BMRB Entry 16372
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16372
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Title: Solution structure of protein af2351 from Archaeoglobus fulgidus. Northeast Structural Genomics Consortium target AtT9/Ontario Center for Structural Proteomics Target af2351
Deposition date: 2009-06-29 Original release date: 2009-06-30
Authors: Wu, Bin; Yee, Adelinda; Fares, Christophe; Lemak, Alexander; Rumpel, Sigrun; Semest, Anthony; Arrowsmith, Cheryl
Citation: Wu, Bin; Yee, Adelinda; Fares, Christophe; Lemak, Alexander; Rumpel, Sigrun; Semest, Anthony; Arrowsmith, Cheryl. "Solution structure of protein af2351 from Archaeoglobus fulgidus. Northeast Structural Genomics Consortium target AtT9/Ontario Center for Structural Proteomics Target af2351" Not known ., .-..
Assembly members:
af2351, polymer, 139 residues, 16693.863 Da.
Natural source: Common Name: Archaeoglobus fulgidus Taxonomy ID: 2234 Superkingdom: Archaea Kingdom: not available Genus/species: Archaeoglobus fulgidus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
af2351: MSKIVGVTYPIPKRFMDRFF
KKGKDVFVKPATVWKELKPG
MKFVFYQSHEDTGFVGEARI
KRVVLSENPMQFFETFGDRV
FLTKDELKEYMKSQERWGRR
RESKKKKLWMAIELEDVKKY
DKPIKPKRLVPVGGQYLRE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 574 |
| 15N chemical shifts | 114 |
| 1H chemical shifts | 963 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | af2351 | 1 |
Entities:
Entity 1, af2351 139 residues - 16693.863 Da.
| 1 | MET | SER | LYS | ILE | VAL | GLY | VAL | THR | TYR | PRO | ||||
| 2 | ILE | PRO | LYS | ARG | PHE | MET | ASP | ARG | PHE | PHE | ||||
| 3 | LYS | LYS | GLY | LYS | ASP | VAL | PHE | VAL | LYS | PRO | ||||
| 4 | ALA | THR | VAL | TRP | LYS | GLU | LEU | LYS | PRO | GLY | ||||
| 5 | MET | LYS | PHE | VAL | PHE | TYR | GLN | SER | HIS | GLU | ||||
| 6 | ASP | THR | GLY | PHE | VAL | GLY | GLU | ALA | ARG | ILE | ||||
| 7 | LYS | ARG | VAL | VAL | LEU | SER | GLU | ASN | PRO | MET | ||||
| 8 | GLN | PHE | PHE | GLU | THR | PHE | GLY | ASP | ARG | VAL | ||||
| 9 | PHE | LEU | THR | LYS | ASP | GLU | LEU | LYS | GLU | TYR | ||||
| 10 | MET | LYS | SER | GLN | GLU | ARG | TRP | GLY | ARG | ARG | ||||
| 11 | ARG | GLU | SER | LYS | LYS | LYS | LYS | LEU | TRP | MET | ||||
| 12 | ALA | ILE | GLU | LEU | GLU | ASP | VAL | LYS | LYS | TYR | ||||
| 13 | ASP | LYS | PRO | ILE | LYS | PRO | LYS | ARG | LEU | VAL | ||||
| 14 | PRO | VAL | GLY | GLY | GLN | TYR | LEU | ARG | GLU |
Samples:
sample_1: af2351, [U-100% 13C; U-100% 15N], 0.5 mM; bis-tris 25 mM; sodium chloride 50 mM; sodium azide 0.01%; benzamidine 1 mM; H2O 90%; D2O 10%
sample_2: af2351, [U-100% 13C; U-100% 15N], 0.5 mM; bis-tris 25 mM; sodium chloride 50 mM; sodium azide 0.01%; benzamidine 1 mM; D2O 99.9%
sample_3: af2351, [U-7% 13C; U-99% 15N], 0.5 mM; bis-tris 25 mM; sodium chloride 50 mM; sodium azide 0.01%; benzamidine 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
Software:
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
MDDGUI v1.0, Gutmanas and Arrowsmith - processing
SPARKY v3.95, Goddard - data analysis, peak picking
FAWN v1.0, Lemak and Arrowsmith - chemical shift assignment
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStruct, Huang, Tejero, Powers and Montelione - NMR structure quality assessment
PSVS, Bhattacharya and Montelione - NMR structure quality assessment
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts