BMRB Entry 52612

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52612

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Title:
Backbone resonance assignments of the C-terminal thioesterase domain of tyrocidine synthetase C
Deposition date:
2024-09-16
Original release date:
2025-01-09
Authors:
Takeda, Mitsuhiro; Saito, Rino; Nagae, Takayuki; Aoyama, Hiroshi; Mishima, Masaki
Citation:

Citation: Takeda, Mitsuhiro; Saito, Rino; Konno, Sho; Nagae, Takayuki; Aoyama, Hiroshi; Yoshinaga, Sosuke; Terasawa, Hiroaki; Taguchi, Akihiro; Taniguchi, Atsuhiko; Hayashi, Yoshio; Mishima, Masaki. "Backbone resonance assignments of the C-terminal thioesterase domain of tyrocidine synthetase C"  Biomol. NMR Assignments ., .-. (2024).
PubMed: 39661265

Assembly members:

Assembly members:
entity_1, polymer, 254 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Brevibacillus parabrevis   Taxonomy ID: 54914   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Brevibacillus parabrevis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGKRFESRYGTAILLNQET ARNVFCFTPIGAQSVYYQKL AAEIQGVSLYSFDFIQDDNR MEQYIAAITAIDPSGPYTLM GYSSGGNLAFEVAKELEERG YGVTDIILFDSYWKDKAIER TVAETENDIAQLFAEIGENT EMFNMTQEDFQLYAANEFVK QSFVRKTVSYVMFHNNLVNT GMTTAAIHLIQSELEADEEA PVAAKWNESAWANATQRLLT YSGHGIHSRMLAGDYASQNA SILQNILQELFILK

Data sets:
Data typeCount
13C chemical shifts719
15N chemical shifts238
1H chemical shifts238

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1The C-terminal thioesterase domain of tyrocidine synthetase C monomer1

Entities:

Entity 1, The C-terminal thioesterase domain of tyrocidine synthetase C monomer 254 residues - Formula weight is not available

1   GLYPROGLYLYSARGPHEGLUSERARGTYR
2   GLYTHRALAILELEULEUASNGLNGLUTHR
3   ALAARGASNVALPHECYSPHETHRPROILE
4   GLYALAGLNSERVALTYRTYRGLNLYSLEU
5   ALAALAGLUILEGLNGLYVALSERLEUTYR
6   SERPHEASPPHEILEGLNASPASPASNARG
7   METGLUGLNTYRILEALAALAILETHRALA
8   ILEASPPROSERGLYPROTYRTHRLEUMET
9   GLYTYRSERSERGLYGLYASNLEUALAPHE
10   GLUVALALALYSGLULEUGLUGLUARGGLY
11   TYRGLYVALTHRASPILEILELEUPHEASP
12   SERTYRTRPLYSASPLYSALAILEGLUARG
13   THRVALALAGLUTHRGLUASNASPILEALA
14   GLNLEUPHEALAGLUILEGLYGLUASNTHR
15   GLUMETPHEASNMETTHRGLNGLUASPPHE
16   GLNLEUTYRALAALAASNGLUPHEVALLYS
17   GLNSERPHEVALARGLYSTHRVALSERTYR
18   VALMETPHEHISASNASNLEUVALASNTHR
19   GLYMETTHRTHRALAALAILEHISLEUILE
20   GLNSERGLULEUGLUALAASPGLUGLUALA
21   PROVALALAALALYSTRPASNGLUSERALA
22   TRPALAASNALATHRGLNARGLEULEUTHR
23   TYRSERGLYHISGLYILEHISSERARGMET
24   LEUALAGLYASPTYRALASERGLNASNALA
25   SERILELEUGLNASNILELEUGLNGLULEU
26   PHEILELEULYS

Samples:

sample_1: The C-terminal thioesterase domain of tyrocidine synthetase C, [U-13C; U-15N; U-2H], 0.8 mM; HEPES 20 mM; potassium chloride 50 mM; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CAsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CACBsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1
3D TROSY-HN(CA)COsample_1isotropicsample_conditions_1

Software:

SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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