BMRB Entry 25003
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25003
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Citation: Thorn, David; Kay, Jennifer; Rhazi, Noureddine; Dumoulin, Mireille; Corazza, Alessandra; Damblon, Christian. "1H, 13C and 15N backbone resonance assignments of the beta-lactamase BlaP from Bacillus licheniformis 749/C and two mutational variants" Biomol NMR Assign 12, 69-77 (2018).
PubMed: 29030803
Assembly members:
BlaP216Q0, polymer, 273 residues, 30368.3 Da.
Natural source: Common Name: firmicutes Taxonomy ID: 1402 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus licheniformis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b
Entity Sequences (FASTA):
BlaP216Q0: TEMKDDFAKLEEQFDAKLGI
FALDTGTNRTVAYRPDERFA
FASTIKALTVGVLLQQKSIE
DLNQRITYTRDDLVNYNPIT
EKHVDTGMTLKELADASLRY
SDNAAQNLILKQIGGPESLK
KELRKIGDEVTNPERFEPEL
NEVNPGETQDTSTARALVTS
LRAFALEDKLPSEKRELLID
WMKRNTTPGGDALIRAGVPD
GWEVADKTGAASYGTRNDIA
IIWPPKGDPVVLAVLSSRDK
KDAKYDDKLIAEATKVVMKA
LNMNGKGPHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 765 |
| 15N chemical shifts | 255 |
| 1H chemical shifts | 253 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BlaP216Q0 | 1 |
Entities:
Entity 1, BlaP216Q0 273 residues - 30368.3 Da.
Residues 267-273 (FASTA sequence) represent a non-native tag
| 1 | THR | GLU | MET | LYS | ASP | ASP | PHE | ALA | LYS | LEU | ||||
| 2 | GLU | GLU | GLN | PHE | ASP | ALA | LYS | LEU | GLY | ILE | ||||
| 3 | PHE | ALA | LEU | ASP | THR | GLY | THR | ASN | ARG | THR | ||||
| 4 | VAL | ALA | TYR | ARG | PRO | ASP | GLU | ARG | PHE | ALA | ||||
| 5 | PHE | ALA | SER | THR | ILE | LYS | ALA | LEU | THR | VAL | ||||
| 6 | GLY | VAL | LEU | LEU | GLN | GLN | LYS | SER | ILE | GLU | ||||
| 7 | ASP | LEU | ASN | GLN | ARG | ILE | THR | TYR | THR | ARG | ||||
| 8 | ASP | ASP | LEU | VAL | ASN | TYR | ASN | PRO | ILE | THR | ||||
| 9 | GLU | LYS | HIS | VAL | ASP | THR | GLY | MET | THR | LEU | ||||
| 10 | LYS | GLU | LEU | ALA | ASP | ALA | SER | LEU | ARG | TYR | ||||
| 11 | SER | ASP | ASN | ALA | ALA | GLN | ASN | LEU | ILE | LEU | ||||
| 12 | LYS | GLN | ILE | GLY | GLY | PRO | GLU | SER | LEU | LYS | ||||
| 13 | LYS | GLU | LEU | ARG | LYS | ILE | GLY | ASP | GLU | VAL | ||||
| 14 | THR | ASN | PRO | GLU | ARG | PHE | GLU | PRO | GLU | LEU | ||||
| 15 | ASN | GLU | VAL | ASN | PRO | GLY | GLU | THR | GLN | ASP | ||||
| 16 | THR | SER | THR | ALA | ARG | ALA | LEU | VAL | THR | SER | ||||
| 17 | LEU | ARG | ALA | PHE | ALA | LEU | GLU | ASP | LYS | LEU | ||||
| 18 | PRO | SER | GLU | LYS | ARG | GLU | LEU | LEU | ILE | ASP | ||||
| 19 | TRP | MET | LYS | ARG | ASN | THR | THR | PRO | GLY | GLY | ||||
| 20 | ASP | ALA | LEU | ILE | ARG | ALA | GLY | VAL | PRO | ASP | ||||
| 21 | GLY | TRP | GLU | VAL | ALA | ASP | LYS | THR | GLY | ALA | ||||
| 22 | ALA | SER | TYR | GLY | THR | ARG | ASN | ASP | ILE | ALA | ||||
| 23 | ILE | ILE | TRP | PRO | PRO | LYS | GLY | ASP | PRO | VAL | ||||
| 24 | VAL | LEU | ALA | VAL | LEU | SER | SER | ARG | ASP | LYS | ||||
| 25 | LYS | ASP | ALA | LYS | TYR | ASP | ASP | LYS | LEU | ILE | ||||
| 26 | ALA | GLU | ALA | THR | LYS | VAL | VAL | MET | LYS | ALA | ||||
| 27 | LEU | ASN | MET | ASN | GLY | LYS | GLY | PRO | HIS | HIS | ||||
| 28 | HIS | HIS | HIS |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks