BMRB Entry 5298
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5298
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Title: 1H, 13C, and 15N Chemical Shift Assignments for the PPIase domain from E. coli trigger factor
Deposition date: 2002-02-20 Original release date: 2003-06-25
Authors: Kozlov, Guennadi; Trempe, Jean-Francois; Perreault, Audry; Wong, Molly; Denisov, Aleksej; Ghandi, Shaifali; Gehring, Kalle; Ekiel, Irena
Citation: Kozlov, Guennadi; Trempe, Jean-Francois; Perreault, Audry; Wong, Molly; Denisov, Aleksej; Ghandi, Shaifali; Gehring, Kalle; Ekiel, Irena. "Solution structure of the closed form of a peptidyl-prolyl isomerase reveals the mechanism of protein folding " . ., .-..
Assembly members:
peptidyl-prolyl isomerase, polymer, 106 residues, 11647 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
peptidyl-prolyl isomerase: GSHMQATWKEKDGAVEAEDR
VTIDFTGSVDGEEFEGGKAS
DFVLAMGQGRMIPGFEDGIK
GHKAGEEFTIDVTFPEEYHA
ENLKGKAAKFAINLKKVEER
ELPELT
- assigned_chemical_shifts
- coupling_constants
Data type | Count |
1H chemical shifts | 536 |
13C chemical shifts | 187 |
15N chemical shifts | 98 |
coupling constants | 82 |
Additional metadata:
Related Database Links:
BMRB | 19835 19836 19837 |
PDB | 1L1P 1W26 2MLX 2MLY 2MLZ 2VRH |
DBJ | BAB33913 BAD98926 BAE76216 BAG75986 BAH62052 |
EMBL | CAP74970 CAQ30908 CAQ90076 CAQ97312 CAR01780 |
GB | AAA62791 AAB40192 AAC73539 AAG54786 AAN42037 |
REF | NP_286178 NP_308517 NP_414970 NP_706330 NP_752485 |
SP | A1A8A5 A6T5H9 A7ZIJ4 A7ZX94 A8AK17 |
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