BMRB Entry 27884

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27884

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Title:
Backbone assignment of HMGA1a S64C mutant phosphorylated by Casein Kinase 2
Deposition date:
2019-04-25
Original release date:
2019-07-25
Authors:
Kohl, Bastian; Zhong, Xueyin; Herrmann, Christian; Stoll, Raphael
Citation:

Citation: Kohl, Bastian; Zhong, Xueyin; Herrmann, Christian; Stoll, Raphael. "Phosphorylation orchestrates the structural ensemble of the intrinsically disordered protein HMGA1a and modulates its DNA binding to the NFkB promoter"  Nucleic Acids Res. 47, 11906-11920 (2019).
PubMed: 31340016

Assembly members:

Assembly members:
HMGA1a, polymer, 107 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:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET9a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HMGA1a: MSESSSKSSQPLASKQEKDG TEKRGRGRPRKQPPVSPGTA LVGSQKEPSEVPTPKRPRGR PKGCKNKGAAKTRKTTTTPG RKPRGRPKKLEKEEEEGIXQ EXXEEEQ

Data sets:
Data typeCount
13C chemical shifts216
15N chemical shifts73
1H chemical shifts61

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CK2 HMGA1a S64C1

Entities:

Entity 1, CK2 HMGA1a S64C 107 residues - Formula weight is not available

Serine 64 is mutated into a cysteine

1   METSERGLUSERSERSERLYSSERSERGLN
2   PROLEUALASERLYSGLNGLULYSASPGLY
3   THRGLULYSARGGLYARGGLYARGPROARG
4   LYSGLNPROPROVALSERPROGLYTHRALA
5   LEUVALGLYSERGLNLYSGLUPROSERGLU
6   VALPROTHRPROLYSARGPROARGGLYARG
7   PROLYSGLYCYSLYSASNLYSGLYALAALA
8   LYSTHRARGLYSTHRTHRTHRTHRPROGLY
9   ARGLYSPROARGGLYARGPROLYSLYSLEU
10   GLULYSGLUGLUGLUGLUGLYILESEPGLN
11   GLUSEPSEPGLUGLUGLUGLN

Samples:

sample_1: HMGA1a, [U-99% 13C; U-99% 15N], 1.5 mM; DSS 0.05 mM; HEPES 50 mM; NaCl 150 mM; DTT 20 mM; NaF 2 mM; beta-Glycerolphosphat 2 mM; Sodium pyrophosphate 2 mM

sample_2: HMGA1a, [U-99% 15N], 1.5 mM; DSS 0.05 mM; HEPES 50 mM; NaCl 150 mM; DTT 20 mM; NaF 2 mM; beta-Glycerolphosphat 2 mM; Sodium pyrophosphate 2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOCACBsample_1isotropicsample_conditions_1
3D IPAP-(H)CANCOsample_1isotropicsample_conditions_1
3D IPAP-(H)CBCACONsample_1isotropicsample_conditions_1
2D IPAP-NCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

CCPNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker DRX 600 MHz

Related Database Links:

UNP P17096
AlphaFold Q9UKB0

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