BMRB Entry 26329

Name: Backbone assignment of the N terminal SH2 domain of PI3K bound to CD28 derived phosphopeptide
Published: 2023-06-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26329

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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 assignment of the N terminal SH2 domain of PI3K bound to CD28 derived phosphopeptide

Deposition date:

2022-03-19

Original release date:

2023-06-05

Authors:

Hosoe, Yuhi; Miyanoiri, Yohei; Re, Suyong; Asahina, Yuya; Kawakami, Toru; Kuroda, Mataka; Mizuguchi, Kenji; Oda, Masayuki

Citation:

Citation: Hosoe, Yuhi; Miyanoiri, Yohei; Re, Suyong; Ochi, Saki; Asahina, Yuya; Kawakami, Toru; Kuroda, Masataka; Mizuguchi, Kenji; Oda, Masayuki. "Structural dynamics of the N-terminal SH2 domain of PI3K in its free and CD28-bound states" FEBS J. 290, 2366-2378 (2023).
PubMed: 36282120

Assembly members:

Assembly members:
N terminal SH2 domain of PI3K, polymer, 107 residues, Formula weight is not available
CD28 derived phosphopeptide, polymer, 12 residues, 1501.584 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: pGEX

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N terminal SH2 domain of PI3K: SNMSLQNAEWYWGDISREEV NEKLRDTADGTFLVRDASTK MHGDYTLTLRKGGNNKLIKI FHRDGKYGFSDPLTFSSVVE LINHYRNESLAQYNPKLDVK LLYPVSK
CD28 derived phosphopeptide: SDXMNMTPRRPG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	310
15N chemical shifts	105
1H chemical shifts	105

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	nSH2	1
2	CD28 derived phosphopeptide	2

Entities:

Entity 1, nSH2 107 residues - Formula weight is not available

1

SER

ASN

MET

SER

LEU

GLN

ASN

ALA

GLU

TRP

2

TYR

TRP

GLY

ASP

ILE

SER

ARG

GLU

VAL

3

ASN

GLU

LYS

LEU

ARG

ASP

THR

ALA

ASP

GLY

4

THR

PHE

LEU

VAL

ARG

ASP

ALA

SER

THR

LYS

5

MET

HIS

GLY

ASP

TYR

THR

LEU

THR

LEU

ARG

6

LYS

GLY

ASN

LYS

LEU

ILE

LYS

ILE

7

PHE

HIS

ARG

ASP

GLY

LYS

TYR

GLY

PHE

SER

8

ASP

PRO

LEU

THR

PHE

SER

VAL

GLU

9

LEU

ILE

ASN

HIS

TYR

ARG

ASN

GLU

SER

LEU

10

ALA

GLN

TYR

ASN

PRO

LYS

LEU

ASP

VAL

LYS

11

LEU

TYR

PRO

VAL

SER

LYS

Entity 2, CD28 derived phosphopeptide 12 residues - 1501.584 Da.

1

SER

ASP

PTR

MET

ASN

MET

THR

PRO

ARG

2

PRO

GLY

Samples:

sample_1: N terminal SH2 domain of PI3K, [U-99% 13C; U-99% 15N], 0.1 – 0.3 mM; CD28 derived phosphopeptide0.2 – 0.6 mM; potassium phosphate 10 mM; sodium 2,2-dimethyl-2-silapentane-5-sulfonate 0.01 % v/v; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 10 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY - chemical shift assignment

TOPSPIN - collection

TOPSPIN - processing

NMR spectrometers:

Bruker AVANCE III HD 600 MHz