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 30086

Title: The structure of chaperone SecB in complex with unstructured MBP binding site e   PubMed: 27501151

Deposition date: 2016-05-09 Original release date: 2016-08-18

Authors: Huang, C.; Saio, T.; Rossi, P.; Kalodimos, C.

Citation: Huang, C.; Saio, T.; Rossi, P.; Kalodimos, C.. "Structural basis for the antifolding activity of a molecular chaperone"  Nature 537, 202-206 (2016).

Assembly members:
Protein-export protein SecB, polymer, 155 residues, 17287.266 Da.
Maltose-binding periplasmic protein, polymer, 40 residues, 4595.211 Da.

Natural source:   Common Name: enterobacteria   Taxonomy ID: 83334   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
Protein-export protein SecB: MSEQNNTEMTFQIQRIYTKD ISFEAPNAPHVFQKDWQPEV KLDLDTASSQLADDVYEVVL RVTVTASLGEETAFLCEVQQ GGIFSIAGIEGTQMAHCLGA YCPNILFPYARECITSMVSR GTFPQLNLAPVNFDALFMNY LQQQAGEGTEEHQDA
Maltose-binding periplasmic protein: KGKSALMFNLQEPYFTWPLI AADGGYAFKYENGKYDIKDV

Data typeCount
13C chemical shifts2550
15N chemical shifts686
1H chemical shifts1966

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