BMRB Entry 51994

Title:
1H, 15N and 13C backbone and side chain solution NMR assignments of the TPM domain-containing protein of the thermophilic bacterium Rhodothermus marinus
Deposition date:
2023-06-08
Original release date:
2023-10-03
Authors:
Pellizza, Leonardo; Arganaraz Araoz, Julio; Ramis, Lila; Aran, Martin
Citation:

Citation: Pellizza, Leonardo; Arganaraz Araoz, Julio; Ramis, Lila; Aran, Martin. "1H, 15N and 13C backbone and side chain solution NMR assignments of the TPM domain-containing protein of the thermophilic bacterium Rhodothermus marinus"  Biomol. NMR Assign. 17, 229-233 (2023).
PubMed: 37542635

Assembly members:

Assembly members:
entity_1, polymer, 145 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Rhodothermus marinus   Taxonomy ID: 29549   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Rhodothermus marinus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b+

Data sets:
Data typeCount
13C chemical shifts578
15N chemical shifts141
1H chemical shifts947

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TPMRM1

Entities:

Entity 1, TPMRM 145 residues - Formula weight is not available

1   GLYMETGLNILEGLUVALILEPROPROSER
2   GLYGLNTRPVALTHRASPLEUALAASPLEU
3   LEUTHRPROALAGLUGLUARGMETLEUSER
4   ARGLYSLEUALATHRTYRALAASPTHRTHR
5   SERTHRGLNILEVALILEVALTHRLEUPRO
6   THRLEUASNGLYVALPROALAALAASPTYR
7   ALAVALGLULEUGLYARGARGTRPGLYVAL
8   GLYGLNLYSGLUTYRASPASNGLYVALVAL
9   ILELEUVALALAARGGLUGLUARGGLUVAL
10   PHEILEALATHRGLYTYRGLYLEUGLUGLY
11   ALAILEPROASPALALEUALAGLYARGILE
12   VALARGASPILEILEVALPROARGPHEARG
13   ARGGLYASPPHETYRGLYGLYLEUSERALA
14   ALAVALASPALAILEILEALAALAALAGLN
15   GLYGLUPHEGLNPRO

Samples:

sample_1: TPMRM Domain, [U-100% 13C; U-100% 15N], 500 uM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

NMRViewJ - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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