BMRB Entry 30556

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30556
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution structure of human Coa6
Deposition date:
2019-01-07
Original release date:
2019-11-12
Authors:
Naik, M.; Soma, S.; Gohil, V.
Citation:

Citation: Soma, Shivatheja; Morgada, Marcos; Naik, Mandar; Boulet, Aren; Roesler, Anna; Dziuba, Nathaniel; Ghosh, Alok; Yu, Qinhong; Lindahl, Paul; Ames, James; Leary, Scot; Vila, Alejandro; Gohil, Vishal. "COA6 Is Structurally Tuned to Function as a Thiol-Disulfide Oxidoreductase in Copper Delivery to Mitochondrial Cytochrome c Oxidase"  Cell Rep. 29, 4114-44126 (2019).
PubMed: 31851937

Assembly members:

Assembly members:
entity_1, polymer, 81 residues, 9586.769 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 BL21(DE3)   Vector: pGEX-4T1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSMAAPSMKERQVCWGARDE YWKCLDENLEDASQCKKLRS SFESSCPQQWIKYFDKRRDY LKFKEKFEAGQFEPSETTAK S

Data sets:
Data typeCount
13C chemical shifts275
15N chemical shifts78
1H chemical shifts441

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 81 residues - 9586.769 Da.

1   GLYSERMETALAALAPROSERMETLYSGLU
2   ARGGLNVALCYSTRPGLYALAARGASPGLU
3   TYRTRPLYSCYSLEUASPGLUASNLEUGLU
4   ASPALASERGLNCYSLYSLYSLEUARGSER
5   SERPHEGLUSERSERCYSPROGLNGLNTRP
6   ILELYSTYRPHEASPLYSARGARGASPTYR
7   LEULYSPHELYSGLULYSPHEGLUALAGLY
8   GLNPHEGLUPROSERGLUTHRTHRALALYS
9   SER

Samples:

sample_1: Coa6, [U-15N], 0.5 ± 0.05 mM; TRIS 50 ± 1 mM; sodium chloride 150 ± 1 mM

sample_2: Coa6, [U-13C; U-15N], 0.5 ± 0.05 mM; TRIS 50 ± 1 mM; sodium chloride 150 ± 1 mM

sample_3: Coa6 0.5 ± 0.05 mM; TRIS 50 ± 1 mM; sodium chloride 150 ± 1 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D COSYsample_3isotropicsample_conditions_1
2D TOCSYsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
2D NOESYsample_3isotropicsample_conditions_1
2D-hbCBcgcdHDsample_2isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 800 MHz

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