BMRB Entry 19523

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19523
MolProbity Validation Chart

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Title:
N-terminal domain of Bilbo1 from Trypanosoma brucei
Deposition date:
2013-09-24
Original release date:
2014-01-02
Authors:
Vidilaseris, Keni; Morriswood, Brooke; Kontaxis, Georg; Dong, Gang
Citation:

Citation: Vidilaseris, Keni; Morriswood, Brooke; Kontaxis, Georg; Dong, Gang. "Structure of the TbBILBO1 protein N-terminal domain from Trypanosoma brucei reveals an essential requirement for a conserved surface patch."  J. Biol. Chem. 289, 3724-3735 (2014).
PubMed: 24362019

Assembly members:

Assembly members:
Bil_NTD, polymer, 110 residues, 12899.675 Da.

Natural source:

Natural source:   Common Name: Trypanosoma brucei   Taxonomy ID: 5691   Superkingdom: Eukaryota   Kingdom: Protista   Genus/species: Trypanosoma brucei

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Bil_NTD: MAFLVQVAADIFNNKVNFEL SFPSRPSISELTRSAETAFS NEISLRRPDNVPSHKFHSSK IKMYDEELNKWVDLIREDQL TDYCQLYVFQPPNEWHKESQ KEIPPAMKPP

Data sets:
Data typeCount
13C chemical shifts409
15N chemical shifts107
1H chemical shifts595

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1N-terminal domain of Bilbo11

Entities:

Entity 1, N-terminal domain of Bilbo1 110 residues - 12899.675 Da.

1   METALAPHELEUVALGLNVALALAALAASP
2   ILEPHEASNASNLYSVALASNPHEGLULEU
3   SERPHEPROSERARGPROSERILESERGLU
4   LEUTHRARGSERALAGLUTHRALAPHESER
5   ASNGLUILESERLEUARGARGPROASPASN
6   VALPROSERHISLYSPHEHISSERSERLYS
7   ILELYSMETTYRASPGLUGLULEUASNLYS
8   TRPVALASPLEUILEARGGLUASPGLNLEU
9   THRASPTYRCYSGLNLEUTYRVALPHEGLN
10   PROPROASNGLUTRPHISLYSGLUSERGLN
11   LYSGLUILEPROPROALAMETLYSPROPRO

Samples:

sample_1: BILBO1-NTD, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; D2O, [U-2H], 10%; H2O 90%; sodium azide 0.2%

sample_conditions_1: pH: 7.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

VNMRJ v2.3, Varian - collection

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

SPARKY, Goddard - chemical shift assignment, data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

  • Varian Inova 800 MHz
  • Varian Direct Drive 600 MHz
  • Varian Inova 500 MHz

Related Database Links:

PDB
EMBL CBH18240
GB AAY90076 EAN80165
REF XP_011780504 XP_829277

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