BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30651

Title: Lasso peptide pandonodin   PubMed: 31742991

Deposition date: 2019-08-06 Original release date: 2019-12-02

Authors: Link, A.; Cheung-Lee, W.

Citation: Cheung-Lee, W.; Cao, L.; Link, A.. "Pandonodin: a proteobacterial lasso peptide with an exceptionally long C-terminal tail."  Acs Chem. Biol. ., .-. (2019).

Assembly members:
entity_1, polymer, 33 residues, 3330.956 Da.

Natural source:   Common Name: Pandoraea norimbergensis   Taxonomy ID: 93219   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pandoraea norimbergensis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21

Entity Sequences (FASTA):
entity_1: GVLGNDAEGITLLPLCFKPI CIPTLPPLTGGHA

Data sets:
Data typeCount
1H chemical shifts235

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 33 residues - 3330.956 Da.

1   GLYVALLEUGLYASNASPALAGLUGLYILE
2   THRLEULEUPROLEUCYSPHELYSPROILE
3   CYSILEPROTHRLEUPROPROLEUTHRGLY
4   GLYHISALA

Samples:

sample_1: pandonodin 6 mg/mL

sample_conditions_1: ionic strength: 0 Not defined; pH: 6.9; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D gCOSYsample_1isotropicsample_conditions_1
2D TOCSYsample_1isotropicsample_conditions_1
2D NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

MestreLab (Mnova / MestReNova / MestReC) v11.0, Mestrelab Research - chemical shift assignment, peak picking, processing

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

  • Bruker AVANCE III 800 MHz