BMRB Entry 53331
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53331
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: Gabrielli, Valeria; Grga, Jelena; Gavalda, Sabine; Perrot, Laura; Cantrelle, Francois-Xavier; Boll, Emmanuelle; Lippens, Guy; Charlier, Cyril. "Towards site-specific information on PET degrading enzymes using NMR near operational temperature" Sci. Rep. 15, 38602-38602 (2025).
PubMed: 41188311
Assembly members:
entity_1, polymer, 258 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21b
Entity Sequences (FASTA):
entity_1: SNPYQRGPNPTRSALTADGP
FSVATYTVSRLSVSGFGGGV
IYYPTGTSLTFGGIAMSPGY
TADASSLAWLGRRLASHGFV
VLVINTNSRFDGPDSRASQL
SAALNYLRTSSPSAVRARLD
ANRLAVAGHAMGGGGTLRIA
EQNPSLKAAVPLTPWHTDKT
FNTSVPVLIVGAEADTVAPV
SQHAIPFYQNLPSTTPKVYV
ELCNASHIAPNSNNAAISVY
TISWMKLWVDNDTRYRQFLC
NVNDPALCDFRTNNRHCQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 652 |
| 15N chemical shifts | 203 |
| 1H chemical shifts | 203 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | LCC-ICCG-S165A | 1 |
Entities:
Entity 1, LCC-ICCG-S165A 258 residues - Formula weight is not available
| 1 | SER | ASN | PRO | TYR | GLN | ARG | GLY | PRO | ASN | PRO | ||||
| 2 | THR | ARG | SER | ALA | LEU | THR | ALA | ASP | GLY | PRO | ||||
| 3 | PHE | SER | VAL | ALA | THR | TYR | THR | VAL | SER | ARG | ||||
| 4 | LEU | SER | VAL | SER | GLY | PHE | GLY | GLY | GLY | VAL | ||||
| 5 | ILE | TYR | TYR | PRO | THR | GLY | THR | SER | LEU | THR | ||||
| 6 | PHE | GLY | GLY | ILE | ALA | MET | SER | PRO | GLY | TYR | ||||
| 7 | THR | ALA | ASP | ALA | SER | SER | LEU | ALA | TRP | LEU | ||||
| 8 | GLY | ARG | ARG | LEU | ALA | SER | HIS | GLY | PHE | VAL | ||||
| 9 | VAL | LEU | VAL | ILE | ASN | THR | ASN | SER | ARG | PHE | ||||
| 10 | ASP | GLY | PRO | ASP | SER | ARG | ALA | SER | GLN | LEU | ||||
| 11 | SER | ALA | ALA | LEU | ASN | TYR | LEU | ARG | THR | SER | ||||
| 12 | SER | PRO | SER | ALA | VAL | ARG | ALA | ARG | LEU | ASP | ||||
| 13 | ALA | ASN | ARG | LEU | ALA | VAL | ALA | GLY | HIS | ALA | ||||
| 14 | MET | GLY | GLY | GLY | GLY | THR | LEU | ARG | ILE | ALA | ||||
| 15 | GLU | GLN | ASN | PRO | SER | LEU | LYS | ALA | ALA | VAL | ||||
| 16 | PRO | LEU | THR | PRO | TRP | HIS | THR | ASP | LYS | THR | ||||
| 17 | PHE | ASN | THR | SER | VAL | PRO | VAL | LEU | ILE | VAL | ||||
| 18 | GLY | ALA | GLU | ALA | ASP | THR | VAL | ALA | PRO | VAL | ||||
| 19 | SER | GLN | HIS | ALA | ILE | PRO | PHE | TYR | GLN | ASN | ||||
| 20 | LEU | PRO | SER | THR | THR | PRO | LYS | VAL | TYR | VAL | ||||
| 21 | GLU | LEU | CYS | ASN | ALA | SER | HIS | ILE | ALA | PRO | ||||
| 22 | ASN | SER | ASN | ASN | ALA | ALA | ILE | SER | VAL | TYR | ||||
| 23 | THR | ILE | SER | TRP | MET | LYS | LEU | TRP | VAL | ASP | ||||
| 24 | ASN | ASP | THR | ARG | TYR | ARG | GLN | PHE | LEU | CYS | ||||
| 25 | ASN | VAL | ASN | ASP | PRO | ALA | LEU | CYS | ASP | PHE | ||||
| 26 | ARG | THR | ASN | ASN | ARG | HIS | CYS | GLN |
Samples:
sample_1: LCC-ICCG-S165A, [U-100% 13C; U-100% 15N], 600 uM; TRIS 25 mM; sodium chloride 100 mM
sample_conditions_1: ionic strength: 100 M; pH: 7.5; pressure: 1 atm; temperature: 323 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN - collection
NMRFAM-SPARKY - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE NEO 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks