BMRB Entry 31309

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31309
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title:
Solution structure of the Cys-rich domain of the 15 kDa selenoprotein
Deposition date:
2026-07-16
Original release date:
2026-10-29
Authors:
Williams, R.; Gierasch, L.
Citation:

Citation: Williams, R.; Guay, K.; Hurlbut Lesk, O.; Hebert, D.; Gierasch, L.. "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. ., 113629-113629 (2026).
PubMed: 42854909

Assembly members:

Assembly members:
entity_1, polymer, 52 residues, 5744.364 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: FGAEFSSEACRELGFSSNLL CSSCDLLGQFNLLQLDPDCR GCCQEEAQFETK

Data sets:
Data typeCount
13C chemical shifts189
15N chemical shifts58
1H chemical shifts331

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_21

Entities:

Entity 1, unit_1 52 residues - 5744.364 Da.

1   PHEGLYALAGLUPHESERSERGLUALACYS
2   ARGGLULEUGLYPHESERSERASNLEULEU
3   CYSSERSERCYSASPLEULEUGLYGLNPHE
4   ASNLEULEUGLNLEUASPPROASPCYSARG
5   GLYCYSCYSGLNGLUGLUALAGLNPHEGLU
6   THRLYS

Samples:

sample_1: CRD, [U-15N], 800 uM; MES 20 mM; sodium chloride 100 mM; DSS 10 uM; sodium azide 0.02 % w/v

sample_2: CRD, [U-13C; U-15N], 800 uM; MES 20 mM; sodium chloride 100 mM; DSS 10 uM; sodium azide 0.02 % w/v

sample_3: CRD 400 uM; MES 20 mM; sodium chloride 100 mM; DSS 10 uM; sodium azide 0.02 % w/v

sample_conditions_1: ionic strength: 100 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D Protonsample_1isotropicsample_conditions_1
1D Protonsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
1D Protonsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure calculation

TopSpin, Bruker Biospin - collection

NMRFAM-SPARKY, Lee - chemical shift assignment, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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