BMRB Entry 34030

Title:
Solution NMR structure of farnesylated PEX19, C-terminal domain
Deposition date:
2016-08-04
Original release date:
2017-03-08
Authors:
Emmanouilidis, L.; Schuetz, U.; Tripsianes, K.; Madl, T.; Radke, J.; Rucktaeschel, R.; Wilmanns, M.; Schliebs, W.; Erdmann, R.; Sattler, M.
Citation:

Citation: Emmanouilidis, Leonidas; Schutz, Ulrike; Tripsianes, Konstantinos; Madl, Tobias; Radke, Juliane; Rucktaschel, Robert; Wilmanns, Matthias; Schliebs, Wolfgang; Erdmann, Ralf; Sattler, Michael. "Allosteric modulation of peroxisomal membrane protein recognition by farnesylation of the peroxisomal import receptor PEX19."  Nat. Commun. 8, 14635-14635 (2017).
PubMed: 28281558

Assembly members:

Assembly members:
entity_1, polymer, 139 residues, 15664.643 Da.
entity_FAR, non-polymer, 206.367 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts486
15N chemical shifts145
1H chemical shifts1019

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 139 residues - 15664.643 Da.

1   GLYMETASPGLUGLYASPGLYGLUGLYASN
2   ILELEUPROILEMETGLNSERILEMETGLN
3   ASNLEULEUSERLYSASPVALLEUTYRPRO
4   SERLEULYSGLUILETHRGLULYSTYRPRO
5   GLUTRPLEUGLNSERHISARGGLUSERLEU
6   PROPROGLUGLNPHEGLULYSTYRGLNGLU
7   GLNHISSERVALMETCYSLYSILECYSGLU
8   GLNPHEGLUALAGLUTHRPROTHRASPSER
9   GLUTHRTHRGLNLYSALAARGPHEGLUMET
10   VALLEUASPLEUMETGLNGLNLEUGLNASP
11   LEUGLYHISPROPROLYSGLULEUALAGLY
12   GLUMETPROPROGLYLEUASNPHEASPLEU
13   ASPALALEUASNLEUSERGLYPROPROGLY
14   ALASERGLYGLUGLNCYSLEUILEMET

Entity 2, entity_2 - C15 H26 - 206.367 Da.

1   FAR

Samples:

sample_1: PEX19, [U-1H; U-13C; U-15N], 1 mM; farnesyl, [U-1H; U-12C], 1 mM

sample_2: PEX19, [U-2H; U-12C; U-15N]; Leu-[1H,13C,15N], 1 mM; farnesyl, [U-1H; U-12C], 1 mM

sample_3: PEX19, [U-2H; U-12C; U-15N]; Lle-[1H,13C,15N], 1 mM; farnesyl, [U-1H; U-12C], 1 mM

sample_4: PEX19, [U-2H; U-12C; U-15N]; Met-[1H,13CH3,15N], 1 mM; farnesyl, [U-1H; U-12C], 1 mM

sample_5: PEX19, [U-2H; U-12C; U-15N]; Ile(delta1),Leu(delta),Val(gamma)-[13CH3], 1 mM; farnesyl, [U-1H; U-12C], 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CNS, BRUNGER A. T. ET.AL. - refinement

NMR spectrometers:

  • Bruker AvanceIII 750 MHz
  • Bruker Avance 900 MHz

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