BMRB Entry 4886

Title:
Backbone 1H and 15N and 1HB chemical shift assignments for Azotobacter vinelandii C69A apoflavodoxin
Deposition date:
2000-10-26
Original release date:
2000-12-04
Authors:
Steensma, Elles; van Mierlo, Carlo
Citation:

Citation: Steensma, Elles; van Mierlo, Carlo. "Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology"  J. Mol. Biol. 282, 653-666 (1998).
PubMed: 9737928

Assembly members:

Assembly members:
Azotobacter vinelandii apoflavodoxin II, polymer, 179 residues, 20000 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 354   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Azotobacter vinelandii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Data sets:
Data typeCount
1H chemical shifts524
15N chemical shifts146
coupling constants76

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C69A apoflavodoxin1

Entities:

Entity 1, C69A apoflavodoxin 179 residues - 20000 Da.

1   ALALYSILEGLYLEUPHEPHEGLYSERASN
2   THRGLYLYSTHRARGLYSVALALALYSSER
3   ILELYSLYSARGPHEASPASPGLUTHRMET
4   SERASPALALEUASNVALASNARGVALSER
5   ALAGLUASPPHEALAGLNTYRGLNPHELEU
6   ILELEUGLYTHRPROTHRLEUGLYGLUGLY
7   GLULEUPROGLYLEUSERSERASPALAGLU
8   ASNGLUSERTRPGLUGLUPHELEUPROLYS
9   ILEGLUGLYLEUASPPHESERGLYLYSTHR
10   VALALALEUPHEGLYLEUGLYASPGLNVAL
11   GLYTYRPROGLUASNTYRLEUASPALALEU
12   GLYGLULEUTYRSERPHEPHELYSASPARG
13   GLYALALYSILEVALGLYSERTRPSERTHR
14   ASPGLYTYRGLUPHEGLUSERSERGLUALA
15   VALVALASPGLYLYSPHEVALGLYLEUALA
16   LEUASPLEUASPASNGLNSERGLYLYSTHR
17   ASPGLUARGVALALAALATRPLEUALAGLN
18   ILEALAPROGLUPHEGLYLEUSERLEU

Samples:

sample_1: Azotobacter vinelandii apoflavodoxin II, [U-15N], 2 mM; potassium pyrophosphate 150 mM; H2O 90%; D2O 10%

Conditions_sample_1: pH*: 6.0; temperature: 303 K; ionic strength: 0.3 M

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCsample_1not availableConditions_sample_1
ct-HNHAsample_1not availableConditions_sample_1
ct-HNHBsample_1not availableConditions_sample_1
TOCSY-HMQCsample_1not availableConditions_sample_1
HMQC-NOESY-HSQCsample_1not availableConditions_sample_1
NOESY-HSQCsample_1not availableConditions_sample_1
triple-resonance 5 mm inverse probe with a self-shielded z-gradientsample_1not availableConditions_sample_1

Software:

Felix v2.3 - processing of data

Xeasy - spectral analysis, peak assignment, measurement peak heights

NMR spectrometers:

  • Bruker AMX 500 MHz

Related Database Links:

BMRB 15474 17465 4881
PDB
GB AAA22154 AAA64735 ACO76434 AGK13779 AGK18380
PRF 752055A
REF WP_012698862 YP_002797409 YP_007891221 YP_007896269
SP P00324
AlphaFold P00324

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