BMRB Entry 34326

Title:
Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1/2 of Drosophila helicase MLE
Deposition date:
2018-11-07
Original release date:
2019-03-14
Authors:
Jagtap, P.; Buelow, S.; Masiewicz, P.; Simon, B.; Hennig, J.
Citation:

Citation: Ankush Jagtap, P.; Muller, M.; Masiewicz, P.; von Bulow, S.; Hollmann, N.; Chen, P.; Simon, B.; Thomae, A.; Becker, P.; Hennig, J.. "Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless."  Nucleic Acids Res. 47, 4319-4333 (2019).
PubMed: 30805612

Assembly members:

Assembly members:
entity_1, polymer, 259 residues, 28589.938 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

Data typeCount
13C chemical shifts1015
15N chemical shifts280
1H chemical shifts1573

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 259 residues - 28589.938 Da.

1   GLYALAMETASPILELYSSERPHELEUTYR
2   GLNPHECYSALALYSSERGLNILEGLUPRO
3   LYSPHEASPILEARGGLNTHRGLYPROLYS
4   ASNARGGLNARGPHELEUCYSGLUVALARG
5   VALGLUPROASNTHRTYRILEGLYVALGLY
6   ASNSERTHRASNLYSLYSASPALAGLULYS
7   ASNALACYSARGASPPHEVALASNTYRLEU
8   VALARGVALGLYLYSLEUASNTHRASNASP
9   VALPROALAASPALAGLYALASERGLYGLY
10   GLYPROARGTHRGLYLEUGLUGLYALAGLY
11   METALAGLYGLYSERGLYGLNGLNLYSARG
12   VALPHEASPGLYGLNSERGLYPROGLNASP
13   LEUGLYGLUALATYRARGPROLEUASNHIS
14   ASPGLYGLYASPGLYGLYASNARGTYRSER
15   VALILEASPARGILEGLNGLUGLNARGASP
16   METASNGLUALAGLUALAPHEASPVALASN
17   ALAALAILEHISGLYASNTRPTHRILEGLU
18   ASNALALYSGLUARGLEUASNILETYRLYS
19   GLNTHRASNASNILEARGASPASPTYRLYS
20   TYRTHRPROVALGLYPROGLUHISALAARG
21   SERPHELEUALAGLULEUSERILETYRVAL
22   PROALALEUASNARGTHRVALTHRALAARG
23   GLUSERGLYSERASNLYSLYSSERALASER
24   LYSSERCYSALALEUSERLEUVALARGGLN
25   LEUPHEHISLEUASNVALILEGLUPROPHE
26   SERGLYTHRLEULYSLYSLYSLYSASP

Samples:

sample_1: MLE dsRBD1,2, [U-13C; U-15N], 0.5 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6; pressure: 1 bar; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

Analysis, CCPN - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ARIA, Linge, O'Donoghue and Nilges - refinement

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 800 MHz

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