BMRB Entry 25175

Title:
NMR resonance assignment of the N-terminal domain of the lantibiotic immunity protein NisI
Deposition date:
2014-08-26
Original release date:
2015-04-27
Authors:
Hacker, Carolin; Christ, Nina Alexandra; Duchardt-Ferner, Elke; Bernigner, Lucija; Koetter, Peter; Entian, Karl-Dieter; Woehnert, Jens
Citation:

Citation: Hacker, Carolin; Christ, Nina Alexandra; Duchardt-Ferner, Elke; Bernigner, Lucija; Koetter, Peter; Entian, Karl-Dieter; Woehnert, Jens. "NMR resonance assignments of the lantibiotic immunity protein NisI from Lactococcus lactis"  Biomol NMR Assign. 9, 293-297 (2015).
PubMed: 25613223

Assembly members:

Assembly members:
NisI, polymer, 109 residues, 12779.5 Da.

Natural source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 1358   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Lactococcus lactis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11a-SUMO

Data sets:
Data typeCount
13C chemical shifts493
15N chemical shifts117
1H chemical shifts783

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NisI1

Entities:

Entity 1, NisI 109 residues - 12779.5 Da.

1   TYRGLNTHRSERHISLYSLYSVALARGPHE
2   ASPGLUGLYSERTYRTHRASNPHEILETYR
3   ASPASNLYSSERTYRPHEVALTHRASPLYS
4   GLUILEPROGLNGLUASNVALASNASNSER
5   LYSVALLYSPHETYRLYSLEULEUILEVAL
6   ASPMETLYSSERGLULYSLEULEUSERSER
7   SERASNLYSASNSERVALTHRLEUVALLEU
8   ASNASNILETYRGLUALASERASPLYSSER
9   LEUCYSMETGLYILEASNASPARGTYRTYR
10   LYSILELEUPROGLUSERASPLYSGLYALA
11   VALLYSALALEUARGLEUGLNASNPHE

Samples:

15N: sodium phosphate 50 mM; sodium chloride 100 mM; DSS 30 uM; NisI2-110, [U-15N], 400 uM; D2O 10%; H2O 90%

15N13C: sodium phosphate 50 mM; sodium chloride 100 mM; DSS 30 uM; NisI2-110, [U-13C; U-15N], 400 uM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15Nisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic15N13Cisotropicsample_conditions_1
2D 1H-13C HSQC aromatic15N13Cisotropicsample_conditions_1
3D CBCA(CO)NH15N13Cisotropicsample_conditions_1
3D HNCO15N13Cisotropicsample_conditions_1
3D HNCACB15N13Cisotropicsample_conditions_1
3D HBHA(CO)NH15N13Cisotropicsample_conditions_1
3D H(CCO)NH15N13Cisotropicsample_conditions_1
3D C(CO)NH15N13Cisotropicsample_conditions_1
3D 1H-15N NOESY15Nisotropicsample_conditions_1
3D 1H-13C NOESY aliphatic15N13Cisotropicsample_conditions_1
3D 1H-13C NOESY aromatic15N13Cisotropicsample_conditions_1
3D HNCACO15N13Cisotropicsample_conditions_1

Software:

CCPN_Analysis, CCPN - chemical shift assignment, data analysis

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

TOPSPIN, Bruker Biospin - collection, data analysis, processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 950 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 25193
PDB
DBJ BAL50562
EMBL CAA54209
GB AAA25193 AAQ89591 AAQ89592 ADJ56356 ADZ63253
REF WP_014570409 WP_015425983 WP_039114828 WP_042748180
SP P42708
AlphaFold P42708

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