BMRB Entry 19193

Name: NMR solution structure of N-terminal domain of (Y81F)-EhCaBP1
Published: 2013-10-17

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PDB ID: 2m7k
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19193
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR solution structure of N-terminal domain of (Y81F)-EhCaBP1

Deposition date:

2013-04-25

Original release date:

2013-10-17

Authors:

Chary, Kandala; Rout, Ashok; Patel, Sunita; Bhattacharya, Alok

Citation:

Citation: Chary, Kandala; Rout, Ashok; Patel, Sunita; Bhattacharya, Alok. "Functional manipulation of a calcium binding protein from E. histolytica guided by paramagnetic NMR" J. Biol. Chem. ., .-..
PubMed: 23782698

Assembly members:

Assembly members:
(Y81F)-EhCaBP1, polymer, 66 residues, 14742.640 Da.

Natural source:

Natural source: Common Name: Eukaryotes 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: pET30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
(Y81F)-EhCaBP1: MAEALFKEIDVNGDGAVSYE EVKAFVSKKRAIKNEQLLQL IFKSIDADGNGEIDQNEFAK FYGSIQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	248
15N chemical shifts	60
1H chemical shifts	323

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	(Y81F)-EhCaBP1	1

Entities:

Entity 1, (Y81F)-EhCaBP1 66 residues - 14742.640 Da.

1

MET

ALA

GLU

ALA

LEU

PHE

LYS

GLU

ILE

ASP

2

VAL

ASN

GLY

ASP

GLY

ALA

VAL

SER

TYR

GLU

3

GLU

VAL

LYS

ALA

PHE

VAL

SER

LYS

ARG

4

ALA

ILE

LYS

ASN

GLU

GLN

LEU

GLN

LEU

5

ILE

PHE

LYS

SER

ILE

ASP

ALA

ASP

GLY

ASN

6

GLY

GLU

ILE

ASP

GLN

ASN

GLU

PHE

ALA

LYS

7

PHE

TYR

GLY

SER

ILE

GLN

Samples:

sample_1: (Y81F)-EhCaBP1, [U-99% 15N], 0.8 ± 0.1 mM; H2O 90%; D2O 10%

sample_2: (Y81F)-EhCaBP1, [U-99% 13C; U-99% 15N], 0.8 ± 0.1 mM; H2O 90%; D2O 10%

sample_3: (Y81F)-EhCaBP1, [U-99% 13C; U-99% 15N], 0.8 ± 0.1 mM; D2O 100%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.4; 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_3	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1

Software:

FELIX, Accelrys Software Inc. - processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - collection, processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

Bruker Avance 800 MHz