BMRB Entry 15474

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15474

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Title:
1H, 15N and 13C assignment and relaxation parameters of the denatured state of Azotobacter vinelandii apoflavodoxin
Deposition date:
2007-09-17
Original release date:
2008-11-20
Authors:
Nabuurs, Sanne; Westphal, Adrie; van Mierlo, Carlo
Citation:

Citation: Nabuurs, Sanne; Westphal, Adrie; van Mierlo, Carlo. "Extensive formation of off-pathway species during folding of an alpha-beta parallel protein is due to docking of (non)native structure elements in unfolded molecules"  J. Am. Chem. Soc. 130, 16914-16920 (2008).
PubMed: 19053416

Assembly members:

Assembly members:
Apoflavodoxin, polymer, 179 residues, Formula weight is not available

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: puc

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Apoflavodoxin: AKIGLFFGSNTGKTRKVAKS IKKRFDDETMSDALNVNRVS AEDFAQYQFLILGTPTLGEG ELPGLSSDAENESWEEFLPK IEGLDFSGKTVALFGLGDQV GYPENYLDALGELYSFFKDR GAKIVGSWSTDGYEFESSEA VVDGKFVGLALDLDNQSGKT DERVAAWLAQIAPEFGLSL

Data sets:
Data typeCount
13C chemical shifts1026
15N chemical shifts345
1H chemical shifts345

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Apoflavodoxin1

Entities:

Entity 1, Apoflavodoxin 179 residues - Formula weight is not available

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:

fld_6M_GuHCl: Apoflavodoxin, [U-99% 13C; U-99% 15N], 1.5 mM; D2O 10%; DSS 5 mM; Potassium Pyrophosphate 100 mM; Guanidinium Hydrochloride 6.0 M

fld_3.4M_GuHCl: Apoflavodoxin, [U-99% 13C; U-99% 15N], 1.5 mM; D2O 10%; DSS 5 mM; Potassium Pyrophosphate 100 mM; Guanidinium Hydrochloride 3.4 M

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOfld_6M_GuHClisotropicsample_conditions_1
3D HNCAfld_6M_GuHClisotropicsample_conditions_1
3D HNCACBfld_6M_GuHClisotropicsample_conditions_1
3D HN(CO)CAfld_6M_GuHClisotropicsample_conditions_1
3D CBCA(CO)NHfld_6M_GuHClisotropicsample_conditions_1
2D 1H-15N HSQCfld_6M_GuHClisotropicsample_conditions_1
3D HNCOfld_3.4M_GuHClisotropicsample_conditions_1
3D HNCAfld_3.4M_GuHClisotropicsample_conditions_1
3D HNCACBfld_3.4M_GuHClisotropicsample_conditions_1
3D HN(CO)CAfld_3.4M_GuHClisotropicsample_conditions_1
3D CBCA(CO)NHfld_3.4M_GuHClisotropicsample_conditions_1
2D 1H-15N HSQCfld_3.4M_GuHClisotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

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