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Entry ID	Original Release date	Data summary	Entry Title	Citation Title	Authors
51793	2023-01-27	Chemical Shifts: 1 set	FapC Full-Length	Solution-state NMR assignment and secondary structure propensity of the full length and minimalistic-truncated prefibrillar monomeric form of biofilm forming functional amyloid FapC from Pseudomonas aeruginosa	Chang-Hyeock Byeon, In-Ja Byeon, Pang Wang, Umit Akbey
51792	2023-01-27	Chemical Shifts: 1 set	FapC L2R3C	Solution-state NMR assignment and secondary structure propensity of the full length and minimalistic-truncated prefibrillar monomeric form of biofilm forming functional amyloid FapC from Pseudomonas aeruginosa	Chang-Hyeock Byeon, In-Ja L Byeon, Pang C Wang, Umit Akbey
4599	2001-02-01	Chemical Shifts: 1 set	High-Resolution Solution Structure of the 18 kDa Substrate-Binding Domain of the Mammalian Chaperone Protein Hsc70	High-Resolution Solution Structure of the 18 kDa Substrate-Binding Domain of the Mammalian Chaperone Protein Hsc70	E RP Zuiderweg, G C Flynn, H Wang, R C Morshauser, W Hu, Y Pang
4497	2000-06-16	Chemical Shifts: 1 set	High resolution solution structure of the Heat shock cognate -70 kd substrate binding domain obtained by multidimensional NMR techniques	High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70	E RP ZUIDERWEG, G C FLYNN, H WANG, R C MORSHAUSER, W HU, Y PANG