BMRB Entry 19872

Title:
Solution structure of the apo form of human glutaredoxin 5
Deposition date:
2014-03-25
Original release date:
2015-06-05
Authors:
Banci, Lucia; Brancaccio, Diego; Ciofi-Baffoni, Simone; Del Conte, Rebecca; Gadepalli, Ravisekhar; Mikolajczyk, Maciej; Neri, Sara; Piccioli, Mario; Winkelmann, Julia
Citation:

Citation: Banci, Lucia; Brancaccio, Diego; Ciofi-Baffoni, Simone; Del Conte, Rebecca; Gadepalli, Ravisekhar; Mikolajczyk, Maciej; Neri, Sara; Piccioli, Mario; Winkelmann, Julia. "[2Fe-2S] cluster transfer in iron-sulfur protein biogenesis"  Proc. Natl. Acad. Sci. U.S.A. 111, 6203-6208 (2014).
PubMed: 24733926

Assembly members:

Assembly members:
entity, polymer, 121 residues, 13171.006 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: pETG-20A

Data sets:
Data typeCount
13C chemical shifts484
15N chemical shifts118
1H chemical shifts663

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1apo glutaredoxin 51

Entities:

Entity 1, apo glutaredoxin 5 121 residues - 13171.006 Da.

Residues 1-5 represent a non-native cloning artefact.

1   GLYSERPHETHRMETGLYALAGLYGLYGLY
2   GLYSERALAGLUGLNLEUASPALALEUVAL
3   LYSLYSASPLYSVALVALVALPHELEULYS
4   GLYTHRPROGLUGLNPROGLNCYSGLYPHE
5   SERASNALAVALVALGLNILELEUARGLEU
6   HISGLYVALARGASPTYRALAALATYRASN
7   VALLEUASPASPPROGLULEUARGGLNGLY
8   ILELYSASPTYRSERASNTRPPROTHRILE
9   PROGLNVALTYRLEUASNGLYGLUPHEVAL
10   GLYGLYCYSASPILELEULEUGLNMETHIS
11   GLNASNGLYASPLEUVALGLUGLULEULYS
12   LYSLEUGLYILEHISSERALALEULEUASP
13   GLU

Samples:

sample_1: apo glutaredoxin 5, [U-100% 15N], 0.5 – 1 mM; potassium phosphate 50 mM; DTT 5 mM; GSH 5 mM; D2O 90%; H2O 10%

sample_2: apo glutaredoxin 5, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; potassium phosphate 50 mM; DTT 5 mM; GSH 5 mM; D2O 90%; H2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_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 HN(CO)CAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA v2.0, Keller and Wuthrich - chemical shift assignment

ATNOS, Herrmann, Guntert and Wuthrich - peak picking

CANDID, Herrmann, Guntert and Wuthrich - automatic noes assignment

TALOS, Cornilescu, Delaglio and Bax - backbone torsion angle calculation

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

XEASY, Bartels et al. - data analysis

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

PSVS, Bhattacharya and Montelione - structure validation

CING, Vuister, Sousa da Silva, and Doreleijers - structure validation

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAF02301
EMBL CAD62364
GB AAH23528 AAH47680 AAZ30731 EAW81607 EDL18773
REF NP_001252564 NP_057501 XP_001154482 XP_002754322 XP_002825117
SP Q86SX6
AlphaFold Q86SX6