BMRB Entry 53231

Name: Backbone assignments of the catalytic domain of MKP5
Published: 2025-11-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53231

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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:

Backbone assignments of the catalytic domain of MKP5

Deposition date:

2025-06-17

Original release date:

2025-11-11

Authors:

Skeens, Erin; Lisi, George

Citation:

Citation: Skeens, Erin; Maschietto, Federica; Manjula, Ramu; Shillingford, Shanelle; Murphy, James; Lolis, Elias; Batista, Victor; Bennett, Anton; Lisi, George. "Dynamic and structural insights into allosteric regulation on MKP5 a dual-specificity phosphatase" Nat. Commun. 16, 7011-7011 (2025).
PubMed: 40745179

Assembly members:

Assembly members:
entity_1, polymer, 151 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: pET28a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMAELTPILPFLFLGNEQD AQDLDTMQRLNIGYVINVTT HLPLYHYEKGLFNYKRLPAT DSNKQNLRQYFEEAFEFIEE AHQCGKGLLIHCQAGVSRSA TIVIAYLMKHTRMTMTDAYK FVKGKRPIISPNLNFMGQLL EFEEDLNNGVT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	279
15N chemical shifts	95
1H chemical shifts	95

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	WT MKP5-CD	1

Entities:

Entity 1, WT MKP5-CD 151 residues - Formula weight is not available

1

GLY

HIS

MET

ALA

GLU

LEU

THR

PRO

ILE

LEU

2

PRO

PHE

LEU

PHE

LEU

GLY

ASN

GLU

GLN

ASP

3

ALA

GLN

ASP

LEU

ASP

THR

MET

GLN

ARG

LEU

4

ASN

ILE

GLY

TYR

VAL

ILE

ASN

VAL

THR

5

HIS

LEU

PRO

LEU

TYR

HIS

TYR

GLU

LYS

GLY

6

LEU

PHE

ASN

TYR

LYS

ARG

LEU

PRO

ALA

THR

7

ASP

SER

ASN

LYS

GLN

ASN

LEU

ARG

GLN

TYR

8

PHE

GLU

ALA

PHE

GLU

PHE

ILE

GLU

9

ALA

HIS

GLN

CYS

GLY

LYS

GLY

LEU

ILE

10

HIS

CYS

GLN

ALA

GLY

VAL

SER

ARG

SER

ALA

11

THR

ILE

VAL

ILE

ALA

TYR

LEU

MET

LYS

HIS

12

THR

ARG

MET

THR

MET

THR

ASP

ALA

TYR

LYS

13

PHE

VAL

LYS

GLY

LYS

ARG

PRO

ILE

SER

14

PRO

ASN

LEU

ASN

PHE

MET

GLY

GLN

LEU

15

GLU

PHE

GLU

ASP

LEU

ASN

GLY

VAL

16

THR

Samples:

sample_1: WT MKP5-CD, [U-13C; U-15N; U-2H], 800 uM; sodium phosphate 40 mM; EDTA 1 mM; DTT 2 mM

sample_conditions_1: ionic strength: 40 mM; pH: 7.4; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCA	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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

CARA - chemical shift assignment

NMRPipe - processing

NMR spectrometers:

Bruker AVANCE NEO 600 MHz

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