BMRB Entry 16627

Title:
Backbone and stereospecific beta-sidechain assignments of 1H, 13C and 15N for Protein G Unfolded in 7.4M Urea, pH 2.0.
Deposition date:
2009-12-04
Original release date:
2010-01-25
Authors:
Vajpai, Navratna; Gentner, Martin; Grzesiek, Stephan
Citation:

Citation: Vajpai, Navratna; Gentner, Martin; Huang, Jie-Rong; Blackledge, Martin; Grzesiek, Stephan. "Side-chain chi(1) conformations in urea-denatured ubiquitin and protein G from (3)J coupling constants and residual dipolar couplings."  J. Am. Chem. Soc. 132, 3196-3203 (2010).
PubMed: 20155903

Assembly members:

Assembly members:
Protein_GB1_(2Q6I), polymer, 56 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Streptococcus sp. (Lancefield Group G)   Taxonomy ID: 1301   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Streptococcus (Lancefield Group G)

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEV2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Protein_GB1_(2Q6I): MQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVD GEWTYDDATKTFTVTE

Data sets:
Data typeCount
13C chemical shifts161
15N chemical shifts55
1H chemical shifts210
coupling constants183

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1monomer1

Entities:

Entity 1, monomer 56 residues - Formula weight is not available

1   METGLNTYRLYSLEUILELEUASNGLYLYS
2   THRLEULYSGLYGLUTHRTHRTHRGLUALA
3   VALASPALAALATHRALAGLULYSVALPHE
4   LYSGLNTYRALAASNASPASNGLYVALASP
5   GLYGLUTRPTHRTYRASPASPALATHRLYS
6   THRPHETHRVALTHRGLU

Samples:

sample_1: Protein GB1 (2Q6I), [U-100% 13C; U-100% 15N], 0.6 mM; urea 7.4 M; H2O 95%; D2O 5%

sample_conditions_1: pH: 2.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRView, Johnson, One Moon Scientific - data analysis

PIPP, Garrett - peak picking

NMR spectrometers:

  • Bruker DRX 800 MHz

Related Database Links:

BMRB 15156 15380 16444 16755 16873 16882 16958 17810 18397 19394 26630
PDB
EMBL CAA37410
GB AAY41168

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