BMRB Entry 18657
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18657
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Title: 1H,13C,15N assignments for an isoform of the type III antifreeze protein from notched-fin eelpout PubMed: 23288342
Deposition date: 2012-08-12 Original release date: 2013-02-13
Authors: Kumeta, Hiroyuki; Ogura, Kenji; Nishimiya, Yoshiyuki; Miura, Ai; Inagaki, Fuyuhiko; Tsuda, Sakae
Citation: Kumeta, Hiroyuki; Ogura, Kenji; Nishimiya, Yoshiyuki; Miura, Ai; Inagaki, Fuyuhiko; Tsuda, Sakae. "NMR structure note: a defective isoform and its activity-improved variant of a type III antifreeze protein from Zoarces elongates Kner." J. Biomol. NMR 55, 225-230 (2013).
Assembly members:
nfeAFP11, polymer, 67 residues, 7071.434 Da.
Natural source: Common Name: not available Taxonomy ID: 291231 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Zoarces elongatus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
nfeAFP11: MNQESVVAAQLIPINTALTL
VMMTTRVVSPTGIPAEDIPR
LISMQVNQVVPMGTTLMPDM
VKGYAPA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 292 |
15N chemical shifts | 67 |
1H chemical shifts | 511 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | nfeAFP11 | 1 |
Entities:
Entity 1, nfeAFP11 67 residues - 7071.434 Da.
1 | MET | ASN | GLN | GLU | SER | VAL | VAL | ALA | ALA | GLN | ||||
2 | LEU | ILE | PRO | ILE | ASN | THR | ALA | LEU | THR | LEU | ||||
3 | VAL | MET | MET | THR | THR | ARG | VAL | VAL | SER | PRO | ||||
4 | THR | GLY | ILE | PRO | ALA | GLU | ASP | ILE | PRO | ARG | ||||
5 | LEU | ILE | SER | MET | GLN | VAL | ASN | GLN | VAL | VAL | ||||
6 | PRO | MET | GLY | THR | THR | LEU | MET | PRO | ASP | MET | ||||
7 | VAL | LYS | GLY | TYR | ALA | PRO | ALA |
Samples:
sample_1: nfeAFP11, [U-100% 13C; U-100% 15N], 2 mM; potassium chloride 20 mM; DSS 0.1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 273 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
PDB |
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