BMRB Entry 18377

Name: MTIP(61-204) from Plasmodium falciparum bound to peptide MyoA(799-818)
Published: 2012-04-16

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18377

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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: MTIP(61-204) from Plasmodium falciparum bound to peptide MyoA(799-818) PubMed: 22932904

Deposition date: 2012-04-03 Original release date: 2012-04-16

Authors: Douse, Christopher

Citation: Douse, Christopher; Green, Judith; Salgado, Paula; Simpson, Peter; Thomas, Jemima; Langsley, Gordon; Holder, Anthony; Tate, Edward; Cota, Ernesto. "Regulation of the Plasmodium motor complex: phosphorylation of myosin A tail-interacting protein (MTIP) loosens its grip on MyoA." J. Biol. Chem. 287, 36968-36977 (2012).

Assembly members:
MTIP(61-204), polymer, 154 residues, 17605 Da.
MyoA(799-818)_peptide, polymer, 20 residues, 2372.91 Da.

Natural source: Common Name: malaria parasite P. falciparum Taxonomy ID: 5833 Superkingdom: Eukaryota Kingdom: not available Genus/species: Plasmodium falciparum

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

Entity Sequences (FASTA):
MTIP(61-204): RGSHHHHHHGSVADIQQLEE KVDESDVRIYFNEKSSGGKI SIDNASYNARKLGLAPSSID EKKIKELYGDNLTYEQYLEY LSICVHDKDNVEELIKMFAH FDNNCTGYLTKSQMKNILTT WGDALTDQEAIDALNAFSSE DNIDYKLFCEDILQ
MyoA(799-818)_peptide: KNIPSLLRVQAHIRKKMVAQ

Data sets:

assigned_chemical_shifts
- assignments_nv_sequence

Data type	Count
13C chemical shifts	423
15N chemical shifts	142
1H chemical shifts	142

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MTIP(61-204)	1
2	MyoA(799-818)	2

Entities:

Entity 1, MTIP(61-204) 154 residues - 17605 Da.

1

ARG

GLY

SER

HIS

GLY

2

SER

VAL

ALA

ASP

ILE

GLN

LEU

GLU

3

LYS

VAL

ASP

GLU

SER

ASP

VAL

ARG

ILE

TYR

4

PHE

ASN

GLU

LYS

SER

GLY

LYS

ILE

5

SER

ILE

ASP

ASN

ALA

SER

TYR

ASN

ALA

ARG

6

LYS

LEU

GLY

LEU

ALA

PRO

SER

ILE

ASP

7

GLU

LYS

ILE

LYS

GLU

LEU

TYR

GLY

ASP

8

ASN

LEU

THR

TYR

GLU

GLN

TYR

LEU

GLU

TYR

9

LEU

SER

ILE

CYS

VAL

HIS

ASP

LYS

ASP

ASN

10

VAL

GLU

LEU

ILE

LYS

MET

PHE

ALA

HIS

11

PHE

ASP

ASN

CYS

THR

GLY

TYR

LEU

THR

12

LYS

SER

GLN

MET

LYS

ASN

ILE

LEU

THR

13

TRP

GLY

ASP

ALA

LEU

THR

ASP

GLN

GLU

ALA

14

ILE

ASP

ALA

LEU

ASN

ALA

PHE

SER

GLU

15

ASP

ASN

ILE

ASP

TYR

LYS

LEU

PHE

CYS

GLU

16

ASP

ILE

LEU

GLN

Entity 2, MyoA(799-818) 20 residues - 2372.91 Da.

1		LYS	ASN	ILE	PRO	SER	LEU	LEU	ARG	VAL	GLN
2		ALA	HIS	ILE	ARG	LYS	LYS	MET	VAL	ALA	GLN

Samples:

sample_1: MTIP(61-204), [U-98% 13C; U-98% 15N], 0.5 mM; MOPS buffer 20 mM; sodium chloride 50 mM; TCEP 1 mM; sodium azide 0.005%; D2O 10%; MyoA(799-818) peptide 1.5 mM; H2O 90%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

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

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

BMRB	18376
PDB	2QAC 4AOM 4MZJ 4MZK 4MZL 4R1E
EMBL	CDO65736
GB	AAN36529 ETW17315 ETW29792 ETW35145 ETW41309
REF	XP_001350849 XP_012764323

Biological Magnetic Resonance Data Bank