BMRB Entry 28088

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28088

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Title:
dUnr CSD456
Deposition date:
2020-02-18
Original release date:
2020-07-13
Authors:
Hollmann, Nele Merret; Hennig, Janosch
Citation:

Citation: Hollmann, Nele Merret; Jagtap, Pravin Kumar Ankush; Masiewicz, Pawel; Guitart, Tanit; Simon, Bernd; Provaznik, Jan; Stein, Frank; Haberkant, Per; Sweetapple, Lara Jayne; Villacorte, Laura; Mooijman, Dylan; Benes, Valdimir; 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).
PubMed: 32697992

Assembly members:

Assembly members:
dUnr_CSD456, polymer, 256 residues, 29461.36 Da.

Natural source:

Natural source:   Common Name: fruit fly   Taxonomy ID: 7227   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM-11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
dUnr_CSD456: EDVDSTVYKGQVLKSLDRNN PVRQNNDPLPGRIRYRALDY SEVEVPFGDKDQKGDFTLRH GDWVQFLLATDRRDQLQRAT SIALLDETFKVSGEKREQGT IASLKEGFGFLRCVERQARL FFHFTEVLDTSREIDINDEV EFTVIQEPGLAYNNSRLQAI RIKHLPPNSVQFETLVASNI EGCVTREAPKSPIKSQDRVE GGVITYEHADVKKTIMYFLK DCEKPPRIGERVRFDIYMVK RNKECIAVNVQQVSLH

Data sets:
Data typeCount
13C chemical shifts334
15N chemical shifts181
1H chemical shifts180

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1dUnr CSD4561

Entities:

Entity 1, dUnr CSD456 256 residues - 29461.36 Da.

1   GLUASPVALASPSERTHRVALTYRLYSGLY
2   GLNVALLEULYSSERLEUASPARGASNASN
3   PROVALARGGLNASNASNASPPROLEUPRO
4   GLYARGILEARGTYRARGALALEUASPTYR
5   SERGLUVALGLUVALPROPHEGLYASPLYS
6   ASPGLNLYSGLYASPPHETHRLEUARGHIS
7   GLYASPTRPVALGLNPHELEULEUALATHR
8   ASPARGARGASPGLNLEUGLNARGALATHR
9   SERILEALALEULEUASPGLUTHRPHELYS
10   VALSERGLYGLULYSARGGLUGLNGLYTHR
11   ILEALASERLEULYSGLUGLYPHEGLYPHE
12   LEUARGCYSVALGLUARGGLNALAARGLEU
13   PHEPHEHISPHETHRGLUVALLEUASPTHR
14   SERARGGLUILEASPILEASNASPGLUVAL
15   GLUPHETHRVALILEGLNGLUPROGLYLEU
16   ALATYRASNASNSERARGLEUGLNALAILE
17   ARGILELYSHISLEUPROPROASNSERVAL
18   GLNPHEGLUTHRLEUVALALASERASNILE
19   GLUGLYCYSVALTHRARGGLUALAPROLYS
20   SERPROILELYSSERGLNASPARGVALGLU
21   GLYGLYVALILETHRTYRGLUHISALAASP
22   VALLYSLYSTHRILEMETTYRPHELEULYS
23   ASPCYSGLULYSPROPROARGILEGLYGLU
24   ARGVALARGPHEASPILETYRMETVALLYS
25   ARGASNLYSGLUCYSILEALAVALASNVAL
26   GLNGLNVALSERLEUHIS

Samples:

sample_1: dUnr CSD456, [U-99% 13C; U-99% 15N], 0.3 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
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_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 peaks
SPARKY: Backbone or all simulated peaks