BMRB Entry 15685

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15685

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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 side chain 1H, 13C, and 15N Chemical Shift Assignments for the complex of Epidermal Growth Factor-like 2 domain from Microneme Protein 6 (Toxoplasma gondii) with the Galectin-like domain of Microneme protein 1

Deposition date:

2008-03-17

Original release date:

2008-10-03

Authors:

Sawmynaden, Kovilen; Saouros, Savvas; Marchant, Jan; Simpson, Peter; Matthews, Stephen

Citation:

Citation: Sawmynaden, Kovilen; Saouros, Savvas; Marchant, Jan; Simpson, Peter; Matthews, Stephen. "Complete NMR assignments for the second EGF domain of MIC6 from Toxoplasma gondii and re-assignment in complex with the galectin-like domain of MIC1" Biomol. NMR Assignments 2, 187-189 (2008).
PubMed: 19636901

Assembly members:

Assembly members:
Epidermal_Growth_Factor-like_domain_2, polymer, 61 residues, 6362.06 Da.
Microneme_Protein_6, polymer, 138 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Toxoplasma gondii Taxonomy ID: 5811 Superkingdom: Eukaryota Kingdom: not available Genus/species: Toxoplasma gondii

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-32 Xa/LIC

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Epidermal_Growth_Factor-like_domain_2: MANFVQLSETPAACSSNPCG PEAAGTCKETNSGYICRCNQ GYRISLDGTGNVTCIVRQES G
Microneme_Protein_6: MKTEIHGDSTKATLEEGQQL TLTFISTKLDVAVGSCHSLV ANFLDGFLKFQTGSNSAFDV VEVEEPAGPAVLTIGLGHKG RLAVVLDYTRLNAALGSAAY VVEDSGCSSSEEVSFQGVGS GATLVVTTLGESPTAVSA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	764
15N chemical shifts	180
1H chemical shifts	1169

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Epidermal Growth Factor-like domain 2	1
2	Galectin-like domain (MIC1)	2

Entities:

Entity 1, Epidermal Growth Factor-like domain 2 61 residues - 6362.06 Da.

1

MET

ALA

ASN

PHE

VAL

GLN

LEU

SER

GLU

THR

2

PRO

ALA

CYS

SER

ASN

PRO

CYS

GLY

3

PRO

GLU

ALA

GLY

THR

CYS

LYS

GLU

THR

4

ASN

SER

GLY

TYR

ILE

CYS

ARG

CYS

ASN

GLN

5

GLY

TYR

ARG

ILE

SER

LEU

ASP

GLY

THR

GLY

6

ASN

VAL

THR

CYS

ILE

VAL

ARG

GLN

GLU

SER

7

GLY

Entity 2, Galectin-like domain (MIC1) 138 residues - Formula weight is not available

1

MET

LYS

THR

GLU

ILE

HIS

GLY

ASP

SER

THR

2

LYS

ALA

THR

LEU

GLU

GLY

GLN

LEU

3

THR

LEU

THR

PHE

ILE

SER

THR

LYS

LEU

ASP

4

VAL

ALA

VAL

GLY

SER

CYS

HIS

SER

LEU

VAL

5

ALA

ASN

PHE

LEU

ASP

GLY

PHE

LEU

LYS

PHE

6

GLN

THR

GLY

SER

ASN

SER

ALA

PHE

ASP

VAL

7

VAL

GLU

VAL

GLU

PRO

ALA

GLY

PRO

ALA

8

VAL

LEU

THR

ILE

GLY

LEU

GLY

HIS

LYS

GLY

9

ARG

LEU

ALA

VAL

LEU

ASP

TYR

THR

ARG

10

LEU

ASN

ALA

LEU

GLY

SER

ALA

TYR

11

VAL

GLU

ASP

SER

GLY

CYS

SER

12

GLU

VAL

SER

PHE

GLN

GLY

VAL

GLY

SER

13

GLY

ALA

THR

LEU

VAL

THR

LEU

GLY

14

GLU

SER

PRO

THR

ALA

VAL

SER

ALA

Samples:

sample_1: Epidermal Growth Factor-like domain 2 0.5 mM; Galectin-like domain (MIC1) 0.5 mM; potassium phosphate 25 mM; sodium chloride 50 mM

sample_2: Epidermal Growth Factor-like domain 2, [U-100% 13C; U-100% 15N], 1-1.3 mM; Galectin-like domain (MIC1) 0.5 mM; potassium phosphate 25 mM; sodium chloride 50 mM

sample_conditions_1: pH: 6.8; temperature: 308 K

sample_conditions_2: ionic strength: 0.1 M; pH: 6.9; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HN(CO)CA	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 800 MHz
Bruker DRX 500 MHz

BMRB	15682 15692 6376
PDB	2K2S 2K2T 2BVB 2K2S
EMBL	CAA96466
GB	EPR59679 EPT28103 ESS33997 KFG30856 KFG41657
REF	XP_002368531
SP	O00834
AlphaFold	O00834