BMRB Entry 31284

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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/BMR31284
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
Gelatinamin A: a figure-of-eight lasso peptide
Deposition date:
2025-11-18
Original release date:
2026-05-30
Authors:
Johnson, T.; Zhu, A.; Svenningsen, T.; Merrild, A.; Wang, F.; Andersen, F.; Iwase, R.; Viennet, T.; Larsen, M.; Link, A.; Torring, T.
Citation:

Citation: Svenningsen, T.; Merrild, A.; Wang, F.; Andersen, F.; Johnson, T.; Zhu, A.; Iwase, R.; Viennet, T.; Larsen, M.; Link, A.; Torring, T.. "Gelatinamin A: a figure-of-eight lasso peptide"  .

Assembly members:

Assembly members:
entity_1, polymer, 17 residues, 1786.131 Da.

Natural source:

Natural source:   Common Name: Brevibacillus gelatini   Taxonomy ID: 1655277   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Brevibacillus gelatini

Experimental source:

Experimental source:   Production method: purified from the natural source

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AKKSKPGDGKHGRGVKK

Data sets:
Data typeCount
13C chemical shifts54
15N chemical shifts15
1H chemical shifts131

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 17 residues - 1786.131 Da.

1   ALALYSLYSSERLYSPROGLYASPGLYLYS
2   HISGLYARGGLYVALLYSLYS

Samples:

sample_1: Gelatinamin A 10 mg/mL

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H NMR with water suppressionsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C HSQC-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N HSQC-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C HSQC-NOESYsample_1isotropicsample_conditions_1
3D 1H-15N HSQC-NOESYsample_1isotropicsample_conditions_1

Software:

MestreLab (Mnova / MestReNova / MestReC), MestreLab - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

  • Bruker AVANCE III 950 MHz

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