BMRB Entry 4919
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR4919
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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, 137 residues, 15506 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: MRGSHHHHHHGSLHTKGALP
LDTVTFYKVIPKSKFVLVKF
DTQYPYGEKQDEFKRLAENS
ASSDDLLVAEVGISDYGDKL
NMELSEKYKLDKESYPVFYL
FRDGDFENPVPYSGAVKVGA
IQRWLKGQGVYLGMPGC
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 910 |
| 13C chemical shifts | 251 |
| 15N chemical shifts | 129 |
Additional metadata:
Related Database Links:
| PDB | 1G7E 2QC7 |
| EMBL | CAA64397 CAA71313 CAG46468 |
| GB | AAC15239 AAF93170 AAH91129 AAI01494 AAI01496 |
| REF | NP_001182664 NP_006808 NP_446413 XP_001139225 XP_002806003 |
| SP | P30040 P52555 |
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