BMRB Entry 34073

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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/BMR34073
MolProbity Validation Chart

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Title:
Trypanosoma brucei Pex14 N-terminal domain
Deposition date:
2016-12-09
Original release date:
2017-03-01
Authors:
Emmanouilidis, L.; Tripsianes, K.; Sattler, M.
Citation:

Citation: Dawidowski, D.; Emmanouilidis, L.; Kalel, V.; Tripsianes, K.; Schorpp, K.; Hadian, K.; Kaiser, M.; Maeser, P.; Kolonko, M.; Tanghe, S.; Rodriguez, A.; Schliebs, W.; Erdmann, R.; Sattler, M.; Popowicz, G.. "Inhibitors of PEX14 disrupt protein import into glycosomes and kill Trypanosoma parasites"  Science 355, 1416-1420 (2017).
PubMed: 28360328

Assembly members:

Assembly members:
entity_1, polymer, 70 residues, 8021.192 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KPEVEHTHSEREKRVSNAVE FLLDSRVRRTPTSSKVHFLK SKGLSAEEICEAFTKVGQPK TLNEIKRILS

Data sets:
Data typeCount
13C chemical shifts245
15N chemical shifts68
1H chemical shifts500

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 70 residues - 8021.192 Da.

1   LYSPROGLUVALGLUHISTHRHISSERGLU
2   ARGGLULYSARGVALSERASNALAVALGLU
3   PHELEULEUASPSERARGVALARGARGTHR
4   PROTHRSERSERLYSVALHISPHELEULYS
5   SERLYSGLYLEUSERALAGLUGLUILECYS
6   GLUALAPHETHRLYSVALGLYGLNPROLYS
7   THRLEUASNGLUILELYSARGILELEUSER

Samples:

sample_1: Pex14, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 20 mM; NaCl 50 mM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 500 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