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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7420 | Chemical Shifts: 1 set |
STRUCTURE OF CCP MODULE 7 OF COMPLEMENT FACTOR H- THE AMD AT RISK VARIENT (402H) | Structure Shows Glycosaminoglycan- and Protein-Recognition Site in Factor H is Perturbed by Age-Related Macular Degeneration-Linked single nucleotide polymorphism | A P Herbert, B S Blaum, C Egan, C Q Schmidt, D Uhrin, J A Deakin, M K Pangburn, M Lyon, P N Barlow, V Ferreira |
7421 | Chemical Shifts: 1 set |
STRUCTURE OF CCP MODULE 7 OF COMPLEMENT FACTOR H- THE AMD NOT AT RISK VARIENT (402Y) | Structure Shows Glycosaminoglycan- and Protein-Recognition Site in Factor H is Perturbed by Age-Related Macular Degeneration-Linked single nucleotide polymorphism | A P Herbert, B S Blaum, C Egan, C Q Schmidt, D Uhrin, J A Deakin, M K Pangburn, M Lyon, P N Barlow, V Ferreira |
6612 | Chemical Shifts: 1 set |
NMR structure of unliagnded MDM2 | Structure of free MDM2 N-terminal domain reveals conformational adjustments that accompany p53-binding. | C McInnes, D Uhrin, D Zheleva, H Powers, K Watt, P Fischer, P N Barlow, S Uhrinova |
6171 | Chemical Shifts: 1 set Coupling Constants: 1 set |
Solution structure of the second complement control protein (CCP) module of the GABA(B)R1a receptor, Pro-119 trans conformer | Structural analysis of the CCP modules of the GABAB receptor 1a: Only one of the two CCP modules is compactly folded | B O Smith, D C Soares, D Uhrin, J H White, P N Barlow, R Ginham, R J McIlhinney, S C Blein, S Veltel |
6166 | Chemical Shifts: 1 set Coupling Constants: 1 set |
Solution structure of the second complement control protein (CCP) module of the GABA(B)R1a receptor, Pro-119 cis conformer | Structural analysis of the CCP modules of the GABAB receptor 1a: Only one of the two CCP modules is compactly folded. | B O Smith, D C Soares, D Uhrin, J H White, P N Barlow, RA J McIlhinney, R Ginham, S C Blein, S Veltel |
5900 | Chemical Shifts: 3 sets |
NMR structure of 16th module of Immune Adherence Receptor, Cr1 (Cd35) | Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces. | C Schmitz, D Uhrin, G M Black, J M O'Leary, J P Atkinson, K Bromek, M Krych, P N Barlow, S Uhrinova, X Wang |
4648 | Chemical Shifts: 1 set Coupling Constants: 1 set |
Solution Structure and Dynamics of an Open B-sheet, Glycolytic Enzyme-monomeric 23.7 kDa Phosphoglycerate Mutase from Schizosaccharomyces pombe | Solution Structure and Dynamics of an Open B-sheet, Glycolytic Enzyme-monomeric 23.7 kDa Phosphoglycerate Mutase from Schizosaccharomyces pombe | D Uhrin, J Nairn, L A Fothergill-Gilmore, N C Price, S Uhrinova |