| Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
| 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 |
