BMRB Entry 27167

Title:
1H, 15N, and 13C chemical shift assignments of the micelle immersed C-terminal FATC domain of the human protein kinase ataxia-telangiectasia mutated (ATM) fused to the B1 domain of streptococcal protein G (GB1)
Deposition date:
2017-07-06
Original release date:
2018-02-02
Authors:
Abd Rahim, Munirah Sufiyah; Dames, Sonja Alexandra; Sommer, Lisa; Shaad, Martin; Wacker, Anja
Citation:

Citation: Rahim, M.; Sommer, L.; Wacker, A.; Schaad, M.; Dames, S.. "1H, 15N, and 13C chemical shift assignments of the micelle immersed FAT C-terminal (FATC) domains of the human protein kinases ataxia-telangiectasia mutated (ATM) and DNA-dependent protein kinase catalytic subunit (DNA-PKcs) fused to the B1 domain of streptococcal protein G (GB1)"  Biomol. NMR Assign. 12, 149-154 (2018).
PubMed: 29349619

Assembly members:

Assembly members:
hatmfatc, polymer, 100 residues, 11010.30 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEV2

Data sets:
Data typeCount
13C chemical shifts332
15N chemical shifts109
1H chemical shifts665

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1gb1ent-atmfatc1

Entities:

Entity 1, gb1ent-atmfatc 100 residues - 11010.30 Da.

Residue 1-56 represent the GB1 tag and are followed by a thrombin (LVPRGS) and an enterokinase (DDDDK) site. Residue 68-100 correspond to the FATC domain.

1   METGLNTYRLYSLEUALALEUASNGLYLYS
2   THRLEULYSGLYGLUTHRTHRTHRGLUALA
3   VALASPALAALATHRALAGLULYSVALPHE
4   LYSGLNTYRALAASNASPASNGLYVALASP
5   GLYGLUTRPTHRTYRASPASPALATHRLYS
6   THRPHETHRVALTHRGLULEUVALPROARG
7   GLYSERASPASPASPASPLYSTHRVALLEU
8   SERVALGLYGLYGLNVALASNLEULEUILE
9   GLNGLNALAILEASPPROLYSASNLEUSER
10   ARGLEUPHEPROGLYTRPLYSALATRPVAL

Samples:

sample_1: gb1ent-atmfatc, [U-100% 13C; U-100% 15N], 0.4 mM; TRIS 50 mM; sodium chloride 100 mM; sodium azide 0.2%; H2O 95%; D2O, [U-100% 2H], 5%; DPC, [U-100% 2H], 150 mM

sample_2: gb1ent-atmfatc, [U-100% 15N], 0.4 mM; TRIS 50 mM; sodium chloride 100 mM; sodium azide 0.2%; H2O 95%; D2O, [U-100% 2H], 5%; DPC, [U-100% 2H], 150 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
15N T1sample_2isotropicsample_conditions_1
15N T2sample_2isotropicsample_conditions_1
{1H}-15N-NOEsample_2isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

X-PLOR_NIH v2. 16. 0, Schwieters, Kuszewski, Tjandra and Clore - structure solution

ProcheckNMR, Laskowski and MacArthur - structure analysis

Molmol, Koradi, Billeter and Wuthrich - structure visualization

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

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