BMRB Entry 28069

Name: Backbone resonances of the nSH2 domain of SHP2
Published: 2020-11-13

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28069

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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 resonances of the nSH2 domain of SHP2

Deposition date:

2020-02-09

Original release date:

2020-11-13

Authors:

Marasco, Michelangelo; Carlomagno, Teresa; Kirkpatrick, John

Citation:

Citation: Marasco, Michelangelo; Kirkpatrick, John; Carlomagno, Teresa. "1H, 13C, 15N chemical shift assignments of SHP2 SH2 domains in complex with PD-1 immune-tyrosine motifs" Biomol. NMR Assign. 14, 179-188 (2020).
PubMed: 32236803

Assembly members:

Assembly members:
nSH2, polymer, 107 residues, 12003.5316 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: pETM22

Entity Sequences (FASTA):

Entity Sequences (FASTA):
nSH2: GPMASRRWFHPNITGVEAEN LLLTRGVDGSFLARPSKSNP GDFTLSVRRNGAVTHIKIQN TGDYYDLYGGEKFATLAELV QYYMEHHGQLKEKNGDVIEL KYPLNCA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	187
15N chemical shifts	94
1H chemical shifts	94

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	nSH2	1

Entities:

Entity 1, nSH2 107 residues - 12003.5316 Da.

1

GLY

PRO

MET

ALA

SER

ARG

TRP

PHE

HIS

2

PRO

ASN

ILE

THR

GLY

VAL

GLU

ALA

GLU

ASN

3

LEU

THR

ARG

GLY

VAL

ASP

GLY

SER

4

PHE

LEU

ALA

ARG

PRO

SER

LYS

SER

ASN

PRO

5

GLY

ASP

PHE

THR

LEU

SER

VAL

ARG

ASN

6

GLY

ALA

VAL

THR

HIS

ILE

LYS

ILE

GLN

ASN

7

THR

GLY

ASP

TYR

ASP

LEU

TYR

GLY

8

GLU

LYS

PHE

ALA

THR

LEU

ALA

GLU

LEU

VAL

9

GLN

TYR

MET

GLU

HIS

GLY

GLN

LEU

10

LYS

GLU

LYS

ASN

GLY

ASP

VAL

ILE

GLU

LEU

11

LYS

TYR

PRO

LEU

ASN

CYS

ALA

Samples:

nSH2_1: nSH2, [U-13C; U-15N], 0.8 mM; MES 100.0 mM; NaCl 150.0 mM; TCEP 3.0 mM

Standard: ionic strength: 0.150 M; pH: 6.800; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	nSH2_1	isotropic	Standard
HNCOCACB (H[N[co[{CA\|ca[C]}]]])	nSH2_1	isotropic	Standard
2D 1H-15N HSQC/HMQC	nSH2_1	isotropic	Standard

Software:

CcpNmr_Analysis v2.4, CCPN - peak picking, chemical shift assignment

NMRPipe v8.7, F. Delaglio, S. Grzesiek, G. Vuister, G. Zhu, J. Pfeifer, A. Bax - data processing

TOPSPIN v3.2, Bruker Biospin - data collection

NMR spectrometers:

Bruker Avance III HD 850 MHz

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