BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19904

Title: Solution structure of the PPIase domain of TbPar42

Deposition date: 2014-04-10 Original release date: 2015-04-13

Authors: Rehic, Edisa; Bayer, Peter

Citation: Rehic, Edisa; Hoenig, Dana; Rueppel, Alma; Matena, Anja; Bayer, Peter. "Solution structure of TbPar42"  Not known ., .-..

Assembly members:
entity, polymer, 120 residues, 13522.351 Da.

Natural source:   Common Name: Trypanosoma brucei   Taxonomy ID: 5691   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma brucei

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

Entity Sequences (FASTA):
entity: PTERHFYHVLVKHKDVRRPS SLAPRNKGEKITRSRADAIN LAQAILAQHKERKTWSLDEF VQVVRDFSECGSAKRDGDLG MVESGTYTEGFDTVAFSLKS GEVSAPVETELGVHLIYRVE

Data sets:
Data typeCount
13C chemical shifts473
15N chemical shifts122
1H chemical shifts818

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PPIase domain of TbPar421

Entities:

Entity 1, PPIase domain of TbPar42 120 residues - 13522.351 Da.

1   PROTHRGLUARGHISPHETYRHISVALLEU
2   VALLYSHISLYSASPVALARGARGPROSER
3   SERLEUALAPROARGASNLYSGLYGLULYS
4   ILETHRARGSERARGALAASPALAILEASN
5   LEUALAGLNALAILELEUALAGLNHISLYS
6   GLUARGLYSTHRTRPSERLEUASPGLUPHE
7   VALGLNVALVALARGASPPHESERGLUCYS
8   GLYSERALALYSARGASPGLYASPLEUGLY
9   METVALGLUSERGLYTHRTYRTHRGLUGLY
10   PHEASPTHRVALALAPHESERLEULYSSER
11   GLYGLUVALSERALAPROVALGLUTHRGLU
12   LEUGLYVALHISLEUILETYRARGVALGLU

Samples:

sample_1: PPIase domain of TbPar42500 – 550 uM; potassium phosphate 50 mM; DSS 50 uM; H2O 90%; D2O 10%

sample_2: PPIase domain of TbPar42500 – 550 uM; potassium phosphate 50 mM; DSS 50 uM; D20 99.9%

sample_3: PPIase domain of TbPar42, [U-100% 13C; U-100% 15N], 500 – 550 uM; potassium phosphate 50 mM; DSS 50 uM; H2O 90%; D2O 10%

sample_5: PPIase domain of TbPar42, [U-100% 15N], 500 – 550 uM; potassium phosphate 50 mM; DSS 50 uM; D20 100%

sample_4: PPIase domain of TbPar42, [U-100% 15N], 500 – 550 uM; potassium phosphate 50 mM; DSS 50 uM; H2O 90%; D20 10%

sample_6: PPIase domain of TbPar42, [U-100% 13C], 500 – 550 uM; potassium phosphate 50 mM; DSS 50 uM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.26; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HN(CA)COsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
3D HNHAHBsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_6isotropicsample_conditions_1
3D HCCH-COSYsample_6isotropicsample_conditions_1
2D 1H-1H COSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_5isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CCPN, CCPN - chemical shift assignment, chemical shift calculation, data analysis, peak picking

TALOS, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance Ultrashield 700 MHz

Related Database Links:

PDB
EMBL CBH12319
GB AAX69643 AAZ12312
REF XP_011774600 XP_845871

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts