BMRB Entry 52892

Title:
Backbone resonance assignments for SEP15 cysteine-rich domain
Deposition date:
2025-02-04
Original release date:
2026-08-27
Authors:
Williams, Robert; Gierasch, Lila
Citation:

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:

Assembly members:
entity_1, polymer, 52 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts146
15N chemical shifts47
1H chemical shifts92

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1CRD1

Entities:

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   PHEGLYALAGLUPHESERSERGLUALACYS
2   ARGGLULEUGLYPHESERSERASNLEULEU
3   CYSSERSERCYSASPLEULEUGLYGLNPHE
4   ASNLEULEUGLNLEUASPPROASPCYSARG
5   GLYCYSCYSGLNGLUGLUALAGLNPHEGLU
6   THRLYS

Samples:

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
IPAP-HSQCsample_1isotropicsample_conditions_1
IPAP-HSQCsample_3anisotropicsample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

Related Database Links:

Uniprot O60613
AlphaFold O60613

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks