BMRB Entry 52953

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52953
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
N-terminal domain of CG18262 from Drosophila melanogaster
Deposition date:
2025-03-07
Original release date:
2026-01-15
Authors:
Dukhalin, Sergey; Mariasina, Sofia; Balagurov, Konstantin; Bocharov, Eduard; Polshakov, Vladimir
Citation:

Citation: Balagurov, Konstantin; Mariasina, Sofia; Dukhalin, Sergey; Sluchanko, Nikolai; Golovnina, Alexandra; Khrustaleva, Anastasia; Maksimenko, Oksana; Arkova, Olga; Stepanenko, Alexandra; Bocharov, Eduard; Polshakov, Vladimir; Georgiev, Pavel; Bonchuk, Artem. "Beyond DNA binding: single C2H2 zinc fingers with adjacent beta-strands mediate dimerization in Drosophila transcription factors"  Nucleic Acids Res. 54, gkaf1425-gkaf1425 (2026).
PubMed: 41495890

Assembly members:

Assembly members:
entity_1, polymer, 68 residues, 15120 Da.
entity_ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: fruit fly   Taxonomy ID: 7227   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: petv9

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SGSPEFMIKVQPPPDVAGGY HNLRCGEVLFSAPASYEVSC LLCDQRLPLDGYPEHFRLKH FTNSSSSL

Data typeCount
13C chemical shifts268
15N chemical shifts56
1H chemical shifts377

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CG18262, chain 11
2CG18262, chain 21
3zinc ion, 12
4zinc ion, 22

Entities:

Entity 1, CG18262, chain 1 68 residues - 15120 Da.

Residues 1-6 represent a non-native affinity tag.

1   SERGLYSERPROGLUPHEMETILELYSVAL
2   GLNPROPROPROASPVALALAGLYGLYTYR
3   HISASNLEUARGCYSGLYGLUVALLEUPHE
4   SERALAPROALASERTYRGLUVALSERCYS
5   LEULEUCYSASPGLNARGLEUPROLEUASP
6   GLYTYRPROGLUHISPHEARGLEULYSHIS
7   PHETHRASNSERSERSERSERLEU

Entity 2, zinc ion, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: CG18262, [U-98% 15N], 1 mM; NaH2PO4/Na2HPO4 20 mM; NaCl 50 mM; NaN3 0.02%

sample_2: CG18262, [U-98% 15N], 0.73 mM; NaH2PO4/Na2HPO4 20 mM; NaCl 50 mM; NaN3 0.02%

sample_3: CG18262, [U-98% 15N], 0.73 mM; NaH2PO4/Na2HPO4 20 mM; NaCl 50 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 90 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D HNCOCAsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HNHBsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D 13C-separated NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1

Software:

TOPSPIN v2.0, 3.0 - collection

NMRPipe vv11.5 - processing

NMRDraw vv11.5 - processing

POKY vbuild 20240829 - chemical shift assignment, data analysis, peak picking

PINE - chemical shift assignment

ARIA2 vv2.3 - structure solution

CNS vv1.3 - refinement, structure solution

NMRest - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • 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