BMRB Entry 34013

Title:
Solution structure of BOLA1 from Homo sapiens
Deposition date:
2016-06-21
Original release date:
2016-08-26
Authors:
Nasta, V.; Ciofi Baffoni, S.; Banci, L.
Citation:

Citation: Uzarska, M.; Nasta, V.; Weiler, B.; Spantgar, F.; Ciofi-Baffoni, S.; Saviello, M.; Gonnelli, L.; M hlenhoff, U.; Banci, L.; Lill, R.. "Mitochondrial Bol1 and Bol3 function as assembly factors for specific iron-sulfur proteins"  Elife 5, e16673-e16673 (2016).
PubMed: 27532772

Assembly members:

Assembly members:
BolA-like protein 1, polymer, 123 residues, 12875.399 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: pET151

Data sets:
Data typeCount
13C chemical shifts465
15N chemical shifts126
1H chemical shifts778

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 123 residues - 12875.399 Da.

1   GLYILEASPPROPHETHRGLNGLYSERALA
2   GLYSERGLYALAILEGLYPROVALGLUALA
3   ALAILEARGTHRLYSLEUGLUGLUALALEU
4   SERPROGLUVALLEUGLULEUARGASNGLU
5   SERGLYGLYHISALAVALPROPROGLYSER
6   GLUTHRHISPHEARGVALALAVALVALSER
7   SERARGPHEGLUGLYLEUSERPROLEUGLN
8   ARGHISARGLEUVALHISALAALALEUALA
9   GLUGLULEUGLYGLYPROVALHISALALEU
10   ALAILEGLNALAARGTHRPROALAGLNTRP
11   ARGGLUASNSERGLNLEUASPTHRSERPRO
12   PROCYSLEUGLYGLYASNLYSLYSTHRLEU
13   GLYTHRPRO

Samples:

sample_1: DTT 5 mM; mitochondrial BOLA1 protein, [U-100% 15N], 1 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%

sample_2: DTT 5 mM; mitochondrial BOLA1 protein, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%

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

sample_conditions_2: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2anisotropicsample_conditions_2
3D HNCOsample_2anisotropicsample_conditions_2
3D HNCAsample_2anisotropicsample_conditions_2
3D HN(CO)CAsample_2anisotropicsample_conditions_2
3D HBHA(CBCACO)NHsample_2anisotropicsample_conditions_2
3D HN(CA)COsample_2anisotropicsample_conditions_2
3D CBCA(CO)NHsample_2anisotropicsample_conditions_2
3D HNCACBsample_2anisotropicsample_conditions_2
3D HNCACBsample_2anisotropicsample_conditions_2
3D 1H-13C NOESYsample_2anisotropicsample_conditions_2
3D HCCH-TOCSYsample_2anisotropicsample_conditions_2
2D 1H-1H TOCSYsample_1anisotropicsample_conditions_1
2D 1H-1H NOESYsample_1anisotropicsample_conditions_1
3D 1H-15N NOESYsample_1anisotropicsample_conditions_1

Software:

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

CARA, Keller and Wuthrich - peak picking

CARA v2, Keller and Wuthrich - chemical shift assignment

TALOS+, Cornilescu, Delaglio and Bax - data analysis

TOPSPIN, Bruker Biospin - collection, processing

UNIO, Serrano, Pedrini, Mohanty, Geralt, Herrmann and Wuthrich, - peak picking, structure calculation

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 950 MHz

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