BMRB Entry 18653
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PDB ID: 2lwy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18653
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Aranko, A. Sesilja; Oeemig, Jesper; Iwai, Hideo. "Structural basis for protein trans-splicing by a bacterial intein-like domain - protein ligation without nucleophilic side chains." FEBS J. 280, 3256-3269 (2013).
PubMed: 23621571
Assembly members:
CthBIL4, polymer, 138 residues, 15297.629 Da.
Natural source: Common Name: Clostridium thermocellum Taxonomy ID: 1515 Superkingdom: Bacteria Kingdom: not available Genus/species: Clostridium thermocellum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pSCFRSF17
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 607 |
| 15N chemical shifts | 139 |
| 1H chemical shifts | 991 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Bacterial Intein-Like domain from Clostridium thermocellum | 1 |
Entities:
Entity 1, Bacterial Intein-Like domain from Clostridium thermocellum 138 residues - 15297.629 Da.
S-3 is from tag cleavage
| 1 | SER | MET | LYS | ALA | PHE | VAL | ALA | GLY | THR | MET | ||||
| 2 | ILE | LEU | THR | ALA | THR | GLY | LEU | VAL | ALA | ILE | ||||
| 3 | GLU | ASN | ILE | LYS | ALA | GLY | ASP | LYS | VAL | ILE | ||||
| 4 | ALA | THR | ASN | PRO | GLU | THR | PHE | GLU | VAL | ALA | ||||
| 5 | GLU | LYS | THR | VAL | LEU | GLU | THR | TYR | VAL | ARG | ||||
| 6 | GLU | THR | THR | GLU | LEU | LEU | HIS | LEU | THR | ILE | ||||
| 7 | GLY | GLY | GLU | VAL | ILE | LYS | THR | THR | PHE | ASP | ||||
| 8 | HIS | PRO | PHE | TYR | VAL | LYS | ASP | VAL | GLY | PHE | ||||
| 9 | VAL | GLU | ALA | GLY | LYS | LEU | GLN | VAL | GLY | ASP | ||||
| 10 | LYS | LEU | LEU | ASP | SER | ARG | GLY | ASN | VAL | LEU | ||||
| 11 | VAL | VAL | GLU | GLU | LYS | LYS | LEU | GLU | ILE | ALA | ||||
| 12 | ASP | LYS | PRO | VAL | LYS | VAL | TYR | ASN | PHE | LYS | ||||
| 13 | VAL | ASP | ASP | PHE | HIS | THR | TYR | HIS | VAL | GLY | ||||
| 14 | ASP | ASN | GLU | VAL | LEU | VAL | HIS | ASN |
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