BMRB Entry 16389
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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/BMR16389
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Title: Solution NMR structure of protein of unknown function (NP_247299.1) from Methanococcus jannaschii PubMed: 20944234
Deposition date: 2009-06-30 Original release date: 2011-05-19
Authors: Jaudzems, Kristaps; Mohanty, Biswaranjan; Geralt, Michael; Serrano, Pedro; Wilson, Ian; Wuthrich, Kurt
Citation: Jaudzems, Kristaps; Geralt, Michael; Serrano, Pedro; Mohanty, Biswaranjan; Horst, Reto; Pedrini, Bill; Elsliger, Marc Andre; Wilson, Ian; Wuthrich, Kurt. "NMR structure of the protein NP_247299.1: comparison with the crystal structure." Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 1367-1380 (2010).
Assembly members:
NP_247299.1, polymer, 106 residues, 12109.914 Da.
Natural source: Common Name: Methanococcus jannaschii Taxonomy ID: 2190 Superkingdom: Archaea Kingdom: not available Genus/species: Methanococcus jannaschii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NP_247299.1: GHMINMKVAISMDVDKISNS
FEDCKYFLIVRIDDNEVKST
KVIFNDESGKKSIVKENVNA
IICKNISEENYKKFSKKIEI
YHAEGDDVDKNISLFIEGEL
SKISNP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 367 |
| 15N chemical shifts | 113 |
| 1H chemical shifts | 781 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NP_247299.1 | 1 |
Entities:
Entity 1, NP_247299.1 106 residues - 12109.914 Da.
| 1 | GLY | HIS | MET | ILE | ASN | MET | LYS | VAL | ALA | ILE | ||||
| 2 | SER | MET | ASP | VAL | ASP | LYS | ILE | SER | ASN | SER | ||||
| 3 | PHE | GLU | ASP | CYS | LYS | TYR | PHE | LEU | ILE | VAL | ||||
| 4 | ARG | ILE | ASP | ASP | ASN | GLU | VAL | LYS | SER | THR | ||||
| 5 | LYS | VAL | ILE | PHE | ASN | ASP | GLU | SER | GLY | LYS | ||||
| 6 | LYS | SER | ILE | VAL | LYS | GLU | ASN | VAL | ASN | ALA | ||||
| 7 | ILE | ILE | CYS | LYS | ASN | ILE | SER | GLU | GLU | ASN | ||||
| 8 | TYR | LYS | LYS | PHE | SER | LYS | LYS | ILE | GLU | ILE | ||||
| 9 | TYR | HIS | ALA | GLU | GLY | ASP | ASP | VAL | ASP | LYS | ||||
| 10 | ASN | ILE | SER | LEU | PHE | ILE | GLU | GLY | GLU | LEU | ||||
| 11 | SER | LYS | ILE | SER | ASN | PRO |
Samples:
sample_1: entity, [U-98% 13C; U-98% 15N], 0.9 mM; sodium phosphate 20 mM; DTT 1 mM; sodium azide 0.03%; H2O 95%; H2O 5%
sample_conditions_1: ionic strength: 0.029 M; pH: 6.5; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D [15N,1H]-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-HACACONH | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY-HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-RESOLVED [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C(aliphatic)-RESOLVED [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C(aromatic)-RESOLVED [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, P.GUNTERT ET AL. - structure solution
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
TOPSPIN, Bruker Biospin - collection, processing
Molmol, Koradi, Billeter and Wuthrich - data analysis
UNIO v1.0.2, T. Herrmann, F. Fiorito, J. Volk - chemical shift assignment, peak picking, structure solution
CARA v1.8.4, Keller - chemical shift assignment
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