BMRB Entry 53258

Name: Backbone 1H and 15N chemical shift assignments for the C-Terminal SH2 domain of SHP2 bound to doubly phosphorylated Gab1
Published: 2025-12-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53258

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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 and 15N chemical shift assignments for the C-Terminal SH2 domain of SHP2 bound to doubly phosphorylated Gab1

Deposition date:

2025-07-05

Original release date:

2025-12-16

Authors:

Machner, Lisa; Shaikhqasem, Alaa; Hamdi, Farzad; Gruber, Tobias; Wiebe, Felix; Breithaupt, Constanze; Kniest, Judith; Lewitzky, Marc; Parthier, Christoph; Kyrilis, Fotios; Balbach, Jochen; Kastritis, Panagiotis; Feller, Stephan; Stubbs, Milton

Citation:

Citation: Machner, Lisa; Shaikhqasem, Alaa; Hamdi, Farzad; Gruber, Tobias; Wiebe, Felix; Breithaupt, Constanze; Kniest, Judith; Lewitzky, Marc; Parthier, Christoph; Kyrilis, Fotios; Balbach, Jochen; Kastritis, Panagiotis; Feller, Stephan; Stubbs, Milton. "Mechanism of SHP2 activation by bis-Tyr-phosphorylated Gab1" Structure ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 124 residues, Formula weight is not available
entity_2, polymer, 68 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: pETSumo

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ELKYPLNCADPTSERWFHGH LSGKEAEKLLTEKGKHGSFL VRESQSHPGDFVLSVRTGDD KGESNDGKSKVTHVMIRCQE LKYDVGGGERFDSLTDLVEH YKKNPMVETLGTVLQLKQPL NTTR
entity_2: IKPKGDKQVEYLDLDLDSGK STPPRKQKSSGSGSSVADER VDYVVVDQQKTLALKSTREA WTDGRQST

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	113
1H chemical shifts	113

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Shp2 C-SH2	1
2	Gab1	2

Entities:

Entity 1, Shp2 C-SH2 124 residues - Formula weight is not available

1

GLU

LEU

LYS

TYR

PRO

LEU

ASN

CYS

ALA

ASP

2

PRO

THR

SER

GLU

ARG

TRP

PHE

HIS

GLY

HIS

3

LEU

SER

GLY

LYS

GLU

ALA

GLU

LYS

LEU

4

THR

GLU

LYS

GLY

LYS

HIS

GLY

SER

PHE

LEU

5

VAL

ARG

GLU

SER

GLN

SER

HIS

PRO

GLY

ASP

6

PHE

VAL

LEU

SER

VAL

ARG

THR

GLY

ASP

7

LYS

GLY

GLU

SER

ASN

ASP

GLY

LYS

SER

LYS

8

VAL

THR

HIS

VAL

MET

ILE

ARG

CYS

GLN

GLU

9

LEU

LYS

TYR

ASP

VAL

GLY

GLU

ARG

10

PHE

ASP

SER

LEU

THR

ASP

LEU

VAL

GLU

HIS

11

TYR

LYS

ASN

PRO

MET

VAL

GLU

THR

LEU

12

GLY

THR

VAL

LEU

GLN

LEU

LYS

GLN

PRO

LEU

13

ASN

THR

ARG

Entity 2, Gab1 68 residues - Formula weight is not available

both tyrosines are phosphorylated

1

ILE

LYS

PRO

LYS

GLY

ASP

LYS

GLN

VAL

GLU

2

TYR

LEU

ASP

LEU

ASP

LEU

ASP

SER

GLY

LYS

3

SER

THR

PRO

ARG

LYS

GLN

LYS

SER

4

GLY

SER

GLY

SER

VAL

ALA

ASP

GLU

ARG

5

VAL

ASP

TYR

VAL

ASP

GLN

LYS

6

THR

LEU

ALA

LEU

LYS

SER

THR

ARG

GLU

ALA

7

TRP

THR

ASP

GLY

ARG

GLN

SER

THR

Samples:

sample_1: Shp2 C-SH2 domain, [U-100% 13C; U-100% 15N], 750 uM; Gab1 617-684 2pY 1.125 mM; Bis Tris / HCl 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.0; pressure: 1 atm; temperature: 273.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1

Software:

NMRView - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 800 MHz

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