BMRB Entry 51790

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51790

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Title:
NMR resonance assignments of the Arabidopsis thaliana minimal interaction domains of DRB7.2:DRB4 complex
Deposition date:
2023-01-22
Original release date:
2023-06-19
Authors:
Paturi, Sneha; Deshmukh, Mandar
Citation:

Citation: Paturi, Sneha; Deshmukh, Mandar. "NMR resonance assignments of 18.5 kDa complex of Arabidopsis thaliana DRB7.2:DRB4 interaction domains"  Biomol. NMR Assignments 17, 173-178 (2023).
PubMed: 37256435

Assembly members:

Assembly members:
entity_1, polymer, 97 residues, Formula weight is not available
entity_2, polymer, 71 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETtrx-1b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMTTEPTTEEETQRSSAKS QLYNLCSVRHWKAPLYEYIA EGPCHMKIFTGKVTVEMKED SRITVLECFGNPQYKKKIAA EQAAEAALWYLKNVGLE
entity_2: METSSCVVDESEKKKLIMGT GHLSIPTGQHVVCRPWNPEI TLPQDAEMLFRDDKFIAYRL VKPLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts334
15N chemical shifts85
1H chemical shifts470

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DRB7.2M1
2DRB4D32

Entities:

Entity 1, DRB7.2M 97 residues - Formula weight is not available

1   GLYALAMETTHRTHRGLUPROTHRTHRGLU
2   GLUGLUTHRGLNARGSERSERALALYSSER
3   GLNLEUTYRASNLEUCYSSERVALARGHIS
4   TRPLYSALAPROLEUTYRGLUTYRILEALA
5   GLUGLYPROCYSHISMETLYSILEPHETHR
6   GLYLYSVALTHRVALGLUMETLYSGLUASP
7   SERARGILETHRVALLEUGLUCYSPHEGLY
8   ASNPROGLNTYRLYSLYSLYSILEALAALA
9   GLUGLNALAALAGLUALAALALEUTRPTYR
10   LEULYSASNVALGLYLEUGLU

Entity 2, DRB4D3 71 residues - Formula weight is not available

1   METGLUTHRSERSERCYSVALVALASPGLU
2   SERGLULYSLYSLYSLEUILEMETGLYTHR
3   GLYHISLEUSERILEPROTHRGLYGLNHIS
4   VALVALCYSARGPROTRPASNPROGLUILE
5   THRLEUPROGLNASPALAGLUMETLEUPHE
6   ARGASPASPLYSPHEILEALATYRARGLEU
7   VALLYSPROLEUGLUHISHISHISHISHIS
8   HIS

Samples:

sample_1: DRB7.2M, [U-13C; U-15N], 2H (~ 90%), 400 uM; DRB4D3, 2H (~ 90%), 400 uM; Kphosh 50 mM; NaCl 50 mM; Na2SO4 50 mM; DTT 2 mM

sample_2: DRB7.2M, [U-13C; U-15N], 2H (~ 50%), 400 uM; DRB4D3, 2H (~ 90%), 400 uM; Kphosh 50 mM; NaCl 50 mM; Na2SO4 50 mM; DTT 2 mM

sample_3: DRB7.2M, [U-15N], 2H (~ 50%), 400 uM; DRB4D3, 2H (~ 90%), 400 uM; Kphosh 50 mM; NaCl 50 mM; Na2SO4 50 mM; DTT 2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D H(CCO)NH TOCSYsample_2isotropicsample_conditions_1
3D (H)C(CO)NH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-15N IPAP HSQCsample_3anisotropicsample_conditions_1

Software:

CARA v1.8.4 - chemical shift assignment

TOPSPIN v4.1 - collection and processing

NMRFAM-SPARKY - data visualization

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz MHz

Related Database Links:

TAIR AT4G00420 AT3G62800.1

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