BMRB Entry 16428
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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
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Title: The structure of the KlcA and ArdB proteins show a novel fold and antirestriction activity against Type I DNA restriction systems in vivo but not in vitro. PubMed: 20007596
Deposition date: 2009-07-28 Original release date: 2010-02-02
Authors: Serfiotis-Mitsa, Dimitra; Herbert, Andrew; Roberts, Gareth; Soares, Dinesh; White, John; Blakely, Garry; Uhrin, Dusan; Dryden, David
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).
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
Entity Sequences (FASTA):
KlcA and ArdB proteins: MNTEEQPVTASLVAEAQRLD
FLPTYFGPRLMMRGEALVYA
WMRRLCERYNGAYWHYYALS
DGGFYMAPDLAGRLEIEVNG
NGFRGELSADAAGIVATLFA
LGQLAAEIADTDAADALIDR
YHFLRGFAAGHPEAAAIYRA
ID
- assigned_chemical_shifts
- RDCs
| Data type | Count |
| 13C chemical shifts | 559 |
| 15N chemical shifts | 149 |
| 1H chemical shifts | 897 |
| residual dipolar couplings | 110 |
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