BMRB Entry 31285

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31285
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

Title:
A6-A11 diselenide glargine insulin
Deposition date:
2025-11-25
Original release date:
2026-07-30
Authors:
Yang, Y.; Dhayalan, B.; Ehnbom, A.; Weiss, M.
Citation:

Citation: Yang, Yanwu; Dhayalan, Balamurugan; Ehnbom, Andreas; Weil-Ktorza, Orit; Metanis, Norman; Weiss, Michael. "Damping amyloid-associated conformational fluctuations in a protein by an engineered diselenide bridge "  Protein Sci. 35, e70697-e70697 (2026).
PubMed: 42478539

Assembly members:

Assembly members:
entity_1, polymer, 21 residues, 2420.437 Da.
entity_2, polymer, 32 residues, 3748.340 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GIVEQUCTSIUSLYQLENYC G
entity_2: FVNQHLCGSHLVEALYLVCG ERGFFYTPKTRR

Data sets:
Data typeCount
13C chemical shifts187
15N chemical shifts56
1H chemical shifts359

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 21 residues - 2420.437 Da.

1   GLYILEVALGLUGLNSECCYSTHRSERILE
2   SECSERLEUTYRGLNLEUGLUASNTYRCYS
3   GLY

Entity 2, unit_2 32 residues - 3748.340 Da.

1   PHEVALASNGLNHISLEUCYSGLYSERHIS
2   LEUVALGLUALALEUTYRLEUVALCYSGLY
3   GLUARGGLYPHEPHETYRTHRPROLYSTHR
4   ARGARG

Samples:

sample_1: Se-glargine insulin 0.3 mM

sample_2: Se-glargine insulin 0.3 mM

sample_conditions_1: ionic strength: 0.5 mM; pH: 2.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1

Software:

TopSpin v4.05, Bruker Biospin - processing

Sparky, Goddard - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

  • Bruker AVANCE NEO 700 MHz

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