Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50917
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Citation: Goodfellow, B.; Freire, F.; Carvalho, A.; Aveiro, S.; Charbonnier, P.; Moulis, J.; Delgado, L.; Ferreira, G.; Rodrigues, J.; Poussin-Courmontagne, P.; Birck, C.; McEwen, A.; Macedo, A.. "The SOUL family of heme-binding proteins: Structure and function 15 years later" Coord. Chem. Rev. 448, 214189-214189 (2021).
Assembly members:
entity_1, polymer, 196 residues, 22031 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28
Data type | Count |
13C chemical shifts | 398 |
15N chemical shifts | 144 |
1H chemical shifts | 274 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HEBP1 | 1 |
Entity 1, HEBP1 196 residues - 22031 Da.
Taketani,S., Adachi,Y., Kohno,H., Ikehara,S., Tokunaga,R. and Ishii,T.: Molecular characterization of a newly identified heme-binding protein induced during differentiation of murine erythroleukemia cells: J. Biol. Chem. 273 (47), 31388-31394 (1998).
1 | HIS | HIS | HIS | HIS | HIS | HIS | LEU | GLU | LEU | GLY | ||||
2 | MET | ILE | LYS | ASN | SER | LEU | PHE | GLY | SER | VAL | ||||
3 | GLU | THR | TRP | PRO | TRP | GLN | VAL | LEU | SER | LYS | ||||
4 | GLY | ASP | LYS | GLU | GLU | VAL | ALA | TYR | GLU | GLU | ||||
5 | ARG | ALA | CYS | GLU | GLY | GLY | LYS | PHE | ALA | THR | ||||
6 | VAL | GLU | VAL | THR | ASP | LYS | PRO | VAL | ASP | GLU | ||||
7 | ALA | LEU | ARG | GLU | ALA | MET | PRO | LYS | VAL | ALA | ||||
8 | LYS | TYR | ALA | GLY | GLY | THR | ASN | ASP | LYS | GLY | ||||
9 | ILE | GLY | MET | GLY | MET | THR | VAL | PRO | ILE | SER | ||||
10 | PHE | ALA | VAL | PHE | PRO | ASN | GLU | ASP | GLY | SER | ||||
11 | LEU | GLN | LYS | LYS | LEU | LYS | VAL | TRP | PHE | ARG | ||||
12 | ILE | PRO | ASN | GLN | PHE | GLN | SER | ASP | PRO | PRO | ||||
13 | ALA | PRO | SER | ASP | LYS | SER | VAL | LYS | ILE | GLU | ||||
14 | GLU | ARG | GLU | GLY | ILE | THR | VAL | TYR | SER | MET | ||||
15 | GLN | PHE | GLY | GLY | TYR | ALA | LYS | GLU | ALA | ASP | ||||
16 | TYR | VAL | ALA | GLN | ALA | THR | ARG | LEU | ARG | ALA | ||||
17 | ALA | LEU | GLU | GLY | THR | ALA | THR | TYR | ARG | GLY | ||||
18 | ASP | ILE | TYR | PHE | CYS | THR | GLY | TYR | ASP | PRO | ||||
19 | PRO | MET | LYS | PRO | TYR | GLY | ARG | ARG | ASN | GLU | ||||
20 | ILE | TRP | LEU | LEU | LYS | THR |
sample_1: phosphate buffer 50 mM; human heme binding protein HEBP1, [U-99% 13C; U-99% 15N], 1 mM
sample_2: phosphate buffer 50 mM; human heme binding protein HEBP1, [U-100% 13C; U-100% 15N; U-80% 2H], 1 mM
sample_3: phosphate buffer 50 mM; human heme binding protein HEBP1, [U-99% 15N], 1 mM
sample_conditions_1: pH: 8.0; temperature: 303 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H15N HSQC | sample_2 | isotropic | sample_conditions_1 |
2D 1H15N TROSY | sample_2 | isotropic | sample_conditions_1 |
3D trHNCOCACB | sample_2 | isotropic | sample_conditions_1 |
3D trHNCA | sample_2 | isotropic | sample_conditions_1 |
3D trHNCOCA | sample_2 | isotropic | sample_conditions_1 |
3D trHNCO | sample_2 | isotropic | sample_conditions_1 |
trHNCACB | sample_3 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N TROSY | sample_2 | isotropic | sample_conditions_1 |
3D trHNCOCACB | sample_2 | isotropic | sample_conditions_1 |
3D trHNCA | sample_2 | isotropic | sample_conditions_1 |
3D trHNCOCA | sample_2 | isotropic | sample_conditions_1 |
3D trHNCACB | sample_2 | isotropic | sample_conditions_1 |
3D trHNCO | sample_2 | isotropic | sample_conditions_1 |
CARA v1.9.1.7 - resonance assignment
TOPSPIN v3.1 - data acquisition and processing
NMRPipe v9.4 - data acquisition and processing
BMRB | 17953 7231 |
PDB | |
DBJ | BAA33770 |
EMBL | CAJ18470 |
GB | AAD32096 AAH12654 AAI68221 EDL10544 EDM01631 |
REF | NP_001102121 NP_038574 XP_006237591 |
SP | Q9R257 |
AlphaFold | O88814 |
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