BMRB Entry 30513

Name: TCR alpha transmembrane domain
Published: 2018-12-04

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PDB ID: 6mf8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30513
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:

TCR alpha transmembrane domain

Deposition date:

2018-09-10

Original release date:

2018-12-04

Authors:

Brazin, K.; Reinherz, E.

Citation:

Citation: Brazin, K.; Mallis, R.; Boeszoermenyi, A.; Feng, Y.; Yoshizawa, A.; Reche, P.; Kaur, P.; Bi, K.; Hussey, R.; Duke-Cohan, J.; Song, L.; Wagner, G.; Arthanari, H.; Lang, M.; Reinherz, E.. "The T Cell Antigen Receptor alpha Transmembrane Domain Coordinates Triggering through Regulation of Bilayer Immersion and CD3 Subunit Associations." Immunity 49, 829-841 (2018).
PubMed: 30389415

Assembly members:

Assembly members:
entity_1, polymer, 46 residues, 5250.164 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DATLTEKSFETDMNLNFQNL SVMGLRILLLKVAGFNLLMT LRLWSS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	151
15N chemical shifts	45
1H chemical shifts	181

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 46 residues - 5250.164 Da.

1

ASP

ALA

THR

LEU

THR

GLU

LYS

SER

PHE

GLU

2

THR

ASP

MET

ASN

LEU

ASN

PHE

GLN

ASN

LEU

3

SER

VAL

MET

GLY

LEU

ARG

ILE

LEU

4

LYS

VAL

ALA

GLY

PHE

ASN

LEU

MET

THR

5

LEU

ARG

LEU

TRP

SER

Samples:

sample_1: TCRa_NOE, [U-15N; U-2H; Ile, Leu, Val selective labeling], 2 mM; Tris 30 mM; 16:0 Lyso PG 100 mM

sample_2: TCRa_backbone, [U-99% 13C; U-99% 15N], 1 mM; Tris 30 mM; 16:0 Lyso PG 100 mM

sample_3: TCRa_HSQC, [U-99% 15N], 0.5 mM; Tris 30 mM; 16:0 Lyso PG 100 mM

sample_conditions_1: ionic strength: 30 mM; pH: 7.0; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 750 MHz
Varian INOVA 600 MHz

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