BMRB Entry 27522

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the tandem-SH2 domain of SHP2 (1-217) with a point mutation E76K
Published: 2018-11-16

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27522

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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 for the tandem-SH2 domain of SHP2 (1-217) with a point mutation E76K

Deposition date:

2018-06-14

Original release date:

2018-11-16

Authors:

Sun, Yizhi; Kern, Dorothee

Citation:

Citation: Padua, Ricardo; Sun, Yizhi; Marko, Ingrid; Pitsawong, Warintra; Stiller, John; Otten, Renee; Kern, Dorothee. "Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2" Nat. Commun. 9, 4507-4507 (2018).
PubMed: 30375376

Assembly members:

Assembly members:
shp2_shnc_e76k, polymer, 220 residues, 24631.708 Da.

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):
shp2_shnc_e76k: GSGMTSRRWFHPNITGVEAE NLLLTRGVDGSFLARPSKSN PGDFTLSVRRNGAVTHIKIQ NTGDYYDLYGGEKFATLAKL VQYYMEHHGQLKEKNGDVIE LKYPLNCADPTSERWFHGHL SGKEAEKLLTEKGKHGSFLV RESQSHPGDFVLSVRTGDDK GESNDGKSKVTHVMIRCQEL KYDVGGGERFDSLTDLVEHY KKNPMVETLGTVLQLKQPLN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list
spectral_peak_list

Data type	Count
13C chemical shifts	378
15N chemical shifts	199
1H chemical shifts	199

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	shp2 shnc e76k	1

Entities:

Entity 1, shp2 shnc e76k 220 residues - 24631.708 Da.

Residue 1-3 represent a non-native sequence to facilitate TEV cleavage.

1	GLY	SER	GLY	MET	THR	SER	ARG	ARG	TRP	PHE
2	HIS	PRO	ASN	ILE	THR	GLY	VAL	GLU	ALA	GLU
3	ASN	LEU	LEU	LEU	THR	ARG	GLY	VAL	ASP	GLY
4	SER	PHE	LEU	ALA	ARG	PRO	SER	LYS	SER	ASN
5	PRO	GLY	ASP	PHE	THR	LEU	SER	VAL	ARG	ARG
6	ASN	GLY	ALA	VAL	THR	HIS	ILE	LYS	ILE	GLN
7	ASN	THR	GLY	ASP	TYR	TYR	ASP	LEU	TYR	GLY
8	GLY	GLU	LYS	PHE	ALA	THR	LEU	ALA	LYS	LEU
9	VAL	GLN	TYR	TYR	MET	GLU	HIS	HIS	GLY	GLN
10	LEU	LYS	GLU	LYS	ASN	GLY	ASP	VAL	ILE	GLU
11	LEU	LYS	TYR	PRO	LEU	ASN	CYS	ALA	ASP	PRO
12	THR	SER	GLU	ARG	TRP	PHE	HIS	GLY	HIS	LEU
13	SER	GLY	LYS	GLU	ALA	GLU	LYS	LEU	LEU	THR
14	GLU	LYS	GLY	LYS	HIS	GLY	SER	PHE	LEU	VAL
15	ARG	GLU	SER	GLN	SER	HIS	PRO	GLY	ASP	PHE
16	VAL	LEU	SER	VAL	ARG	THR	GLY	ASP	ASP	LYS
17	GLY	GLU	SER	ASN	ASP	GLY	LYS	SER	LYS	VAL
18	THR	HIS	VAL	MET	ILE	ARG	CYS	GLN	GLU	LEU
19	LYS	TYR	ASP	VAL	GLY	GLY	GLY	GLU	ARG	PHE
20	ASP	SER	LEU	THR	ASP	LEU	VAL	GLU	HIS	TYR
21	LYS	LYS	ASN	PRO	MET	VAL	GLU	THR	LEU	GLY
22	THR	VAL	LEU	GLN	LEU	LYS	GLN	PRO	LEU	ASN

Samples:

shp2-sh2sh2-e76k-protonated: shp2_shnc_e76k, [U-13C; U-15N], 0.9 mM; ADA 50 mM; TCEP 2 mM; H2O 90%; D2O 10%

Default: ionic strength: 0.100 M; pH: 6.500; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC/HMQC	shp2-sh2sh2-e76k-protonated	isotropic	Default
3D HNCA	shp2-sh2sh2-e76k-protonated	isotropic	Default
3D HNCACB	shp2-sh2sh2-e76k-protonated	isotropic	Default

Software:

CcpNmr_Analysis v2.4, CCPN - Spetrum analysis, Spetrum display

nmrPipe vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Spectrum processing

