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 34498

Title: solution structure of cold-shock domain 9 of drosophila Upstream of N-Ras (Unr)   PubMed: 32697992

Deposition date: 2020-03-06 Original release date: 2020-07-14

Authors: Sweetapple, L.; Hollmann, N.; Simon, B.; Hennig, J.

Citation: Hollmann, N.; Jagtap, P.; Masiewicz, P.; Guitart, T.; Simon, B.; Provaznik, J.; Stein, F.; Haberkant, P.; Sweetapple, L.; Villacorte, L.; Mooijman, D.; Benes, V.; Savitski, M.; Gebauer, F.; Hennig, J.. "Pseudo-RNA binding domains mediate RNA structure specificity in Upstream of N-Ras"  Cell Rep. 32, 107930-107930 (2020).

Assembly members:
entity_1, polymer, 94 residues, 10246.532 Da.

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

Entity Sequences (FASTA):
entity_1: GAKGDLVSFRIDESGRAACV NAVRQKKRATVDSIKGQFGF LNFEVEDGKKLFFHMSEVQG NTVALHPGDTVEFSVVTNQR NGKSSACNVLKIND

Data sets:
Data typeCount
13C chemical shifts360
15N chemical shifts91
1H chemical shifts562

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 94 residues - 10246.532 Da.

1   GLYALALYSGLYASPLEUVALSERPHEARG
2   ILEASPGLUSERGLYARGALAALACYSVAL
3   ASNALAVALARGGLNLYSLYSARGALATHR
4   VALASPSERILELYSGLYGLNPHEGLYPHE
5   LEUASNPHEGLUVALGLUASPGLYLYSLYS
6   LEUPHEPHEHISMETSERGLUVALGLNGLY
7   ASNTHRVALALALEUHISPROGLYASPTHR
8   VALGLUPHESERVALVALTHRASNGLNARG
9   ASNGLYLYSSERSERALACYSASNVALLEU
10   LYSILEASNASP

Samples:

sample_1: protein, [U-99% 13C; U-99% 15N], 0.24 mM; sodium phosphate 50 mM; sodium chloride 50 mM; DTT 1 mM

sample_2: protein, [U-99% 13C; U-99% 15N], 0.24 mM; sodium phosphate 50 mM; sodium chloride 50 mM; DTT 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

TopSpin, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 800 MHz

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