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 34492

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34492

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Title: drosophila Unr CSD78   PubMed: 32697992

Deposition date: 2020-02-21 Original release date: 2020-07-13

Authors: 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, 168 residues, 18672.947 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 BL21(DE3)

Entity Sequences (FASTA):
entity_1: GAGSDAGQVYRGFIAVMKEN FGFIETLSHDEEVFFHFSNY MGNPNWLELGQEVEYTLARN GNTSVSGNCLPAENVRMLPK NSIPQPAVLETTHNGVVARP LRCINPDQQEYAGLIEILDE LRTTVISQHEFGITSLVNKR DLLQKGDLVSFRIDESGRAA CVNAVRQK

Data sets:
Data typeCount
13C chemical shifts666
15N chemical shifts172
1H chemical shifts1152

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 168 residues - 18672.947 Da.

1   GLYALAGLYSERASPALAGLYGLNVALTYR
2   ARGGLYPHEILEALAVALMETLYSGLUASN
3   PHEGLYPHEILEGLUTHRLEUSERHISASP
4   GLUGLUVALPHEPHEHISPHESERASNTYR
5   METGLYASNPROASNTRPLEUGLULEUGLY
6   GLNGLUVALGLUTYRTHRLEUALAARGASN
7   GLYASNTHRSERVALSERGLYASNCYSLEU
8   PROALAGLUASNVALARGMETLEUPROLYS
9   ASNSERILEPROGLNPROALAVALLEUGLU
10   THRTHRHISASNGLYVALVALALAARGPRO
11   LEUARGCYSILEASNPROASPGLNGLNGLU
12   TYRALAGLYLEUILEGLUILELEUASPGLU
13   LEUARGTHRTHRVALILESERGLNHISGLU
14   PHEGLYILETHRSERLEUVALASNLYSARG
15   ASPLEULEUGLNLYSGLYASPLEUVALSER
16   PHEARGILEASPGLUSERGLYARGALAALA
17   CYSVALASNALAVALARGGLNLYS

Samples:

sample_1: dCSD78, [U-99% 13C; U-99% 15N], 0.5 mM; sodium chloride 150 mM; sodium phosphate 20 mM; DTT 1 mM

sample_2: dCSD78, [U-99% 13C; U-99% 15N], 0.5 mM; sodium chloride 150 mM; sodium phosphate 20 mM; DTT 1 mM

sample_conditions_1: ionic strength: 150 mM; 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
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ARIA, Linge, O'Donoghue and Nilges - refinement

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