BMRB Entry 25920

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

Click here to enlarge.

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
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
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 the Integrin alphaIIb-beta3(A711P) Transmembrane Complex PubMed: 27436065

Deposition date: 2015-12-14 Original release date: 2016-07-28

Authors: Schmidt, Thomas; Situ, Alan; Ulmer, Tobias

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

Assembly members:
entity_1, polymer, 42 residues, 4783.942 Da.
entity_2, polymer, 43 residues, 4744.895 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

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

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
Hide all

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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts