BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30556

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: Soma, S.; Naik, M.; Gohil, V.. "Redox role of COA6 in CuA site formation in cytochrome c oxidase"  . ., .-..

Assembly members:
entity_1, polymer, 81 residues, 9586.769 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts