BMRB Entry 34693

Title:
Solution structure of the complex between plasmodial ZNHIT3 and NUFIP1 proteins
Deposition date:
2021-11-30
Original release date:
2022-03-28
Authors:
Chagot, M.; Quinternet, M.
Citation:

Citation: Chagot, M.; Boutilliat, A.; Kriznik, A.; Quinternet, M.. "Structural Analysis of the Plasmodial Proteins ZNHIT3 and NUFIP1 Provides Insights into the Selectivity of a Conserved Interaction"  Biochemistry 61, 479-493 (2022).
PubMed: 35315277

Assembly members:

Assembly members:
entity_1, polymer, 72 residues, 8578.843 Da.
entity_2, polymer, 25 residues, 3107.529 Da.

Natural source:

Natural source:   Common Name: Plasmodium falciparum   Taxonomy ID: 36329   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Plasmodium falciparum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts469
15N chemical shifts102
1H chemical shifts739

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 72 residues - 8578.843 Da.

1   GLYPROHISMETASPTYRASPMETLEUTHR
2   GLUGLUGLNLYSLYSLYSLEULYSGLUASP
3   HISTHRLEULYSILELEULEULYSASNASN
4   TYRVALARGGLUVALPHELYSGLNPHETHR
5   LEUSERASNASPLYSILEGLYTYRLEUSER
6   HISTYRILEASNASPPROTHRILEVALGLN
7   VALILEASPHISILEMETLYSTHRILEASP
8   ASPTHR

Entity 2, unit_2 25 residues - 3107.529 Da.

1   ASPILETYRTHRTYRGLULYSLYSLEUILE
2   LYSSERILEGLUTYRILETHRLYSASNLYS
3   PHEPHEASPASPSER

Samples:

sample_1: pfZNHIT3, [U-100% 13C; U-100% 15N], 0.7 mM; pfNUFIP1, [U-100% 13C; U-100% 15N], 0.7 mM; sodium chloride 150 mM; sodium phosphate 10 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCO ECosysample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

TopSpin v3.6.2, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

TALOS-N, Yang Shen, and Ad Bax - structure calculation

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

Amber v14, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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