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BMRB Entry 25834

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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/BMR25834
MolProbity Validation Chart

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Title: Solution structure of the FHA domain of TbPar42

Deposition date: 2015-10-04 Original release date: 2016-10-06

Authors: Rehic, Edisa; Bayer, Peter

Citation: Rehic, Edisa; Bayer, Peter. "Solution structure of the FHA domain of TbPar42"  Not known ., .-..

Assembly members:
entity, polymer, 179 residues, 19288.570 Da.

Natural source:   Common Name: kinetoplastids   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: GPMVTSTGLLSRVAAVEKAA EIAKPPPPKVVELTEAAKQL PQHIIGVTDPTKLNAQVSYF QCPPWAALPSVACHLQCTRD GLPLPALGLHRFPFYLFGRS KVCDYVLEHPSISSVHAVLV FHGGQRCFVLMDLGSTNGVK LNGNRIEKRRPLPAPVGSSI QFGFSSRVYKVQLGPPSSS

Data sets:
Data typeCount
13C chemical shifts724
15N chemical shifts172
1H chemical shifts1182

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 179 residues - 19288.570 Da.

1   GLYPROMETVALTHRSERTHRGLYLEULEU
2   SERARGVALALAALAVALGLULYSALAALA
3   GLUILEALALYSPROPROPROPROLYSVAL
4   VALGLULEUTHRGLUALAALALYSGLNLEU
5   PROGLNHISILEILEGLYVALTHRASPPRO
6   THRLYSLEUASNALAGLNVALSERTYRPHE
7   GLNCYSPROPROTRPALAALALEUPROSER
8   VALALACYSHISLEUGLNCYSTHRARGASP
9   GLYLEUPROLEUPROALALEUGLYLEUHIS
10   ARGPHEPROPHETYRLEUPHEGLYARGSER
11   LYSVALCYSASPTYRVALLEUGLUHISPRO
12   SERILESERSERVALHISALAVALLEUVAL
13   PHEHISGLYGLYGLNARGCYSPHEVALLEU
14   METASPLEUGLYSERTHRASNGLYVALLYS
15   LEUASNGLYASNARGILEGLULYSARGARG
16   PROLEUPROALAPROVALGLYSERSERILE
17   GLNPHEGLYPHESERSERARGVALTYRLYS
18   VALGLNLEUGLYPROPROSERSERSER

Samples:

15N13C_FHA: 15N13C FHA domain in 50mM KPiBuffer+2mM DTT, [U-13C; U-15N], 0.6 mM; KPiBuffer 50 mM; DTT 2 mM; D2O 10%; H2O 90%

15NFHA: 15N FHA domain in 50mM KpiBuffer+2mM DTT, [U-15N], 1mM mM; KPiBuffer 50 mM; DTT 2 mM; D2O 10%; H2O 90%

13C_FHA: 13C FHA domain in 50mM KpiBuffer+2mM DTT, [U-13C], 0.6 mM; KPiBuffer 50 mM; DTT 2 mM; D2O 100%

natural_abundance: FHA domain in 50mM KPiBuffer+2mM DTT 1 mM; KPiBuffer 50 mM; DTT 2 mM

Potassium_phosphate_buffer: pH: 6.23; temperature: 300.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15NFHAisotropicPotassium_phosphate_buffer
2D 1H-13C HSQC aliphatic13C_FHAisotropicPotassium_phosphate_buffer
2D 1H-1H COSYnatural_abundanceisotropicPotassium_phosphate_buffer
2D 1H-1H TOCSYnatural_abundanceisotropicPotassium_phosphate_buffer
2D 1H-1H NOESYnatural_abundanceisotropicPotassium_phosphate_buffer
3D CBCA(CO)NH15N13C_FHAisotropicPotassium_phosphate_buffer
3D HNCACB15N13C_FHAisotropicPotassium_phosphate_buffer
3D HBHA(CO)NH15N13C_FHAisotropicPotassium_phosphate_buffer
3D HNHA15N13C_FHAisotropicPotassium_phosphate_buffer
3D HN(CO)CA15N13C_FHAisotropicPotassium_phosphate_buffer
3D HCACO15N13C_FHAisotropicPotassium_phosphate_buffer
3D HNCO15N13C_FHAisotropicPotassium_phosphate_buffer
2D 1H-13C HSQC aromatic15N13C_FHAisotropicPotassium_phosphate_buffer
3D C(CO)NH15N13C_FHAisotropicPotassium_phosphate_buffer
3D H(CCO)NH15N13C_FHAisotropicPotassium_phosphate_buffer
3D HCCH-COSY13C_FHAisotropicPotassium_phosphate_buffer
3D HCCH-TOCSY13C_FHAisotropicPotassium_phosphate_buffer
3D 1H-13C NOESY aromatic13C_FHAisotropicPotassium_phosphate_buffer
3D 1H-15N TOCSY15NFHAisotropicPotassium_phosphate_buffer
3D 1H-15N NOESY15NFHAisotropicPotassium_phosphate_buffer

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - processing

CCPN, CCPN - chemical shift assignment, peak picking

Talos, Cornilescu, Delaglio and Bax - structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

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