BMRB Entry 52758

Name: Backbone 1H, 13C, and 15N chemical shift assignments of apo T42A-NSH2 domain of SHP2 phosphatase
Published: 2025-12-29

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52758

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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 1H, 13C, and 15N chemical shift assignments of apo T42A-NSH2 domain of SHP2 phosphatase

Deposition date:

2024-12-16

Original release date:

2025-12-29

Authors:

Ojoawo, Adedolapo; Glaser, Andrew

Citation:

Citation: Glaser, Andrew; Padua, Ricardo; Ojoawo, Adedolapo; Sullivan, Camille; Kern, Dorothee. "Phosphatase SHP2 pathogenic mutations enhance activity by altering conformational sampling" Proc. Natl. Acad. Sci. U.S.A. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 105 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: pET-28a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MTSRRWFHPNITGVEAENLL LTRGVDGSFLARPSKSNPGD FALSVRRNGAVTHIKIQNTG DYYDLYGGEKFATLAELVQY YMEHHGQLKEKNGDVIELKY PLNCA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	200
15N chemical shifts	100
1H chemical shifts	100

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NSH2 domain	1

Entities:

Entity 1, NSH2 domain 105 residues - Formula weight is not available

1

MET

THR

SER

ARG

TRP

PHE

HIS

PRO

ASN

2

ILE

THR

GLY

VAL

GLU

ALA

GLU

ASN

LEU

3

LEU

THR

ARG

GLY

VAL

ASP

GLY

SER

PHE

LEU

4

ALA

ARG

PRO

SER

LYS

SER

ASN

PRO

GLY

ASP

5

PHE

ALA

LEU

SER

VAL

ARG

ASN

GLY

ALA

6

VAL

THR

HIS

ILE

LYS

ILE

GLN

ASN

THR

GLY

7

ASP

TYR

ASP

LEU

TYR

GLY

GLU

LYS

8

PHE

ALA

THR

LEU

ALA

GLU

LEU

VAL

GLN

TYR

9

TYR

MET

GLU

HIS

GLY

GLN

LEU

LYS

GLU

10

LYS

ASN

GLY

ASP

VAL

ILE

GLU

LEU

LYS

TYR

11

PRO

LEU

ASN

CYS

ALA

Samples:

sample_1: TCEP 1 mM; sodium chloride 50 mM; Bis-tris 50 mM; T42A-NSH2 APO, [U-99% 13C; U-99% 15N], 1.1 mM

sample_2: TCEP 1 mM; Bis-tris 50 mM; sodium chloride 50 mM; T42A-NSH2 APO, [U-100% 15N], 1.1 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
T1/R1 relaxation	sample_2	isotropic	sample_conditions_1
T2/R2 relaxation	sample_2	isotropic	sample_conditions_1
1H-15N heteronoe	sample_2	isotropic	sample_conditions_1
15N CPMG	sample_2	isotropic	sample_conditions_1
15N CEST	sample_2	isotropic	sample_conditions_1

Software:

POKY - chemical shift assignment, peak picking

NMRbox - data analysis

NMRPipe - processing

Relax - data analysis

TOPSPIN - collection

PyMOL - data analysis

ChemEx - data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker US2 900 MHz
Bruker AVANCE III 900 MHz

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