BMRB Entry 27659

Title:
Backbone assignment of human ribonuclease 6
Deposition date:
2018-10-22
Original release date:
2018-11-28
Authors:
Bernard, David; Gagne, Donald; Letourneau, Myriam; Doucet, Nicolas
Citation:

Citation: Narayanan, Chitra; Bernard, David; Letourneau, Myriam; Gagnon, Jacinthe; Gagne, Donald; Bafna, Khushboo; Calmettes, Charles; Couture, Jean-Francois; Agarwal, Pratul; Doucet, Nicolas. "Insights into Structural and Dynamical Changes Experienced by Human RNase 6 upon Ligand Binding"  Biochemistry 59, 755-765 (2020).
PubMed: 31909602

Assembly members:

Assembly members:
RNase6, polymer, 127 residues, 14653 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pJ414

Data typeCount
13C chemical shifts257
15N chemical shifts137
1H chemical shifts146

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RNase 6, Major_conformer1
2RNase 6, Minor_conformer1

Entities:

Entity 1, RNase 6, Major_conformer 127 residues - 14653 Da.

1   TRPPROLYSARGLEUTHRLYSALAHISTRP
2   PHEGLUILEGLNHISILEGLNPROSERPRO
3   LEUGLNCYSASNARGALAMETSERGLYILE
4   ASNASNTYRTHRGLNHISCYSLYSHISGLN
5   ASNTHRPHELEUHISASPSERPHEGLNASN
6   VALALAALAVALCYSASPLEULEUSERILE
7   VALCYSLYSASNARGARGHISASNCYSHIS
8   GLNSERSERLYSPROVALASNMETTHRASP
9   CYSARGLEUTHRSERGLYLYSTYRPROGLN
10   CYSARGTYRSERALAALAALAGLNTYRLYS
11   PHEPHEILEVALALACYSASPPROPROGLN
12   LYSSERASPPROPROTYRLYSLEUVALPRO
13   VALHISLEUASPSERILELEU

Samples:

sample_1: RNase6, [U-99% 13C; U-99% 15N], 680 uM; D2O, [U-99% 2H], 10%; sodium acetate 15 mM

sample_conditions_1: ionic strength: 0.015 M; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CcpNMR v2.4, CCPN - chemical shift assignment, peak picking

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

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

UNP Q93091
PDB
AlphaFold Q93091

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