BMRB Entry 52412

Name: Backbone and side-chain resonance assignments of GRB2 with a SOS1 PRM and an EGFR phosphorylated peptide
Published: 2024-10-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52412

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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 side-chain resonance assignments of GRB2 with a SOS1 PRM and an EGFR phosphorylated peptide

Deposition date:

2024-04-15

Original release date:

2024-10-22

Authors:

Tateno, Keita; Ando, Takami; Tabta, Maako; Sugasawa, Haruka; Hayashi, Toshifumi; PM, Sayeesh; Inomata, Kohsuke; Mikawa, Tsutomu; Ito, Yutaka; Ikeya, Teppei

Citation:

Citation: Tateno, Keita; Ando, Takami; Tabata, Maako; Sugasawa, Haruka; Hayashi, Toshifumi; Yu, Sangya; Pm, Sayeesh; Inomata, Kohsuke; Mikawa, Tsutomu; Ito, Yutaka; Ikeya, Teppei. "Different molecular recognition by three domains of the full-length GRB2 to SOS1 proline-rich motifs and EGFR phosphorylated sites" Chem. Sci. 15, 15858-15872 (2024).
PubMed: 39282643

Assembly members:

Assembly members:
entity_1, polymer, 217 residues, Formula weight is not available
entity_2, polymer, 10 residues, Formula weight is not available
entity_3, polymer, 7 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: pET14b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MEAIAKYDFKATADDELSFK RGDILKVLNEESDQNWYKAE LNGKDGFIPKNYIEMKPHPW FFGKIPRAKAEEMLSKQRHD GAFLIRESESAPGDFSLSVK FGNDVQHFKVLRDGAGKYFL WVVKFNSLNELVDYHRSTSV SRNQQIFLRDIEQVPQQPTY VQALFDFDPQEDGELGFRRG DFIHVMDNSDPNWWKGAAHG QTGMFPRNYVTPVNRNV
entity_2: VPPPVPPRRR
entity_3: EXINSQV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	684
15N chemical shifts	190
1H chemical shifts	790

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GRB2	1
2	SOS1 PRM	2
3	EGFR peptide	3

Entities:

Entity 1, GRB2 217 residues - Formula weight is not available

1

MET

GLU

ALA

ILE

ALA

LYS

TYR

ASP

PHE

LYS

2

ALA

THR

ALA

ASP

GLU

LEU

SER

PHE

LYS

3

ARG

GLY

ASP

ILE

LEU

LYS

VAL

LEU

ASN

GLU

4

GLU

SER

ASP

GLN

ASN

TRP

TYR

LYS

ALA

GLU

5

LEU

ASN

GLY

LYS

ASP

GLY

PHE

ILE

PRO

LYS

6

ASN

TYR

ILE

GLU

MET

LYS

PRO

HIS

PRO

TRP

7

PHE

GLY

LYS

ILE

PRO

ARG

ALA

LYS

ALA

8

GLU

MET

LEU

SER

LYS

GLN

ARG

HIS

ASP

9

GLY

ALA

PHE

LEU

ILE

ARG

GLU

SER

GLU

SER

10

ALA

PRO

GLY

ASP

PHE

SER

LEU

SER

VAL

LYS

11

PHE

GLY

ASN

ASP

VAL

GLN

HIS

PHE

LYS

VAL

12

LEU

ARG

ASP

GLY

ALA

GLY

LYS

TYR

PHE

LEU

13

TRP

VAL

LYS

PHE

ASN

SER

LEU

ASN

GLU

14

LEU

VAL

ASP

TYR

HIS

ARG

SER

THR

SER

VAL

15

SER

ARG

ASN

GLN

ILE

PHE

LEU

ARG

ASP

16

ILE

GLU

GLN

VAL

PRO

GLN

PRO

THR

TYR

17

VAL

GLN

ALA

LEU

PHE

ASP

PHE

ASP

PRO

GLN

18

GLU

ASP

GLY

GLU

LEU

GLY

PHE

ARG

GLY

19

ASP

PHE

ILE

HIS

VAL

MET

ASP

ASN

SER

ASP

20

PRO

ASN

TRP

LYS

GLY

ALA

HIS

GLY

21

GLN

THR

GLY

MET

PHE

PRO

ARG

ASN

TYR

VAL

22

THR

PRO

VAL

ASN

ARG

ASN

VAL

Entity 2, SOS1 PRM 10 residues - Formula weight is not available

1

VAL

PRO

VAL

PRO

ARG

Entity 3, EGFR peptide 7 residues - Formula weight is not available

1

GLU

PTR

ILE

ASN

SER

GLN

VAL

Samples:

sample_1: GRB2, [U-100% 15N], 400 ± 100 uM; Na2HPO4-NaH2PO4 20 mM; NaN3 0.05%

sample_2: GRB2, [U-100% 13C; U-100% 15N], 400 ± 100 uM; Na2HPO4-NaH2PO4 20 mM; NaN3 0.05%

sample_3: GRB2, [U-100% 13C; U-100% 15N; U-90% 2H], 400 ± 100 uM; Na2HPO4-NaH2PO4 20 mM; NaN3 0.05%

sample_conditions_1: ionic strength: 20 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 20 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 20 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HN(CA)CO	sample_2	isotropic	sample_conditions_2
3D CBCACONH	sample_2	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_2	isotropic	sample_conditions_2
3D HN(CA)CO	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2
3D HCCH-COSY	sample_2	isotropic	sample_conditions_2
3D C(CO)NH	sample_2	isotropic	sample_conditions_2
3D H(CCO)NH	sample_2	isotropic	sample_conditions_2
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_2
3D TROSY-HNCO	sample_3	isotropic	sample_conditions_3
3D TROSY-HNCA	sample_3	isotropic	sample_conditions_3
3D TROSY-HN(CA)CO	sample_3	isotropic	sample_conditions_3
3D TROSY-HN(CO)CA	sample_3	isotropic	sample_conditions_3
3D TROSY-HNCACB	sample_3	isotropic	sample_conditions_3
3D TROSY-HN(CO)CACB	sample_3	isotropic	sample_conditions_3
3D 13C-separated NOESY	sample_2	isotropic	sample_conditions_2
3D 15N-separated NOESY	sample_2	isotropic	sample_conditions_2

Software:

TOPSPIN v3.5 PL7 - collection

AZARA v2.8.1 - processing

CcpNMR v2.5.0 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE III 800 MHz