BMRB Entry 19718

Title:
Yah1 reduced
Deposition date:
2014-01-07
Original release date:
2014-11-17
Authors:
Gallo, Angelo; Banci, Lucia
Citation:

Citation: Webert, Holger; Freibert, Sven; Gallo, Angelo; Heidenreich, Torsten; Linne, Uwe; Amlacher, Stefan; Hurt, Ed; Muhlenhoff, Ulrich; Banci, Lucia; Lill, Roland. "Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin"  Nat. Commun. 5, 5013-5013 (2014).
PubMed: 25358379

Assembly members:

Assembly members:
entity, polymer, 115 residues, 12970.414 Da.
FE2/S2 (INORGANIC) CLUSTER, non-polymer, 175.820 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETDuet-1

Data sets:
Data typeCount
13C chemical shifts347
15N chemical shifts83
1H chemical shifts362

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Yah1 reduced1
2FE2/S2 (INORGANIC) CLUSTER2

Entities:

Entity 1, Yah1 reduced 115 residues - 12970.414 Da.

1   GLYGLUGLULEULYSILETHRPHEILELEU
2   LYSASPGLYSERGLNLYSTHRTYRGLUVAL
3   CYSGLUGLYGLUTHRILELEUASPILEALA
4   GLNGLYHISASNLEUASPMETGLUGLYALA
5   CYSGLYGLYSERCYSALACYSSERTHRCYS
6   HISVALILEVALASPPROASPTYRTYRASP
7   ALALEUPROGLUPROGLUASPASPGLUASN
8   ASPMETLEUASPLEUALATYRGLYLEUTHR
9   GLUTHRSERARGLEUGLYCYSGLNILELYS
10   METSERLYSASPILEASPGLYILEARGVAL
11   ALALEUPROGLNMETTHRARGASNVALASN
12   ASNASNASPPHESER

Entity 2, FE2/S2 (INORGANIC) CLUSTER - Fe2 S2 - 175.820 Da.

1   FES

Samples:

sample_1: entity, [U-100% 15N], 0.8 mM; potassium phosphate 50 mM; sodium dithionite 1 mM; H2O 90%; D2O 10%

sample_2: entity, [U-13C; U-15N], 0.8 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1

Software:

TOPSPIN vTopspin-2.1, Bruker Biospin - collection, processing

CARA vCARA 2, Keller and Wuthrich - chemical shift assignment

CYANA vCYANA-2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER vAMBER 11, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 19717
PDB
DBJ GAA26726
EMBL CAA91592 CAA97975 CAY86707
GB AHY77932 AJP41900 AJU23344 AJU24032 AJU24707
REF NP_015071
SP Q12184
TPG DAA11185
AlphaFold Q12184

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