BMRB Entry 34202

Name: PH domain from PfAPH
Published: 2018-12-04

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PDB ID: 6f24
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34202
MolProbity Validation Chart

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

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Title: PH domain from PfAPH

Deposition date: 2017-11-23 Original release date: 2018-12-04

Authors: Darvill, N.; Liu, B.; Matthews, S.; Soldati-Favre, D.; Rouse, S.; Benjamin, S.; Blake, T.; Dubois, D.; Hammoudi, P.; Pino, P.

Citation: Darvill, N.; Matthews, S.; Liu, B.; Soldati-Favre, D.; Rouse, S.; Benjamin, S.; Blake, T.; Dubois, D.; Hammoudi, P.; Pino, P.. "C-terminal PH domain from P. falciparum acylated plekstrin homology domain containing protein (APH)" .

Assembly members:
entity_1, polymer, 119 residues, 13905.197 Da.

Natural source: Common Name: Plasmodium falciparum Taxonomy ID: 1036725 Superkingdom: Eukaryota Kingdom: not available Genus/species: Plasmodium falciparum

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

Entity Sequences (FASTA):
entity_1: SAKDIKDEKIQQYRKTLTKI VKIKTAIFHETVKVTCSKDG KMLEWYKGKNDSDGKKKPIG SFPLNKITSIRTKVDNLKSL EISVSSVHISTYLFTFKTRE ERESWQNNLESFRKIMSMK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	557
15N chemical shifts	122
1H chemical shifts	885

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 119 residues - 13905.197 Da.

1

SER

ALA

LYS

ASP

ILE

LYS

ASP

GLU

LYS

ILE

2

GLN

TYR

ARG

LYS

THR

LEU

THR

LYS

ILE

3

VAL

LYS

ILE

LYS

THR

ALA

ILE

PHE

HIS

GLU

4

THR

VAL

LYS

VAL

THR

CYS

SER

LYS

ASP

GLY

5

LYS

MET

LEU

GLU

TRP

TYR

LYS

GLY

LYS

ASN

6

ASP

SER

ASP

GLY

LYS

PRO

ILE

GLY

7

SER

PHE

PRO

LEU

ASN

LYS

ILE

THR

SER

ILE

8

ARG

THR

LYS

VAL

ASP

ASN

LEU

LYS

SER

LEU

9

GLU

ILE

SER

VAL

SER

VAL

HIS

ILE

SER

10

THR

TYR

LEU

PHE

THR

PHE

LYS

THR

ARG

GLU

11

GLU

ARG

GLU

SER

TRP

GLN

ASN

LEU

GLU

12

SER

PHE

ARG

LYS

ILE

MET

SER

MET

LYS

Samples:

sample_1: C-terminal PH domain from PfAPH, [U-100% 15N; U-100% 13C], 830 uM; NaCl 300 mM

sample_conditions_1: ionic strength: 300 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

ARIA, Linge, O'Donoghue and Nilges - structure calculation

NMRView, Brunger A. T. et.al., Johnson, One Moon Scientific - chemical shift assignment, peak picking, refinement

NMR spectrometers:

Bruker AvanceIII 600 MHz
Bruker DRX 800 MHz

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