BMRB Entry 52067

Title:
Chemical shift assignments for N-Myc 64-137
Deposition date:
2023-08-02
Original release date:
2024-10-08
Authors:
Rejnowicz, Ewa; Batchelor, Matthew; Leen, Eoin; Bayliss, Richard
Citation:

Citation: Rejnowicz, Ewa; Batchelor, Matthew; Leen, Eoin; Ahangar, Mohd Syed; Burgess, Selena; Richards, Mark; Kalverda, Arnout; Bayliss, Richard. "Exploring the dynamics and interactions of the N-myc transactivation domain through solution NMR"  Biochem. J. ., .-. (2024).
PubMed: 39370942

Assembly members:

Assembly members:
entity_1, polymer, 78 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: pETM6T1

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts218
15N chemical shifts71
1H chemical shifts71

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-Myc 64-1371

Entities:

Entity 1, N-Myc 64-137 78 residues - Formula weight is not available

Residue 5 in the sequence relates to Ser64 in N-Myc

1   GLYALAMETGLYSERARGGLYPHEALAGLU
2   HISSERSERGLUPROPROSERTRPVALTHR
3   GLUMETLEULEUGLUASNGLULEUTRPGLY
4   SERPROALAGLUGLUASPALAPHEGLYLEU
5   GLYGLYLEUGLYGLYLEUTHRPROASNPRO
6   VALILELEUGLNASPCYSMETTRPSERGLY
7   PHESERALAARGGLULYSLEUGLUARGALA
8   VALSERGLULYSLEUGLNHISGLY

Samples:

sample_1: N-Myc 64-137, [U-99% 13C; U-99% 15N], 200 uM; TRIS 25 mM; sodium chloride 137 mM; potassium chloride 2.7 mM; D2O 5%; TCEP 2 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.9; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

CcpNMR vAnalysis v 2.5 - chemical shift assignment, data analysis

NMR spectrometers:

  • Oxford/Bruker AVANCE III 750 MHz

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