BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25924

Title: Drosha Quad   PubMed: 28792523

Deposition date: 2015-12-17 Original release date: 2016-12-15

Authors: Showalter, Scott; Sahu, Debashish; Kranick, Joshua

Citation: Kranick, Joshua; Chadalavada, Durga; Sahu, Debashish; Showalter, Scott. "Engineering double-stranded RNA binding activity into the Drosha double-stranded RNA binding domain results in a loss of microRNA processing function"  PLoS ONE 12, e0182445-e0182445 (2017).

Assembly members:
entity, polymer, 82 residues, 8973.405 Da.

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET49b

Entity Sequences (FASTA):
entity: GPGNDPISQLQQCCLTLRTE GKEPDIPLYKTLQTVGPSHA RTYTVAVYFKGERIGCGKGP SKKQAKMGAAMDALEKYNFP QM

Data sets:
Data typeCount
13C chemical shifts298
15N chemical shifts67
1H chemical shifts356

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 82 residues - 8973.405 Da.

1   GLYPROGLYASNASPPROILESERGLNLEU
2   GLNGLNCYSCYSLEUTHRLEUARGTHRGLU
3   GLYLYSGLUPROASPILEPROLEUTYRLYS
4   THRLEUGLNTHRVALGLYPROSERHISALA
5   ARGTHRTYRTHRVALALAVALTYRPHELYS
6   GLYGLUARGILEGLYCYSGLYLYSGLYPRO
7   SERLYSLYSGLNALALYSMETGLYALAALA
8   METASPALALEUGLULYSTYRASNPHEPRO
9   GLNMET

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 850 mM; cacodylate pH 7.29 100 mM; potassium chloride 100 mM; beta-mercaptoethanol 5 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.29; 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D (H)CCO)NHsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

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