BMRB Entry 5298
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
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
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:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | PPIase | 1 |
Entities:
Entity 1, PPIase 106 residues - 11647 Da.
1 | GLY | SER | HIS | MET | GLN | ALA | THR | TRP | LYS | GLU | ||||
2 | LYS | ASP | GLY | ALA | VAL | GLU | ALA | GLU | ASP | ARG | ||||
3 | VAL | THR | ILE | ASP | PHE | THR | GLY | SER | VAL | ASP | ||||
4 | GLY | GLU | GLU | PHE | GLU | GLY | GLY | LYS | ALA | SER | ||||
5 | ASP | PHE | VAL | LEU | ALA | MET | GLY | GLN | GLY | ARG | ||||
6 | MET | ILE | PRO | GLY | PHE | GLU | ASP | GLY | ILE | LYS | ||||
7 | GLY | HIS | LYS | ALA | GLY | GLU | GLU | PHE | THR | ILE | ||||
8 | ASP | VAL | THR | PHE | PRO | GLU | GLU | TYR | HIS | ALA | ||||
9 | GLU | ASN | LEU | LYS | GLY | LYS | ALA | ALA | LYS | PHE | ||||
10 | ALA | ILE | ASN | LEU | LYS | LYS | VAL | GLU | GLU | ARG | ||||
11 | GLU | LEU | PRO | GLU | LEU | THR |
Samples:
sample_1: peptidyl-prolyl isomerase2.0 3.0 mM; NaCl 100 mM
sample_2: peptidyl-prolyl isomerase, [U-15N], 2.0 3.0 mM; NaCl 100 mM
sample_3: peptidyl-prolyl isomerase, [U-13C; U-15N], 2.0 3.0 mM; NaCl 100 mM
conditions_1: pH: 6.8; temperature: 303 K; ionic strength: 0.1 M; pressure: 1 atm
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-1H NOESY | not available | not available | not available |
3D 1H-1H-15N NOESY | not available | not available | not available |
3D 1H-1H-15N TOCSY | not available | not available | not available |
3D HNHA | not available | not available | not available |
3D CBCA(CO)NH | not available | not available | not available |
3D HNCACB | not available | not available | not available |
Software:
XWINNMR v2.1 - data collection
GIFA v4.31 - data processing
XEASY v1.3.13 - peak assignments
NMR spectrometers:
- Bruker DRX 500 MHz