BMRB Entry 51463

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51463

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Title:
Backbone 1H, 13C and 15N chemical shift assignments of ubiquitin C-terminally functionalized with an azide group (UbG75Aha)
Deposition date:
2022-05-21
Original release date:
2023-07-27
Authors:
Schneider, Tobias; Sawade, Kevin; Berner, Frederic; Peter, Christine; Kovermann, Michael
Citation:

Citation: Schneider, Tobias; Sawade, Kevin; Berner, Frederic; Peter, Christine; Kovermann, Michael. "Specifying conformational heterogeneity of multi-domain proteins at atomic resolution"  Structure 31, 1259-1274 (2023).
PubMed: 37557171

Assembly members:

Assembly members:
entity_1, polymer, 80 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: pGEX2TK UbG75M

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: RASVGSQIFVKTLTGKTITL EVEPSDTIENVKAKIQDKEG IPPDQQRLIFAGKQLEDGRT LSDYNIQKESTLHLVLRLRX

Data sets:
Data typeCount
13C chemical shifts78
15N chemical shifts74
1H chemical shifts74

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UbG75Aha1

Entities:

Entity 1, UbG75Aha 80 residues - Formula weight is not available

residues 1-5 result from an N-terminal thrombin cleavage site

1   ARGALASERVALGLYSERGLNILEPHEVAL
2   LYSTHRLEUTHRGLYLYSTHRILETHRLEU
3   GLUVALGLUPROSERASPTHRILEGLUASN
4   VALLYSALALYSILEGLNASPLYSGLUGLY
5   ILEPROPROASPGLNGLNARGLEUILEPHE
6   ALAGLYLYSGLNLEUGLUASPGLYARGTHR
7   LEUSERASPTYRASNILEGLNLYSGLUSER
8   THRLEUHISLEUVALLEUARGLEUARGX

Samples:

sample_1: UbG75Aha, [U-13C; U-15N], 280 uM; sodium phosphate 20 mM

sample_conditions_1: pH: 6.8; temperature: 298 K

Experiments:

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

Software:

TOPSPIN - collection

NMRPipe - processing

NMRView - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

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