BMRB Entry 19233

Name: 1H, 13C, 15N assignments for P. yoelii Merozoite Surface Protein 1
Published: 2015-09-02

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PDB ID: 2mgp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19233
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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:

1H, 13C, 15N assignments for P. yoelii Merozoite Surface Protein 1

Deposition date:

2013-05-08

Original release date:

2015-09-02

Authors:

Curd, Rachel; Birdsall, Berry; Kadekoppala, Madhusudan; Ogun, Solabomi; Kelly, Geoff; Holder, Anthony

Citation:

Citation: Curd, Rachel; Birdsall, Berry; Kadekoppala, Madhusudan; Ogun, Solabomi; Kelly, Geoff; Holder, Anthony. "The structure of Plasmodium yoelii merozoite surface protein 119, antibody specificity and implications for malaria vaccine design" Open Biol. 4, 130091-130091 (2014).
PubMed: 24403012

Assembly members:

Assembly members:
MSP1, polymer, 99 residues, Formula weight is not available

Natural source:

Natural source: Common Name: apicomplexans Taxonomy ID: 5861 Superkingdom: Eukaryota Kingdom: not available Genus/species: Plasmodium Yoelii

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Pichia pastoris Vector: pPICK9K

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MSP1: GVDPKHVCVDTRDIPKNAGC FRDDDGTEEWRCLLGYKKGE GNTCVENNNPTCDINNGGCD PTASCQNAESTENSKKIICT CKEPTPNAYYEGVFCSSSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	382
15N chemical shifts	108
1H chemical shifts	618

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MSP1	1

Entities:

Entity 1, MSP1 99 residues - Formula weight is not available

1

GLY

VAL

ASP

PRO

LYS

HIS

VAL

CYS

VAL

ASP

2

THR

ARG

ASP

ILE

PRO

LYS

ASN

ALA

GLY

CYS

3

PHE

ARG

ASP

GLY

THR

GLU

TRP

4

ARG

CYS

LEU

GLY

TYR

LYS

GLY

GLU

5

GLY

ASN

THR

CYS

VAL

GLU

ASN

PRO

6

THR

CYS

ASP

ILE

ASN

GLY

CYS

ASP

7

PRO

THR

ALA

SER

CYS

GLN

ASN

ALA

GLU

SER

8

THR

GLU

ASN

SER

LYS

ILE

CYS

THR

9

CYS

LYS

GLU

PRO

THR

PRO

ASN

ALA

TYR

10

GLU

GLY

VAL

PHE

CYS

SER

Samples:

sample_1: MSP1, [U-99% 13C; U-99% 15N], 1.0 mM; potassium chloride 50.0 mM; potassium phosphate 25.0 mM; H2O 95%; D2O 5%

sample_conditions_1: pH*: 6.5; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 600 MHz
Bruker Avance 700 MHz
Bruker Avance 600 MHz

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