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Entry ID	Data summary	Entry Title	Citation Title	Authors
18003	Chemical Shifts: 2 sets	solution structure of apo-NmtR	Solution structure of Mycobacterium tuberculosis NmtR in the apo state: insights into Ni(II)-mediated allostery.	Chul Won Lee, David P Giedroc, Dhruva K Chakravorty, Feng-Ming James Chang, Hermes Reyes-Caballero, Kenneth M Merz, Yuzhen Ye
7189	Chemical Shifts: 2 sets	NMR assignments of the low molecular weight protein tyrosine phosphatase from Campylobacter Jejuni	Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni	David C Watson, Dmitri Tolkatchev, Feng Ni, Josee Plamondon, N Martin Young, Ping Xu, Rustem Shaykhutdinov
5933	Chemical Shifts: 1 set	Sequence-specific backbone and sidechain resonance assignments of the Ste50 binding domain of the MAPKKK Ste11	Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its interactions with the adaptor protein Ste50 from the budding yeast: implications for Ste11 activation and signal transmission through the Ste50-Ste11 complex	C Wu, Feng Ni, M Whiteway, Ping Xu, R Gingras, R Shaykhutdinov, Surajit Bhattacharjya
4969	Chemical Shifts: 1 set	Backbone 1H, 13C and 15N chemical shift assignments for the Brucella D4.4 VH antibody fragment	Solution Structure of a Llama Single-domain Antibody with Hydrophobic Residues typical of the VH/VL Interface	Dmitri Tolkatchev, Feng Ni, Jamshid Tanha, Ping Xu, Saran Narang, Wim F Vranken, Zhigang Chen
4778	Chemical Shifts: 1 set	Backbone 1HN, 15N and 13C shifts for GMPPNP-loaded Cdc42 from Candida albicans	Efficient expression of isotopically labeled peptides for high resolution NMR studies: application to the Cdc42/Rac binding domains of virulent kinases in Candida albicans	Feng Ni, Michael J Osborne, V Sridaran, Z Su
4770	Chemical Shifts: 1 set	Backbone 1HN, 15N and 13C shifts for GDP-loaded Cdc42 from Candida albicans	Efficient expression of isotopically labeled peptides for high resolution NMR studies: Application to the Cdc42/Rac binding domains of virulent kinases in Candida albicans	Feng Ni, Michael J Osborne, Vasanth Sridaran, Zhengding Su
4351	Chemical Shifts: 1 set Coupling Constants: 1 set	A 30-residue Fragment of the Carp Granulin-1 Protein Folds into a Stack of two Beta-hairpins Similar to that found in the Native Protein	A 30-residue Fragment of the Carp Granulin-1 Protein Folds into a Stack of two Beta-hairpins Similar to that found in the Native Protein	Feng Ni, Hugh PJ Bennett, Ping Xu, Susan James, Wim F Vranken, Z G Chen
401	Chemical Shifts: 1 set	High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen	High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen	Feng Ni, H A Scheraga, Lea Doerr Bullock, Meheryar N Rivetna, Yasuo Konishi
417	Chemical Shifts: 1 set	High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen	High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen	Feng Ni, H A Scheraga, Lea Doerr Bullock, Meheryar N Rivetna, Yasuo Konishi
490	Chemical Shifts: 1 set	Thrombin-Bound Conformation of the C-Terminal Fragments of Hirudin Determined by Transferred Nuclear Overhauser Effects	Thrombin-Bound Conformation of the C-Terminal Fragments of Hirudin Determined by Transferred Nuclear Overhauser Effects	Feng Ni, H A Scheraga, Yasuo Konishi
402	Chemical Shifts: 1 set	High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen	High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen	Feng Ni, H A Scheraga, Lea Doerr Bullock, Meheryar N Rivetna, Yasuo Konishi