BMRB Entry 30418

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30418
MolProbity Validation Chart

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Title:
Solution Structure of Amebosin
Deposition date:
2018-02-27
Original release date:
2019-02-01
Authors:
Mendoza, A.; Flores-Solis, D.; Del Rio Portilla, F.; Brieba de Castro, L.
Citation:

Citation: Flores-Solis, David; Mendoza, Angeles; Renteria-Gonzalez, Itzel; Casados-Vazquez, Luz; Trasvina-Arenas, Carlos; Jimenez-Sandoval, Pedro; Benitez-Cardoza, Claudia; Del Rio-Portilla, Federico; Brieba, Luis. "Solution structure of the inhibitor of cysteine proteases 1 from Entamoeba histolytica reveals a possible auto regulatory mechanism"  Biochim. Biophys. Acta Proteins Proteom. 1868, 140512-140512 (2020).
PubMed: 32731033

Assembly members:

Assembly members:
entity_1, polymer, 105 residues, 11379.565 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPHMSLTEDNNNTTITIAKG ENKEIILHGNPTTGYSWVVD SSEGLSNTVEYVADQHAPGI SGSGGKYHIKITGTQTGEGK IVLVYRRPWAPNANDRTFTL KVNVQ

Data sets:
Data typeCount
13C chemical shifts294
15N chemical shifts109
1H chemical shifts599

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 105 residues - 11379.565 Da.

1   GLYPROHISMETSERLEUTHRGLUASPASN
2   ASNASNTHRTHRILETHRILEALALYSGLY
3   GLUASNLYSGLUILEILELEUHISGLYASN
4   PROTHRTHRGLYTYRSERTRPVALVALASP
5   SERSERGLUGLYLEUSERASNTHRVALGLU
6   TYRVALALAASPGLNHISALAPROGLYILE
7   SERGLYSERGLYGLYLYSTYRHISILELYS
8   ILETHRGLYTHRGLNTHRGLYGLUGLYLYS
9   ILEVALLEUVALTYRARGARGPROTRPALA
10   PROASNALAASNASPARGTHRPHETHRLEU
11   LYSVALASNVALGLN

Samples:

sample_1: Amebosin 1 ± 0.1 mM

sample_2: Amebosin, [U-99% 15N], 1 ± 0.1 mM

sample_3: Amebosin, [U-99% 13C; U-99% 15N], 1 ± 0.1 mM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D 1H-15N TOCSYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CS-Rosetta, Shen, Vernon, Baker and Bax - structure calculation

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

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian VXRS 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks