BMRB Entry 34662

Name: Structure of Insulin receptor-related receptor&#039;s transmembrane domain
Published: 2022-09-02

Click here to enlarge.

PDB ID: 7pl4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34662
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Structure of Insulin receptor-related receptor's transmembrane domain

Deposition date:

2021-08-28

Original release date:

2022-09-02

Authors:

Bershatsky, Y.; Nadezhdin, K.; Bocharova, O.; Bocharov, E.

Citation:

Citation: Bershatsky, Yaroslav; Kuznetsov, Andrey; Idiatullina, Aisha; Bocharova, Olga; Dolotova, Sofya; Gavrilenkova, Alina; Serova, Oxana; Deyev, Igor; Rakitina, Tatiana; Zangieva, Olga; Pavlov, Konstantin; Batishchev, Oleg; Britikov, Vladimir; Usanov, Sergey; Arseniev, Alexander; Efremov, Roman; Bocharov, Eduard. "Diversity of Structural, Dynamic, and Environmental Effects Explain a Distinctive Functional Role of Transmembrane Domains in the Insulin Receptor Subfamily" Int. J. Mol. Sci. 24, 3906-3906 (2023).
PubMed: 36835322

Assembly members:

Assembly members:
entity_1, polymer, 31 residues, 3243.968 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGLHVLLTATPVGLTLLIVL AALGFFYGKKR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	135
15N chemical shifts	30
1H chemical shifts	230

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 31 residues - 3243.968 Da.

1

GLY

LEU

HIS

VAL

LEU

THR

ALA

THR

2

PRO

VAL

GLY

LEU

THR

LEU

ILE

VAL

LEU

3

ALA

LEU

GLY

PHE

TYR

GLY

LYS

4

ARG

Samples:

sample_1: IRRtm, [U-100% 13C; U-100% 15N], 0.5 mM; DPC, [U-99% 2H], 100 mM; Sodium azide 0.3 mM; KH2PO4 30 mM; K2HPO4 20 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.7; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C CT HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

TopSpin, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - processing

NMR spectrometers:

Bruker AVANCE 600 MHz
Bruker AVANCE III 800 MHz

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