BMRB Entry 51427

Name: B-Myb association with DNA is mediated by its negative regulatory domain and Cdk phosphorylation
Published: 2022-10-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51427

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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:

B-Myb association with DNA is mediated by its negative regulatory domain and Cdk phosphorylation

Deposition date:

2022-05-04

Original release date:

2022-10-19

Authors:

Wijeratne, Tilini; Guiley, Keelan; Lee, Hsiau-Wei; Muller, Gerd; Rubin, Seth

Citation:

Citation: Wijeratne, Tilini; Guiley, Keelan; Lee, Hsiau-Wei; Muller, Gerd; Rubin, Seth. "Cyclin-dependent kinase-mediated phosphorylation and the negative regulatory domain of transcription factor B-Myb modulate its DNA binding" J. Biol. Chem. 298, 102319-102319 (2022).
PubMed: 35926712

Assembly members:

Assembly members:
entity_1, polymer, 93 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: pGEX

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KYSMDNTPHTPTPFKNALEK YGPLKPLPQTPHLEEDLKEV LRSEAGIELIIEDDIRPEKQ KRKPGLRRSPIKKVRKSLAL DIVDEDVKLMMST

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	257
15N chemical shifts	81
1H chemical shifts	78

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NRD	1

Entities:

Entity 1, NRD 93 residues - Formula weight is not available

1

LYS

TYR

SER

MET

ASP

ASN

THR

PRO

HIS

THR

2

PRO

THR

PRO

PHE

LYS

ASN

ALA

LEU

GLU

LYS

3

TYR

GLY

PRO

LEU

LYS

PRO

LEU

PRO

GLN

THR

4

PRO

HIS

LEU

GLU

ASP

LEU

LYS

GLU

VAL

5

LEU

ARG

SER

GLU

ALA

GLY

ILE

GLU

LEU

ILE

6

ILE

GLU

ASP

ILE

ARG

PRO

GLU

LYS

GLN

7

LYS

ARG

LYS

PRO

GLY

LEU

ARG

SER

PRO

8

ILE

LYS

VAL

ARG

LYS

SER

LEU

ALA

LEU

9

ASP

ILE

VAL

ASP

GLU

ASP

VAL

LYS

LEU

MET

10

MET

SER

THR

Samples:

sample_1: NRD, B-Myb, [U-100% 13C; U-100% 15N], 300 uM; sodium phosphate 20 mM; DTT 1 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CCONH	sample_1	isotropic	sample_conditions_1
2D CON	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment

TOPSPIN - collection

VNMRj - collection

NMR spectrometers:

Bruker AVANCE III HD 800 MHz
Varian INOVA 600 MHz

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