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Entry ID	Data summary	Entry Title	Citation Title	Authors
51174	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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	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