BMRB Entry 30861

Name: Solution NMR structure of the PNUTS amino-terminal Domain fused to Myc Homology Box 0
Published: 2021-03-01

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PDB ID: 7lqt
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30861
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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:

Solution NMR structure of the PNUTS amino-terminal Domain fused to Myc Homology Box 0

Deposition date:

2021-02-15

Original release date:

2021-03-01

Authors:

Lemak, A.; Wei, Y.; Duan, S.; Houliston, S.; Penn, L.; Arrowsmith, C.

Citation:

Citation: Wei, Yong; Redel, Cornelia; Ahlner, Alexandra; Lemak, Alexander; Johansson-Akhe, Isak; Houliston, Scott; Kenney, Tristan; Tamachi, Aaliya; Morad, Vivian; Duan, Shili; Andrews, David; Wallner, Bjorn; Sunnerhagen, Maria; Arrowsmith, Cheryl; Penn, Linda. "The MYC oncoprotein directly interacts with its chromatin cofactor PNUTS to recruit PP1 phosphatase" Nucleic Acids Res. 50, 3505-3522 (2022).
PubMed: 35244724

Assembly members:

Assembly members:
entity_1, polymer, 174 residues, 19391.191 Da.

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSGPIDPKELLKGLDSFLT RDGEVKSVDGIAKIFSLMKE ARKMVSRCTYLNIILQTRAP EVLVKFIDVGGYKLLNSWLT YSKTTNNIPLLQQILLTLQH LPLTVDHLKQNNTAKLVKQL SKSSEDEELRKLASVLVSDW MAVIRSQSGGGSGGGSDLDY DSVQPYFYCDEEEN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	702
15N chemical shifts	176
1H chemical shifts	1184

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 174 residues - 19391.191 Da.

1

MET

GLY

SER

GLY

PRO

ILE

ASP

PRO

LYS

GLU

2

LEU

LYS

GLY

LEU

ASP

SER

PHE

LEU

THR

3

ARG

ASP

GLY

GLU

VAL

LYS

SER

VAL

ASP

GLY

4

ILE

ALA

LYS

ILE

PHE

SER

LEU

MET

LYS

GLU

5

ALA

ARG

LYS

MET

VAL

SER

ARG

CYS

THR

TYR

6

LEU

ASN

ILE

LEU

GLN

THR

ARG

ALA

PRO

7

GLU

VAL

LEU

VAL

LYS

PHE

ILE

ASP

VAL

GLY

8

GLY

TYR

LYS

LEU

ASN

SER

TRP

LEU

THR

9

TYR

SER

LYS

THR

ASN

ILE

PRO

LEU

10

LEU

GLN

ILE

LEU

THR

LEU

GLN

HIS

11

LEU

PRO

LEU

THR

VAL

ASP

HIS

LEU

LYS

GLN

12

ASN

THR

ALA

LYS

LEU

VAL

LYS

GLN

LEU

13

SER

LYS

SER

GLU

ASP

GLU

LEU

ARG

14

LYS

LEU

ALA

SER

VAL

LEU

VAL

SER

ASP

TRP

15

MET

ALA

VAL

ILE

ARG

SER

GLN

SER

GLY

16

GLY

SER

GLY

SER

ASP

LEU

ASP

TYR

17

ASP

SER

VAL

GLN

PRO

TYR

PHE

TYR

CYS

ASP

18

GLU

ASN

Samples:

sample_1: HEPES 20 mM; sodium chloride 200 mM; DTT 2 mM; glycerol 5%; labeled protein, [U-100% 13C; U-100% 15N], 400 uM

sample_conditions_1: ionic strength: 200 mM; pH: 6.9; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

FMCGUI, A. Lemak & C.H. Arrowsmith - chemical shift assignment

Sparky, Goddard - peak picking

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE II 800 MHz

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