BMRB Entry 15847
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15847
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Title: Solution NMR Structure of XF2673 from Xylella fastidiosa. Northeast Structural Genomics Consortium Target XfR39 PubMed: TBA
Deposition date: 2008-06-30 Original release date: 2008-09-19
Authors: Tang, Yuefeng; Wang, Huang; Jiang, Mei; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation: Tang, Yuefeng; Wang, Huang; Jiang, Mei; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "Solution NMR Structure of XF2673 from Xylella fastidiosa. Northeast Structural Genomics Consortium Target XfR39" Not known ., .-..
Assembly members:
XF2673, polymer, 97 residues, 10981.5 Da.
Natural source: Common Name: Xylella fastidiosa Taxonomy ID: 2371 Superkingdom: Bacteria Kingdom: not available Genus/species: Xylella fastidiosa
Experimental source: Production method: recombinant technology Host organism: BL21(DE3)+magic
Entity Sequences (FASTA):
XF2673: MDRKLLHLLCSPDTRQPLSL
LESKGLEALNKAIVSGTVQR
ADGSIQNQSLHEALITRDRK
QVFRIEDSIPVLLPEEAIAT
IQIANFPDKLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 393 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 654 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | XF2673 | 1 |
Entities:
Entity 1, XF2673 97 residues - 10981.5 Da.
| 1 | MET | ASP | ARG | LYS | LEU | LEU | HIS | LEU | LEU | CYS | ||||
| 2 | SER | PRO | ASP | THR | ARG | GLN | PRO | LEU | SER | LEU | ||||
| 3 | LEU | GLU | SER | LYS | GLY | LEU | GLU | ALA | LEU | ASN | ||||
| 4 | LYS | ALA | ILE | VAL | SER | GLY | THR | VAL | GLN | ARG | ||||
| 5 | ALA | ASP | GLY | SER | ILE | GLN | ASN | GLN | SER | LEU | ||||
| 6 | HIS | GLU | ALA | LEU | ILE | THR | ARG | ASP | ARG | LYS | ||||
| 7 | GLN | VAL | PHE | ARG | ILE | GLU | ASP | SER | ILE | PRO | ||||
| 8 | VAL | LEU | LEU | PRO | GLU | GLU | ALA | ILE | ALA | THR | ||||
| 9 | ILE | GLN | ILE | ALA | ASN | PHE | PRO | ASP | LYS | LEU | ||||
| 10 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: XfR39, [U-100% 13C; U-100% 15N], 1.0 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%; DSS 50 uM
sample_2: XfR39, [U-5% 13C; U-100% 15N], 1.0 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%; DSS 50 uM
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293 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 |
| 2D 1H-13C HSQC_armatic | 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D simutaeous NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY_aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC_high resolution | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection
AutoAssign v2.2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
SPARKY v3.110, Goddard - data analysis, peak picking
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
PSVS v1.3, Bhattacharya and Montelione - data analysis
PDBStat v5.0, Tejero and Montelione - PDBanalysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| GB | AAF85470 AAO29861 ACA13079 ACB93534 ADN62897 |
| REF | WP_004084759 WP_010895087 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts