Entry ID | Original Release date | Data summary | Entry Title | Citation Title | Authors |
---|---|---|---|---|---|
51174 | 2022-03-04 | Heteronuclear NOE Values: 2 sets T1 Relaxation Values: 2 sets T2 Relaxation Values: 2 sets |
Molecular Dynamics-Assisted Optimization of Protein NMR Relaxation Analysis | Molecular Dynamics-Assisted Optimization of Protein NMR Relaxation Analysis | David M LeMaster, Griselda Hernandez, Janet S Anderson |
28037 | 2020-02-26 | Chemical Shifts: 1 set |
1H, 13C, 15N chemical shift assignments of FKBP12 protein from the pathogenic fungi Candida glabrata | 1H, 13C, 15 N chemical shift assignments of the FKBP12 protein from the pathogenic fungi Candida auris and Candida glabrata | David M LeMaster, Griselda Hernandez, Qamar Bashir |
28038 | 2020-02-26 | Chemical Shifts: 1 set |
1H, 13C, 15N chemical shift assignments of FKBP12 protein from the pathogenic fungi Candida auris | 1H, 13C, 15 N chemical shift assignments of the FKBP12 protein from the pathogenic fungi Candida auris and Candida glabrata | David M LeMaster, Griselda Hernandez, Qamar Bashir |
26845 | 2016-12-29 | T1 Relaxation Values: 4 sets T2 Relaxation Values: 4 sets |
Field dependent R1 and R2 relaxation in B3 domain of protein G (GB3) | Quantifying protein dynamics in the ps-ns time regime by NMR relaxation | David M LeMaster, Griselda Hernandez |
19787 | 2014-08-06 | Chemical Shifts: 1 set |
Human FKBP51-FK506 binding domain 1 | Differential Conformational Dynamics in the Closely Homologous FK506-binding Domains of FKBP51 and FKBP52 | David M LeMaster, Griselda Hernandez, Sourajit Mitra Mustafi |
19788 | 2014-08-06 | Chemical Shifts: 1 set |
Human FKBP52-FK506 binding domain 1 | Differential Conformational Dynamics in the Closely Homologous FK506-binding Domains of FKBP51 and FKBP52 | David M LeMaster, Griselda Hernandez, Sourajit Mitra Mustafi |
19324 | 2014-02-13 | Chemical Shifts: 1 set |
Human FKBP12.6-Minor Form | Analysing the visible conformational substates of the FK506-binding protein FKBP12. | David M Lemaster, Griselda Hernandez, Hongmin Li, Hui Chen, Sourajit M Mustafi |
19323 | 2014-02-13 | Chemical Shifts: 1 set |
Human FKBP12.6-Major Form | Analysing the visible conformational substates of the FK506-binding protein FKBP12. | David M Lemaster, Griselda Hernandez, Hongmin Li, Hui Chen, Sourajit M Mustafi |
19240 | 2013-07-15 | Chemical Shifts: 1 set |
Human FKBP12-Major Form | Analyzing the visible conformational substates of the FK506-binding protein FKBP12. | David M Lemaster, Griselda Hernandez, Hongmin Li, Hui Chen, Sourajit M Mustafi |
19241 | 2013-07-15 | Chemical Shifts: 1 set |
Human FKBP12-Minor Form | Analyzing the visible conformational substates of the FK506-binding protein FKBP12. | David M Lemaster, Griselda Hernandez, Hongmin Li, Hui Chen, Sourajit M Mustafi |
16781 | 2010-05-03 | Chemical Shifts: 1 set |
Backbone chemical shift assignments for the microtubule binding domain of the Dictyostelium discoideum dynein heavy chain | A low affinity ground state conformation for the Dynein microtubule binding domain. | David M LeMaster, Irina Tikhonenko, Lynn McNaughton, Michael P Koonce, Nilesh K Banavali |
16690 | 2010-05-05 | Chemical Shifts: 1 set |
Backbone 1H, 13C and 15N chemical shift assignments for the prolyl isomerase Ess1 from Candida albicans | Restricted domain mobility in the Candida albicans Ess1 prolyl isomerase. | David M Lemaster, Lynn McNaughton, Patrick Van Roey, Steven D Hanes, Zhong Li |
4439 | 2000-01-12 | Chemical Shifts: 1 set |
Hyperfine Cys Proton Signals from Oxidized Human Ferredoxin | Electron-Nuclear Interactions in two Prototypical [2Fe-2S] Proteins: Selective (Chiral) Deuteration and Analysis of 1H and 2H NMR Signals from the Alpha and Beta Hydrogens of Cysteinyl Residues that Ligate the Iron in the Active Sites of Human Ferredoxin and Anabaena 7120 Vegetative Ferredoxin | Bin Xia, Daniel Jenk, David M LeMaster, John L Markley, William M Westler |
