BMRB Entry 17492

Title:
Trn- peptide of the two-component bacteriocin Thuricin CD
Deposition date:
2011-02-25
Original release date:
2011-05-05
Authors:
Sit, Clarissa; McKay, Ryan; Hill, Colin; Ross, R.; Vederas, John
Citation:

Citation: Sit, Clarissa; McKay, Ryan; Hill, Colin; Ross, R. Paul; Vederas, John. "The 3D Structure of Thuricin CD, a Two-Component Bacteriocin with Cysteine Sulfur to -Carbon Cross-links."  J. Am. Chem. Soc. 133, 7680-7683 (2011).
PubMed: 21526839

Assembly members:

Assembly members:
Thuricin, polymer, 30 residues, 2770.219 Da.

Natural source:

Natural source:   Common Name: B.thuringiensis   Taxonomy ID: 1428   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus thuringiensis

Experimental source:

Experimental source:   Production method: purified from the natural source   Host organism: Bacillus thuringiensis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Thuricin: GNAACVIGCIGSCVISEGIG SLVGTAFXLG

Data sets:
Data typeCount
13C chemical shifts105
15N chemical shifts30
1H chemical shifts177

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Thuricin1

Entities:

Entity 1, Thuricin 30 residues - 2770.219 Da.

1   GLYASNALAALACYSVALILEGLYCYSILE
2   GLYSERCYSVALILESERGLUGLYILEGLY
3   SERLEUVALGLYTHRALAPHEDTHLEUGLY

Samples:

Trna: Trna, [U-99% 13C; U-99% 15N], 0.5 mM; DSS 100 uM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCTrnaisotropicsample_conditions_1
3D HNHATrnaisotropicsample_conditions_1
3D CBCA(CO)NHTrnaisotropicsample_conditions_1
3D HCCH-TOCSYTrnaisotropicsample_conditions_1
3D HNCOTrnaisotropicsample_conditions_1
rtm-HNCATrnaisotropicsample_conditions_1
3D HNCACBTrnaisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticTrnaisotropicsample_conditions_1
3D 1H-15N NOESYTrnaisotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB

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