BMRB Entry 28074

Name: Backbone and sidechain resonances of the nSH2 domain of SHP2 in complex with the ITIM of PD-1
Published: 2020-11-13

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR28074

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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 and sidechain resonances of the nSH2 domain of SHP2 in complex with the ITIM of PD-1

Deposition date:

2020-02-09

Original release date:

2020-11-13

Authors:

Marasco, Michelangelo; Kirkpatrick, John; Carlomagno, Teresa

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.
ITIM, polymer, 11 residues, 1396.34276 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
nsh2: GPMASRRWFHPNITGVEAEN LLLTRGVDGSFLARPSKSNP GDFTLSVRRNGAVTHIKIQN TGDYYDLYGGEKFATLAELV QYYMEHHGQLKEKNGDVIEL KYPLNCA
ITIM: FSVDXGELDFQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	484
15N chemical shifts	116
1H chemical shifts	818

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	nsh2	1
2	ITIM	2

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

Entity 2, ITIM 11 residues - 1396.34276 Da.

1

PHE

SER

VAL

ASP

PTR

GLY

GLU

LEU

ASP

PHE

2

GLN

Samples:

peptide_excess: ITIM 1.6 mM; nsh2, [U-13C; U-15N], 0.8 mM; MES 100.0 mM; NaCl 150.0 mM; TCEP 3.0 mM

protein_excess: ITIM 0.6 mM; nsh2, [U-13C; U-15N], 0.8 mM; NaCl 150.0 mM; TCEP 3.0 mM; Deuterated PIPES, [U-2H], 100.0 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 HNCO	peptide_excess	isotropic	Standard
3D HNCACB	peptide_excess	isotropic	Standard
nsh2-pep6-HNCOCAB (H[N[co[{CA\|ca[C]}]]])	peptide_excess	isotropic	Standard
2D 1H-15N HSQC/HMQC	peptide_excess	isotropic	Standard
2D 1H-13C HSQC/HMQC	peptide_excess	isotropic	Standard
2D 1H-13C HSQC/HMQC	peptide_excess	isotropic	Standard
ITIM-NOESY (H{[n(0)]+[c(0)]}_H{[n(0)]+[c(0)]}.through-space)	protein_excess	isotropic	Standard
ITIM-TOCSY (H{[n(0)]+[c(0)]}_H{[n(0)]+[c(0)]}.relayed)	protein_excess	isotropic	Standard
3D 1H-15N NOESY	peptide_excess	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
Bruker Avance III HD 600 MHz

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