BMRB Entry 30810

Name: Structure of the integrin aIIb(W968V)b3 transmembrane complex
Published: 2021-09-08

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PDB ID: 7kn0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30810
MolProbity Validation Chart

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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:

Structure of the integrin aIIb(W968V)b3 transmembrane complex

Deposition date:

2020-11-03

Original release date:

2021-09-08

Authors:

Situ, A.; Kim, J.; An, W.; Kim, C.; Ulmer, T.

Citation:

Citation: Situ, A.; Kim, J.; An, W.; Kim, C.; Ulmer, T.. "Insight Into Pathological Integrin aIIbb3 Activation From Safeguarding The Inactive State" J. Mol. Biol. 433, 166832-166832 (2021).
PubMed: 33539882

Assembly members:

Assembly members:
entity_1, polymer, 43 residues, 4753.871 Da.
entity_2, polymer, 44 residues, 4775.867 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GALEERCGIPIWVVLVGVLG GLLLLTILVLAMWKVGFFKR NRP
entity_2: GESPKCGPDILVVLLSVMGA ILLIGLAALLIWKLLITIHD RKEF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	140
15N chemical shifts	72
1H chemical shifts	104

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2

Entities:

Entity 1, unit_1 43 residues - 4753.871 Da.

1

GLY

ALA

LEU

GLU

ARG

CYS

GLY

ILE

PRO

2

ILE

TRP

VAL

LEU

VAL

GLY

VAL

LEU

GLY

3

GLY

LEU

THR

ILE

LEU

VAL

LEU

4

ALA

MET

TRP

LYS

VAL

GLY

PHE

LYS

ARG

5

ASN

ARG

PRO

Entity 2, unit_2 44 residues - 4775.867 Da.

1

GLY

GLU

SER

PRO

LYS

CYS

GLY

PRO

ASP

ILE

2

LEU

VAL

LEU

SER

VAL

MET

GLY

ALA

3

ILE

LEU

ILE

GLY

LEU

ALA

LEU

4

ILE

TRP

LYS

LEU

ILE

THR

ILE

HIS

ASP

5

ARG

LYS

GLU

PHE

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N; U-80% 2H], 0.8 mM; entity_2, [U-100% 13C; U-100% 15N; U-80% 2H], 0.8 mM

sample_conditions_1: ionic strength: 25 mM; pH: 7.4; pressure: 1 atm; temperature: 313.2 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

Bruker AVANCE 700 MHz

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