BMRB Entry 26760

Name: 1H, 13C and 15N NMR assignments of an unusual Ca2+-binding protein from Entamoeba histolytica in its apo form
Published: 2017-03-02

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26760

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: 1H, 13C and 15N NMR assignments of an unusual Ca2+-binding protein from Entamoeba histolytica in its apo form PubMed: 27990612

Deposition date: 2016-03-18 Original release date: 2017-03-02

Authors: Verma, Deepshikha; Chary, Kandala

Citation: Verma, Deepshikha; Sakuntala, Mutyala; Murmu, Aruna; Bhattacharya, Alok; Chary, Kandala. "(1)H, (13)C and (15)N NMR assignments of an unusual Ca(2+)-binding protein from Entamoeba histolytica in its apo form." Biomol. NMR Assign. 11, 63-67 (2017).

Assembly members:
apo-EhCaBP6, polymer, 156 residues, Formula weight is not available

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET21C

Entity Sequences (FASTA):
apo-EhCaBP6: MSMEIEAPNANTQKIRDCFN FYDRDYDGKIDVKQLGTLIR SLGCAPTEDEVNSYIKEFAI EGETFQIEQFELIMEREQSK PDTREIKLRKAFEVFDQDKD GKIKASDLAHNLTTVGDKMT KEEVEKVFSILGITMESDID LATFLKLVALHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	345
15N chemical shifts	123
1H chemical shifts	763

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	apo-EhCaBP6	1

Entities:

Entity 1, apo-EhCaBP6 156 residues - Formula weight is not available

1

MET

SER

MET

GLU

ILE

GLU

ALA

PRO

ASN

ALA

2

ASN

THR

GLN

LYS

ILE

ARG

ASP

CYS

PHE

ASN

3

PHE

TYR

ASP

ARG

ASP

TYR

ASP

GLY

LYS

ILE

4

ASP

VAL

LYS

GLN

LEU

GLY

THR

LEU

ILE

ARG

5

SER

LEU

GLY

CYS

ALA

PRO

THR

GLU

ASP

GLU

6

VAL

ASN

SER

TYR

ILE

LYS

GLU

PHE

ALA

ILE

7

GLU

GLY

GLU

THR

PHE

GLN

ILE

GLU

GLN

PHE

8

GLU

LEU

ILE

MET

GLU

ARG

GLU

GLN

SER

LYS

9

PRO

ASP

THR

ARG

GLU

ILE

LYS

LEU

ARG

LYS

10

ALA

PHE

GLU

VAL

PHE

ASP

GLN

ASP

LYS

ASP

11

GLY

LYS

ILE

LYS

ALA

SER

ASP

LEU

ALA

HIS

12

ASN

LEU

THR

VAL

GLY

ASP

LYS

MET

THR

13

LYS

GLU

VAL

GLU

LYS

VAL

PHE

SER

ILE

14

LEU

GLY

ILE

THR

MET

GLU

SER

ASP

ILE

ASP

15

LEU

ALA

THR

PHE

LEU

LYS

LEU

VAL

ALA

LEU

16

HIS

Samples:

sample_1: apo-EhCaBP6, [U-100% 13C; U-100% 15N], 1 mM; TRIS 50 mM; sodium chloride 50 mM; beta-mercaptoethanol 5 mM

sample_2: apo-EhCaBP6, [U-100% 13C; U-100% 15N], 1 mM; TRIS 50 mM; sodium chloride 50 mM; beta-mercaptoethanol 5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 298 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
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 800 MHz

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