BMRB Entry 50695

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50695

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Title:
1H, 15N, 13C backbone resonance assignment of the monomer C-terminal domain of Enzyme I from Thermoanaerobacter tengcongensis
Deposition date:
2021-01-06
Original release date:
2021-05-27
Authors:
Nguyen, Trang; Venditti, Vincenzo
Citation:

Citation: Nguyen, Trang; Ghirlando, Rodolfo; Roche, Julien; Venditti, Vincenzo. "Structure elucidation of the elusive Enzyme I monomer reveals the molecular mechanisms linking oligomerization and enzymatic activity"  Proc. Natl. Acad. Sci. U.S.A. 118, e2100298118-e2100298118 (2021).
PubMed: 33975952

Assembly members:

Assembly members:
entity_1, polymer, 315 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Thermus thermophilus   Taxonomy ID: 274   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermus thermophilus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet21A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SMAETPDGKKVMLAANIGTP KDVASALANGAEGVGLFRTE FLYMDRNSLPSEEEQFEAYK EVVEKMGGRPVTIRTLDIGG DKELPYLDMPKEMNPFLGYR AIRLCLDRPDIFKTQLRAIL RASAYGNVQIMYPMISSVEE VEKANSILEEVKAELDREGV KYDKEIKVGIMVEIPSAAVT ARILAKEVDFFSIGTNDLTQ YTLAVDRMNEHVKEYYQPFH PAILRLVKMVIDAAHKEGKF AAMCGEMAGDPLAAVILLGL GLDEFSMSATSIPEIKNIIR NVEYEKAKEIAEKALNMSEA EEIEKMMKDVIKDIG

Data sets:
Data typeCount
13C chemical shifts824
15N chemical shifts288
1H chemical shifts286

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1homodimer 3m-tEIC, chain 11
2homodimer 3m-tEIC, chain 21

Entities:

Entity 1, homodimer 3m-tEIC, chain 1 315 residues - Formula weight is not available

1   SERMETALAGLUTHRPROASPGLYLYSLYS
2   VALMETLEUALAALAASNILEGLYTHRPRO
3   LYSASPVALALASERALALEUALAASNGLY
4   ALAGLUGLYVALGLYLEUPHEARGTHRGLU
5   PHELEUTYRMETASPARGASNSERLEUPRO
6   SERGLUGLUGLUGLNPHEGLUALATYRLYS
7   GLUVALVALGLULYSMETGLYGLYARGPRO
8   VALTHRILEARGTHRLEUASPILEGLYGLY
9   ASPLYSGLULEUPROTYRLEUASPMETPRO
10   LYSGLUMETASNPROPHELEUGLYTYRARG
11   ALAILEARGLEUCYSLEUASPARGPROASP
12   ILEPHELYSTHRGLNLEUARGALAILELEU
13   ARGALASERALATYRGLYASNVALGLNILE
14   METTYRPROMETILESERSERVALGLUGLU
15   VALGLULYSALAASNSERILELEUGLUGLU
16   VALLYSALAGLULEUASPARGGLUGLYVAL
17   LYSTYRASPLYSGLUILELYSVALGLYILE
18   METVALGLUILEPROSERALAALAVALTHR
19   ALAARGILELEUALALYSGLUVALASPPHE
20   PHESERILEGLYTHRASNASPLEUTHRGLN
21   TYRTHRLEUALAVALASPARGMETASNGLU
22   HISVALLYSGLUTYRTYRGLNPROPHEHIS
23   PROALAILELEUARGLEUVALLYSMETVAL
24   ILEASPALAALAHISLYSGLUGLYLYSPHE
25   ALAALAMETCYSGLYGLUMETALAGLYASP
26   PROLEUALAALAVALILELEULEUGLYLEU
27   GLYLEUASPGLUPHESERMETSERALATHR
28   SERILEPROGLUILELYSASNILEILEARG
29   ASNVALGLUTYRGLULYSALALYSGLUILE
30   ALAGLULYSALALEUASNMETSERGLUALA
31   GLUGLUILEGLULYSMETMETLYSASPVAL
32   ILELYSASPILEGLY

Samples:

sample_1: 3m-tEIC, [U-100% 13C; U-100% 15N], 0.75 mM; TRIS 20 mM; DTT 2 mM; EDTA 1 mM; sodium chloride 100 mM; MgCl2 4 mM

sample_conditions_1: pH: 7.4; pressure: 1 bar; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1

Software:

SPARKY - chemical shift assignment, data analysis

NMRPipe - processing

TOPSPIN - collection

NMR spectrometers:

  • Bruker Avance 700 MHz

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