BMRB Entry 4919
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR4919
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
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).
PubMed: 11435111
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 Vector: pQE30
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:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ERp29 N-domain | 1 |
Entities:
Entity 1, ERp29 N-domain 137 residues - 15506 Da.
| 1 | MET | ARG | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | GLY | SER | LEU | HIS | THR | LYS | GLY | ALA | LEU | PRO | ||||
| 3 | LEU | ASP | THR | VAL | THR | PHE | TYR | LYS | VAL | ILE | ||||
| 4 | PRO | LYS | SER | LYS | PHE | VAL | LEU | VAL | LYS | PHE | ||||
| 5 | ASP | THR | GLN | TYR | PRO | TYR | GLY | GLU | LYS | GLN | ||||
| 6 | ASP | GLU | PHE | LYS | ARG | LEU | ALA | GLU | ASN | SER | ||||
| 7 | ALA | SER | SER | ASP | ASP | LEU | LEU | VAL | ALA | GLU | ||||
| 8 | VAL | GLY | ILE | SER | ASP | TYR | GLY | ASP | LYS | LEU | ||||
| 9 | ASN | MET | GLU | LEU | SER | GLU | LYS | TYR | LYS | LEU | ||||
| 10 | ASP | LYS | GLU | SER | TYR | PRO | VAL | PHE | TYR | LEU | ||||
| 11 | PHE | ARG | ASP | GLY | ASP | PHE | GLU | ASN | PRO | VAL | ||||
| 12 | PRO | TYR | SER | GLY | ALA | VAL | LYS | VAL | GLY | ALA | ||||
| 13 | ILE | GLN | ARG | TRP | LEU | LYS | GLY | GLN | GLY | VAL | ||||
| 14 | TYR | LEU | GLY | MET | PRO | GLY | CYS |
Samples:
sample_1: Endoplasmic reticulum protein p29, [U-15N; U-13C], 0.3 mM
sample_2: Endoplasmic reticulum protein p29 0.3 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 | CAA64397 CAA71313 CAG46468 |
| GB | AAC15239 AAF93170 AAH91129 AAI01494 AAI01496 |
| REF | NP_001182664 NP_006808 NP_446413 XP_001139225 XP_002806003 |
| SP | P30040 P52555 |
| AlphaFold | P30040 P52555 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks