BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 27168

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27168

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Title: 1H, 15N, and 13C chemical shift assignments of the micelle immersed C-terminal FATC domain of the human DNA-dependent protein kinase catalytic subunit (DNA-PKcs) fused to the B1 domain of streptococcal protein G (GB1)   PubMed: 29349619

Deposition date: 2017-07-06 Original release date: 2018-02-02

Authors: Abd Rahim, Munirah Sufiyah; Dames, Sonja; Sommer, Lisa; Shaad, Martin

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).

Assembly members:
hdnapkfatc, polymer, 100 residues, 11170.25 Da.

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: pGEV2

Entity Sequences (FASTA):
hdnapkfatc: MQYKLALNGKTLKGETTTEA VDAATAEKVVKQFANDNGVD GEWTYDDATKTFTVTELVPR GSDDDDKSGLSEETQVKCLM DQATDPNILGRTWEGWEPWM

Data sets:
Data typeCount
13C chemical shifts288
15N chemical shifts105
1H chemical shifts569

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1gb1ent-dnapkfatc1

Entities:

Entity 1, gb1ent-dnapkfatc 100 residues - 11170.25 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   VALASPALAALATHRALAGLULYSVALVAL
4   LYSGLNPHEALAASNASPASNGLYVALASP
5   GLYGLUTRPTHRTYRASPASPALATHRLYS
6   THRPHETHRVALTHRGLULEUVALPROARG
7   GLYSERASPASPASPASPLYSSERGLYLEU
8   SERGLUGLUTHRGLNVALLYSCYSLEUMET
9   ASPGLNALATHRASPPROASNILELEUGLY
10   ARGTHRTRPGLUGLYTRPGLUPROTRPMET

Samples:

sample_1: gb1ent-dnapkfatc, [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-dnapkfatc, [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-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_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

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 750 MHz

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