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 PubMed: 19053416
Deposition date: 2007-09-17 Original release date: 2008-11-20
Authors: Nabuurs, Sanne; Westphal, Adrie; van Mierlo, Carlo
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).
Assembly members:
Apoflavodoxin, polymer, 179 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: puc
Entity Sequences (FASTA):
Apoflavodoxin: AKIGLFFGSNTGKTRKVAKS
IKKRFDDETMSDALNVNRVS
AEDFAQYQFLILGTPTLGEG
ELPGLSSDAENESWEEFLPK
IEGLDFSGKTVALFGLGDQV
GYPENYLDALGELYSFFKDR
GAKIVGSWSTDGYEFESSEA
VVDGKFVGLALDLDNQSGKT
DERVAAWLAQIAPEFGLSL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 1026 |
| 15N chemical shifts | 345 |
| 1H chemical shifts | 345 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Apoflavodoxin | 1 |
Entities:
Entity 1, Apoflavodoxin 179 residues - Formula weight is not available
| 1 | ALA | LYS | ILE | GLY | LEU | PHE | PHE | GLY | SER | ASN | ||||
| 2 | THR | GLY | LYS | THR | ARG | LYS | VAL | ALA | LYS | SER | ||||
| 3 | ILE | LYS | LYS | ARG | PHE | ASP | ASP | GLU | THR | MET | ||||
| 4 | SER | ASP | ALA | LEU | ASN | VAL | ASN | ARG | VAL | SER | ||||
| 5 | ALA | GLU | ASP | PHE | ALA | GLN | TYR | GLN | PHE | LEU | ||||
| 6 | ILE | LEU | GLY | THR | PRO | THR | LEU | GLY | GLU | GLY | ||||
| 7 | GLU | LEU | PRO | GLY | LEU | SER | SER | ASP | ALA | GLU | ||||
| 8 | ASN | GLU | SER | TRP | GLU | GLU | PHE | LEU | PRO | LYS | ||||
| 9 | ILE | GLU | GLY | LEU | ASP | PHE | SER | GLY | LYS | THR | ||||
| 10 | VAL | ALA | LEU | PHE | GLY | LEU | GLY | ASP | GLN | VAL | ||||
| 11 | GLY | TYR | PRO | GLU | ASN | TYR | LEU | ASP | ALA | LEU | ||||
| 12 | GLY | GLU | LEU | TYR | SER | PHE | PHE | LYS | ASP | ARG | ||||
| 13 | GLY | ALA | LYS | ILE | VAL | GLY | SER | TRP | SER | THR | ||||
| 14 | ASP | GLY | TYR | GLU | PHE | GLU | SER | SER | GLU | ALA | ||||
| 15 | VAL | VAL | ASP | GLY | LYS | PHE | VAL | GLY | LEU | ALA | ||||
| 16 | LEU | ASP | LEU | ASP | ASN | GLN | SER | GLY | LYS | THR | ||||
| 17 | ASP | GLU | ARG | VAL | ALA | ALA | TRP | LEU | ALA | GLN | ||||
| 18 | ILE | ALA | PRO | GLU | PHE | GLY | LEU | SER | LEU |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | fld_6M_GuHCl | isotropic | sample_conditions_1 |
| 3D HNCA | fld_6M_GuHCl | isotropic | sample_conditions_1 |
| 3D HNCACB | fld_6M_GuHCl | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | fld_6M_GuHCl | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | fld_6M_GuHCl | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | fld_6M_GuHCl | isotropic | sample_conditions_1 |
| 3D HNCO | fld_3.4M_GuHCl | isotropic | sample_conditions_1 |
| 3D HNCA | fld_3.4M_GuHCl | isotropic | sample_conditions_1 |
| 3D HNCACB | fld_3.4M_GuHCl | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | fld_3.4M_GuHCl | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | fld_3.4M_GuHCl | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | fld_3.4M_GuHCl | isotropic | sample_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 shifts
SPARKY: Backbone
or all simulated shifts