BMRB Entry 53287

Name: Chemical shift assignments for the C2 domain of a Trichomonas vaginalis C2-XYPPX-repeat family protein.
Published: 2025-08-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53287

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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:

Chemical shift assignments for the C2 domain of a Trichomonas vaginalis C2-XYPPX-repeat family protein.

Deposition date:

2025-07-18

Original release date:

2025-08-19

Authors:

Buchko, Garry

Citation:

Citation: Buchko, Garry; Liu, Lijun; Battaile, Keven; Craig, Justin; Harmon, Elizabeth; Van Voorhis, Wesley; Myler, Peter; Lovell, Scott. "The C2 domain of one of the Trichomonas vaginalis C2-XYPPX-repeat family proteins is structured and functional" .

Assembly members:

Assembly members:
entity_1, polymer, 138 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Trichomonas vaginalis Taxonomy ID: 5722 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trichomonas vaginalis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: BG1861

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAHHHHHHMTLTFNIKVIEA KDLPKVDTFGKVDPYVQIQL GNEKCKTKVIKKSYNPVWNE TFSIPVTNPKAPLNITVVDY DFIGSNDAFAYIHFNQQEFN VGQVVDKWYMLNSYKAGRSA GQIHLVIHLATQNMKPFE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	517
15N chemical shifts	142
1H chemical shifts	765

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	T83	1

Entities:

Entity 1, T83 138 residues - Formula weight is not available

1

MET

ALA

HIS

MET

THR

2

LEU

THR

PHE

ASN

ILE

LYS

VAL

ILE

GLU

ALA

3

LYS

ASP

LEU

PRO

LYS

VAL

ASP

THR

PHE

GLY

4

LYS

VAL

ASP

PRO

TYR

VAL

GLN

ILE

GLN

LEU

5

GLY

ASN

GLU

LYS

CYS

LYS

THR

LYS

VAL

ILE

6

LYS

SER

TYR

ASN

PRO

VAL

TRP

ASN

GLU

7

THR

PHE

SER

ILE

PRO

VAL

THR

ASN

PRO

LYS

8

ALA

PRO

LEU

ASN

ILE

THR

VAL

ASP

TYR

9

ASP

PHE

ILE

GLY

SER

ASN

ASP

ALA

PHE

ALA

10

TYR

ILE

HIS

PHE

ASN

GLN

GLU

PHE

ASN

11

VAL

GLY

GLN

VAL

ASP

LYS

TRP

TYR

MET

12

LEU

ASN

SER

TYR

LYS

ALA

GLY

ARG

SER

ALA

13

GLY

GLN

ILE

HIS

LEU

VAL

ILE

HIS

LEU

ALA

14

THR

GLN

ASN

MET

LYS

PRO

PHE

GLU

Samples:

sample_1: T83, [U-99% 13C; U-99% 15N], 0.8 ± 0.2 mM; sodium chloride 100 ± 1 mM; TRIS 20 ± 0.2 mM; DTT 1 ± 0.1 mM

sample_conditions_1: ionic strength: 120 mM; pH: 7; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

Poky - data analysis

NMRPipe - processing

NMR spectrometers:

Bruker Ascend 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks