BMRB Entry 25931

Name: Transmembrane Structure of the Cytokine Receptor Common Subunit beta
Published: 2016-07-05

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PDB ID: 2na8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25931
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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:

Transmembrane Structure of the Cytokine Receptor Common Subunit beta

Deposition date:

2015-12-21

Original release date:

2016-07-05

Authors:

Schmidt, Thomas; Ye, Feng; Situ, Alan; An, Woojin; Ginsberg, Mark; Ulmer, Tobias

Citation:

Citation: Schmidt, Thomas; Ye, Feng; Situ, Alan; An, Woojin; Ginsberg, Mark; Ulmer, Tobias. "A Conserved Ectodomain-Transmembrane Domain Linker Motif Tunes the Allosteric Regulation of Cell Surface Receptors" J. Biol. Chem. 291, 17536-17546 (2016).
PubMed: 27365391

Assembly members:

Assembly members:
entity, polymer, 44 residues, 5146.327 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-bc

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GKRSWDTESVLPMWVLALIV IFLTIAVLLALRFCGIYGYR LRRK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	119
15N chemical shifts	42
1H chemical shifts	43

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 44 residues - 5146.327 Da.

1

GLY

LYS

ARG

SER

TRP

ASP

THR

GLU

SER

VAL

2

LEU

PRO

MET

TRP

VAL

LEU

ALA

LEU

ILE

VAL

3

ILE

PHE

LEU

THR

ILE

ALA

VAL

LEU

ALA

4

LEU

ARG

PHE

CYS

GLY

ILE

TYR

GLY

TYR

ARG

5

LEU

ARG

LYS

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N; 80% 2H], 0.5 mM; H20 93%; D20 6%; 1,2-dihexanoyl-sn-glycero-3-phosphocholine (DHPC) 350 mM; 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) 105 mM; tris(2-carboxyethyl)phosphine 10 mM; HEPES NaOH 25 mM; NaN3 0.02%

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

Experiments:

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