BMRB Entry 50917

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50917

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Title:
The solution structure of human HEBP1
Deposition date:
2021-04-29
Original release date:
2022-05-30
Authors:
Freire, Filipe; Rodrugues, Joao; Delgado, Leonildo; Macedo, Anjos; Goodfellow, Brian
Citation:

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:

Assembly members:
entity_1, polymer, 196 residues, 22031 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HHHHHHLELGMIKNSLFGSV ETWPWQVLSKGDKEEVAYEE RACEGGKFATVEVTDKPVDE ALREAMPKVAKYAGGTNDKG IGMGMTVPISFAVFPNEDGS LQKKLKVWFRIPNQFQSDPP APSDKSVKIEEREGITVYSM QFGGYAKEADYVAQATRLRA ALEGTATYRGDIYFCTGYDP PMKPYGRRNEIWLLKT

Data sets:
Data typeCount
13C chemical shifts398
15N chemical shifts144
1H chemical shifts274

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HEBP11

Entities:

Entity 1, HEBP1 196 residues - 22031 Da.

Taketani,S., Adachi,Y., Kohno,H., Ikehara,S., Tokunaga,R. and Ishii,T.: Molecular characterization of a newly identified heme-binding protein induced during differentiation of murine erythroleukemia cells: J. Biol. Chem. 273 (47), 31388-31394 (1998).

1   HISHISHISHISHISHISLEUGLULEUGLY
2   METILELYSASNSERLEUPHEGLYSERVAL
3   GLUTHRTRPPROTRPGLNVALLEUSERLYS
4   GLYASPLYSGLUGLUVALALATYRGLUGLU
5   ARGALACYSGLUGLYGLYLYSPHEALATHR
6   VALGLUVALTHRASPLYSPROVALASPGLU
7   ALALEUARGGLUALAMETPROLYSVALALA
8   LYSTYRALAGLYGLYTHRASNASPLYSGLY
9   ILEGLYMETGLYMETTHRVALPROILESER
10   PHEALAVALPHEPROASNGLUASPGLYSER
11   LEUGLNLYSLYSLEULYSVALTRPPHEARG
12   ILEPROASNGLNPHEGLNSERASPPROPRO
13   ALAPROSERASPLYSSERVALLYSILEGLU
14   GLUARGGLUGLYILETHRVALTYRSERMET
15   GLNPHEGLYGLYTYRALALYSGLUALAASP
16   TYRVALALAGLNALATHRARGLEUARGALA
17   ALALEUGLUGLYTHRALATHRTYRARGGLY
18   ASPILETYRPHECYSTHRGLYTYRASPPRO
19   PROMETLYSPROTYRGLYARGARGASNGLU
20   ILETRPLEULEULYSTHR

Samples:

sample_1: phosphate buffer 50 mM; human heme binding protein HEBP1, [U-99% 13C; U-99% 15N], 1 mM

sample_2: phosphate buffer 50 mM; human heme binding protein HEBP1, [U-100% 13C; U-100% 15N; U-80% 2H], 1 mM

sample_3: phosphate buffer 50 mM; human heme binding protein HEBP1, [U-99% 15N], 1 mM

sample_conditions_1: pH: 8.0; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H15N HSQCsample_2isotropicsample_conditions_1
2D 1H15N TROSYsample_2isotropicsample_conditions_1
3D trHNCOCACBsample_2isotropicsample_conditions_1
3D trHNCAsample_2isotropicsample_conditions_1
3D trHNCOCAsample_2isotropicsample_conditions_1
3D trHNCOsample_2isotropicsample_conditions_1
trHNCACBsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_2isotropicsample_conditions_1
3D trHNCOCACBsample_2isotropicsample_conditions_1
3D trHNCAsample_2isotropicsample_conditions_1
3D trHNCOCAsample_2isotropicsample_conditions_1
3D trHNCACBsample_2isotropicsample_conditions_1
3D trHNCOsample_2isotropicsample_conditions_1

Software:

CARA v1.9.1.7 - resonance assignment

TOPSPIN v3.1 - data acquisition and processing

NMRPipe v9.4 - data acquisition and processing

NMR spectrometers:

  • Bruker Avance II 800 800MHz MHz
  • Bruker Avance III HD 700 700MHz MHz

Related Database Links:

BMRB 17953 7231
PDB
DBJ BAA33770
EMBL CAJ18470
GB AAD32096 AAH12654 AAI68221 EDL10544 EDM01631
REF NP_001102121 NP_038574 XP_006237591
SP Q9R257
AlphaFold O88814

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