Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4886
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NMR-STAR v3 text file.
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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:
Azotobacter vinelandii apoflavodoxin II, polymer, 179 residues, 20000 Da.
Natural source: Common Name: not available Taxonomy ID: 354 Superkingdom: Eubacteria Kingdom: not available Genus/species: Azotobacter vinelandii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Azotobacter vinelandii apoflavodoxin II: AKIGLFFGSNTGKTRKVAKS
IKKRFDDETMSDALNVNRVS
AEDFAQYQFLILGTPTLGEG
ELPGLSSDAENESWEEFLPK
IEGLDFSGKTVALFGLGDQV
GYPENYLDALGELYSFFKDR
GAKIVGSWSTDGYEFESSEA
VVDGKFVGLALDLDNQSGKT
DERVAAWLAQIAPEFGLSL
| Data type | Count |
| 1H chemical shifts | 524 |
| 15N chemical shifts | 146 |
| coupling constants | 76 |
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | C69A apoflavodoxin | 1 |
Entity 1, C69A apoflavodoxin 179 residues - 20000 Da.
| 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 |
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
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H-15N HSQC | sample_1 | not available | Conditions_sample_1 |
| ct-HNHA | sample_1 | not available | Conditions_sample_1 |
| ct-HNHB | sample_1 | not available | Conditions_sample_1 |
| TOCSY-HMQC | sample_1 | not available | Conditions_sample_1 |
| HMQC-NOESY-HSQC | sample_1 | not available | Conditions_sample_1 |
| NOESY-HSQC | sample_1 | not available | Conditions_sample_1 |
| triple-resonance 5 mm inverse probe with a self-shielded z-gradient | sample_1 | not available | Conditions_sample_1 |
Felix v2.3 - processing of data
Xeasy - spectral analysis, peak assignment, measurement peak heights
| 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:
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or all simulated peaks