BMRB Entry 51258

Name: Backbone and sidechain assignments of Actophorin protein from Entamoeba histolytica
Published: 2022-01-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51258

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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 and sidechain assignments of Actophorin protein from Entamoeba histolytica

Deposition date:

2022-01-05

Original release date:

2022-01-14

Authors:

Aggarwal, Priyanka; Kumar, Nitesh; Samudrala, Gourinath; Bhavesh, Neel

Citation:

Citation: Kumar, Nitesh; Rath, Pragyan Parimita; Aggarwal, Priyanka; Maiti, Sankar; Bhavesh, Neel Sarovar; Gourinath, Samudrala. "Unravelling the Biology of EhActo as the First Cofilin From Entamoeba histolytica" Front. Cell Dev. Biol. 10, 785680-785680 (2022).
PubMed: 35281106

Assembly members:

Assembly members:
entity_1, polymer, 146 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Entamoeba histolytica Taxonomy ID: 5759 Superkingdom: Eukaryota Kingdom: not available Genus/species: Entamoeba histolytica

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAMAGIQLADEVTSVYNDFK LSHKYRYIVFKMNDGMTEVV VEKTAEKNATYDDFLKDLPE KSARYAVYDLEYDTPEGLRQ KIIFYLWTPEGCKIREKMLY SATKATIKQALVGLSAEIQA TDAGELNLDEVIAKVKTILE HHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	534
15N chemical shifts	130
1H chemical shifts	130

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Actophorin	1

Entities:

Entity 1, Actophorin 146 residues - Formula weight is not available

1

MET

ALA

MET

ALA

GLY

ILE

GLN

LEU

ALA

ASP

2

GLU

VAL

THR

SER

VAL

TYR

ASN

ASP

PHE

LYS

3

LEU

SER

HIS

LYS

TYR

ARG

TYR

ILE

VAL

PHE

4

LYS

MET

ASN

ASP

GLY

MET

THR

GLU

VAL

5

VAL

GLU

LYS

THR

ALA

GLU

LYS

ASN

ALA

THR

6

TYR

ASP

PHE

LEU

LYS

ASP

LEU

PRO

GLU

7

LYS

SER

ALA

ARG

TYR

ALA

VAL

TYR

ASP

LEU

8

GLU

TYR

ASP

THR

PRO

GLU

GLY

LEU

ARG

GLN

9

LYS

ILE

PHE

TYR

LEU

TRP

THR

PRO

GLU

10

GLY

CYS

LYS

ILE

ARG

GLU

LYS

MET

LEU

TYR

11

SER

ALA

THR

LYS

ALA

THR

ILE

LYS

GLN

ALA

12

LEU

VAL

GLY

LEU

SER

ALA

GLU

ILE

GLN

ALA

13

THR

ASP

ALA

GLY

GLU

LEU

ASN

LEU

ASP

GLU

14

VAL

ILE

ALA

LYS

VAL

LYS

THR

ILE

LEU

GLU

15

HIS

Samples:

sample_1: Actophorin, [U-99% 13C; U-99% 15N], 1 ± 0.01 mM; sodium phosphate 10 mM; potassium phosphate 1.8 mM; NaCl 60 mM; KCl 2.7 mM

sample_conditions_1: ionic strength: 60 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.5pl6 - collection, processing

CARA - chemical shift assignment, data analysis

CS-Rosetta - structure solution

NMR spectrometers:

Bruker AVANCE III 500.15 MHz

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