BMRB Entry 27400

Name: Assignment of 1H, 13C and 15N resonances of the extrecclular domain of human Death Receptor DR5
Published: 2018-06-20

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27400

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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:

Assignment of 1H, 13C and 15N resonances of the extrecclular domain of human Death Receptor DR5

Deposition date:

2018-02-09

Original release date:

2018-06-20

Authors:

Odaert, Benoit; Baudin, Antoine; Berbon, Melanie; Mackereth, Cameron; Guichard, Gilles

Citation:

Citation: Baudin, Antoine; Guichard, Anne; Collie, Gavin; Rousseau, Sabrina; Chaignepain, Stephane; Hocquellet, Agnes; Berbon, Melanie; Loquet, Antoine; Mackereth, Cameron; Guichard, Gilles; Odaert, Benoit. "1H, 13C, 15N NMR resonance assignments and secondary structure determination of the extra-cellular domain from the human proapoptotic TRAIL-R2 death receptor 5 (DR5-ECD)" Biomol. NMR Assignments 12, 309-314 (2018).
PubMed: 29869749

Assembly members:

Assembly members:
DR5, polymer, 135 residues, 14998 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: pETNus_1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DR5: GAMESALITQQDLAPQQRAA PQQKRSSPSEGLCPPGHHIS EDGRDCISCKYGQDYSTHWN DLLFCLRCTRCDSGEVELSP CTTTRNTVCQCEEGTFREED SPEMCRKCRTGCPRGMVKVG DCTPWSDIECVHKES

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	447
15N chemical shifts	114
1H chemical shifts	653

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DR5 monomer	1

Entities:

Entity 1, DR5 monomer 135 residues - 14998 Da.

Residus 1-4 represent a non-native cleavage site for the TeV protease

1

GLY

ALA

MET

GLU

SER

ALA

LEU

ILE

THR

GLN

2

GLN

ASP

LEU

ALA

PRO

GLN

ARG

ALA

3

PRO

GLN

LYS

ARG

SER

PRO

SER

GLU

4

GLY

LEU

CYS

PRO

GLY

HIS

ILE

SER

5

GLU

ASP

GLY

ARG

ASP

CYS

ILE

SER

CYS

LYS

6

TYR

GLY

GLN

ASP

TYR

SER

THR

HIS

TRP

ASN

7

ASP

LEU

PHE

CYS

LEU

ARG

CYS

THR

ARG

8

CYS

ASP

SER

GLY

GLU

VAL

GLU

LEU

SER

PRO

9

CYS

THR

ARG

ASN

THR

VAL

CYS

GLN

10

CYS

GLU

GLY

THR

PHE

ARG

GLU

ASP

11

SER

PRO

GLU

MET

CYS

ARG

LYS

CYS

ARG

THR

12

GLY

CYS

PRO

ARG

GLY

MET

VAL

LYS

VAL

GLY

13

ASP

CYS

THR

PRO

TRP

SER

ASP

ILE

GLU

CYS

14

VAL

HIS

LYS

GLU

SER

Samples:

sample_1: DR5, [U-13C; U-15N], 300 uM; Na2HPO4 20 mM; NaCl 50 mM

sample_2: DR5, [U-15N], 90 uM; Na2HPO4 20 mM; NaCl 50 mM

sample_3: DR5, [U-13C; U-15N], 300 uM; Na2HPO4 20 mM; NaCl 50 mM

sample_4: DR5 300 uM; Na2HPO4 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 70 mM; pH: 6.3; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_4	isotropic	sample_conditions_1
2D DQF-COSY	sample_4	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_4	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
2D CBHD	sample_3	isotropic	sample_conditions_1
2D CBHE	sample_3	isotropic	sample_conditions_1
3D HCCH-COSY	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 700 MHz