4440 | 2000-01-12 | Chemical Shifts: 1 set |
Hyperfine Cys Proton Signals from Reduced Human Ferredoxin | Electron-Nuclear Interactions in two Prototypical [2Fe-2S] Proteins: Selective (Chiral) Deuteration and Analysis of 1H and 2H NMR Signals from the Alpha and Beta Hydrogens of Cysteinyl Residues that Ligate the Iron in the Active Sites of Human Ferredoxin and Anabaena 7120 Vegetative Ferredoxin | Bin Xia, Daniel Jenk, David M LeMaster, John L Markley, William M Westler |
4441 | 2000-05-05 | Chemical Shifts: 1 set |
Hyperfine Cys Proton Signals from Anabaena 7120 Vegetative Ferredoxin | Interactions in two Prototypical [2Fe-2S] Proteins: Selective (Chiral) Deuteration and Analysis of 1H and 2H NMR Signals from the Alpha and Beta Hydrogens of Cysteinyl Residues that Ligate the Iron in the Active Sites of Human Ferredoxin and Anabaena 7120 | Bin Xia, Daniel Jenk, David M LeMaster, John L Markley, William M Westler |
4442 | 2000-05-24 | Chemical Shifts: 1 set |
Hyperfine Cys Proton Signals from Reduced Anabaena 7120 Vegetative Ferredoxin | Interactions in two Prototypical [2Fe-2S] Proteins: Selective (Chiral) Deuteration and Analysis of 1H and 2H NMR Signals from the Alpha and Beta Hydrogens of Cysteinyl Residues that Ligate the Iron in the Active Sites of Human Ferredoxin and Anabaena 712 | Bin Xia, Daniel Jenk, David M LeMaster, John L Markley, William M Westler |
494 | 1995-07-31 | Chemical Shifts: 1 set |
Two-Dimensional NMR Studies of Staphylococcal Nuclease. 1. Sequence-Specific Assignments of Hydrogen-1 Signals and Solution Structure of the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex | Two-Dimensional NMR Studies of Staphylococcal Nuclease. 1. Sequence-Specific Assignments of Hydrogen-1 Signals and Solution Structure of the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex | David M LeMaster, Jinfeng Wang, John L Markley |
495 | 1995-07-31 | Chemical Shifts: 1 set |
Two-Dimensional NMR Studies of Staphylococcal Nuclease. 1. Sequence-Specific Assignments of Hydrogen-1 Signals and Solution Structure of the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex | Two-Dimensional NMR Studies of Staphylococcal Nuclease. 1. Sequence-Specific Assignments of Hydrogen-1 Signals and Solution Structure of the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex | David M LeMaster, Jinfeng Wang, John L Markley |
1874 | 1995-07-31 | Chemical Shifts: 1 set |
Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium | Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium | Andrew P Hinck, David M LeMaster, Jinfeng Wang, John L Markley, Stewart N Loh |
1878 | 1995-07-31 | Chemical Shifts: 1 set |
Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium | Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium | Andrew P Hinck, David M LeMaster, Jinfeng Wang, John L Markley, Stewart N Loh |
62 | 1995-07-31 | Chemical Shifts: 1 set |
NMR Sequential Assignment of Escherichia coli Thioredoxin Utilizing Random Fractional Deuteriation | NMR Sequential Assignment of Escherichia coli Thioredoxin Utilizing Random Fractional Deuteriation | David M LeMaster, Frederic M Richards |
1877 | 1995-07-31 | Chemical Shifts: 1 set |
Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium | Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium | Andrew P Hinck, David M LeMaster, Jinfeng Wang, John L Markley, Stewart N Loh |
1876 | 1995-07-31 | Chemical Shifts: 1 set |
Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium | Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium | Andrew P Hinck, David M LeMaster, Jinfeng Wang, John L Markley, Stewart N Loh |
1875 | 1995-07-31 | Chemical Shifts: 1 set |
Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium | Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium | Andrew P Hinck, David M LeMaster, Jinfeng Wang, John L Markley, Stewart N Loh |