BMRB Entry 19670

Title:
Solution structure of lysine-free (K0) ubiquitin
Deposition date:
2013-12-09
Original release date:
2014-03-31
Authors:
Huang, Tao; Li, Jess; Byrd, Andrew
Citation:

Citation: Huang, Tao; Li, Jess; Byrd, R. Andrew. "Solution structure of lysine-free (K0) ubiquitin."  Protein Sci. 23, 662-667 (2014).
PubMed: 24591328

Assembly members:

Assembly members:
entity, polymer, 76 residues, 8773.008 Da.

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: pET

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts219
15N chemical shifts70
1H chemical shifts258

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1lysine-free (K0) ubiquitin1

Entities:

Entity 1, lysine-free (K0) ubiquitin 76 residues - 8773.008 Da.

1   METGLNILEPHEVALARGTHRLEUTHRGLY
2   ARGTHRILETHRLEUGLUVALGLUPROSER
3   ASPTHRILEGLUASNVALARGALAARGILE
4   GLNASPARGGLUGLYILEPROPROASPGLN
5   GLNARGLEUILEPHEALAGLYARGGLNLEU
6   GLUASPGLYARGTHRLEUSERASPTYRASN
7   ILEGLNARGGLUSERTHRLEUHISLEUVAL
8   LEUARGLEUARGGLYGLY

Samples:

sample_1: K-free ubiquitin, [U-13C; U-15N], 0.5 mM; TRIS 50 mM; D2O, [U-100% 2H], 5%; H2O 95%

sample_conditions_1: ionic strength: 0.01 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

CS-Rosetta, Shen, Vernon, Baker and Bax - structure solution

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

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB

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