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 25194

Title: NMR resonance assignment of the C-terminal domain of the lantibiotic immunity protein NisI   PubMed: 25613223

Authors: Hacker, Carolin; Christ, Nina Alexandra; Duchardt-Ferner, Elke; Bernigner, Lucija; Koetter, Peter; Entian, Karl-Dieter; Woehnert, Jens

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).

Assembly members:
NisI, polymer, 130 residues, 14562.9 Da.

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

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

Entity Sequences (FASTA):
NisI: SDKGAVKALRLQNFDVTSDI SDDNFVIDKNDSRKIDYMGN IYSISDTTVSDEELGEYQDV LAEVRVFDSVSGKSIPRSEW GRIDKDGSNSKQSRTEWDYG EIHSIRGKSLTEAFAVEIND DFKLATKVGN

Data sets:
Data typeCount
13C chemical shifts537
15N chemical shifts138
1H chemical shifts836

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NisI1

Entities:

Entity 1, NisI 130 residues - 14562.9 Da.

1   SERASPLYSGLYALAVALLYSALALEUARG
2   LEUGLNASNPHEASPVALTHRSERASPILE
3   SERASPASPASNPHEVALILEASPLYSASN
4   ASPSERARGLYSILEASPTYRMETGLYASN
5   ILETYRSERILESERASPTHRTHRVALSER
6   ASPGLUGLULEUGLYGLUTYRGLNASPVAL
7   LEUALAGLUVALARGVALPHEASPSERVAL
8   SERGLYLYSSERILEPROARGSERGLUTRP
9   GLYARGILEASPLYSASPGLYSERASNSER
10   LYSGLNSERARGTHRGLUTRPASPTYRGLY
11   GLUILEHISSERILEARGGLYLYSSERLEU
12   THRGLUALAPHEALAVALGLUILEASNASP
13   ASPPHELYSLEUALATHRLYSVALGLYASN

Samples:

15N: sodium phosphate 50 mM; sodium chloride 100 mM; DSS 30 uM; NisI97-226, [U-15N], 400 uM; H2O 90%; D2O 10%

15N13C: sodium phosphate 50 mM; sodium chloride 100 mM; DSS 30 uM; NisI97-226, [U-13C; U-15N], 400 uM; H2O 90%; D2O 10%

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 CAA79465
GB AAA25193 AAQ89591 AAQ89592 ACM62695 ADA64984
REF WP_012897848 WP_014570409 WP_015425983 WP_017864237 WP_039114828
SP P42708