BMRB Entry 27702

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Myc bHLH-LZ domain in presence of 2.4 M GdmCl
Deposition date:
2018-11-24
Original release date:
2019-08-15
Authors:
Panova, Stanislava; Cliff, Matthew; Macek, Pavel; Blackledge, Martin; Jensen, Malene; Nissink, J. Willem; Embrey, Kevin; Davies, Rick; Waltho, Jonathan
Citation:

Citation: Panova, Stanislava; Cliff, Matthew; Macek, Pavel; Blackledge, Martin; Jensen, Malene; Nissink, J. Willem; Embrey, Kevin; Davies, Rick; Waltho, Jonathan. "Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration"  Structure 27, 1537-1546 (2019).
PubMed: 31402220

Assembly members:

Assembly members:
bHLHZip_domain_of_Myc, polymer, 87 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: pET

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts168
15N chemical shifts84
1H chemical shifts84

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1bHLHZip domain of Myc1

Entities:

Entity 1, bHLHZip domain of Myc 87 residues - Formula weight is not available

1   GLYSERASNVALLYSARGARGTHRHISASN
2   VALLEUGLUARGGLNARGARGASNGLULEU
3   LYSARGSERPHEPHEALALEUARGASPGLN
4   ILEPROGLULEUGLUASNASNGLULYSALA
5   PROLYSVALVALILELEULYSLYSALATHR
6   ALATYRILELEUSERVALGLNALAGLUGLU
7   GLNLYSLEUILESERGLUGLUASPLEULEU
8   ARGLYSARGARGGLUGLNLEULYSHISLYS
9   LEUGLUGLNLEUARGASNSER

Samples:

sample_1: bHLHZip domain of Myc, [U-13C; U-15N], 1 ± 0.1 mM; sodium phosphate 20 ± 2 mM; TSP 1 ± 0.1 mM; GdmCl 2.4 ± 0.1 M

sample_conditions_1: ionic strength: 2.4 M; pH: 6.5; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
(H)N(CA)NNHsample_1isotropicsample_conditions_1

Software:

CCPNMR v2.4.2, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

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