BMRB Entry 25920

Name: Structure of the Integrin alphaIIb-beta3(A711P) Transmembrane Complex
Published: 2016-07-28

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PDB ID: 2n9y
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25920
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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 alphaIIb-beta3(A711P) Transmembrane Complex

Deposition date:

2015-12-14

Original release date:

2016-07-28

Authors:

Schmidt, Thomas; Situ, Alan; Ulmer, Tobias

Citation:

Citation: Schmidt, Thomas; Situ, Alan; Ulmer, Tobias. "Structural and thermodynamic basis of proline-induced transmembrane complex stabilization" Sci. Rep. 6, 29809-29809 (2016).
PubMed: 27436065

Assembly members:

Assembly members:
entity_1, polymer, 42 residues, 4783.942 Da.
entity_2, polymer, 43 residues, 4744.895 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 Vector: pET44-GB3-aIIb

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GALEERCIPIWWVLVGVLGG LLLLTILVLAMWKVGFFKRN RP
entity_2: GESPKCPDILVVLLSVMGAI LLIGLAPLLIWKLLITIHDR KEF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	219
15N chemical shifts	76
1H chemical shifts	134

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 42 residues - 4783.942 Da.

1

GLY

ALA

LEU

GLU

ARG

CYS

ILE

PRO

ILE

2

TRP

VAL

LEU

VAL

GLY

VAL

LEU

GLY

3

LEU

THR

ILE

LEU

VAL

LEU

ALA

4

MET

TRP

LYS

VAL

GLY

PHE

LYS

ARG

ASN

5

ARG

PRO

Entity 2, entity_2 43 residues - 4744.895 Da.

1

GLY

GLU

SER

PRO

LYS

CYS

PRO

ASP

ILE

LEU

2

VAL

LEU

SER

VAL

MET

GLY

ALA

ILE

3

LEU

ILE

GLY

LEU

ALA

PRO

LEU

ILE

4

TRP

LYS

LEU

ILE

THR

ILE

HIS

ASP

ARG

5

LYS

GLU

PHE

Samples:

sample_1: entity_1, [U-15N; U-2H], 0.8 mM; entity_2 0.8 mM; DHPC 350 mM; DMPC 105 mM; NaH2PO4/Na2HPO4 25 mM; NaN3 0.02 % w/v

sample_2: entity_1 0.8 mM; entity_2, [U-15N; U-2H], 0.8 mM; DHPC 350 mM; DMPC 105 mM; NaH2PO4/Na2HPO4 25 mM; NaN3 0.02 % w/v

sample_3: entity_1, [U-99% 13C; U-99% 15N; 80% 2H], 0.8 mM; entity_2, [U-99% 13C; U-99% 15N; 80% 2H], 0.8 mM; DHPC 350 mM; DMPC 105 mM; NaH2PO4/Na2HPO4 25 mM; NaN3 0.02 % w/v

sample_conditions_1: ionic strength: 0.05 M; pH: 7.4; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	anisotropic	sample_conditions_1

Software:

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

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