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 19193

Title: NMR solution structure of N-terminal domain of (Y81F)-EhCaBP1   PubMed: 23782698

Deposition date: 2013-04-25 Original release date: 2013-10-17

Authors: Chary, Kandala; Rout, Ashok; Patel, Sunita; Bhattacharya, Alok

Citation: Chary, Kandala; Rout, Ashok; Patel, Sunita; Bhattacharya, Alok. "Functional manipulation of a calcium binding protein from E. histolytica guided by paramagnetic NMR"  J. Biol. Chem. ., .-..

Assembly members:
(Y81F)-EhCaBP1, polymer, 66 residues, 14742.640 Da.

Natural source:   Common Name: Eukaryotes   Taxonomy ID: 5759   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Entamoeba histolytica

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

Entity Sequences (FASTA):
(Y81F)-EhCaBP1: MAEALFKEIDVNGDGAVSYE EVKAFVSKKRAIKNEQLLQL IFKSIDADGNGEIDQNEFAK FYGSIQ

Data sets:
Data typeCount
13C chemical shifts248
15N chemical shifts60
1H chemical shifts323

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1(Y81F)-EhCaBP11

Entities:

Entity 1, (Y81F)-EhCaBP1 66 residues - 14742.640 Da.

1   METALAGLUALALEUPHELYSGLUILEASP
2   VALASNGLYASPGLYALAVALSERTYRGLU
3   GLUVALLYSALAPHEVALSERLYSLYSARG
4   ALAILELYSASNGLUGLNLEULEUGLNLEU
5   ILEPHELYSSERILEASPALAASPGLYASN
6   GLYGLUILEASPGLNASNGLUPHEALALYS
7   PHETYRGLYSERILEGLN

Samples:

sample_1: (Y81F)-EhCaBP1, [U-99% 15N], 0.8 ± 0.1 mM; H2O 90%; D2O 10%

sample_2: (Y81F)-EhCaBP1, [U-99% 13C; U-99% 15N], 0.8 ± 0.1 mM; H2O 90%; D2O 10%

sample_3: (Y81F)-EhCaBP1, [U-99% 13C; U-99% 15N], 0.8 ± 0.1 mM; D2O 100%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1

Software:

FELIX, Accelrys Software Inc. - processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - collection, processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 19196
PDB

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