BMRB Entry 27984

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for Cezanne UBA domain (residues 2-55)
Deposition date:
2019-07-23
Original release date:
2020-01-15
Authors:
Rogov, Vladimir; Huber, Jessica; Doetsch, Volker; Mader, Julia; Bremm, Anja
Citation:

Citation: Mader, Julia; Huber, Jessica; Bonn, Florian; Doetsch, Volker; Rogov, Vladimir; Bremm, Anja. "Oxygen-dependent asparagine hydroxylation of the ubiquitin-associated (UBA) domain in Cezanne regulates ubiquitin binding"  J. Biol. Chem. 295, 2160-2174 (2020).
PubMed: 31937588

Assembly members:

Assembly members:
Cezanne_UBA_domain, polymer, 55 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: pOPINK

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Cezanne_UBA_domain: MTLDMDAVLSDFVRSTGAEP GLARDLLEGKNWDVNAALSD FEQLRQVHAGNLPPS

Data sets:
Data typeCount
13C chemical shifts102
15N chemical shifts52
1H chemical shifts52

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Cezanne UBA domain1

Entities:

Entity 1, Cezanne UBA domain 55 residues - Formula weight is not available

1   METTHRLEUASPMETASPALAVALLEUSER
2   ASPPHEVALARGSERTHRGLYALAGLUPRO
3   GLYLEUALAARGASPLEULEUGLUGLYLYS
4   ASNTRPASPVALASNALAALALEUSERASP
5   PHEGLUGLNLEUARGGLNVALHISALAGLY
6   ASNLEUPROPROSER

Samples:

sample_1: Cezanne UBA domain, [U-98% 13C; U-98% 15N], 0.8 mM; HEPES 25 mM; sodium chloride 50 mM; D2O 5%; DSS 1 mM; protease inhibitors cocktail 5 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin, Goddard - chemical shift assignment, collection, data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • 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