BMRB Entry 52066

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52066

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Title:
Chemical shift assignments for N-Myc 1-137
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, 140 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):

Entity Sequences (FASTA):
entity_1: GAMMPSCSTSTMPGMICKNP DLEFDSLQPCFYPDEDDFYF GGPDSTPPGEDIWKKFELLP TPPLSPSRGFAEHSSEPPSW VTEMLLENELWGSPAEEDAF GLGGLGGLTPNPVILQDCMW SGFSAREKLERAVSEKLQHG

Data sets:
Data typeCount
13C chemical shifts403
15N chemical shifts140
1H chemical shifts460

Additional metadata:

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

Assembly:

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

Entities:

Entity 1, N-Myc 1-137 140 residues - Formula weight is not available

1   GLYALAMETMETPROSERCYSSERTHRSER
2   THRMETPROGLYMETILECYSLYSASNPRO
3   ASPLEUGLUPHEASPSERLEUGLNPROCYS
4   PHETYRPROASPGLUASPASPPHETYRPHE
5   GLYGLYPROASPSERTHRPROPROGLYGLU
6   ASPILETRPLYSLYSPHEGLULEULEUPRO
7   THRPROPROLEUSERPROSERARGGLYPHE
8   ALAGLUHISSERSERGLUPROPROSERTRP
9   VALTHRGLUMETLEULEUGLUASNGLULEU
10   TRPGLYSERPROALAGLUGLUASPALAPHE
11   GLYLEUGLYGLYLEUGLYGLYLEUTHRPRO
12   ASNPROVALILELEUGLNASPCYSMETTRP
13   SERGLYPHESERALAARGGLULYSLEUGLU
14   ARGALAVALSERGLULYSLEUGLNHISGLY

Samples:

sample_1: N-Myc 1-137, [U-99% 13C; U-99% 15N], 250 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
2D 1H-13C 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
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D C-detected CONsample_1isotropicsample_conditions_1
2D C-detected haCACOsample_1isotropicsample_conditions_1
2D C-detected haCAnCOsample_1isotropicsample_conditions_1
2D N-detected haCANsample_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
  • Bruker Avance 950 MHz

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