BMRB Entry 26328

Name: Backbone assignment of the N-terminal SH2 domain of PI3K
Published: 2023-06-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26328

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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

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

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	301
15N chemical shifts	100
1H chemical shifts	100

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	nSH2 of PI3K	1

Entities:

Entity 1, nSH2 of PI3K 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

Samples:

sample_1: N-terminal SH2 domain of PI3K, [U-99% 13C; U-99% 15N], 0.1 – 0.3 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY - chemical shift assignment

TOPSPIN - processing

TOPSPIN - collection

NMR spectrometers:

Bruker AVANCE III HD 600 MHz