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 27798

Title: 1H, 13C and 15N backbone chemical shift assignments of a mutated variant of UBE2S   PubMed: 31230944

Deposition date: 2019-02-22 Original release date: 2019-06-27

Authors: Schweimer, Kristian; Liess, Anna; Lorenz, Sonja

Citation: Liess, Anna; Kucerova, Alena; Schweimer, Kristian; Yu, Lu; Roumeliotis, Theodoros; Diebold, Mathias; Dybkov, Olexandr; Sotriffer, Christoph; Urlaub, Henning; Choudhary, Jyoti; Mansfeld, Jorg; Lorenz, Sonja. "Autoinhibition Mechanism of the Ubiquitin-Conjugating Enzyme UBE2S by Autoubiquitination"  Structure 27, 1195-1210 (2019).

Assembly members:
UBE2S, polymer, 156 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
UBE2S: MNSNVENLPPHIIRLVYKEV TTLTADPPDGIKVFPNEEDL TDLQVTIEGPEGTPYAGGLF RMKLLLGKDFPASPPKGYFL TKIFHPNVGANGEISVNVLC RDWTAELGIRHVLLTIKMLL IHPNPESALNEEAGRLLLEN YEEYAARARLLTEIHG

Data sets:
Data typeCount
13C chemical shifts423
15N chemical shifts137
1H chemical shifts137

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBE2S UBC1

Entities:

Entity 1, UBE2S UBC 156 residues - Formula weight is not available

1   METASNSERASNVALGLUASNLEUPROPRO
2   HISILEILEARGLEUVALTYRLYSGLUVAL
3   THRTHRLEUTHRALAASPPROPROASPGLY
4   ILELYSVALPHEPROASNGLUGLUASPLEU
5   THRASPLEUGLNVALTHRILEGLUGLYPRO
6   GLUGLYTHRPROTYRALAGLYGLYLEUPHE
7   ARGMETLYSLEULEULEUGLYLYSASPPHE
8   PROALASERPROPROLYSGLYTYRPHELEU
9   THRLYSILEPHEHISPROASNVALGLYALA
10   ASNGLYGLUILESERVALASNVALLEUCYS
11   ARGASPTRPTHRALAGLULEUGLYILEARG
12   HISVALLEULEUTHRILELYSMETLEULEU
13   ILEHISPROASNPROGLUSERALALEUASN
14   GLUGLUALAGLYARGLEULEULEUGLUASN
15   TYRGLUGLUTYRALAALAARGALAARGLEU
16   LEUTHRGLUILEHISGLY

Samples:

sample_1: UBE2S, [U-100% 13C; U-100% 15N], 0.6 mM; D2O 5%; sodium phosphate 75 mM; DTT 5 mM; EDTA 1 mM; TCEP 2 mM

sample_conditions_1: pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB

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