BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 52207

Title: SDHAF4 assembly factor of Human Complex II   PubMed: 38212624

Deposition date: 2023-11-10 Original release date: 2023-11-17

Authors: Sharma, Pankaj; Maklashina, Elena; Voehler, Markus; Balinthova, Sona; Dvorakova, Sarka; Kraus, Michal; Hadrava Vanova, Katerina; Nahacka, Zuzana; Zobalova, Renata; Boukalova, Stepana; Cunatova, Kristyna; Mracek, Tomas; Ghayee, Hans; Pacak, Karel; Rohlena, Jakub; Neuzil, Jiri; Cecchini, Gary; Iverson, Tina

Citation: Sharma, Pankaj; Maklashina, Elena; Voehler, Markus; Balinthova, Sona; Dvorakova, Sarka; Kraus, Michal; Hadrava Vanova, Katerina; Nahacka, Zuzana; Zobalova, Renata; Boukalova, Stepana; Cunatova, Kristyna; Mracek, Tomas; Ghayee, Hans; Pacak, Karel; Rohlena, Jakub; Neuzil, Jiri; Cecchini, Gary; Iverson, Tina. "Disordered-to-ordered transitions in assembly factors allow the complex II catalytic subunit to switch binding partners"  Nat. Commun. 15, 473-473 (2024).

Assembly members:
entity_1, polymer, 98 residues, Formula weight is not available

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: pQT-SDHAF4

Entity Sequences (FASTA):
entity_1: MRSHHHHHHENLYFQGIDPF TGSSSSQGGKSELVKQSLKK PKLPEGRFDAPEDSHLEKEP LEKFPDDVNPVTKEKGGPRG PEPTRYGDWERKGRCIDF

Data typeCount
13C chemical shifts262
15N chemical shifts93
1H chemical shifts77

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SDHAF41

Entities:

Entity 1, SDHAF4 98 residues - Formula weight is not available

1   METARGSERHISHISHISHISHISHISGLU
2   ASNLEUTYRPHEGLNGLYILEASPPROPHE
3   THRGLYSERSERSERSERGLNGLYGLYLYS
4   SERGLULEUVALLYSGLNSERLEULYSLYS
5   PROLYSLEUPROGLUGLYARGPHEASPALA
6   PROGLUASPSERHISLEUGLULYSGLUPRO
7   LEUGLULYSPHEPROASPASPVALASNPRO
8   VALTHRLYSGLULYSGLYGLYPROARGGLY
9   PROGLUPROTHRARGTYRGLYASPTRPGLU
10   ARGLYSGLYARGCYSILEASPPHE

Samples:

sample_1: SDHAF4, [U-100% 13C; U-100% 15N], 9.5 mg/mL; potassium phosphate 20 mM; TCEP 10 mM

sample_conditions_1: ionic strength: 0.025 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 13C-detected hCONCOsample_1isotropicsample_conditions_1
3D 13C-detected hNNCOsample_1isotropicsample_conditions_1
2D 13C-detected CONsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.6.2 - collection

NMRViewJ v9.2.0-b24 - chemical shift assignment

TALOS+ v3.80F1 Rev 2012.080.14.41 - data analysis

NMR spectrometers:

  • Bruker AVANCE III 900 MHz

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