BMRB Entry 26599

Name: 1H, 13Ca, 13Cb and 15N chemical shift assignment of coiled-coil motif from human Thanatos-associated protein 11
Published: 2016-05-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26599

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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:

1H, 13Ca, 13Cb and 15N chemical shift assignment of coiled-coil motif from human Thanatos-associated protein 11

Deposition date:

2015-07-06

Original release date:

2016-05-09

Authors:

Cukier, Cyprian; Milon, Alain; Gervais, Virginie

Citation:

Citation: Cukier, Cyprian; Gervais, Virginie. "The C-terminal region of the transcriptional regulator THAP11 forms a parallel coiled-coil domain involved in protein dimerization" J. Struct. Biol. 194, 337-346 (2016).
PubMed: 26975212

Assembly members:

Assembly members:
THAP11, polymer, 68 residues, 8038 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: pETM-20

Entity Sequences (FASTA):

Entity Sequences (FASTA):
THAP11: GAMGTTEEELLRKLNEQRDI LALMEVKMKEMKGSIRHLRL TEAKLREELREKDRLLAMAV IRKKHGMY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	130
15N chemical shifts	66
1H chemical shifts	66

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	THAP11 coiled-coil, chain A	1
2	THAP11 coiled-coil, chain B	1

Entities:

Entity 1, THAP11 coiled-coil, chain A 68 residues - 8038 Da.

N-terminal GAM residues are the result of clonic procedure. The C-terminal Y residue was introduced to facilitate protein quantification. This is a coiled-coil motif of THAP11 protein.

1

GLY

ALA

MET

GLY

THR

GLU

LEU

2

LEU

ARG

LYS

LEU

ASN

GLU

GLN

ARG

ASP

ILE

3

LEU

ALA

LEU

MET

GLU

VAL

LYS

MET

LYS

GLU

4

MET

LYS

GLY

SER

ILE

ARG

HIS

LEU

ARG

LEU

5

THR

GLU

ALA

LYS

LEU

ARG

GLU

LEU

ARG

6

GLU

LYS

ASP

ARG

LEU

ALA

MET

ALA

VAL

7

ILE

ARG

LYS

HIS

GLY

MET

TYR

Samples:

sample_1: THAP11, [U-15N], 0.28 – 0.46 mM; sodium/potassium phosphate 10 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_2: THAP11, [U-13C; U-15N], 0.3 – 0.5 mM; sodium/potassium phosphate 10 mM; sodium chloride 50 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 600 MHz

UNP	Q96EK4
AlphaFold	O94795