BMRB Entry 52223

Name: Transduction of motion through an intermolecular dynamic network at the protein-protein interface
Published: 2025-04-25

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52223

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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:

Transduction of motion through an intermolecular dynamic network at the protein-protein interface

Deposition date:

2023-12-01

Original release date:

2025-04-25

Authors:

Medina Gomez, Sara; Vasa, Suresh; Linser, Rasmus

Citation:

Citation: Medina Gomez, Sara; Gonzalez, Tye; Vasa, Suresh; Linser, Rasmus. "Allostery at a Protein-Protein Interface Harboring an Intermolecular Motional Networke" Angew. Chem. Int. Ed. Engl. 63, e202411472-e202411472 (2024).
PubMed: 39157914

Assembly members:

Assembly members:
entity_1, polymer, 62 residues, 7134.15 Da.

Natural source:

Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET3D

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MDETGKELVLALYDYQEKSP AEVTMKKGDILTLLNSTNKD WWKVEVNDRQGFVPAAYVKK LD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	138
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	SH3 domain	1

Entities:

Entity 1, SH3 domain 62 residues - 7134.15 Da.

1

MET

ASP

GLU

THR

GLY

LYS

GLU

LEU

VAL

LEU

2

ALA

LEU

TYR

ASP

TYR

GLN

GLU

LYS

SER

PRO

3

ALA

GLU

VAL

THR

MET

LYS

GLY

ASP

ILE

4

LEU

THR

LEU

ASN

SER

THR

ASN

LYS

ASP

5

TRP

LYS

VAL

GLU

VAL

ASN

ASP

ARG

GLN

6

GLY

PHE

VAL

PRO

ALA

TYR

VAL

LYS

7

LEU

ASP

Samples:

sample_1: Spectrin alpha SH3 domain, [U-100% 13C; U-100% 15N; U-99% 2H], 4 mg

sample_conditions_1: pH: 8; pressure: 1 atm; temperature: 295 K

Experiments:

Name	Sample	Sample state	Sample conditions
hNH	sample_1	isotropic	sample_conditions_1
hCONH	sample_1	isotropic	sample_conditions_1
hCANH	sample_1	isotropic	sample_conditions_1
hCAcoNH	sample_1	isotropic	sample_conditions_1
hcaCBcaNH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.1.4 - collection

CcpNMR v3.2.0 - chemical shift assignment

SSA - processing

NMR spectrometers:

Bruker AVANCE NEO 700 MHz

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