NMR spectrometers:

Varian DD2 600 MHz

UniProt	Q06124-2
AlphaFold	Q96HD7

1	GLY	SER	GLY	MET	THR	SER	ARG	ARG	TRP	PHE
2	HIS	PRO	ASN	ILE	THR	GLY	VAL	GLU	ALA	GLU
3	ASN	LEU	LEU	LEU	THR	ARG	GLY	VAL	ASP	GLY
4	SER	PHE	LEU	ALA	ARG	PRO	SER	LYS	SER	ASN
5	PRO	GLY	ASP	PHE	THR	LEU	SER	VAL	ARG	ARG
6	ASN	GLY	ALA	VAL	THR	HIS	ILE	LYS	ILE	GLN
7	ASN	THR	GLY	ASP	TYR	TYR	ASP	LEU	TYR	GLY
8	GLY	GLU	LYS	PHE	ALA	THR	LEU	ALA	LYS	LEU
9	VAL	GLN	TYR	TYR	MET	GLU	HIS	HIS	GLY	GLN
10	LEU	LYS	GLU	LYS	ASN	GLY	ASP	VAL	ILE	GLU
11	LEU	LYS	TYR	PRO	LEU	ASN	CYS	ALA	ASP	PRO
12	THR	SER	GLU	ARG	TRP	PHE	HIS	GLY	HIS	LEU
13	SER	GLY	LYS	GLU	ALA	GLU	LYS	LEU	LEU	THR
14	GLU	LYS	GLY	LYS	HIS	GLY	SER	PHE	LEU	VAL
15	ARG	GLU	SER	GLN	SER	HIS	PRO	GLY	ASP	PHE
16	VAL	LEU	SER	VAL	ARG	THR	GLY	ASP	ASP	LYS
17	GLY	GLU	SER	ASN	ASP	GLY	LYS	SER	LYS	VAL
18	THR	HIS	VAL	MET	ILE	ARG	CYS	GLN	GLU	LEU
19	LYS	TYR	ASP	VAL	GLY	GLY	GLY	GLU	ARG	PHE
20	ASP	SER	LEU	THR	ASP	LEU	VAL	GLU	HIS	TYR
21	LYS	LYS	ASN	PRO	MET	VAL	GLU	THR	LEU	GLY
22	THR	VAL	LEU	GLN	LEU	LYS	GLN	PRO	LEU	ASN

1	GLY	SER	GLY	MET	THR	SER	ARG	ARG	TRP	PHE
2	HIS	PRO	ASN	ILE	THR	GLY	VAL	GLU	ALA	GLU
3	ASN	LEU	LEU	LEU	THR	ARG	GLY	VAL	ASP	GLY
4	SER	PHE	LEU	ALA	ARG	PRO	SER	LYS	SER	ASN
5	PRO	GLY	ASP	PHE	THR	LEU	SER	VAL	ARG	ARG
6	ASN	GLY	ALA	VAL	THR	HIS	ILE	LYS	ILE	GLN
7	ASN	THR	GLY	ASP	TYR	TYR	ASP	LEU	TYR	GLY
8	GLY	GLU	LYS	PHE	ALA	THR	LEU	ALA	LYS	LEU
9	VAL	GLN	TYR	TYR	MET	GLU	HIS	HIS	GLY	GLN
10	LEU	LYS	GLU	LYS	ASN	GLY	ASP	VAL	ILE	GLU
11	LEU	LYS	TYR	PRO	LEU	ASN	CYS	ALA	ASP	PRO
12	THR	SER	GLU	ARG	TRP	PHE	HIS	GLY	HIS	LEU
13	SER	GLY	LYS	GLU	ALA	GLU	LYS	LEU	LEU	THR
14	GLU	LYS	GLY	LYS	HIS	GLY	SER	PHE	LEU	VAL
15	ARG	GLU	SER	GLN	SER	HIS	PRO	GLY	ASP	PHE
16	VAL	LEU	SER	VAL	ARG	THR	GLY	ASP	ASP	LYS
17	GLY	GLU	SER	ASN	ASP	GLY	LYS	SER	LYS	VAL
18	THR	HIS	VAL	MET	ILE	ARG	CYS	GLN	GLU	LEU
19	LYS	TYR	ASP	VAL	GLY	GLY	GLY	GLU	ARG	PHE
20	ASP	SER	LEU	THR	ASP	LEU	VAL	GLU	HIS	TYR
21	LYS	LYS	ASN	PRO	MET	VAL	GLU	THR	LEU	GLY
22	THR	VAL	LEU	GLN	LEU	LYS	GLN	PRO	LEU	ASN