BMRB Entry 4881

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4881

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Title:
Backbone 1H, 13C, 15N and 13CB and 1HB chemical shift assignments for Azotobacter vinelandii C69A holoflavodoxin
Deposition date:
2000-10-25
Original release date:
2000-12-05
Authors:
Steensma, Elles; Nijman, Melanie; Bollen, Yves; de Jager, P.; van den Berg, Willy; van Dongen, Walter; van Mierlo, Carlo
Citation:

Citation: Steensma, Elles; Nijman, Melanie; Bollen, Yves; de Jager, P.; van den Berg, Willy; van Dongen, Walter; van Mierlo, Carlo. "Apparent stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding"  Protein Sci. 7, 306-317 (1998).

Assembly members:

Assembly members:
Azotobacter vinelandii holoflavodoxin II, polymer, 179 residues, 20000 Da.
FMN, non-polymer, 456.344 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Azotobacter vinelandii holoflavodoxin II: AKIGLFFGSNTGKTRKVAKS IKKRFDDETMSDALNVNRVS AEDFAQYQFLILGTPTLGEG ELPGLSSDAENESWEEFLPK IEGLDFSGKTVALFGLGDQV GYPENYLDALGELYSFFKDR GAKIVGSWSTDGYEFESSEA VVDGKFVGLALDLDNQSGKT DERVAAWLAQIAPEFGLSL

Data sets:
Data typeCount
13C chemical shifts517
1H chemical shifts666
15N chemical shifts186
coupling constants122

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C69A holoflavodoxin1
2FMN2

Entities:

Entity 1, C69A holoflavodoxin 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

Entity 2, FMN - C17 H21 N4 O9 P - 456.344 Da.

1   FMN

Samples:

sample_1: Azotobacter vinelandii holoflavodoxin II, [U-100% 15N; U-100% 13C], 5.2 mM; potassium pyrophosphate 150 mM

sample_2: Azotobacter vinelandii holoflavodoxin II, [U-100% 15N], 3.5 mM; potassium pyrophosphate 150 mM

Conditions_sample_1: pH: 6.0; temperature: 303 K; ionic strength: 3 M

Conditions_sample_2: pH: 6.0; temperature: 303 K; ionic strength: 3 M

Experiments:

NameSampleSample stateSample conditions
triple-resonance 5 mm inverse probe with and withoutnot availablenot availablenot available
a self-shielded z-gradient"not availablenot availablenot available

Software:

Felix v2.3 - processing of data

Xeasy - spectral analysis (peak assignment, measurement peak heights)

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker AMX2 600 MHz

Related Database Links:

BMRB 15474 17465 4886
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