BMRB Entry 25102

Title:
The NMR structure of the rubredoxin domain of the NO Reductase Flavorubredoxin from Escherichia coli
Deposition date:
2014-07-22
Original release date:
2015-07-20
Authors:
Turner, David; Silva, Elisio; Lamosa, Pedro; Teixeira, Miguel
Citation:

Citation: Turner, David; Silva, Elisio; Lamosa, Pedro; Teixeira, Miguel. "The NMR structure of the rubredoxin domain of the NO Reductase Flavorubredoxin from Escherichia coli"  .

Assembly members:

Assembly members:
rubredoxin_domain_of_the_NO_Reductase_Flavorubredoxin, polymer, 57 residues, 6292.105 Da.
entity_ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PT7-7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
rubredoxin_domain_of_the_NO_Reductase_Flavorubredoxin: GPRMQCSVCQWIYDPAKGEP MQDVAPGTPWSEVPDNFLCP ECSLGKDVFEELASEAK

Data sets:
Data typeCount
15N chemical shifts54
1H chemical shifts368

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1rubredoxin domain of the NO Reductase Flavorubredoxin1
2ZINC ION2

Entities:

Entity 1, rubredoxin domain of the NO Reductase Flavorubredoxin 57 residues - 6292.105 Da.

1   GLYPROARGMETGLNCYSSERVALCYSGLN
2   TRPILETYRASPPROALALYSGLYGLUPRO
3   METGLNASPVALALAPROGLYTHRPROTRP
4   SERGLUVALPROASPASNPHELEUCYSPRO
5   GLUCYSSERLEUGLYLYSASPVALPHEGLU
6   GLULEUALASERGLUALALYS

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: rubredoxin domain of the NO Reductase Flavorubredoxin, [U-99% 15N], 1.1 mM; sodium chloride 100 mM; potassium phosphate 10 mM; sodium azide 0.04%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 7.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY v3.111, Goddard - chemical shift calculation, data analysis

DYANA, Guntert, Braun and Wuthrich - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB36989 BAE76787 BAG78482 BAI26966 BAI31996
EMBL CAP77145 CAQ33042 CAQ87930 CAQ99627 CAR04219
GB AAA69220 AAC75752 AAG57817 AAN44224 AAP18050
REF NP_311593 NP_417190 NP_708517 WP_000029585 WP_000029586
SP A1AEQ0 A7ZQD9 A8A3I7 B1IUW9 B1LQ28
AlphaFold B1IUW9 A7ZQD9 A1AEQ0 B1LQ28 A8A3I7

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