BMRB Entry 52047

Name: Chemical shift assignments for GB1-N-Myc 18-59 fusion
Published: 2024-10-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52047

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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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Title:

Chemical shift assignments for GB1-N-Myc 18-59 fusion

Deposition date:

2023-07-20

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, 103 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: GAMAQYKLALNGKTLKGETT TEAVDAATAEKVFKQYANDN GVDGEWTYDDATKTFTVTET SDLEFDSLQPSFYPDEDDFY FGGPDSTPPGEDIWKKFELL PTP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	296
15N chemical shifts	103
1H chemical shifts	388

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GB1-N-Myc 15-59	1

Entities:

Entity 1, GB1-N-Myc 15-59 103 residues - Formula weight is not available

1

GLY

ALA

MET

ALA

GLN

TYR

LYS

LEU

ALA

LEU

2

ASN

GLY

LYS

THR

LEU

LYS

GLY

GLU

THR

3

THR

GLU

ALA

VAL

ASP

ALA

THR

ALA

GLU

4

LYS

VAL

PHE

LYS

GLN

TYR

ALA

ASN

ASP

ASN

5

GLY

VAL

ASP

GLY

GLU

TRP

THR

TYR

ASP

6

ALA

THR

LYS

THR

PHE

THR

VAL

THR

GLU

THR

7

SER

ASP

LEU

GLU

PHE

ASP

SER

LEU

GLN

PRO

8

SER

PHE

TYR

PRO

ASP

GLU

ASP

PHE

TYR

9

PHE

GLY

PRO

ASP

SER

THR

PRO

GLY

10

GLU

ASP

ILE

TRP

LYS

PHE

GLU

LEU

11

PRO

THR

PRO

Samples:

sample_1: GB1-N-Myc 18-59, [U-99% 13C; U-99% 15N], 325 uM; (K/H)3PO4 20 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

CcpNMR vAnalysis v 2.5 - chemical shift assignment

NMR spectrometers:

Oxford/Bruker Avance 600 MHz

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