BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 28086

Title: Unr CSD789   PubMed: 32697992

Deposition date: 2020-02-18 Original release date: 2020-07-13

Authors: Hollmann, Nele Merret; Hennig, Janosch

Citation: Hollmann, Nele Merret; Jagtap, Kumar Ankush; Masiewicz, Pawel; Guitart, Tanit; Simon, Bernd; Provaznik, Jan; Stein, Frank; Haberkant, Per; Sweetapple, Lara Jayne; Villacorte, Laura; Mooijman, Dylan; Benes, Vladimir; Savitski, Mikhail; Gebauer, Fatima; Hennig, Janosch. "Pseudo-RNA binding domains mediate RNA structure specificity in Upstream of N-Ras"  Cell Rep. 32, 107930-107930 (2020).

Assembly members:
Unr_CSD789, polymer, 235 residues, 26165.47 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   Vector: pETM-11

Entity Sequences (FASTA):
Unr_CSD789: GSDAGQVYRGFIAVMKENFG FIETLSHDEEVFFHFSNYMG NPNWLELGQEVEYTLARNGN TSVSGNCLPAENVRMLPKNS IPQPAVLETTHNGVVARPLR CINPDQQEYAGLIEILDELR TTVISQHEFGITSLVNKRDL LQKGDLVSFRIDESGRAACV NAVRQKKRATVDSIKGQFGF LNFEVEDGKKLFFHMSEVQG NTVALHPGDTVEFSVVTNQR NGKSSACNVLKINDR

Data sets:
Data typeCount
13C chemical shifts408
15N chemical shifts214
1H chemical shifts214

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Unr CSD7891

Entities:

Entity 1, Unr CSD789 235 residues - 26165.47 Da.

CSD789 from Drosophila melanogaster Unr (757-991).

1   GLYSERASPALAGLYGLNVALTYRARGGLY
2   PHEILEALAVALMETLYSGLUASNPHEGLY
3   PHEILEGLUTHRLEUSERHISASPGLUGLU
4   VALPHEPHEHISPHESERASNTYRMETGLY
5   ASNPROASNTRPLEUGLULEUGLYGLNGLU
6   VALGLUTYRTHRLEUALAARGASNGLYASN
7   THRSERVALSERGLYASNCYSLEUPROALA
8   GLUASNVALARGMETLEUPROLYSASNSER
9   ILEPROGLNPROALAVALLEUGLUTHRTHR
10   HISASNGLYVALVALALAARGPROLEUARG
11   CYSILEASNPROASPGLNGLNGLUTYRALA
12   GLYLEUILEGLUILELEUASPGLULEUARG
13   THRTHRVALILESERGLNHISGLUPHEGLY
14   ILETHRSERLEUVALASNLYSARGASPLEU
15   LEUGLNLYSGLYASPLEUVALSERPHEARG
16   ILEASPGLUSERGLYARGALAALACYSVAL
17   ASNALAVALARGGLNLYSLYSARGALATHR
18   VALASPSERILELYSGLYGLNPHEGLYPHE
19   LEUASNPHEGLUVALGLUASPGLYLYSLYS
20   LEUPHEPHEHISMETSERGLUVALGLNGLY
21   ASNTHRVALALALEUHISPROGLYASPTHR
22   VALGLUPHESERVALVALTHRASNGLNARG
23   ASNGLYLYSSERSERALACYSASNVALLEU
24   LYSILEASNASPARG

Samples:

sample_1: Unr CSD789, [U-99% 13C; U-99% 15N], 0.5 mM; sodium chloride 50 mM; sodium phosphate 20 mM; DTT 1 mM

sample_conditions_1: pH: 6.4; 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

Software:

TOPSPIN, Bruker Biospin - collection

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

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

NMR spectrometers:

  • Bruker Avance III 800 MHz

Related Database Links:

UNP Q9VSK3
AlphaFold Q9VSK3

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