BMRB Entry 50476

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50476

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Title:
NfsB chemical shifts
Deposition date:
2020-09-22
Original release date:
2021-01-25
Authors:
Hyde, Eva; Chau, Alex; Smith, Lorna
Citation:

Citation: Hyde, Eva; Chau, Alex; Smith, Lorna. "Backbone assignment of E. coli NfsB and the effects of addition of the cofactor analogue nicotinic acid"  Biomol. NMR Assignments 15, 143-151 (2021).
PubMed: 33423170

Assembly members:

Assembly members:
entity_1, polymer, 217 residues, 23905.1 Da.
entity_FMN, non-polymer, 456.344 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11c

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MDIISVALKRHSTKAFDASK KLTPEQAEQIKTLLQYSPSS TNSQPWHFIVASTEEGKARV AKSAAGNYVFNERKMLDASH VVVFCAKTAMDDVWLKLVVD QEDADGRFATPEAKAANDKG RKFFADMHRKDLHDDAEWMA KQVYLNVGNFLLGVAALGLD AVPIEGFDAAILDAEFGLKE KGYTSLVVVPVGHHSVEDFN ATLPKSRLPQNITLTEV

Data sets:
Data typeCount
13C chemical shifts619
15N chemical shifts198
1H chemical shifts201

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1E. coli NfsB, chain 11
2E. coli NfsB, chain 21
3FMN, 12
4FMN, 22

Entities:

Entity 1, E. coli NfsB, chain 1 217 residues - 23905.1 Da.

1   METASPILEILESERVALALALEULYSARG
2   HISSERTHRLYSALAPHEASPALASERLYS
3   LYSLEUTHRPROGLUGLNALAGLUGLNILE
4   LYSTHRLEULEUGLNTYRSERPROSERSER
5   THRASNSERGLNPROTRPHISPHEILEVAL
6   ALASERTHRGLUGLUGLYLYSALAARGVAL
7   ALALYSSERALAALAGLYASNTYRVALPHE
8   ASNGLUARGLYSMETLEUASPALASERHIS
9   VALVALVALPHECYSALALYSTHRALAMET
10   ASPASPVALTRPLEULYSLEUVALVALASP
11   GLNGLUASPALAASPGLYARGPHEALATHR
12   PROGLUALALYSALAALAASNASPLYSGLY
13   ARGLYSPHEPHEALAASPMETHISARGLYS
14   ASPLEUHISASPASPALAGLUTRPMETALA
15   LYSGLNVALTYRLEUASNVALGLYASNPHE
16   LEULEUGLYVALALAALALEUGLYLEUASP
17   ALAVALPROILEGLUGLYPHEASPALAALA
18   ILELEUASPALAGLUPHEGLYLEULYSGLU
19   LYSGLYTYRTHRSERLEUVALVALVALPRO
20   VALGLYHISHISSERVALGLUASPPHEASN
21   ALATHRLEUPROLYSSERARGLEUPROGLN
22   ASNILETHRLEUTHRGLUVAL

Entity 2, FMN, 1 - C17 H21 N4 O9 P - 456.344 Da.

1   FMN

Samples:

sample_1: E. coli NfsB homodimer, [U-100% 13C; U-100% 15N; U-80% 2H], 1 mM; sodium phosphate 20 mM; EDTA 0.05 mM; D2O, [U-2H], 10%; AEBSF protease inhibitor 1 uM

sample_2: E. coli NfsB homodimer, [U-100% 15N], 1 mM; sodium phosphate 20 mM; EDTA 0.05 mM; D2O, [U-2H], 10%; AEBSF protease inhibitor 1 uM

sample_conditions_1: ionic strength: 0.025 M; pH: 7.0; pressure: 1 atm; temperature: 310 K

sample_conditions_2: ionic strength: 0.025 M; pH: 7.0; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_2
3D HN(CO)CAsample_1isotropicsample_conditions_2
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 15N-separated NOESYsample_2isotropicsample_conditions_2

Software:

NMRPipe - processing

SPARKY v3 - chemical shift assignment

CcpNMR vV2 - chemical shift assignment

TALOS-N - structure solution

DANGLE - structure solution

VNMR - collection

NMRView v5 - chemical shift assignment

NMR spectrometers:

  • Varian Unity 800 MHz
  • Varian Unity 600 MHz

Related Database Links:

UNP P38489
AlphaFold P19575

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