Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53382

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Name: Backbone 1H, 13C and 15N assignments of L-MYC 1-80
Published: 2026-05-21

Title:

Backbone 1H, 13C and 15N assignments of L-MYC 1-80

Deposition date:

2025-10-08

Original release date:

2026-05-21

Authors:

Kenney, Tristan; Houliston, Scott; Penn, Linda; Arrowsmith, Cheryl

Citation:

Citation: Kenney, Tristan; Houliston, Scott; Lin, Peter; Movahedi, Nikan; Arrowsmith, Cheryl; Penn, Linda. "Structure and function of the L-MYC N-terminus impacts strategies to inhibit the MYC family of oncoproteins" Biochem. J. 483, 993-991006 (2026).
PubMed: 42030451

Assembly members:

Assembly members:
entity_1, polymer, 81 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: pNH-TrxT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SMDYDSYQHYFYDYDCGEDF YRSTAPSEDIWKKFELVPSP PTSPPWGLGPGAGDPAPGIG PPEPWPGGCTGDEAESRGHS K

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	208
15N chemical shifts	65
1H chemical shifts	248

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	L-MYC	1

Entities:

Entity 1, L-MYC 81 residues - Formula weight is not available

1

SER

MET

ASP

TYR

ASP

SER

TYR

GLN

HIS

TYR

2

PHE

TYR

ASP

TYR

ASP

CYS

GLY

GLU

ASP

PHE

3

TYR

ARG

SER

THR

ALA

PRO

SER

GLU

ASP

ILE

4

TRP

LYS

PHE

GLU

LEU

VAL

PRO

SER

PRO

5

PRO

THR

SER

PRO

TRP

GLY

LEU

GLY

PRO

6

GLY

ALA

GLY

ASP

PRO

ALA

PRO

GLY

ILE

GLY

7

PRO

GLU

PRO

TRP

PRO

GLY

CYS

THR

8

GLY

ASP

GLU

ALA

GLU

SER

ARG

GLY

HIS

SER

9

LYS

Samples:

sample_1: L-MYC, [U-99% 13C; U-99% 15N], 200 uM; HEPES 20 mM; sodium chloride 200 mM; glycerol 5%; DTT 2 mM

sample_conditions_1: ionic strength: 220 mM; pH: 6.9; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

MddNMR - processing

SPARKY - peak picking

FMCGUI - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 800 MHz

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

BMRB Entry 53382