BMRB Entry 18210

Name: Structure of the Plasmodium 6-cysteine s48/45 Domain
Published: 2012-05-08

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PDB ID: 2loe
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18210
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Structure of the Plasmodium 6-cysteine s48/45 Domain PubMed: 22493233

Deposition date: 2012-01-23 Original release date: 2012-05-08

Authors: Cai, Mengli; Arredondo, Silvia A.; Clore, Marius; Miller, Louis; Takayama, Yuki; Macdonald, Nicholas; Enderson, Eric; Aravind, L.

Citation: Arredondo, Silvia; Cai, Mengli; Takayama, Yuki; Macdonald, Nicholas; Anderson, D. Eric; Aravind, L.; Clore, G. Marius; Miller, Louis. "Structure of the Plasmodium 6-cysteine s48/45 domain." Proc. Natl. Acad. Sci. U.S.A. 109, 6692-6697 (2012).

Assembly members:
entity, polymer, 128 residues, 14553.378 Da.

Natural source: Common Name: Malaria parasite 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):
entity: EKVKGCDFTTSESTIFSKGY SINEISNKSSNNQQDIVCTV KAHANDLIGFKCPSNYSVEP HDCFVSAFNLSGKNENLENK LKLTNIIMDHYNNTFYSRLP SLISDNWKFFCVCSKDNEKK LVFTVEAX

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	573
15N chemical shifts	96
1H chemical shifts	791

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	pf12 C terminal domain	1

Entities:

Entity 1, pf12 C terminal domain 128 residues - 14553.378 Da.

1

GLU

LYS

VAL

LYS

GLY

CYS

ASP

PHE

THR

2

SER

GLU

SER

THR

ILE

PHE

SER

LYS

GLY

TYR

3

SER

ILE

ASN

GLU

ILE

SER

ASN

LYS

SER

4

ASN

GLN

ASP

ILE

VAL

CYS

THR

VAL

5

LYS

ALA

HIS

ALA

ASN

ASP

LEU

ILE

GLY

PHE

6

LYS

CYS

PRO

SER

ASN

TYR

SER

VAL

GLU

PRO

7

HIS

ASP

CYS

PHE

VAL

SER

ALA

PHE

ASN

LEU

8

SER

GLY

LYS

ASN

GLU

ASN

LEU

GLU

ASN

LYS

9

LEU

LYS

LEU

THR

ASN

ILE

MET

ASP

HIS

10

TYR

ASN

THR

PHE

TYR

SER

ARG

LEU

PRO

11

SER

LEU

ILE

SER

ASP

ASN

TRP

LYS

PHE

12

CYS

VAL

CYS

SER

LYS

ASP

ASN

GLU

LYS

13

LEU

VAL

PHE

THR

VAL

GLU

ALA

ANI

Samples:

sample_1: Pf1 phage, [U-99% 13C; U-99% 15N], 0.4 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0 M; pH: 5.0; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1

Software:

PIPP, Garrett - chemical shift assignment

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

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz
Bruker Avance 900 MHz

PDB	2LOE 2YMO
EMBL	CAG25366
GB	AAA29649 AAF59950 ACR09927 ACR09928 ACR09929
REF	XP_966114
SP	C6KSX0 P19259

Biological Magnetic Resonance Data Bank