BMRB Entry 25930

Name: Transmembrane domain of human Fas/CD95 death receptor
Published: 2016-01-25

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PDB ID: 2na7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25930
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:

Transmembrane domain of human Fas/CD95 death receptor

Deposition date:

2015-12-21

Original release date:

2016-01-25

Authors:

Fu, Qingshan; Chou, James

Citation:

Citation: Fu, Qingshan; Fu, Tianmin; Cruz, Anthony; Sengupta, Prabuddha; Thomas, Stacy; Wang, Shuqing; Siegel, Richard; Wu, Hao; Chou, James. "Structural Basis and Functional Role of Intramembrane Trimerization of the Fas/CD95 Death Receptor" Mol. Cell 61, 602-613 (2016).
PubMed: 26853147

Assembly members:

Assembly members:
Human_Fas_Transmembrane_Domain, polymer, 28 residues, 3306.097 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: pMM-LR6

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Human_Fas_Transmembrane_Domain: RSNLGWLSLLLLPIPLIVWV KRKEVQKT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	51
15N chemical shifts	24
1H chemical shifts	24

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	1
3	entity_3	1

Entities:

Entity 1, entity_1 28 residues - 3306.097 Da.

1

ARG

SER

ASN

LEU

GLY

TRP

LEU

SER

LEU

2

LEU

PRO

ILE

PRO

LEU

ILE

VAL

TRP

VAL

3

LYS

ARG

LYS

GLU

VAL

GLN

LYS

THR

Samples:

NC-labeled: Human Fas Transmembrane Domain, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; DMPC, [U-100% 2H] acyl chains, 60 ± 1 mM; DHPC, [U-100% 2H] acyl chains, 120 ± 5 mM; sodium phosphate 20 ± 1 mM; H2O 95%; D2O 5%

NCD-labeled: Human Fas Transmembrane Domain, [U-100% 13C; U-100% 15N; U-85% 2H], 1 ± 0.05 mM; DMPC 60 ± 1 mM; DHPC 120 ± 5 mM; sodium phosphate 20 ± 1 mM; H2O 95%; D2O 5%

Mix-labeled: Human Fas Transmembrane Domain, [U-100% 15N; U-100% 2H], 0.5 ± 0.05 mM; Human Fas Transmembrane Domain, [U-15% 13C], 0.5 ± 0.05 mM; DMPC, [U-100% 2H] acyl chains, 60 ± 1 mM; DHPC, [U-100% 2H] acyl chains, 120 ± 5 mM; sodium phosphate 20 ± 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY HSQC	NCD-labeled	isotropic	sample_conditions_1
3D TROSY HNCA	NCD-labeled	isotropic	sample_conditions_1
3D TROSY HN(CA)CO	NCD-labeled	isotropic	sample_conditions_1
3D TROSY HNCO	NCD-labeled	isotropic	sample_conditions_1
3D 15N NOESY TROSY	NC-labeled	isotropic	sample_conditions_1
3D 13C NOESY for methyls	NC-labeled	isotropic	sample_conditions_1
3D 15N NOESY TROSY	Mix-labeled	isotropic	sample_conditions_1
2D 1H-13C HSQC	Mix-labeled	isotropic	sample_conditions_1
2D 1H-15N TROSY HSQC	Mix-labeled	isotropic	sample_conditions_1

Software:

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

XEASY, Bartels et al. - chemical shift assignment, data analysis

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

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

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