BMRB Entry 15002

Name: Solution structure of the THAP domain from C. elegans C-terminal binding protein (CtBP)
Published: 2015-04-23

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15002

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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 the THAP domain from C. elegans C-terminal binding protein (CtBP)

Deposition date:

2006-09-21

Original release date:

2015-04-23

Authors:

Liew, Chu Kong; Crossley, Merlin; Mackay, Joel; Nicholas, Hannah

Citation:

Citation: Liew, Chu Kong; Crossley, Merlin; Mackay, Joel; Nicholas, Hannah. "Solution structure of the THAP domain from Caenorhabditis elegans C-terminal binding protein (CtBP)" J. Mol. Biol. 366, 382-390 (2007).
PubMed: 17174978

Assembly members:

Assembly members:
CtBP THAP domain, polymer, 91 residues, 10536.343 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: C. elegans Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-2T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CtBP THAP domain: GSMPTTCGFPNCKFRSRYRG LEDNRHFYRIPKRPLILRQR WLTAIGRTEETVVSQLRICS AHFEGGEKKEGDIPVPDPTV DKQIKIELPPK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
coupling_constants
- coupling_constant_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	412
15N chemical shifts	95
1H chemical shifts	641
coupling constants	28

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Polypeptide chain	1
2	ZINC (II) ION	2

Entities:

Entity 1, Polypeptide chain 91 residues - 10536.343 Da.

Residues 1 and 2 are non-native residues left over following thrombin cleavage

1

GLY

SER

MET

PRO

THR

CYS

GLY

PHE

PRO

2

ASN

CYS

LYS

PHE

ARG

SER

ARG

TYR

ARG

GLY

3

LEU

GLU

ASP

ASN

ARG

HIS

PHE

TYR

ARG

ILE

4

PRO

LYS

ARG

PRO

LEU

ILE

LEU

ARG

GLN

ARG

5

TRP

LEU

THR

ALA

ILE

GLY

ARG

THR

GLU

6

THR

VAL

SER

GLN

LEU

ARG

ILE

CYS

SER

7

ALA

HIS

PHE

GLU

GLY

GLU

LYS

GLU

8

GLY

ASP

ILE

PRO

VAL

PRO

ASP

PRO

THR

VAL

9

ASP

LYS

GLN

ILE

LYS

ILE

GLU

LEU

PRO

10

LYS

Entity 2, ZINC (II) ION - Zn - 65.409 Da.

1

ZN

Name	Sample	Sample state	Sample conditions
3D HNCO	15N_13C_labelled_sample	isotropic	condition_H2O
3D HNCA	15N_13C_labelled_sample	isotropic	condition_H2O
3D HNCACB	15N_13C_labelled_sample	isotropic	condition_H2O
3D HN(CO)CA	15N_13C_labelled_sample	isotropic	condition_H2O
3D CBCACONH	15N_13C_labelled_sample	isotropic	condition_H2O
3D HCCH-TOCSY	D2O_sample	isotropic	condition_D2O
3D HCCH-COSY	D2O_sample	isotropic	condition_D2O
3D 1H-15N NOESY	15N_sample	isotropic	condition_H2O
3D 1H-13C NOESY	D2O_sample	isotropic	condition_D2O
2D NOESY	Unlabelled_sample	isotropic	condition_H2O
C(CO)NH-TOCSY	15N_13C_labelled_sample	isotropic	condition_H2O
H(CCO)NH-TOCSY	15N_13C_labelled_sample	isotropic	condition_H2O
3D HNHA	15N_sample	isotropic	condition_H2O
3D HN(CA)CO	15N_13C_labelled_sample	isotropic	condition_H2O

UNP	Q20595
AlphaFold	Q20596

BMRB Entry 15002

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: