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 30080

Title: The structure of chaperone SecB in complex with unstructured proPhoA   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.
Alkaline phosphatase, polymer, 471 residues, 49492.367 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
Alkaline phosphatase: MKQSTIALALLPLLFTPVTK ARTPEMPVLENRAAQGDITA PGGARRLTGDQTAALRDSLS DKPAKNIILLIGDGMGDSEI TAARNYAEGAGGFFKGIDAL PLTGQYTHYALNKKTGKPDY VTDSAASATAWSTGVKTYNG ALGVDIHEKDHPTILEMAKA AGLATGNVSTAELQDATPAA LVAHVTSRKCYGPSATSEKC PGNALEKGGKGSITEQLLNA RADVTLGGGAKTFAETATAG EWQGKTLREQAQARGYQLVS DAASLNSVTEANQQKPLLGL FADGNMPVRWLGPKATYHGN IDKPAVTCTPNPQRNDSVPT LAQMTDKAIELLSKNEKGFF LQVEGASIDKQDHAANPCGQ IGETVDLDEAVQRALEFAKK EGNTLVIVTADHAHASQIVA PDTKAPGLTQALNTKDGAVM VMSYGNSEEDSQEHTGSQLR IAAYGPHAANVVGLTDQTDL FYTMKAALGLK

Data typeCount
13C chemical shifts3011
15N chemical shifts926
1H chemical shifts2479

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