BMRB Entry 15977
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PDB ID: 2lt3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15977
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Mirassou, Yasmina; Garcia-Moreno, Diana; Santiveri, Clara; Santoro, Jorge; Elias-Arnanz, Montserrat; Padmanabhan, S.; Jimenez, M. Angeles. "1H, 13C and 15N backbone and side chain resonance assignments of the C-terminal domain of CdnL from Myxococcus xanthus" Biomol. NMR Assignments 3, 9-12 (2009).
PubMed: 19636935
Assembly members:
CdnLC, polymer, 113 residues, Formula weight is not available
Natural source: Common Name: Myxococcus xanthus Taxonomy ID: 34 Superkingdom: Bacteria Kingdom: not available Genus/species: Myxococcus xanthus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b
Entity Sequences (FASTA):
CdnLC: GSHMGSVGLREIISEEDVKQ
VYSILKEKDISVDSTTWNRR
YREYMEKIKTGSVFEIAEVL
RDLYLLKGDKDLSFGERKML
DTARSLLIKELSLAKDCSED
EIESDLKKIFNLA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 499 |
| 15N chemical shifts | 119 |
| 1H chemical shifts | 834 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CdnLC | 1 |
Entities:
Entity 1, CdnLC 113 residues - Formula weight is not available
The three N-terminal GSH residues are a cloning tag
| 1 | GLY | SER | HIS | MET | GLY | SER | VAL | GLY | LEU | ARG | ||||
| 2 | GLU | ILE | ILE | SER | GLU | GLU | ASP | VAL | LYS | GLN | ||||
| 3 | VAL | TYR | SER | ILE | LEU | LYS | GLU | LYS | ASP | ILE | ||||
| 4 | SER | VAL | ASP | SER | THR | THR | TRP | ASN | ARG | ARG | ||||
| 5 | TYR | ARG | GLU | TYR | MET | GLU | LYS | ILE | LYS | THR | ||||
| 6 | GLY | SER | VAL | PHE | GLU | ILE | ALA | GLU | VAL | LEU | ||||
| 7 | ARG | ASP | LEU | TYR | LEU | LEU | LYS | GLY | ASP | LYS | ||||
| 8 | ASP | LEU | SER | PHE | GLY | GLU | ARG | LYS | MET | LEU | ||||
| 9 | ASP | THR | ALA | ARG | SER | LEU | LEU | ILE | LYS | GLU | ||||
| 10 | LEU | SER | LEU | ALA | LYS | ASP | CYS | SER | GLU | ASP | ||||
| 11 | GLU | ILE | GLU | SER | ASP | LEU | LYS | LYS | ILE | PHE | ||||
| 12 | ASN | LEU | ALA |
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