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 50921

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50921

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Title: Backbone resonance assignment of human HEBP2

Deposition date: 2021-05-05 Original release date: 2022-05-30

Authors: Freire, Filipe; Aveiro, Susana; Delgado, Leonildo; Rodrigues, Joao; Goodfellow, Brian; Macedo, Anjos

Citation: Goodfellow, B.; Freire, F.; Carvalho, A.; Aveiro, S.; Charbonnier, P.; Moulis, J.; Delgado, L.; Ferreira, G.; Rodrigues, J.; Poussin-Courmontagne, P.; Birck, C.; McEwen, A.; Macedo, A.. "The SOUL family of heme-binding proteins: Structure and function 15 years later"  Coord. Chem. Rev. 448, 214189-214189 (2021).

Assembly members:
entity_1, polymer, 208 residues, 23141 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: hSOUL-pTYB12

Entity Sequences (FASTA):
entity_1: AGHMAEPLQPDPGAAEDAAA QAVETPGWKAPEDAGPQPGS YEIRHYGPAKWVSTSVESMD WDSAIQTGFTKLNSYIQGKN EKEMKIKMTAPVTSYVEPGS GPFSESTITISLYIPSEQQF DPPRPLESDVFIEDRAEMTV FVRSFDGFSSAQKNQEQLLT LASILREDGKVFDEKVYYTA GYNSPVKLLNRNNEVWLIQK NEPTKENE

Data sets:
Data typeCount
13C chemical shifts460
15N chemical shifts169
1H chemical shifts169

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hHEBP21

Entities:

Entity 1, hHEBP2 208 residues - 23141 Da.

1   ALAGLYHISMETALAGLUPROLEUGLNPRO
2   ASPPROGLYALAALAGLUASPALAALAALA
3   GLNALAVALGLUTHRPROGLYTRPLYSALA
4   PROGLUASPALAGLYPROGLNPROGLYSER
5   TYRGLUILEARGHISTYRGLYPROALALYS
6   TRPVALSERTHRSERVALGLUSERMETASP
7   TRPASPSERALAILEGLNTHRGLYPHETHR
8   LYSLEUASNSERTYRILEGLNGLYLYSASN
9   GLULYSGLUMETLYSILELYSMETTHRALA
10   PROVALTHRSERTYRVALGLUPROGLYSER
11   GLYPROPHESERGLUSERTHRILETHRILE
12   SERLEUTYRILEPROSERGLUGLNGLNPHE
13   ASPPROPROARGPROLEUGLUSERASPVAL
14   PHEILEGLUASPARGALAGLUMETTHRVAL
15   PHEVALARGSERPHEASPGLYPHESERSER
16   ALAGLNLYSASNGLNGLUGLNLEULEUTHR
17   LEUALASERILELEUARGGLUASPGLYLYS
18   VALPHEASPGLULYSVALTYRTYRTHRALA
19   GLYTYRASNSERPROVALLYSLEULEUASN
20   ARGASNASNGLUVALTRPLEUILEGLNLYS
21   ASNGLUPROTHRLYSGLUASNGLU

Samples:

sample_1: phosphate buffer 50 mM; hHEBP2, [U-99% 13C; U-99% 15N], 1 mM

sample_2: phosphate buffer 50 mM; hHEBP2, [U-99% 15N], 1 mM

sample_3: phosphate buffer 50 mM; hHEBP2, [U-13C; U-15N; U-2H], 1 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 8.0; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H15N HSQCsample_2isotropicsample_conditions_1
2D 1H15N TROSYsample_2isotropicsample_conditions_1
3D trHNCACBsample_1isotropicsample_conditions_1
3D trHNCOCACBsample_1isotropicsample_conditions_1
3D trHNCAsample_1isotropicsample_conditions_1
3D trHNCOCAsample_1isotropicsample_conditions_1
3D 15N HSQC-NOESYsample_2isotropicsample_conditions_1
3D 15N HSQC-TOCSYsample_2isotropicsample_conditions_1
3D trHNCOsample_1isotropicsample_conditions_1
3D trHNCACOsample_2isotropicsample_conditions_1

Software:

NMRPipe - nmr data processing

XEASY - resonance assignment

TOPSPIN v3.7 - data acquisition and processing

NMR spectrometers:

  • Bruker AVANCE III 600MHz MHz

Related Database Links:

UniProt Q9Y5Z4
AlphaFold Q96P57

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