BMRB Entry 17026
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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/BMR17026
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Title: Solution NMR Structure of protein BT2368 from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR375
Deposition date: 2010-06-29 Original release date: 2010-08-23
Authors: Eletsky, Alexander; Lee, Hsiau-Wei; Wang, Dongyan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas
Citation: Eletsky, Alexander; Lee, Hsiau-Wei; Wang, Dongyan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of protein BT2368 from Bacteroides thetaiotaomicron" To be published ., .-..
Assembly members:
BtR375, polymer, 82 residues, 9220.528 Da.
Natural source: Common Name: B. thetaiotaomicron Taxonomy ID: 818 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacteroides thetaiotaomicron
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BtR375: MDKKIVGANAGKVWHALNEA
DGISIPELARKVNLSVESTA
LAVGWLARENKVVIERKNGL
IEIYNEGHFDFSFGLEHHHH
HH
| Data type | Count |
| 13C chemical shifts | 334 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 554 |
| residual dipolar couplings | 94 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BtR375_1 | 1 |
| 2 | BtR375_2 | 1 |
Entities:
Entity 1, BtR375_1 82 residues - 9220.528 Da.
Residues 75-82 represent a non-native affinity tag
| 1 | MET | ASP | LYS | LYS | ILE | VAL | GLY | ALA | ASN | ALA | ||||
| 2 | GLY | LYS | VAL | TRP | HIS | ALA | LEU | ASN | GLU | ALA | ||||
| 3 | ASP | GLY | ILE | SER | ILE | PRO | GLU | LEU | ALA | ARG | ||||
| 4 | LYS | VAL | ASN | LEU | SER | VAL | GLU | SER | THR | ALA | ||||
| 5 | LEU | ALA | VAL | GLY | TRP | LEU | ALA | ARG | GLU | ASN | ||||
| 6 | LYS | VAL | VAL | ILE | GLU | ARG | LYS | ASN | GLY | LEU | ||||
| 7 | ILE | GLU | ILE | TYR | ASN | GLU | GLY | HIS | PHE | ASP | ||||
| 8 | PHE | SER | PHE | GLY | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 9 | HIS | HIS |
Samples:
NC5_PAAG: BtR375, [U-5% 13C; U-100% 15N], 1.2 mM; ammonium acetate 18 mM; sodium chloride 91 mM; calcium chloride 4.6 mM; sodium azide 0.018%; H2O 80%; D2O 20%
NC: BtR375, [U-100% 13C; U-100% 15N], 1.1 mM; ammonium acetate 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.02%; H2O 90%; D2O 10%
NC5: BtR375, [U-5% 13C; U-100% 15N], 1.1 mM; ammonium acetate 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.02%; H2O 90%; D2O 10%
NC5_PEG: BtR375, [U-5% 13C; U-100% 15N], 0.9 mM; ammonium acetate 18 mM; sodium chloride 91 mM; calcium chloride 4.6 mM; sodium azide 0.018%; C12E5 polyethylene glycol 4%; hexanol 4%; H2O 80%; D2O 20%
sample_conditions_1: pH: 6.5; pressure: 1 .; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC aliphatic | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HNCACB | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC aromatic | NC | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | NC | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | NC | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HCCH-COSY aliphatic | NC | isotropic | sample_conditions_1 |
| 3D HCCH-COSY aromatic | NC | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY aliphatic | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC methyl | NC5 | isotropic | sample_conditions_1 |
| 2D J-modulation 1H-15N HSQC | NC5 | isotropic | sample_conditions_1 |
| 2D J-modulation 1H-15N HSQC | NC5_PEG | anisotropic | sample_conditions_1 |
| 2D J-modulation 1H-15N HSQC | NC5_PAAG | anisotropic | sample_conditions_1 |
| 2D 1H-15N LR-HSQC for Histidine | NC | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis
AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY v1.3.13, Bartels et al. - data analysis
TOPSPIN v2.1, Bruker Biospin - collection, processing
VNMRJ v2.1B, Varian - collection
TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - geometry optimization
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
PROSA v6.4, Guntert - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| EMBL | CDE77590 CUN18104 CUQ04359 CUQ17116 |
| GB | AAO77475 ALJ40308 EES66434 EFI02088 EOS01101 |
| REF | NP_811281 WP_008763800 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts