation iamge Adam Colyer, Adam F Cunningham, Alvin Ck C Teo, Amanda E Rossiter, Christopher Icke, David I Roper, Dema Alodaini, Douglas F Browning, Douglas G Ward, Emily Ca C Goodall, Eva Heinz, Faye C Morris, Gabriela Boelter, Ian R Henderson, Jack Alfred A Bryant, Kara A Staunton, Manuel Banzhaf, Mark Jeeves, Michael Overduin, Peter J Wotherspoon, Pooja Sridhar, Riyaz Maderbocus, Shu-Sin S Chng, Timothy J Knowles, Timothy J Wells, Trevor Lithgow, Vassiliy N Bavro, Yanina R Sevastsyanovich, Zhi-Soon S Chong
4425 Chemical Shifts: 1 set
Solution structure of apo-biotinyl domain from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance NMR spectroscopy SOLUTION STRUCTURES OF APO- AND HOLO-BIOTINYL DOMAINS FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOP Download bibtex for citation iamge A CHAPMAN-SMITH, E L ROBERTS, J C WALLACE, J E CRONAN, M J HOWARD, N SHU, R N PERHAM, R W BROADHURST, T MORRIS
4426 Chemical Shifts: 1 set
Solution Structure of Holo-biotinyl Domain from Acetyl Coenzyme A Carboxylase of Escherichia coli Determined by Triple-Resonance NMR Spectroscopy Solution Structure of Apo- and Holo-biotinyl Domain from Acetyl Coenzyme A Carboxylase of Escherichia coli Determined by Triple-Resonance NMR Spectroscopy Download bibtex for citation iamge A Chapman-smith, E L Roberts, J C Wallace, J E Cronan, M J Howard, N Shu, R N Perham, R W Broadhurst, T Morris