BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 26025

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26025
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Title: 1H, 13C, and 15N Chemical Shift Assignments for Q4DY78   PubMed: 27356988

Deposition date: 2016-04-03 Original release date: 2016-07-12

Authors: D'Andrea, Everton; Diehl, Anne; Schmieder, Peter; Oschkinat, Hartmut; Pires, Jose

Citation: D'Andrea, Everton; Diehl, Anne; Schmieder, Peter; Oschkinat, Hartmut; Pires, Jose. "Chemical shift assignments and secondary structure prediction for Q4DY78, a conserved kinetoplastid-specific protein from Trypanosoma cruzi"  Biomol. NMR Assign. 10, 325-328 (2016).

Assembly members:
Q4DY78, polymer, 112 residues, Formula weight is not available

Natural source:   Common Name: Trypanosoma cruzi   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):
Q4DY78: GSAMGHMVKISHEDTQRIKT AFLSYAQGQDKVTEAMIDQL ICGAFPGLSWEQLQEKKKGR AAANGYDRSAFFSLVASDEQ YVRFIAQHFPCAPEEEKPPE IDALELKTQKGF

Data sets:
Data typeCount
13C chemical shifts451
15N chemical shifts106
1H chemical shifts718

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Q4DY78 monomer1

Entities:

Entity 1, Q4DY78 monomer 112 residues - Formula weight is not available

1   GLYSERALAMETGLYHISMETVALLYSILE
2   SERHISGLUASPTHRGLNARGILELYSTHR
3   ALAPHELEUSERTYRALAGLNGLYGLNASP
4   LYSVALTHRGLUALAMETILEASPGLNLEU
5   ILECYSGLYALAPHEPROGLYLEUSERTRP
6   GLUGLNLEUGLNGLULYSLYSLYSGLYARG
7   ALAALAALAASNGLYTYRASPARGSERALA
8   PHEPHESERLEUVALALASERASPGLUGLN
9   TYRVALARGPHEILEALAGLNHISPHEPRO
10   CYSALAPROGLUGLUGLULYSPROPROGLU
11   ILEASPALALEUGLULEULYSTHRGLNLYS
12   GLYPHE

Samples:

sample_1: Q4DY78 0.4 mM; Na2HPO4 10 mM; KH2PO4 1.8 mM; NaCl 140 mM; KCl 2.7 mM; DTT 10 mM

sample_2: Q4DY78, [U-15N], 0.3 mM; Na2HPO4 10 mM; KH2PO4 1.8 mM; NaCl 140 mM; KCl 2.7 mM; DTT 10 mM

sample_3: Q4DY78, [U-100% 13C; U-100% 15N], 0.8 mM; Na2HPO4 10 mM; KH2PO4 1.8 mM; NaCl 140 mM; KCl 2.7 mM; DTT 10 mM

sample_1_conditions: pH: 7.4; pressure: 1 atm; temperature: 298 K

sample_2_conditions: pH: 7.4; pressure: 1 atm; temperature: 298 K

sample_3_conditions: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_2_conditions
2D 1H-13C HSQCsample_3isotropicsample_3_conditions
2D 1H-1H TOCSYsample_1isotropicsample_1_conditions
2D 1H-1H NOESYsample_1isotropicsample_1_conditions
3D CBCA(CO)NHsample_3isotropicsample_3_conditions
3D HNCACBsample_3isotropicsample_3_conditions
3D HBHA(CO)NHsample_2isotropicsample_2_conditions
3D 1H-15N TOCSYsample_2isotropicsample_2_conditions
3D HCCH-COSYsample_3isotropicsample_3_conditions
3D HCCH-TOCSYsample_3isotropicsample_3_conditions
3D HNCOsample_3isotropicsample_3_conditions
3D 1H-15N NOESYsample_2isotropicsample_2_conditions
3D 1H-13C NOESYsample_3isotropicsample_3_conditions

Software:

SPARKY v3.114, Goddard - chemical shift assignment, data analysis, peak picking

TALOS v+, Shen, Delaglio, Cornilescu, Bax - secondary structure prediction

TOPSPIN v3.1, Bruker Biospin - data acquisition, data processing

AVS, Moseley and Montelione - chemical shift validation

NMR spectrometers:

  • Bruker Avance III 600 MHz
  • Bruker Avance III 800 MHz

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