BMRB Entry 27804

Title:
Backbone 1H and 15N Chemical Shift Assignments for K11-linked ubiquitin dimer artificially conjugated via propargyl acrylate
Deposition date:
2019-02-27
Original release date:
2020-01-07
Authors:
Kovermann, Michael; Schneider, Tobias
Citation:

Citation: Schneider, Tobias; Berg, Andrej; Ulusoy, Zeynel; Gamerdinger, Martin; Peter, Christine; Kovermann, Michael. "Conformational and functional characterization of artificially conjugated non-canonical ubiquitin dimers"  Sci. Rep. 9, 19991-19991 (2019).
PubMed: 31882959

Assembly members:

Assembly members:
K11-linked_ubiquitin_dimer, polymer, 76 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET3a/pGEX2TK

Entity Sequences (FASTA):

Entity Sequences (FASTA):
K11-linked_ubiquitin_dimer: MQIFVKTLTGCTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG

Data sets:
Data typeCount
15N chemical shifts70
1H chemical shifts70

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1K11-linked ubiquitin dimer A1
2K11-linked ubiquitin dimer B1

Entities:

Entity 1, K11-linked ubiquitin dimer A 76 residues - Formula weight is not available

1   METGLNILEPHEVALLYSTHRLEUTHRGLY
2   CYSTHRILETHRLEUGLUVALGLUPROSER
3   ASPTHRILEGLUASNVALLYSALALYSILE
4   GLNASPLYSGLUGLYILEPROPROASPGLN
5   GLNARGLEUILEPHEALAGLYLYSGLNLEU
6   GLUASPGLYARGTHRLEUSERASPTYRASN
7   ILEGLNLYSGLUSERTHRLEUHISLEUVAL
8   LEUARGLEUARGGLYGLY

Samples:

sample_1: K11C-linked ubiquitin dimer, [U-99% 13C; U-99% 15N], 0.4 mM; sodium phosphate 20 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific - chemical shift assignment, collection, data analysis, processing

NMR spectrometers:

  • Bruker Avance 600 MHz

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