BMRB Entry 53717

Title:
Backbone chemical shift assignments for human ribonuclease 7
Deposition date:
2026-04-11
Original release date:
2026-09-02
Authors:
Tran, Thi Thanh Quynh; Larda, Sacha; Doucet, Nicolas
Citation:

Citation: Tran, Thi Thanh Quynh; Larda, Sacha; Nieves, Cecilia; Veyrier, Frederic; Calmettes, Charles; Doucet, Nicolas. "Engineering human RNase 7 with an eosinophil RNase segment reveals determinants of cytotoxic and antimicrobial activity "  J. Biol. Chem. 302, 113189-113189 (2026).
PubMed: 42203172

Assembly members:

Assembly members:
entity_1, polymer, 128 residues, 14633.02 Da.
entity_ZN, non-polymer, 65.409 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: pJExpress414

Data sets:
Data typeCount
13C chemical shifts233
15N chemical shifts111
1H chemical shifts111

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RNase 7 monomer1
2zinc ion, 12
3zinc ion, 22
4zinc ion, 32
5zinc ion, 42

Entities:

Entity 1, RNase 7 monomer 128 residues - 14633.02 Da.

1   LYSPROLYSGLYMETTHRSERSERGLNTRP
2   PHELYSILEGLNHISMETGLNPROSERPRO
3   GLNALACYSASNSERALAMETLYSASNILE
4   ASNLYSHISTHRLYSARGCYSLYSASPLEU
5   ASNTHRPHELEUHISGLUPROPHESERSER
6   VALALAALATHRCYSGLNTHRPROLYSILE
7   ALACYSLYSASNGLYASPLYSASNCYSHIS
8   GLNSERHISGLYALAVALSERLEUTHRMET
9   CYSLYSLEUTHRSERGLYLYSHISPROASN
10   CYSARGTYRLYSGLULYSARGGLNASNLYS
11   SERTYRVALVALALACYSLYSPROPROGLN
12   LYSLYSASPSERGLNGLNPHEHISLEUVAL
13   PROVALHISLEUASPARGVALLEU

Entity 2, zinc ion, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Human ribonuclease 7, [U-99% 13C; U-99% 15N], 269 uM; 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:

NMRbox - chemical shift assignment, peak picking, processing

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

Related Database Links:

PDB
NCBI 84659

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