BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15381

Title: Solution structure of the E. coli Tat proofreading chaperone protein NapD   PubMed: 17901208

Deposition date: 2007-07-17 Original release date: 2007-08-16

Authors: Spronk, Chris; Vuister, Geerten; Sargent, Frank

Citation: Maillard, Julien; Spronk, Chris; Buchanan, Grant; Lyall, Verity; Richardson, David; Palmer, Tracy; Vuister, Geerten; Sargent, Frank. "Structural diversity in twin-arginine signal peptide binding proteins"  Proc. Natl. Acad. Sci. U.S.A. 104, 15641-15646 (2007).

Assembly members:
NapD, polymer, 95 residues, 10549.718 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
NapD: MHTNWQVCSLVVQAKSERIS DISTQLNAFPGCEVAVSDAP SGQLIVVVEAEDSETLIQTI ESVRNVEGVLAVSLVYHQQE EQGEETPRSHHHHHH

Data sets:
Data typeCount
13C chemical shifts266
15N chemical shifts85
1H chemical shifts561

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Related Database Links:

PDB 2JSX 2PQ4
DBJ BAA15990 BAB36519 BAG77999 BAI26345 BAI31453
EMBL CAP76709 CAQ32610 CAQ89798 CAQ99134 CAR03635
GB AAA16400 AAC75267 AAG57342 AAN43810 AAN81200
REF NP_311123 NP_416711 NP_708103 WP_000557371 WP_000557372
SP P0A9I5 P0A9I6 P0A9I7

Download simulated HSQC data in one of the following formats:
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