BMRB Entry 25193

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25193

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Title:
NMR resonance assignment of the lantibiotic immunity protein NisI
Deposition date:
2014-09-02
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, 227 residues, 25836.6 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: pQE9-His6-TEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NisI: GSYQTSHKKVRFDEGSYTNF IYDNKSYFVTDKEIPQENVN NSKVKFYKLLIVDMKSEKLL SSSNKNSVTLVLNNIYEASD KSLCMGINDRYYKILPESDK GAVKALRLQNFDVTSDISDD NFVIDKNDSRKIDYMGNIYS ISDTTVSDEELGEYQDVLAE VRVFDSVSGKSIPRSEWGRI DKDGSNSKQSRTEWDYGEIH SIRGKSLTEAFAVEINDDFK LATKVGN

Data sets:
Data typeCount
13C chemical shifts641
15N chemical shifts217
1H chemical shifts217

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NisI1

Entities:

Entity 1, NisI 227 residues - 25836.6 Da.

1   GLYSERTYRGLNTHRSERHISLYSLYSVAL
2   ARGPHEASPGLUGLYSERTYRTHRASNPHE
3   ILETYRASPASNLYSSERTYRPHEVALTHR
4   ASPLYSGLUILEPROGLNGLUASNVALASN
5   ASNSERLYSVALLYSPHETYRLYSLEULEU
6   ILEVALASPMETLYSSERGLULYSLEULEU
7   SERSERSERASNLYSASNSERVALTHRLEU
8   VALLEUASNASNILETYRGLUALASERASP
9   LYSSERLEUCYSMETGLYILEASNASPARG
10   TYRTYRLYSILELEUPROGLUSERASPLYS
11   GLYALAVALLYSALALEUARGLEUGLNASN
12   PHEASPVALTHRSERASPILESERASPASP
13   ASNPHEVALILEASPLYSASNASPSERARG
14   LYSILEASPTYRMETGLYASNILETYRSER
15   ILESERASPTHRTHRVALSERASPGLUGLU
16   LEUGLYGLUTYRGLNASPVALLEUALAGLU
17   VALARGVALPHEASPSERVALSERGLYLYS
18   SERILEPROARGSERGLUTRPGLYARGILE
19   ASPLYSASPGLYSERASNSERLYSGLNSER
20   ARGTHRGLUTRPASPTYRGLYGLUILEHIS
21   SERILEARGGLYLYSSERLEUTHRGLUALA
22   PHEALAVALGLUILEASNASPASPPHELYS
23   LEUALATHRLYSVALGLYASN

Samples:

15N: sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 200 uM; DTT 1 mM; DSS 30 uM; NisI2-226, [U-15N], 400 mM; H2O 90%; D2O 10%

2H15N13C: sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 200 uM; DTT 1 mM; DSS 30 uM; NisI2-226, [U-13C; U-15N; U-2H], 400 uM; H2O 90%; D2O 10%

13CTyr-15NLys: sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 200 uM; DTT 1 mM; DSS 30 uM; NisI2-226, [13C]-Tyr, [15N]-Lys, 400 uM; H2O 90%; D2O 10%

13CThr-15NLys: sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 200 uM; DTT 1 mM; DSS 30 uM; NisI2-226, [13C]-Thr, [15N]-Lys, 400 uM; H2O 90%; D2O 10%

15NTyr: sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 200 uM; DTT 1 mM; DSS 30 uM; NisI2-226, [15N]-Tyr, 200 uM; H2O 90%; D2O 10%

13CHis-15NLys: sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 200 uM; DTT 1 mM; DSS 30 uM; NisI2-226, [13C]-His, [15N]-Lys, 300 uM; H2O 90%; D2O 10%

13CPRro-15NArg: sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 200 uM; DTT 1 mM; DSS 30 uM; NisI2-226, [13C]-Pro, [15N]-Arg, 100 uM; H2O 90%; D2O 10%

15NPhe: sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 200 uM; DTT 1 mM; DSS 30 uM; NisI2-226, [15N]-Phe, 500 uM; H2O 90%; D2O 10%

sample_conditions_01: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15Nisotropicsample_conditions_01
3D HNCA2H15N13Cisotropicsample_conditions_01
3D HNCACB2H15N13Cisotropicsample_conditions_01
3D HNCACO2H15N13Cisotropicsample_conditions_01
3D HNCO2H15N13Cisotropicsample_conditions_01
3D HN(CO)CA2H15N13Cisotropicsample_conditions_01
2D 1H-15N HSQC13CTyr-15NLysisotropicsample_conditions_01
2D HNCO13CTyr-15NLysisotropicsample_conditions_01
2D 1H-15N HSQC13CThr-15NLysisotropicsample_conditions_01
2D HNCO13CThr-15NLysisotropicsample_conditions_01
2D 1H-15N HSQC15NTyrisotropicsample_conditions_01
2D 1H-15N HSQC13CHis-15NLysisotropicsample_conditions_01
2D HNCO13CHis-15NLysisotropicsample_conditions_01
2D 1H-15N HSQC13CPRro-15NArgisotropicsample_conditions_01
2D HNCO13CPRro-15NArgisotropicsample_conditions_01
2D 1H-15N HSQC15NPheisotropicsample_conditions_01

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 25194
DBJ BAL50562
EMBL CAA54209 CAA79465
GB AAA25193 AAQ89591 AAQ89592 ACM62695 ADJ56356
REF WP_014570409 WP_015425983 WP_017864237 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