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 51286

Title: CLAMP-interacting disordered region of male-specific lethal protein 2 (Msl2)   PubMed: 35648444

Deposition date: 2022-01-21 Original release date: 2022-02-02

Authors: Mariasina, Sofia; Bonchuk, Artem; Polshakov, Vladimir

Citation: Tihonova, Evgeniya; Mariasina, Sofia; Efimov, Sergey; Polshakov, Vladimir; Maksimenko, Oksana; Georgiev, Pavel; Bonchuk, Artem. "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).

Assembly members:
entity_1, polymer, 42 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a(+)

Entity Sequences (FASTA):
entity_1: SGSISLVPLNNLQQSQHPLV LVQNEKGEYQGFNIFQGSKP LD

Data sets:
Data typeCount
13C chemical shifts111
15N chemical shifts38
1H chemical shifts139

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Msl21

Entities:

Entity 1, Msl2 42 residues - Formula weight is not available

First three residues (S-615, G-616, and S-617) are parts of the affinity tag. The numbering used in the project corresponds to the whole protein (since I618).

1   SERGLYSERILESERLEUVALPROLEUASN
2   ASNLEUGLNGLNSERGLNHISPROLEUVAL
3   LEUVALGLNASNGLULYSGLYGLUTYRGLN
4   GLYPHEASNILEPHEGLNGLYSERLYSPRO
5   LEUASP

Samples:

sample_1: Msl2, [U-98% 13C; U-98% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 50 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRFAM-SPARKY - data analysis

TOPSPIN - collection

PINE - chemical shift assignment

NMRPipe - processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker AVANCE III 700 MHz

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