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Biological Magnetic Resonance Data Bank


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BMRB Entry 19196

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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/BMR19196
MolProbity Validation Chart

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

Deposition date: 2013-04-26 Original release date: 2013-06-17

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

Citation: Rout, Ashok; Patel, Sunita; Somlata, .; Shukla, Manish; Saraswathi, Deepa; Bhattacharya, Alok; Chary, Kandala. "Functional manipulation of a calcium-binding protein from Entamoeba histolytica guided by paramagnetic NMR."  J. Biol. Chem. 288, 23473-23487 (2013).

Assembly members:
(Y81F)-EhCaBP1, polymer, 66 residues, 7380.329 Da.
EhCaBP1, polymer, 134 residues, 851.608 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
EhCaBP1: MAEALFKEIDVNGDGAVSYE EVKAFVSKKRAIKNEQLLQL IFKSIDADGNGEIDQNEFAK FYGSIQGQDLSDDKIGLKVL FKLMDVDGDGKLTKEEVTSF FKKHGIEKVAEQVMKADANG DGYITLEEFLEFSL

Data sets:
Data typeCount
13C chemical shifts248
15N chemical shifts60
1H chemical shifts321

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1(Y81F)-EhCaBP11
2EhCaBP12

Entities:

Entity 1, (Y81F)-EhCaBP1 66 residues - 7380.329 Da.

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

Entity 2, EhCaBP1 134 residues - 851.608 Da.

1   METALAGLUALALEUPHELYSGLUILEASP
2   VALASNGLYASPGLYALAVALSERTYRGLU
3   GLUVALLYSALAPHEVALSERLYSLYSARG
4   ALAILELYSASNGLUGLNLEULEUGLNLEU
5   ILEPHELYSSERILEASPALAASPGLYASN
6   GLYGLUILEASPGLNASNGLUPHEALALYS
7   PHETYRGLYSERILEGLNGLYGLNASPLEU
8   SERASPASPLYSILEGLYLEULYSVALLEU
9   PHELYSLEUMETASPVALASPGLYASPGLY
10   LYSLEUTHRLYSGLUGLUVALTHRSERPHE
11   PHELYSLYSHISGLYILEGLULYSVALALA
12   GLUGLNVALMETLYSALAASPALAASNGLY
13   ASPGLYTYRILETHRLEUGLUGLUPHELEU
14   GLUPHESERLEU

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 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, data analysis, processing

FELIX, Accelrys Software Inc. - data analysis, processing

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

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 19193 19197 4271
PDB
DBJ BAN39246
GB AAA29089 EAL48959 EKE39141 EMD43507 EMH75928
REF XP_008858522 XP_654345
SP P38505

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