BMRB Entry 35015

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR35015
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
tbPEX38(65-134) in complex with tbPEX19(1-50)
Deposition date:
2025-08-22
Original release date:
2026-06-25
Authors:
Gaussmann, S.
Citation:

Citation: Krishna, C.; Gaussmann, S.; Das, H.; Jung, M.; Oeljeklaus, S.; Sattler, M.; Warscheid, B.; Kalel, V.; Erdmann, R.. "PEX38 is a novel essential peroxisomal membrane protein import co-receptor of kinetoplastids. "  .

Assembly members:

Assembly members:
entity_1, polymer, 54 residues, 5983.396 Da.
entity_2, polymer, 70 residues, 8086.023 Da.

Natural source:

Natural source:   Common Name: Trypanosoma brucei brucei   Taxonomy ID: 5702   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma brucei

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSHPDNDADLDALLDDCLNT MDEQERIHEEKAQERAATRA VDQKSATAELSGGY
entity_2: TGVAVLPAFQQALNEMKKSV SIQQDDKFNAFLDLLRKKGY FAGAEEGSEEYNSRLEKARE KFEKRNNPYE

Data sets:
Data typeCount
13C chemical shifts407
15N chemical shifts135
1H chemical shifts848

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 54 residues - 5983.396 Da.

1   METSERHISPROASPASNASPALAASPLEU
2   ASPALALEULEUASPASPCYSLEUASNTHR
3   METASPGLUGLNGLUARGILEHISGLUGLU
4   LYSALAGLNGLUARGALAALATHRARGALA
5   VALASPGLNLYSSERALATHRALAGLULEU
6   SERGLYGLYTYR

Entity 2, unit_2 70 residues - 8086.023 Da.

1   THRGLYVALALAVALLEUPROALAPHEGLN
2   GLNALALEUASNGLUMETLYSLYSSERVAL
3   SERILEGLNGLNASPASPLYSPHEASNALA
4   PHELEUASPLEULEUARGLYSLYSGLYTYR
5   PHEALAGLYALAGLUGLUGLYSERGLUGLU
6   TYRASNSERARGLEUGLULYSALAARGGLU
7   LYSPHEGLULYSARGASNASNPROTYRGLU

Samples:

sample_1: tbPEX19, [U-100% 15N], 400 uM; tbPEX38 1000 uM; sodium phosphate 20 mM; sodium chloride 100 mM; dithiothreitol 1 mM

sample_2: tbPEX19, [U-100% 13C; U-100% 15N], 400 uM; tbPEX38 1000 mM; sodium phosphate 20 mM; sodium chloride 100 mM; dithiothreitol 1 mM

sample_3: tbPEX19 800 uM; tbPEX38, [U-100% 15N], 300 uM; sodium phosphate 20 mM; sodium chloride 100 mM; dithiothreitol 1 mM

sample_4: tbPEX19 800 uM; tbPEX38, [U-100% 13C; U-100% 15N], 300 uM; sodium phosphate 20 mM; sodium chloride 100 mM; dithiothreitol 1 mM

sample_5: tbPEX19, [U-100% 13C; U-100% 15N], 400 uM; tbPEX38 1000 mM; sodium phosphate 20 mM; sodium chloride 100 mM; dithiothreitol 1 mM

sample_6: tbPEX19 800 uM; tbPEX38, [U-100% 13C; U-100% 15N], 300 uM; sodium phosphate 20 mM; sodium chloride 100 mM; dithiothreitol 1 mM

sample_conditions_1: ionic strength: 0.22 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_5isotropicsample_conditions_1
3D HNCOsample_5isotropicsample_conditions_1
3D H(CCO)NHsample_5isotropicsample_conditions_1
3D HNCACBsample_5isotropicsample_conditions_1
2D 1H-13C HSQCsample_5isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_4isotropicsample_conditions_1
3D HCACOsample_6isotropicsample_conditions_1
3D HNCOsample_6isotropicsample_conditions_1
3D H(CCO)NHsample_6isotropicsample_conditions_1
3D HNCACBsample_6isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_6isotropicsample_conditions_1
2D 1H-15N HSQCsample_6isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_5isotropicsample_conditions_1
3D HCACOsample_5isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_6isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1

Software:

TopSpin v3.6, Bruker Biospin - collection

CcpNmr Analysis v2.4.2, Vranken, Boucher et al. 2005 - chemical shift assignment, peak picking

CYANA v3.98.15, Guntert, Mumenthaler and Wuthrich - structure calculation

Amber v20, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker AVANCE III HD 900 MHz
  • Bruker AVANCE III HD 950 MHz
  • Bruker AVANCE NEO 1200 MHz

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