BMRB Entry 17616

Name: Backbone Resonance assignment of 1H, 13C, 15N for P2 of plasmodium falciparum in 9M urea.
Published: 2012-05-09

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17616

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone Resonance assignment of 1H, 13C, 15N for P2 of plasmodium falciparum in 9M urea.

Deposition date:

2011-05-02

Original release date:

2012-05-09

Authors:

Mishra, Pushpa

Citation:

Citation: Mishra, Pushpa; Das, Sudipta; Panicker, Lata; Hosur, Madhusoodan; Sharma, Shobhona; Hosur, Ramakrishna. "NMR Insights into Folding and Self-Association of Plasmodium falciparum P2." PLoS ONE 7, .-. (2012).
PubMed: 22567147

Assembly members:

Assembly members:
plasmodium_falciparum_p2, polymer, 142 residues, 15664.3 Da.

Natural source:

Natural source: Common Name: Malaria Parasite Taxonomy ID: 5833 Superkingdom: Eukaryota Kingdom: not available Genus/species: Plasmodium Falciparum

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
plasmodium_falciparum_p2: MSYYHHHHHHDYDIPTTENL YFQGAMDPEFMAMKYVAAYL MCVLGGNENPSTKEVKNVLG AVNADVEDEVLNNFIDSLKG KSCHELITDGLKKLQNIGGG VAAAPAGAAAVETAEAKKED KKEEKKEEEEEEEDDLGFSL FG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	342
15N chemical shifts	124
1H chemical shifts	546

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	P2	1

Entities:

Entity 1, P2 142 residues - 15664.3 Da.

Residues 1-30 represent sequence coming from vector. 31 onwards P2 protein sequence starts.

1

MET

SER

TYR

HIS

2

ASP

TYR

ASP

ILE

PRO

THR

GLU

ASN

LEU

3

TYR

PHE

GLN

GLY

ALA

MET

ASP

PRO

GLU

PHE

4

MET

ALA

MET

LYS

TYR

VAL

ALA

TYR

LEU

5

MET

CYS

VAL

LEU

GLY

ASN

GLU

ASN

PRO

6

SER

THR

LYS

GLU

VAL

LYS

ASN

VAL

LEU

GLY

7

ALA

VAL

ASN

ALA

ASP

VAL

GLU

ASP

GLU

VAL

8

LEU

ASN

PHE

ILE

ASP

SER

LEU

LYS

GLY

9

LYS

SER

CYS

HIS

GLU

LEU

ILE

THR

ASP

GLY

10

LEU

LYS

LEU

GLN

ASN

ILE

GLY

11

VAL

ALA

PRO

ALA

GLY

ALA

12

VAL

GLU

THR

ALA

GLU

ALA

LYS

GLU

ASP

13

LYS

GLU

LYS

GLU

14

GLU

ASP

LEU

GLY

PHE

SER

LEU

15

PHE

GLY

Samples:

sample_1: plasmodium falciparum p2, [U-99% 15N], 1 mM; H2O 90%; D2O 10%; Urea 9 M; MES Buffer 0.1 M; NaCl 150 mM; DTT 5 mM

sample_2: plasmodium falciparum p2, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%; D2O 10%; Urea 9 M; MES Buffer 0.1 M; NaCl 150 mM; DTT 5 mM

sample_conditions_1: pH: 5.6; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D HNN	sample_2	isotropic	sample_conditions_1
3D HN(C)N	sample_2	isotropic	sample_conditions_1
3D HNCAN	sample_2	isotropic	sample_conditions_1
3D HSQC-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.0, Bruker Biospin - collection

CARA v1.9.1, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

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

NMR spectrometers:

Bruker Avance 800 MHz

EMBL	CAB11115 CDO62522
GB	AAB51131 AAF15361 ETW20710 ETW38756 ETW45178
REF	XP_001351169 XP_012761169
SP	O00806
AlphaFold	O00806