BMRB Entry 50803

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50803

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Title:
Chemical shift assignment of NDRG1-C, the C-terminal domain of NDRG1
Deposition date:
2021-03-07
Original release date:
2022-10-13
Authors:
Ciurli, Stefano; Zambelli, Barbara
Citation:

Citation: Beniamino, Ylenia; Cenni, Vittoria; Piccioli, Mario; Ciurli, Stefano; Zambelli, Barbara. "The Ni(II)-Binding Activity of the Intrinsically Disordered Region of Human NDRG1, a Protein Involved in Cancer Development"  Biomolecules 12, 1272-1272 (2022).
PubMed: 36139110

Assembly members:

Assembly members:
entity_1, polymer, 85 residues, 8826.57 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: pETZZ_1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMGYMPSASMTRLMRSRTA SGSSVTSLDGTRSRSHTSEG TRSRSHTSEGTRSRSHTSEG AHLDITPNSGAAGNSAGPKS MEVSC

Data sets:
Data typeCount
13C chemical shifts322
15N chemical shifts81
1H chemical shifts481

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NDRG1-C1

Entities:

Entity 1, NDRG1-C 85 residues - 8826.57 Da.

1   GLYHISMETGLYTYRMETPROSERALASER
2   METTHRARGLEUMETARGSERARGTHRALA
3   SERGLYSERSERVALTHRSERLEUASPGLY
4   THRARGSERARGSERHISTHRSERGLUGLY
5   THRARGSERARGSERHISTHRSERGLUGLY
6   THRARGSERARGSERHISTHRSERGLUGLY
7   ALAHISLEUASPILETHRPROASNSERGLY
8   ALAALAGLYASNSERALAGLYPROLYSSER
9   METGLUVALSERCYS

Samples:

sample_1: NDRG1-C, [U-100% 13C; U-100% 15N], 0.9 ± 0.05 mM; HEPES 20 mM; NaCl 150 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.0.3 - collection

NMRPipe v10.9 - processing

NMRFAM-SPARKY v3.19 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 1200 MHz

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