BMRB Entry 26604

Title:
Protein resonance assignment at MAS frequencies approaching 100 kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods
Deposition date:
2015-07-10
Original release date:
2015-09-30
Authors:
Penzel, Susanne; Smith, Albert; Agarwal, Vipin; Hunkeler, Andreas; Samoson, Ago; Bockmann, Anja; Ernst, Matthias; Meier, Beat
Citation:

Citation: Penzel, Susanne; Smith, Albert; Agarwal, Vipin; Hunkeler, Andreas; Samoson, Ago; Bockmann, Anja; Ernst, Matthias; Meier, Beat. "Protein resonance assignment at MAS frequencies approaching 100 kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods"  J. Biomol. NMR 63, 165-186 (2015).
PubMed: 26267840

Assembly members:

Assembly members:
Ubiquitin_(microcrystalline), 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: PET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ubiquitin_(microcrystalline): MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG

Data sets:
Data typeCount
13C chemical shifts203
15N chemical shifts66
1H chemical shifts66

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ubiquitin (microcrystal)1

Entities:

Entity 1, ubiquitin (microcrystal) 76 residues - Formula weight is not available

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

Samples:

sample_1: Ubiquitin (microcrystalline), 100% HN -[U-2H, U-13C, U-15N], 100%

sample_conditions_1: pH: 4; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
3D (H)CANHsample_1isotropicsample_conditions_1
3D (H)CA(CO)NHsample_1isotropicsample_conditions_1
3D (HCA)CB(CA)NHsample_1isotropicsample_conditions_1
3D (HNCA)CB(CA)NHsample_1isotropicsample_conditions_1
3D (HN)CONHsample_1isotropicsample_conditions_1
3D (H)CO(CA)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CCPN, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 850 MHz

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