BMRB Entry 51209

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51209

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Title:
Backbone and sidechain 1H, 15N and 13C resonance assignments of the free tandem zinc finger domain of the tristetraprolin family member from Selaginella moellendorffii
Deposition date:
2021-12-02
Original release date:
2022-12-02
Authors:
Hicks, Stephanie; Venters, Ronald; Blackshear, Perry
Citation:

Citation: Hicks, Stephanie; Venters, Ronald; Blackshear, Perry. "Backbone and sidechain 1H, 15N and 13C resonance assignments of the free and RNA-bound tandem zinc finger domain of the tristetraprolin family member from Selaginella moellendorffii"  Biomol. NMR Assign. 16, 153-158 (2022).
PubMed: 35279790

Assembly members:

Assembly members:
entity_1, polymer, 69 residues, 7784.89 Da.
entity_ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Selaginella moellendorffii   Taxonomy ID: 88036   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Selaginella moellendorffii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28/30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: NALYKTELCRSWEETGSCRY GNKCQFAHGKEDLRPVNRHP KYKTEVCRTFSAAGTCPYGK RCRFIHATP

Data sets:
Data typeCount
13C chemical shifts281
15N chemical shifts62
1H chemical shifts395

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tandem Zinc Finger1
2Zn12
3Zn22

Entities:

Entity 1, Tandem Zinc Finger 69 residues - 7784.89 Da.

This tandem zinc finger domain represents residues 10-76 from the full length protein; The first two residues in the assigned chemical shifts list (ASN and ALA) are not part of the S. moellendorfii TTP TZF sequence but are there because of the TEV cleavage site.

1   ASNALALEUTYRLYSTHRGLULEUCYSARG
2   SERTRPGLUGLUTHRGLYSERCYSARGTYR
3   GLYASNLYSCYSGLNPHEALAHISGLYLYS
4   GLUASPLEUARGPROVALASNARGHISPRO
5   LYSTYRLYSTHRGLUVALCYSARGTHRPHE
6   SERALAALAGLYTHRCYSPROTYRGLYLYS
7   ARGCYSARGPHEILEHISALATHRPRO

Entity 2, Zn1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Spikemoss TZF single polypeptide domain, [U-98% 13C; U-98% 15N], 0.6 mM; D2O, [U-99% 2H], 5%; sodium phosphate 20 mM; potassium chloride 100 mM; ZnSO4 25 uM; beta-mercaptoethanol 2 mM; glycerol 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.2; 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 HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HA(CA)NHsample_1isotropicsample_conditions_1
3D HA(CACO)NHsample_1isotropicsample_conditions_1
4D HC(CCO)NHsample_1isotropicsample_conditions_1
4D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2 - collection

NMRPipe - processing

NMRViewJ v8.0 - data analysis

PINE - chemical shift assignment

AutoAssign - chemical shift assignment

TALOS+ - data analysis

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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