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 19893

Title: Chemical Shift Assignments and structure of Q4D059, a hypothetical protein from Trypanosoma cruzi

Authors: Lopez, Aracelys; Pires, Jose Ricardo

Citation: Lopez, Aracelys; Pires, Jose Ricardo. "1H, 15N and 13C resonance assignments and secondary structure prediction of Q4D059, a conserved and specific hypothetical protein from Trypanosoma cruzi"  Biomol. NMR Assignments ., .-..

Assembly members:
HP_Q4D059, polymer, 92 residues, 10429.040 Da.

Natural source:   Common Name: kinetoplastids   Taxonomy ID: 5693   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma cruzi

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

Entity Sequences (FASTA):
HP_Q4D059: GSAMGHMPAVDVEIHFPLKR IAAEGYAEDELLLNQMGKVN DTPEEEGMPLRAWVIKCAHE ALEKNPKIREVYLKPRAVKN SSVQFHVIFDEE

Data sets:
Data typeCount
13C chemical shifts335
15N chemical shifts84
1H chemical shifts514

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HP_Q4D0591

Entities:

Entity 1, HP_Q4D059 92 residues - 10429.040 Da.

1   GLYSERALAMETGLYHISMETPROALAVAL
2   ASPVALGLUILEHISPHEPROLEULYSARG
3   ILEALAALAGLUGLYTYRALAGLUASPGLU
4   LEULEULEUASNGLNMETGLYLYSVALASN
5   ASPTHRPROGLUGLUGLUGLYMETPROLEU
6   ARGALATRPVALILELYSCYSALAHISGLU
7   ALALEUGLULYSASNPROLYSILEARGGLU
8   VALTYRLEULYSPROARGALAVALLYSASN
9   SERSERVALGLNPHEHISVALILEPHEASP
10   GLUGLU

Samples:

Q4D059_15N: HP_Q4D059, [U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O, [U-100% 2H], 10%

Q4D059_15N_13C: HP_Q4D059, [U-100% 13C; U-100% 15N], 0.3 mM; sodium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O, [U-100% 2H], 10%

Q4D059_1H: HP_Q4D059 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O, [U-100% 2H], 10%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCQ4D059_15Nisotropicsample_conditions_1
2D 1H-1H TOCSYQ4D059_1Hisotropicsample_conditions_1
2D 1H-1H NOESYQ4D059_1Hisotropicsample_conditions_1
3D CBCA(CO)NHQ4D059_15N_13Cisotropicsample_conditions_1
3D HNCOQ4D059_15N_13Cisotropicsample_conditions_1
3D HNCACBQ4D059_15N_13Cisotropicsample_conditions_1
3D HBHA(CO)NHQ4D059_15N_13Cisotropicsample_conditions_1
3D HCCH-TOCSYQ4D059_15N_13Cisotropicsample_conditions_1
3D 1H-15N NOESYQ4D059_15Nisotropicsample_conditions_1
3D 1H-15N TOCSYQ4D059_15Nisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticQ4D059_15N_13Cisotropicsample_conditions_1
3D 1H-13C NOESY aromaticQ4D059_15N_13Cisotropicsample_conditions_1
3D HCCH-COSYQ4D059_15N_13Cisotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

TOPSPIN, Bruker Biospin - collection, processing

ARIA v1.2, Linge, O, . - data analysis, structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB EAN85913
REF XP_807764