BMRB Entry 34600

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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/BMR34600
MolProbity Validation Chart

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Title:
N-terminal C2H2 Zn-finger domain of Clamp
Deposition date:
2021-02-05
Original release date:
2021-12-31
Authors:
Mariasina, S.; Bonchuk, A.; Tikhonova, E.; Efimov, S.; Maksimenko, O.; Georgiev, P.; Polshakov, V.
Citation:

Citation: Tikhonova, E.; Mariasina, S.; Efimov, S.; Polshakov, V.; Maksimenko, O.; Georgiev, P.; Bonchuk, A.. "Structural basis for interaction between CLAMP and MSL2 proteins involved in the specific recruitment of the dosage compensation complex in Drosophila"  Nucleic Acids Res. 50, 6521-6531 (2022).
PubMed: 35648444

Assembly members:

Assembly members:
entity_1, polymer, 70 residues, 7412.407 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SGSNGMPLNQGAALGIATVD AQGRIQIVNQNKPIAANTIS NISFKCDVCSDMFPHLALLN AHKRMHTDGE

Data sets:
Data typeCount
13C chemical shifts244
15N chemical shifts72
1H chemical shifts362

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 70 residues - 7412.407 Da.

1   SERGLYSERASNGLYMETPROLEUASNGLN
2   GLYALAALALEUGLYILEALATHRVALASP
3   ALAGLNGLYARGILEGLNILEVALASNGLN
4   ASNLYSPROILEALAALAASNTHRILESER
5   ASNILESERPHELYSCYSASPVALCYSSER
6   ASPMETPHEPROHISLEUALALEULEUASN
7   ALAHISLYSARGMETHISTHRASPGLYGLU

Entity 2, unit_2 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Clamp[86...153], [U-95% 15N], 0.3 mM; Na2HPO4/HaH2PO4 20 mM; NaCl 50 mM; DTT 1 mM

sample_2: Clamp[86...153], [U-99% 13C; U-99% 15N], 0.3 mM; Na2HPO4/HaH2PO4 20 mM; NaCl 50 mM; DTT 1 mM

sample_3: Clamp[86...153], [U-99% 13C; U-99% 15N], 0.3 mM; Na2HPO4/HaH2PO4 20 mM; NaCl 50 mM; DTT 1 mM

sample_4: Clamp[86...153], [U-95% 15N], 0.3 mM; Na2HPO4/HaH2PO4 20 mM; NaCl 50 mM; DTT 1 mM

sample_conditions_1: ionic strength: 70 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
2D 15N HSQC-NOESYsample_4isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

TopSpin vv3.1, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRFAM-SPARKY, Woonghee Lee - data analysis, peak picking

TALOS+, Yang Shen, Frank Delaglio, Gabriel Cornilescu, and Ad Bax - data analysis

NMR spectrometers:

  • Bruker AVANCE III 700 MHz
  • Bruker AVANCE 600 MHz

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