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 34493

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34493

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Title: solution structure of cold-shock domain 1 and 2 of drosophila Upstream of N-Ras (Unr)   PubMed: 32697992

Deposition date: 2020-02-26 Original release date: 2020-07-14

Authors: Simon, B.; Hollmann, N.; 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, 165 residues, 18494.502 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: GADDEERETGIIEKLLHSYG FIQCCERQARLFFHFSQFSG NIDHLKIGDPVEFEMTYDRR TGKPIASQVSKIAPEVVLSE ERVTGTVTTELRTDSANNVL NSSETTGRISYENRGECFFL PYTKDDVEGNVNLRAGDKVS FQIATNQRGNLGACHIRLEN PAQPV

Data sets:
Data typeCount
13C chemical shifts518
15N chemical shifts168
1H chemical shifts1016

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 165 residues - 18494.502 Da.

1   GLYALAASPASPGLUGLUARGGLUTHRGLY
2   ILEILEGLULYSLEULEUHISSERTYRGLY
3   PHEILEGLNCYSCYSGLUARGGLNALAARG
4   LEUPHEPHEHISPHESERGLNPHESERGLY
5   ASNILEASPHISLEULYSILEGLYASPPRO
6   VALGLUPHEGLUMETTHRTYRASPARGARG
7   THRGLYLYSPROILEALASERGLNVALSER
8   LYSILEALAPROGLUVALVALLEUSERGLU
9   GLUARGVALTHRGLYTHRVALTHRTHRGLU
10   LEUARGTHRASPSERALAASNASNVALLEU
11   ASNSERSERGLUTHRTHRGLYARGILESER
12   TYRGLUASNARGGLYGLUCYSPHEPHELEU
13   PROTYRTHRLYSASPASPVALGLUGLYASN
14   VALASNLEUARGALAGLYASPLYSVALSER
15   PHEGLNILEALATHRASNGLNARGGLYASN
16   LEUGLYALACYSHISILEARGLEUGLUASN
17   PROALAGLNPROVAL

Samples:

sample_1: sodium chloride 50 mM; sodium phosphate 20 mM; DTT 10 mM; protein, [U-99% 13C; U-99% 15N], 0.3 mM; RNA 0.36 mM

sample_2: sodium chloride 50 mM; sodium phosphate 20 mM; DTT 10 mM; protein, [U-99% 13C; U-99% 15N], 0.3 mM; RNA 0.36 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment

CARA, Keller and Wuthrich - peak picking

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

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