BMRB Entry 52712

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52712

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Title:
Chemical shifts of the LC8-binding region of rGKAP residues
Deposition date:
2024-11-19
Original release date:
2025-08-28
Authors:
Nagy-Kanta, Eszter; Tossavainen, Helena; Gaspari, Zoltan; Peterfia, Balint; Permi, Perttu
Citation:

Citation: Nagy-Kanta, Eszter; Kalman, Zsofia; Tossavainen, Helena; Juhasz, Tunde; Farkas, Fanni; Hegedus, Jozsef; Keresztes, Melinda; Beke-Somfai, Tamas; Gaspari, Zoltan; Permi, Perttu; Peterfia, Balint. "Residual flexibility in the topologically constrained multivalent complex between the GKAP scaffold and LC8 hub proteins"  FEBS J. ., .-. (2025).
PubMed: 40843979

Assembly members:

Assembly members:
entity_1, polymer, 61 residues, 7015 Da.

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMRKKDFKKNRCLSIGIQ VDDAEESEKMAESKTSSKFQ SVGVQVEEEKCFRRFTRSNS V

Data sets:
Data typeCount
13C chemical shifts192
15N chemical shifts57
1H chemical shifts283

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1rGKAP_655-7111

Entities:

Entity 1, rGKAP_655-711 61 residues - 7015 Da.

The construct includes 4 residues on the N terminus (GSHM), which are remaining from the non-native affinity tag and the protease cleavage site.

1   GLYSERHISMETARGLYSLYSASPPHELYS
2   LYSASNARGCYSLEUSERILEGLYILEGLN
3   VALASPASPALAGLUGLUSERGLULYSMET
4   ALAGLUSERLYSTHRSERSERLYSPHEGLN
5   SERVALGLYVALGLNVALGLUGLUGLULYS
6   CYSPHEARGARGPHETHRARGSERASNSER
7   VAL

Samples:

sample_1: rGKAP_655-711, [U-100% 13C][U-100% 15N], 280 uM; sodium azide 0.02%; sodium chloride 20 mM; sodium phosphate 50 mM; TCEP 5 mM

sample_conditions_1: ionic strength: 70 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D iHNCOsample_1isotropicsample_conditions_1
3D H(CC)(CO)NHsample_1isotropicsample_conditions_1
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5.7 - collection, processing

CcpNMR v3.1.1 - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

Related Database Links:

UNP P97836-1

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