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BMRB Entry 19372

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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/BMR19372
MolProbity Validation Chart

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Title: Solution structure of Ani s 5 Anisakis simplex allergen   PubMed: 24603892

Deposition date: 2013-07-17 Original release date: 2014-04-14

Authors: Garcia-Mayoral, Maria Flor; Trevino, Miguel; Perez-Pinar, Teresa; Caballero, Maria Luisa; Knaute, Tobias; Umpierrez, Ana; Bruix, Marta; Rodriguez-Perez, Rosa

Citation: Garcia-Mayoral, Maria Flor; Trevino, Miguel Angel; Perez-Pinar, Teresa; Caballero, Maria Luisa; Knaute, Tobias; Umpierrez, Ana; Bruix, Marta; Rodriguez-Perez, Rosa. "Relationships between IgE/IgG4 Epitopes, Structure and Function in Anisakis simplex Ani s 5, a Member of the SXP/RAL-2 Protein Family."  PLoS Negl. Trop. Dis. 8, e2735-e2735 (2014).

Assembly members:
entity, polymer, 134 residues, 14759.873 Da.

Natural source:   Common Name: Herring worm   Taxonomy ID: 6269   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Anisakis simplex

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

Entity Sequences (FASTA):
entity: DDTPPPPPFLAGAPQDVVKA FFELLKKDETKTDPEIEKDL DAWVDTLGGDYKAKFETFKK EMKAKEAELAKAHEEAVAKM TPEAKKADAELSKIAEDDSL NGIQKAQKIQAIYKTLPQSV KDELEKGIGPAVPQ

Data sets:
Data typeCount
13C chemical shifts418
15N chemical shifts125
1H chemical shifts834

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Ani s 5 Anisakis simplex allergen1

Entities:

Entity 1, Ani s 5 Anisakis simplex allergen 134 residues - 14759.873 Da.

1   ASPASPTHRPROPROPROPROPROPHELEU
2   ALAGLYALAPROGLNASPVALVALLYSALA
3   PHEPHEGLULEULEULYSLYSASPGLUTHR
4   LYSTHRASPPROGLUILEGLULYSASPLEU
5   ASPALATRPVALASPTHRLEUGLYGLYASP
6   TYRLYSALALYSPHEGLUTHRPHELYSLYS
7   GLUMETLYSALALYSGLUALAGLULEUALA
8   LYSALAHISGLUGLUALAVALALALYSMET
9   THRPROGLUALALYSLYSALAASPALAGLU
10   LEUSERLYSILEALAGLUASPASPSERLEU
11   ASNGLYILEGLNLYSALAGLNLYSILEGLN
12   ALAILETYRLYSTHRLEUPROGLNSERVAL
13   LYSASPGLULEUGLULYSGLYILEGLYPRO
14   ALAVALPROGLN

Samples:

sample_1: Ani s 5, [U-13C; U-15N], 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 3.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAF43534

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