BMRB Entry 36084

Name: Solution structure of C-terminal domain of TRADD
Published: 2017-06-26

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PDB ID: 5xme
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36084
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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:

Solution structure of C-terminal domain of TRADD

Deposition date:

2017-05-15

Original release date:

2017-06-26

Authors:

Lin, Z.; Zhang, N.

Citation:

Citation: Zhang, Ning; Yuan, Wensu; Fan, Jing-Song; Lin, Zhi. "Structure of the C-terminal domain of TRADD reveals a novel fold in the death domain superfamily" Sci. Rep. 7, 7073-7073 (2017).
PubMed: 28765645

Assembly members:

Assembly members:
entity_1, polymer, 127 residues, 14429.224 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHHHHHHSSGRGSAQTFLFQ GQPVVNRPLSLKDQQTFARS VGLKWRKVGRSLQRGCRALR DPALDSLAYEYEREGLYEQA FQLLRRFVQAEGRRATLQRL VEALEENELTSLAEDLLGLT DPNGGLA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	384
15N chemical shifts	126
1H chemical shifts	810

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_1 127 residues - 14429.224 Da.

1

MET

HIS

SER

GLY

2

ARG

GLY

SER

ALA

GLN

THR

PHE

LEU

PHE

GLN

3

GLY

GLN

PRO

VAL

ASN

ARG

PRO

LEU

SER

4

LEU

LYS

ASP

GLN

THR

PHE

ALA

ARG

SER

5

VAL

GLY

LEU

LYS

TRP

ARG

LYS

VAL

GLY

ARG

6

SER

LEU

GLN

ARG

GLY

CYS

ARG

ALA

LEU

ARG

7

ASP

PRO

ALA

LEU

ASP

SER

LEU

ALA

TYR

GLU

8

TYR

GLU

ARG

GLU

GLY

LEU

TYR

GLU

GLN

ALA

9

PHE

GLN

LEU

ARG

PHE

VAL

GLN

ALA

10

GLU

GLY

ARG

ALA

THR

LEU

GLN

ARG

LEU

11

VAL

GLU

ALA

LEU

GLU

ASN

GLU

LEU

THR

12

SER

LEU

ALA

GLU

ASP

LEU

GLY

LEU

THR

13

ASP

PRO

ASN

GLY

LEU

ALA

Samples:

sample_1: TRADD DD, [U-99% 13C; U-99% 15N; U-98% 2H], 0.6 mM; D10-DTT 10 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: pH: 5.0; pressure: 1 atm; temperature: 301 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
4D 13C, 15N-edited NOESY	sample_1	isotropic	sample_conditions_1

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRView, Johnson, One Moon Scientific - data analysis

NMRpipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

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