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:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ERp29 C-domain | 1 |
Entities:
Entity 1, ERp29 C-domain 120 residues - 13478 Da.
| 1 | MET | ARG | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS | |
| 2 | GLY | ILE | ARG | MET | PRO | GLY | CYS | LEU | PRO | ALA | |
| 3 | TYR | ASP | ALA | LEU | ALA | GLY | GLN | PHE | ILE | GLU | |
| 4 | ALA | SER | SER | ARG | GLU | ALA | ARG | GLN | ALA | ILE | |
| 5 | LEU | LYS | GLN | GLY | GLN | ASP | GLY | LEU | SER | GLY | |
| 6 | VAL | LYS | GLU | THR | ASP | LYS | LYS | TRP | ALA | SER | |
| 7 | GLN | TYR | LEU | LYS | ILE | MET | GLY | LYS | ILE | LEU | |
| 8 | ASP | GLN | GLY | GLU | ASP | PHE | PRO | ALA | SER | GLU | |
| 9 | LEU | ALA | ARG | ILE | SER | LYS | LEU | ILE | GLU | ASN | |
| 10 | LYS | MET | SER | GLU | GLY | LYS | LYS | GLU | GLU | LEU | |
| 11 | GLN | ARG | SER | LEU | ASN | ILE | LEU | THR | ALA | PHE | |
| 12 | ARG | LYS | LYS | GLY | ALA | GLU | LYS | GLU | GLU | LEU |
Samples:
sample_1: Endoplasmic reticulum protein p29, [U-15N; U-13C], 2 mM
sample_2: Endoplasmic reticulum protein p29 2 mM
Ex-cond_1: pH: 4.9; temperature: 308 K; ionic strength: 0.15 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | not available | not available | not available |
| 2D 1H-1H COSY | not available | not available | not available |
| 2D 1H-1H CLEAN TOCSY | not available | not available | not available |
| 2D 1H-15N HSQC | not available | not available | not available |
| 3D 1H-1H-15N NOESY | not available | not available | not available |
| 3D HNCA | not available | not available | not available |
| 3D HN(CO)CA | not available | not available | not available |
| 3D HNCO | not available | not available | not available |
Software:
No software information available
NMR spectrometers:
- Bruker DRX 600 MHz
- Varian UnityPlus 800 MHz
Related Database Links:
| PDB | |
| EMBL | CAA71313 |
| GB | AAC15239 AAF93170 AAH91129 EDM13737 EDM13738 |
| REF | NP_446413 |
| SP | P52555 |
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