BMRB Entry 17439

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17439

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Title:
1H, 13C and 15N backbone chemical shift assignments of ubiquitin at pH 7.2
Deposition date:
2011-02-01
Original release date:
2011-03-09
Authors:
Lorenz, Sonja; Wemmer, David; Kuriyan, John; Pelton, Jeffrey
Citation:

Citation: Wickliffe, Katherine; Lorenz, Sonja; Wemmer, David; Kuriyan, John; Rape, Michael. "The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit e2"  Cell 144, 769-781 (2011).
PubMed: 21376237

Assembly members:

Assembly members:
ubiquitin, polymer, 76 residues, 8564.8 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: pET30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ubiquitin: MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG

Data sets:
Data typeCount
13C chemical shifts135
15N chemical shifts70
1H chemical shifts70

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ubiquitin1

Entities:

Entity 1, ubiquitin 76 residues - 8564.8 Da.

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

Samples:

sample_1: ubiquitin, [U-99% 13C; U-99% 15N], 1640 uM; sodium phosphate 75mM mM; D2O 7.5%; DSS 30 uM; H2O 92.5%

sample_conditions_1: ionic strength: 185 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1

Software:

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

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

BMRB 11505 11547 15047 15410 15689 15907 16228 16582 16626 16895 17181 17769 17919 18582 18583 18584 18610 18611 18737 19406 19412 25070 25123 25601 26604 4245 4375
PDB
DBJ BAA03983 BAA09860 BAA11842 BAA11843 BAA23486
EMBL CAA25706 CAA26488 CAA28495 CAA30183 CAA30815
GB AAA02769 AAA28154 AAA28997 AAA28998 AAA28999
PIR I50437 I51568 I65237 JN0790 S13928
PRF 0412265A 1101405A 1212243A 1212243B 1212243C
REF NP_001005123 NP_001006688 NP_001009117 NP_001009202 NP_001009286
SP P0C273 P0C275 P0C276 P0CG47 P0CG48
TPD FAA00319
TPE CEL68433 CEL70397 CEL75964 CEL78064
TPG DAA18802 DAA20663 DAA20672 DAA24675 DAA28295
AlphaFold P0C273 P0C275 P0C276 P0CG47 P0CG48

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