BMRB Entry 34216

Name: PH domain from TgAPH
Published: 2019-01-28

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PDB ID: 6f8e
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34216
MolProbity Validation Chart

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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:

PH domain from TgAPH

Deposition date:

2017-12-13

Original release date:

2019-01-28

Authors:

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

Citation:

Citation: Darvill, N.; Dubois, D.; Rouse, S.; Hammoudi, P.; Blake, T.; Benjamin, S.; Liu, B.; Soldati-Favre, D.; Matthews, S.. "Structural Basis of Phosphatidic Acid Sensing by APH in Apicomplexan Parasites." Structure 26, 1059-1071 (2018).
PubMed: 29910186

Assembly members:

Assembly members:
entity_1, polymer, 121 residues, 13759.891 Da.

Natural source:

Natural source: Common Name: Toxoplasma gondii Taxonomy ID: 508771 Superkingdom: Eukaryota Kingdom: not available Genus/species: Toxoplasma gondii

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SASDIRMKKVMQYRRALTKV VKLKTHLFSETVKVTCSKDG EEVQWFKGKSTAGAQDRKKP SGGFPVDKITSVKSQADNTK VLVITVNNPQPTTYNFTFKS PGERESWQEQIQSLMKFMSM K

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	538
15N chemical shifts	126
1H chemical shifts	846

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_1 121 residues - 13759.891 Da.

1

SER

ALA

SER

ASP

ILE

ARG

MET

LYS

VAL

2

MET

GLN

TYR

ARG

ALA

LEU

THR

LYS

VAL

3

VAL

LYS

LEU

LYS

THR

HIS

LEU

PHE

SER

GLU

4

THR

VAL

LYS

VAL

THR

CYS

SER

LYS

ASP

GLY

5

GLU

VAL

GLN

TRP

PHE

LYS

GLY

LYS

SER

6

THR

ALA

GLY

ALA

GLN

ASP

ARG

LYS

PRO

7

SER

GLY

PHE

PRO

VAL

ASP

LYS

ILE

THR

8

SER

VAL

LYS

SER

GLN

ALA

ASP

ASN

THR

LYS

9

VAL

LEU

VAL

ILE

THR

VAL

ASN

PRO

GLN

10

PRO

THR

TYR

ASN

PHE

THR

PHE

LYS

SER

11

PRO

GLY

GLU

ARG

GLU

SER

TRP

GLN

GLU

GLN

12

ILE

GLN

SER

LEU

MET

LYS

PHE

MET

SER

MET

13

LYS

Samples:

sample_1: C-terminal PH domain from TgAPH, [U-100% 15N]; [U-100% 13C], 730 uM; NaCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7; 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 H(CCO)NH	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

Software:

CNS, Brunger A. T. et.al. - refinement

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

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

NMR spectrometers:

Bruker DRX 800 MHz

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