Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52892
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Williams, Robert; Guay, Kevin; Hurlbut Lesk, Owen; Hebert, Daniel; Gierasch, Lila. "The cysteine-rich domain of SEP15, a selenoprotein co-chaperone of the ER chaperone, UDP-glucose:glycoprotein glucosyltransferase, adopts a novel fold
" J. Biol. Chem. ., .-..
PubMed: 40832263
Assembly members:
entity_1, polymer, 52 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET29
Entity Sequences (FASTA):
entity_1: FGAEFSSEACRELGFSSNLL
CSSCDLLGQFNLLQLDPDCR
GCCQEEAQFETK
| Data type | Count |
| 13C chemical shifts | 146 |
| 15N chemical shifts | 47 |
| 1H chemical shifts | 92 |
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CRD | 1 |
Entity 1, CRD 52 residues - Formula weight is not available
This construct represents the mature form of SEP15 CRD following ER signal sequence cleavage. It comprises residues 32 to 81 from Uniprot entry O60613.
| 1 | PHE | GLY | ALA | GLU | PHE | SER | SER | GLU | ALA | CYS | ||||
| 2 | ARG | GLU | LEU | GLY | PHE | SER | SER | ASN | LEU | LEU | ||||
| 3 | CYS | SER | SER | CYS | ASP | LEU | LEU | GLY | GLN | PHE | ||||
| 4 | ASN | LEU | LEU | GLN | LEU | ASP | PRO | ASP | CYS | ARG | ||||
| 5 | GLY | CYS | CYS | GLN | GLU | GLU | ALA | GLN | PHE | GLU | ||||
| 6 | THR | LYS |
sample_1: SEP15 CRD, [U-15N], 300 uM; sodium phosphate 20 mM; sodium chloride 100 mM; DSS 10 uM; sodium azide 0.02 w/v
sample_2: SEP15 CRD, [U-15N], 300 uM; sodium phosphate 20 mM; sodium chloride 100 mM; DSS 10 uM; sodium azide 0.02 w/v; Pf1 phage 15 mg/mL
sample_3: SEP15 CRD, [U-13C; U-15N], 300 uM; sodium phosphate 20 mM; sodium chloride 100 mM; DSS 10 uM; sodium azide 0.02 w/v
sample_conditions_1: ionic strength: 200 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| IPAP-HSQC | sample_1 | isotropic | sample_conditions_1 |
| IPAP-HSQC | sample_3 | anisotropic | sample_conditions_1 |
TOPSPIN - collection
NMRPipe - processing
NMRFAM-SPARKY - chemical shift assignment, data analysis, peak picking
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks