BMRB Entry 15162

Name: Backbone Chemical Shift Assignments of Cholera Toxin Enzymatic Domain (1-167)
Published: 2007-06-20

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15162

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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:

Backbone Chemical Shift Assignments of Cholera Toxin Enzymatic Domain (1-167)

Deposition date:

2007-03-06

Original release date:

2007-06-20

Authors:

Ampapathi, Ravi; Lou, In Hye; Creath, Andrea; Blanke, Steven; Legge, Glen

Citation:

Citation: Ampapathi, Ravi; Creath, Andrea; Lou, Dianne; Craft, John; Blanke, Steven; Legge, Glen. "Order-disorder-order transitions mediate the activation of cholera toxin" J. Mol. Biol. 377, 748-60 (2008).
PubMed: 18272180

Assembly members:

Assembly members:
CTA1-T2, polymer, 167 residues, 18891.8 Da.

Natural source:

Natural source: Common Name: Vibrio comma Taxonomy ID: 666 Superkingdom: Bacteria Kingdom: not available Genus/species: Vibrio cholerae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-20(b)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CTA1-T2: NDDKLYRADSRPPDEIKQSG GLMPRGQSDYFDRGTQMNIN LYDHARGTQTGFVRHDDGYV STSISLRSAHLVGQTILSGH STYYIYVIATAPNMFNVNDV LGAYSPHPDEQDVSALGGIP YSQIVGWYRVHFGVLDEQLH RNRGYRDRYYSNLDIAPAAD GYGLAGF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	390
15N chemical shifts	131
1H chemical shifts	131

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CTA1-T2	1

Entities:

Entity 1, CTA1-T2 167 residues - 18891.8 Da.

This is a truncated version(1-167) of Full length CTA1 (1-192), which increases the stability of the construct in solution.

1

ASN

ASP

LYS

LEU

TYR

ARG

ALA

ASP

SER

2

ARG

PRO

ASP

GLU

ILE

LYS

GLN

SER

GLY

3

GLY

LEU

MET

PRO

ARG

GLY

GLN

SER

ASP

TYR

4

PHE

ASP

ARG

GLY

THR

GLN

MET

ASN

ILE

ASN

5

LEU

TYR

ASP

HIS

ALA

ARG

GLY

THR

GLN

THR

6

GLY

PHE

VAL

ARG

HIS

ASP

GLY

TYR

VAL

7

SER

THR

SER

ILE

SER

LEU

ARG

SER

ALA

HIS

8

LEU

VAL

GLY

GLN

THR

ILE

LEU

SER

GLY

HIS

9

SER

THR

TYR

ILE

TYR

VAL

ILE

ALA

THR

10

ALA

PRO

ASN

MET

PHE

ASN

VAL

ASN

ASP

VAL

11

LEU

GLY

ALA

TYR

SER

PRO

HIS

PRO

ASP

GLU

12

GLN

ASP

VAL

SER

ALA

LEU

GLY

ILE

PRO

13

TYR

SER

GLN

ILE

VAL

GLY

TRP

TYR

ARG

VAL

14

HIS

PHE

GLY

VAL

LEU

ASP

GLU

GLN

LEU

HIS

15

ARG

ASN

ARG

GLY

TYR

ARG

ASP

ARG

TYR

16

SER

ASN

LEU

ASP

ILE

ALA

PRO

ALA

ASP

17

GLY

TYR

GLY

LEU

ALA

GLY

PHE

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	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

GB	VC1457 AAA27514 AAD51359 AAF94614 AAL09681 AAL60525
SWS	301555
PDB	1S5B 1S5C 1S5D 1S5E 1S5F 1XTC 2A5D 2A5F 2A5G
DBJ	BAA06288 BAA06290 BAG06738 BAG66065 BAI50777
EMBL	CAA24995 CAA41590 CAA41592 CAE11218 CRZ40571
PRF	1001196A
REF	NP_231100 WP_001881225 WP_001888508 WP_001911232 WP_005514365
SP	P01555
AlphaFold	P01555

BMRB Entry 15162

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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