BMRB Entry 26031

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26031
MolProbity Validation Chart

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Title:
Solution structure of BOLA3 from Homo sapiens
Deposition date:
2016-04-11
Original release date:
2016-09-02
Authors:
Ciofi-Baffoni, Simone; Nasta, Veronica; Banci, Lucia
Citation:

Citation: Uzarska, Marta; Nasta, Veronica; Weiler, Benjamin; Spantgar, Farah; Ciofi-Baffoni, Simone; Saviello, Maria; Gonnelli, Leonardo; Muhlenhoff, Ulrich; Banci, Lucia; Lill, Roland. "Mitochondrial Bol1 and Bol3 function as assembly factors for specific iron-sulfur proteins"  eLife 5, e16673-e16673 (2016).
PubMed: 27532772

Assembly members:

Assembly members:
BOLA3, polymer, 81 residues, 9306.844 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: pET15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BOLA3: ATQTEGELRVTQILKEKFPR ATAIKVTDISGGCGAMYEIK IESEEFKEKRTVQQHQMVNQ ALKEEIKEMHGLRIFTSVPK R

Data sets:
Data typeCount
13C chemical shifts351
15N chemical shifts87
1H chemical shifts602

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BOLA31

Entities:

Entity 1, BOLA3 81 residues - 9306.844 Da.

The mitochondrial targeting sequence of 1-26 amino acids was removed from the native protein.

1   ALATHRGLNTHRGLUGLYGLULEUARGVAL
2   THRGLNILELEULYSGLULYSPHEPROARG
3   ALATHRALAILELYSVALTHRASPILESER
4   GLYGLYCYSGLYALAMETTYRGLUILELYS
5   ILEGLUSERGLUGLUPHELYSGLULYSARG
6   THRVALGLNGLNHISGLNMETVALASNGLN
7   ALALEULYSGLUGLUILELYSGLUMETHIS
8   GLYLEUARGILEPHETHRSERVALPROLYS
9   ARG

Samples:

sample_1: BOLA3, [U-100% 15N], 0.75 mM; potassium phosphate 50 mM; DTT 5 mM

sample_2: BOLA3, [U-100% 13C; U-100% 15N], 0.75 mM; potassium phosphate 50 mM; DTT 5 mM

sample_3: BOLA3 1 mM; potassium phosphate 50 mM; DTT 5 mM

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_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 HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - data analysis, peak picking

UNIO, Herrmann, Guntert and Wuthrich - peak picking, structure solution

TALOS+, Cornilescu, Delaglio and Bax - data analysis

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

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

PSVS, Bhattacharya and Montelione - structure validation

NMR spectrometers:

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

Related Database Links:

UniProtKB Q53S33

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