BMRB Entry 50106

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments of human Grb2 N-terminal SH3 domain conjugated with Sos1-derived modified peptide
Published: 2020-01-13

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR50106

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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 1H, 13C, and 15N Chemical Shift Assignments of human Grb2 N-terminal SH3 domain conjugated with Sos1-derived modified peptide

Deposition date:

2019-11-29

Original release date:

2020-01-13

Authors:

Luzik, Dmitrii; Rogacheva, Olga; Izmailov, Sergei; Indeykina, Maria; Kononikhin, Alexei; Skrynnikov, Nikolai

Citation:

Citation: Luzik, Dmitrii; Rogacheva, Olga; Izmailov, Sergei; Indeykina, Maria; Kononikhin, Alexei; Skrynnikov, Nikolai. "Molecular Dynamics model of peptide-protein conjugation: case study of covalent complex between Sos1 peptide and N-terminal SH3 domain from Grb2" Sci. Rep. 9, 20219-20219 (2019).
PubMed: 31882608

Assembly members:

Assembly members:
entity_1, polymer, 74 residues, Formula weight is not available
entity_2, polymer, 12 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: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGHHHHHHGLVPRGSEAIAK YDFKATADDELSFKRGDILK VLNEECDQNWYKAELNGKDG FIPKNYIEMKPHPG
entity_2: VPPPVPPRRRKX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	151
15N chemical shifts	52
1H chemical shifts	52

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Grb2 N-SH3	1
2	Sos1X'	2

Entities:

Entity 1, Grb2 N-SH3 74 residues - Formula weight is not available

1

MET

GLY

HIS

GLY

LEU

2

VAL

PRO

ARG

GLY

SER

GLU

ALA

ILE

ALA

LYS

3

TYR

ASP

PHE

LYS

ALA

THR

ALA

ASP

GLU

4

LEU

SER

PHE

LYS

ARG

GLY

ASP

ILE

LEU

LYS

5

VAL

LEU

ASN

GLU

CYS

ASP

GLN

ASN

TRP

6

TYR

LYS

ALA

GLU

LEU

ASN

GLY

LYS

ASP

GLY

7

PHE

ILE

PRO

LYS

ASN

TYR

ILE

GLU

MET

LYS

8

PRO

HIS

PRO

GLY

Entity 2, Sos1X' 12 residues - Formula weight is not available

1

VAL

PRO

VAL

PRO

ARG

2

LYS

X

Samples:

sample_1: entity_1, [U-13C; U-15N], 1.2 mM; entity_2 2.5 mM; Sodium Phosphate 20 mM; NaCl 150 mM; DTT 10 mM; NaN3 0.03%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.2; 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_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection, processing

CARA v1.9.2, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 500 MHz

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