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PDB ID: 2kmg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16428
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Citation: Serfiotis-Mitsa, Dimitra; Herbert, Andrew; Roberts, Gareth; Soares, Dinesh; White, John; Blakely, Garry; Uhrin, Dusan; Dryden, David. "The structure of the KlcA and ArdB proteins reveals a novel fold and antirestriction activity against Type I DNA restriction systems in vivo but not in vitro." Nucleic Acids Res. 38, 1723-1737 (2010).
PubMed: 20007596
Assembly members:
KlcA and ArdB proteins, polymer, 142 residues, Formula weight is not available
Natural source: Common Name: B. pertussis Taxonomy ID: 520 Superkingdom: Bacteria Kingdom: not available Genus/species: Bordetella pertussis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-24a
Entity Sequences (FASTA):
KlcA and ArdB proteins: MNTEEQPVTASLVAEAQRLD
FLPTYFGPRLMMRGEALVYA
WMRRLCERYNGAYWHYYALS
DGGFYMAPDLAGRLEIEVNG
NGFRGELSADAAGIVATLFA
LGQLAAEIADTDAADALIDR
YHFLRGFAAGHPEAAAIYRA
ID
Data type | Count |
13C chemical shifts | 559 |
15N chemical shifts | 149 |
1H chemical shifts | 897 |
residual dipolar couplings | 110 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | KlcA and ArdB proteins | 1 |
Entity 1, KlcA and ArdB proteins 142 residues - Formula weight is not available
1 | MET | ASN | THR | GLU | GLU | GLN | PRO | VAL | THR | ALA | ||||
2 | SER | LEU | VAL | ALA | GLU | ALA | GLN | ARG | LEU | ASP | ||||
3 | PHE | LEU | PRO | THR | TYR | PHE | GLY | PRO | ARG | LEU | ||||
4 | MET | MET | ARG | GLY | GLU | ALA | LEU | VAL | TYR | ALA | ||||
5 | TRP | MET | ARG | ARG | LEU | CYS | GLU | ARG | TYR | ASN | ||||
6 | GLY | ALA | TYR | TRP | HIS | TYR | TYR | ALA | LEU | SER | ||||
7 | ASP | GLY | GLY | PHE | TYR | MET | ALA | PRO | ASP | LEU | ||||
8 | ALA | GLY | ARG | LEU | GLU | ILE | GLU | VAL | ASN | GLY | ||||
9 | ASN | GLY | PHE | ARG | GLY | GLU | LEU | SER | ALA | ASP | ||||
10 | ALA | ALA | GLY | ILE | VAL | ALA | THR | LEU | PHE | ALA | ||||
11 | LEU | GLY | GLN | LEU | ALA | ALA | GLU | ILE | ALA | ASP | ||||
12 | THR | ASP | ALA | ALA | ASP | ALA | LEU | ILE | ASP | ARG | ||||
13 | TYR | HIS | PHE | LEU | ARG | GLY | PHE | ALA | ALA | GLY | ||||
14 | HIS | PRO | GLU | ALA | ALA | ALA | ILE | TYR | ARG | ALA | ||||
15 | ILE | ASP |
EMBL | BAF33451.1 |
UNP | Q08L07 |
PDB | 2KMG |
DBJ | BAF33451 |
REF | WP_011666376 YP_787932 |
AlphaFold | Q08L07 |
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