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 4920

Title: Thioredoxin fold as a Homodimerization Module in the Putative Chaperone ERp29: NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer   PubMed: 11435111

Deposition date: 2000-12-13 Original release date: 2001-08-08

Authors: Liepinsh, Edvards; Baryshev, Michail; Sharipo, Anatoly; Ingelman-Sundberg, Magnus; Otting, Gottfried; Mkrtchian, Souren

Citation: Liepinsh, Edvards; Baryshev, Michail; Sharipo, Anatoly; Ingelman-Sundberg, Magnus; Otting, Gottfried; Mkrtchian, Souren. "Thioredoxin fold as a Homodimerization Module in the Putative Chaperone ERp29: NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer"  Structure 9, 457-471 (2001).

Assembly members:
Endoplasmic reticulum protein p29, polymer, 120 residues, 13478 Da.

Natural source:   Common Name: Norway rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

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

Entity Sequences (FASTA):
Endoplasmic reticulum protein p29: MRGSHHHHHHGIRMPGCLPA YDALAGQFIEASSREARQAI LKQGQDGLSGVKETDKKWAS QYLKIMGKILDQGEDFPASE LARISKLIENKMSEGKKEEL QRSLNILTAFRKKGAEKEEL

Data sets:
Data typeCount
1H chemical shifts838
13C chemical shifts224
15N chemical shifts127

Additional metadata:

  • Assembly
  • Samples and Experiments
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Related Database Links:

PDB 1G7D 2M66
EMBL CAA71313
GB AAC15239 AAF93170 AAH91129 EDM13737 EDM13738
REF NP_446413
SP P52555

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