BMRB Entry 26623

Name: Backbone 1H, 13C, and 15N chemical shift assignments for integrin beta3 transmembrane and cytoplasmic tail domains
Published: 2017-03-03

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26623

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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 for integrin beta3 transmembrane and cytoplasmic tail domains

Deposition date:

2015-08-02

Original release date:

2017-03-03

Authors:

Lu, Zhenwei

Citation:

Citation: Lu, Zhenwei; Mathew, Sijo; Chen, Jiang; Hadziselimovic, Arina; Palamuttam, Riya; Hudson, Billy; Fassler, Reinhard; Pozzi, Ambra; Sanders, Charles; Zent, Roy. "Implications of the differing roles of the beta1 and beta3 transmembrane and cytoplasmic domains for integrin function" Elife 5, e18633-e18633 (2016).
PubMed: 27929375

Assembly members:

Assembly members:
integrin_beta3_TM-CT, polymer, 85 residues, 9651.1 Da.

Natural source:

Natural source: Common Name: enterobacteria Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
integrin_beta3_TM-CT: HHHHHHGPESPKGPDILVVL LSVMGAILLIGLAALLIWKL LITIHDRKEFAKFEEERARA KWDTANNPLYKEATSTFTNI TYRGT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	183
15N chemical shifts	70
1H chemical shifts	71

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	integrin beta3 TM/CT	1

Entities:

Entity 1, integrin beta3 TM/CT 85 residues - 9651.1 Da.

'Residues 1-7 represent a non-native affinity tag This is the membrane and cytoplasmic globular domain of integrin beta3'

1

HIS

GLY

PRO

GLU

SER

2

PRO

LYS

GLY

PRO

ASP

ILE

LEU

VAL

LEU

3

LEU

SER

VAL

MET

GLY

ALA

ILE

LEU

ILE

4

GLY

LEU

ALA

LEU

ILE

TRP

LYS

LEU

5

LEU

ILE

THR

ILE

HIS

ASP

ARG

LYS

GLU

PHE

6

ALA

LYS

PHE

GLU

ARG

ALA

ARG

ALA

7

LYS

TRP

ASP

THR

ALA

ASN

PRO

LEU

TYR

8

LYS

GLU

ALA

THR

SER

THR

PHE

THR

ASN

ILE

9

THR

TYR

ARG

GLY

THR

Samples:

sample_1: integrin beta3 TM/CT, [U-100% 13C; U-100% 15N], 0.3 mM; DHPC 88 mM; DMPC 293 mM; imidazole 250 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.25 M; pH: 6.5; pressure: 1 atm; temperature: 318 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 900 MHz

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