BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 5298

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

Data sets:
Data typeCount
1H chemical shifts536
13C chemical shifts187
15N chemical shifts98
coupling constants82

Additional metadata:

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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

Download simulated HSQC data in one of the following formats:
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