BMRB Entry 51625

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51625

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Title:
Backbone 1H, 13C, and 15N chemical shift assignments for the N-terminal fragment of human YY1
Deposition date:
2022-09-14
Original release date:
2022-12-29
Authors:
Luchinat, Enrico; Banci, Lucia; Gorecki, Andrzej
Citation:

Citation: Figiel, Malgorzata; Szubert, Filip; Luchinat, Enrico; Bonarek, Piotr; Baranowska, Anna; Wajda-Nikiel, Katarzyna; Wilamowski, Mateusz; Milek, Piotr; Dziedzicka-Wasylewska, Marta; Banci, Lucia; Gorecki, Andrzej. "Zinc controls operator affinity of human transcription factor YY1 by mediating dimerization via its N-terminal region"  Biochim. Biophys. Acta Gene Regul. Mech. 1866, 194905-194905 (2023).

Assembly members:

Assembly members:
entity_1, polymer, 295 residues, 31189 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: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MASGDTLYIATDGSEMPAEI VELHEIEVETIPVETIETTV VGEEEEEDDDDEDGGGGDHG GGGGHGHAGHHHHHHHHHHH PPMIALQPLVTDDPTQVHHH QEVILVQTREEVVGGDDSDG LRAEDGFEDQILIPVPAPAG GDDDYIEQTLVTVAAAGKSG GGGSSSSGGGRVKKGGGKKS GKKSYLSGGAGAAGGGGADP GNKKWEQKQVQIKTLEGEFS VTMWSSDEKKDIDHETVVEE QIIGENSPPDYSEYMTGKKL PPGGIPGIDLSDPKQLAEFA RMKPRKIKEDDAPRT

Data sets:
Data typeCount
13C chemical shifts723
15N chemical shifts268
1H chemical shifts240

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1monomeric polypeptide1

Entities:

Entity 1, monomeric polypeptide 295 residues - 31189 Da.

Residues 1-295 of the human protein Ying Yang 1 (YY1), corresponding to the N-terminal fragment.

1   METALASERGLYASPTHRLEUTYRILEALA
2   THRASPGLYSERGLUMETPROALAGLUILE
3   VALGLULEUHISGLUILEGLUVALGLUTHR
4   ILEPROVALGLUTHRILEGLUTHRTHRVAL
5   VALGLYGLUGLUGLUGLUGLUASPASPASP
6   ASPGLUASPGLYGLYGLYGLYASPHISGLY
7   GLYGLYGLYGLYHISGLYHISALAGLYHIS
8   HISHISHISHISHISHISHISHISHISHIS
9   PROPROMETILEALALEUGLNPROLEUVAL
10   THRASPASPPROTHRGLNVALHISHISHIS
11   GLNGLUVALILELEUVALGLNTHRARGGLU
12   GLUVALVALGLYGLYASPASPSERASPGLY
13   LEUARGALAGLUASPGLYPHEGLUASPGLN
14   ILELEUILEPROVALPROALAPROALAGLY
15   GLYASPASPASPTYRILEGLUGLNTHRLEU
16   VALTHRVALALAALAALAGLYLYSSERGLY
17   GLYGLYGLYSERSERSERSERGLYGLYGLY
18   ARGVALLYSLYSGLYGLYGLYLYSLYSSER
19   GLYLYSLYSSERTYRLEUSERGLYGLYALA
20   GLYALAALAGLYGLYGLYGLYALAASPPRO
21   GLYASNLYSLYSTRPGLUGLNLYSGLNVAL
22   GLNILELYSTHRLEUGLUGLYGLUPHESER
23   VALTHRMETTRPSERSERASPGLULYSLYS
24   ASPILEASPHISGLUTHRVALVALGLUGLU
25   GLNILEILEGLYGLUASNSERPROPROASP
26   TYRSERGLUTYRMETTHRGLYLYSLYSLEU
27   PROPROGLYGLYILEPROGLYILEASPLEU
28   SERASPPROLYSGLNLEUALAGLUPHEALA
29   ARGMETLYSPROARGLYSILELYSGLUASP
30   ASPALAPROARGTHR

Samples:

sample_1: YY1-NTF, [U-98% 13C; U-98% 15N], 210 uM; TRIS 50 mM; sodium chloride 100 mM

sample_conditions_1: pH: 7.2; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY-HN(CA)COsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CACBsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1
3D HN(CA)NNHsample_1isotropicsample_conditions_1
2D 13C-detected CONsample_1isotropicsample_conditions_1
3D 13C-detected CBCACONsample_1isotropicsample_conditions_1
3D 13C-detected CBCANCOsample_1isotropicsample_conditions_1
3D 13C-detected COCONsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.0 - collection

NMRPipe - processing

CARA v1.9.1.7 - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE NEO 900 MHz
  • Bruker AVANCE NEO 700 MHz

Related Database Links:

Uniprot P25490
AlphaFold Q14935

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