BMRB Entry 4920
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4920
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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
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 838 |
13C chemical shifts | 224 |
15N chemical shifts | 127 |
Additional metadata:
Related Database Links:
PDB | 1G7D 2M66 |
EMBL | CAA71313 |
GB | AAC15239 AAF93170 AAH91129 EDM13737 EDM13738 |
REF | NP_446413 |
SP | P52555 |
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