Biological Magnetic Resonance Data BankA Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules |
Member of |
Entry ID | Data summary | Entry Title | Citation Title | Authors |
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19072 | Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set |
Backbone 1H, 13C, and 15N Chemical Shift Assignment for inactive HIV-1 protease Bmut5 | Backbone H, C, and N chemical shift assignment for HIV-1 protease subtypes and multi-drug resistant variant MDR 769. | Angelo M Veloro, Ben M Dunn, Carlos Simmerling, Gail E Fanucci, Ian Mitchelle S de Vera, James R Rocca, Xi Huang |
18138 | Chemical Shifts: 1 set |
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Multi-Drug Resistant HIV-1 Protease Variant, MDR 769 | Backbone 1H, 13C, and 15N chemical shift assignment for HIV-1 protease subtypes and multi-drug resistant variant MDR 769. | Angelo M Veloro, Ben M Dunn, Carlos Simmerling, Gail E Fanucci, Ian Mitchelle S de Vera, James R Rocca, Xi Huang |
6078 | Chemical Shifts: 1 set |
IA3, an Aspartic Proteinase Inhibitor for Saccharomyces cerevisiae, Is Intrinsically Unstructured in Solution | IA3, an Aspartic Proteinase Inhibitor from Saccharomyces cerevisiae, Is Intrinsically Unstructured in Solution. | Arthur S Edison, Ben M Dunn, Kyle Perry, Leif Smith, Lowri H Phylip, Omjoy Ganesh, Stephen J Hagen, Terry B Green, Timothy M Logan |