BMRB Entry 52759

Name: Backbone 1H, 13C, and 15N chemical shift assignments of GAB1-bound WT-NSH2 domain of SHP2 phosphatase
Published: 2025-12-29

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52759

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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 GAB1-bound WT-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
entity_2, polymer, 10 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 FTLSVRRNGAVTHIKIQNTG DYYDLYGGEKFATLAELVQY YMEHHGQLKEKNGDVIELKY PLNCA
entity_2: QVEXLDLDLD

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	N-SH2 domain	1
2	peptide	2

Entities:

Entity 1, N-SH2 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

THR

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

Entity 2, peptide 10 residues - Formula weight is not available

1

GLN

VAL

GLU

PTR

LEU

ASP

LEU

ASP

LEU

ASP

Samples:

sample_1: WT-NSH2 GAB1, [U-99% 13C; U-99% 15N], 1.1 mM; TCEP 1 mM; sodium chloride 50 mM; BIS-TRIS 50 mM

sample_2: WT-NSH2 GAB1, [U-99% 15N], 1.1 mM; TCEP 1 mM; sodium chloride 50 mM; BIS-TRIS 50 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_2	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

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