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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 | Authors |
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18604 | Chemical Shifts: 1 set |
Solution structure of CCP modules 10-11 of complement factor H |
Solution structure of CCP modules 10-12 illuminates functional architecture of the complement regulator, factor H.
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Andrew P Herbert, Christoph Q Schmidt, Dinesh C Soares, Dmitri I Svergun, Elisavet Makou, Haydyn DT Mertens, Ilias Matis, Mateusz Maciejewski, Paul N Barlow |
18599 | Chemical Shifts: 1 set |
Solution structure of CCP modules 11-12 of complement factor H |
Solution structure of CCP modules 10-12 illuminates functional architecture of the complement regulator, factor H.
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Andrew P Herbert, Christoph Q Schmidt, Dinesh C Soares, Dmitri I Svergun, Elisavet Makou, Haydyn DT Mertens, Ilias Matis, Mateusz Maciejewski, Paul N Barlow |
16439 | Chemical Shifts: 1 set |
Combined high- and low-resolution techniques reveal compact structure in central portion of factor H despite long inter-modular linkers |
The central portion of factor H (modules 10-15) is compact and contains a structurally deviant CCP module.
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Andrew P Herbert, Arthur J Rowe, Christoph Q Schmidt, Dinesh C Soares, Dmitri I Svergun, Dusan Uhrin, Haydyn DT Mertens, Mara Guariento, Paul N Barlow |
16428 | Chemical Shifts: 1 set Residual Dipolar Couplings: 1 set |
The structure of the KlcA and ArdB proteins show a novel fold and antirestriction activity against Type I DNA restriction systems in vivo but not in vitro. |
The structure of the KlcA and ArdB proteins reveals a novel fold and antirestriction activity against Type I DNA restriction systems in vivo but not in vitro.
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Andrew P Herbert, David TF Dryden, Dimitra Serfiotis-Mitsa, Dinesh C Soares, Dusan Uhrin, Gareth A Roberts, Garry W Blakely, John H White |