BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 34202

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:
Data typeCount
13C chemical shifts557
15N chemical shifts122
1H chemical shifts885

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 119 residues - 13905.197 Da.

1   SERALALYSASPILELYSASPGLULYSILE
2   GLNGLNTYRARGLYSTHRLEUTHRLYSILE
3   VALLYSILELYSTHRALAILEPHEHISGLU
4   THRVALLYSVALTHRCYSSERLYSASPGLY
5   LYSMETLEUGLUTRPTYRLYSGLYLYSASN
6   ASPSERASPGLYLYSLYSLYSPROILEGLY
7   SERPHEPROLEUASNLYSILETHRSERILE
8   ARGTHRLYSVALASPASNLEULYSSERLEU
9   GLUILESERVALSERSERVALHISILESER
10   THRTYRLEUPHETHRPHELYSTHRARGGLU
11   GLUARGGLUSERTRPGLNASNASNLEUGLU
12   SERPHEARGLYSILEMETSERMETLYS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts