BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 52308

Title: Backbone chemical shift assignments of human ZNF706   PubMed: 37790366

Deposition date: 2024-02-05 Original release date: 2024-04-17

Authors: Sahoo, Bikash; Bardwell, James

Citation: Sahoo, Bikash; Kocman, Vojc; Clark, Nathan; Myers, Nikhil; Deng, Xiexiong; Wong, Ee; Yang, Harry; Kotar, Anita; Guzman, Bryan; Dominguez, Daniel; Plavec, Janez; Bardwell, James. "Effects of protein G-quadruplex interactions on phase transitions and protein aggregation."  bioRxiv ., .-. (2023).

Assembly members:
entity_1, polymer, 76 residues, 8498 Da.
entity_ZN, non-polymer, 65.409 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: pET28

Entity Sequences (FASTA):
entity_1: MARGQQKIQSQQKNAKKQAG QKKKQGHDQKAAAKAALIYT CTVCRTQMPDPKTFKQHFES KHPKTPLPPELADVQA

Data sets:
Data typeCount
13C chemical shifts178
15N chemical shifts62
1H chemical shifts62

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Human ZNF7061
2ZINC ION2

Entities:

Entity 1, Human ZNF706 76 residues - 8498 Da.

1   METALAARGGLYGLNGLNLYSILEGLNSER
2   GLNGLNLYSASNALALYSLYSGLNALAGLY
3   GLNLYSLYSLYSGLNGLYHISASPGLNLYS
4   ALAALAALALYSALAALALEUILETYRTHR
5   CYSTHRVALCYSARGTHRGLNMETPROASP
6   PROLYSTHRPHELYSGLNHISPHEGLUSER
7   LYSHISPROLYSTHRPROLEUPROPROGLU
8   LEUALAASPVALGLNALA

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Human ZNF706, [U-15N], 750 uM; Human ZNF706, [U-13C], 750 uM; sodium phosphate 20 mM; NaCl 20 mM; D2O, [U-2H], 7.5%

sample_conditions_1: ionic strength: 0.02 M; pH: 7.4; pressure: 1 atm; temperature: 277.1 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TopSpin, NMRFAM-SPARKY v4.1.4; 1.470 - chemical shift assignment, collection, data analysis

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

Related Database Links:

UNP Q9Y5V0

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