BMRB Entry 26331

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for tyrosine kinase A domain 5
Deposition date:
2022-06-15
Original release date:
2022-08-11
Authors:
Suzuki, Rika; Ekimoto, Toru; Tosaka, Ayami; Takahashi, Maho; Sakakura, Masayoshi; Yamane, Tsutomu; Mizukoshi, Yumiko; Takeuchi, Koh; Simada, Ichio; Ikeguchi, Mitsunori; Takahash, Hideo
Citation:

Citation: Suzuki, Rika; Ekimoto, Toru; Tosaka, Ayami; Takahashi, Maho; Sakakura, Masayoshi; Yamane, Tsutomu; Mizukoshi, Yumiko; Takeuchi, Koh; Simada, Ichio; Ikeguchi, Mitsunori; Takahash, Hideo. "Dynamic Interaction Modes of Peptide Ligands Revealed by Integrated Use of NMR and REST Simulations"  J. Chem. Inf. Model. ., .-..

Assembly members:

Assembly members:
TrkAd5, polymer, 108 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet21a

Experimental source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet21a

Data sets:
Data typeCount
13C chemical shifts175
15N chemical shifts91
1H chemical shifts91

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TrkAd51

Entities:

Entity 1, TrkAd5 108 residues - Formula weight is not available

1   GLYSERHISMETVALASNVALSERPHEPRO
2   ALASERVALGLNLEUHISTHRALAVALGLU
3   METHISHISTRPCYSILEPROPHESERVAL
4   ASPGLYGLNPROALAPROSERLEUARGTRP
5   LEUPHEASNGLYSERVALLEUASNGLUTHR
6   SERPHEILEPHETHRGLUPHELEUGLUPRO
7   ALAALAASNGLUTHRVALARGHISGLYCYS
8   LEUARGLEUASNGLNPROTHRHISVALASN
9   ASNGLYASNTYRTHRLEULEUALAALAASN
10   PROPHEGLYGLNALASERALASERILEMET
11   ALAALAPHEMETASPASNPROPHE

Samples:

sample_1: TrkAd5, [U-13C; U-15N], protein mM; DSS 2 mM; sodium phosphate 50 mM; sodium chloride 150 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: pH: 7.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

CARA - 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