BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16739

Title: 1H, 13C, and 15N Chemical Shift Assignments for plectasin   PubMed: 20508130

Deposition date: 2010-02-20 Original release date: 2010-06-01

Authors: Schneider, Tanja; Kruse, Thomas; Wimmer, Reinhard; Wiedemann, Imke; Sass, Vera; Pag, Ulrike; Jansen, Andrea; Nielsen, Allan; Mygind, Per; Raventos, Dorotea; Neve, Soeren; Ravn, Birthe; Bonvin, Alexandre; De Maria, Leonardo; Kamenova, Lora; Sahl, Hans-Georg; Kristensen, Hans-Henrik

Citation: Schneider, Tanja; Kruse, Thomas; Wimmer, Reinhard; Wiedemann, Imke; Sass, Vera; Pag, Ulrike; Jansen, Andrea; Nielsen, Allan; Mygind, Per; Raventos, Dorotea; Neve, Sren; Ravn, Birthe; Bonvin, Alexandre; De Maria, Leonardo; Andersen, Anders; Gammelgaard, Lora; Sahl, Hans-Georg; Kristensen, Hans-Henrik. "Plectasin, a Fungal Defensin, Targets the Bacterial Cell Wall Precursor Lipid II."  Science 328, 1168-1172 (2010).

Assembly members:
plectasin, polymer, 40 residues, Formula weight is not available

Natural source:   Common Name: Pseudoplectania nigrella   Taxonomy ID: 96584   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Pseudoplectania nigrella

Experimental source:   Production method: recombinant technology   Host organism: Aspergillus oryzae   Vector: N/A

Entity Sequences (FASTA):
plectasin: GFGCNGPWDEDDMQCHNHCK SIKGYKGGYCAKGGFVCKCY

Data sets:
Data typeCount
13C chemical shifts148
15N chemical shifts42
1H chemical shifts207

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1plectasin1

Entities:

Entity 1, plectasin 40 residues - Formula weight is not available

1   GLYPHEGLYCYSASNGLYPROTRPASPGLU
2   ASPASPMETGLNCYSHISASNHISCYSLYS
3   SERILELYSGLYTYRLYSGLYGLYTYRCYS
4   ALALYSGLYGLYPHEVALCYSLYSCYSTYR

Samples:

sample_1: plectasin 1.12 mM; DSS 1.7 mM; citric acid 1.8 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 4.28; pressure: 1 atm; temperature: 298.1 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3 and 2.1, Bruker Biospin, Keller and Wuthrich - chemical shift assignment, collection, data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
EMBL CAI83768
SP Q53I06
AlphaFold Q53I06

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