BMRB Entry 16107
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16107
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Title: Solution NMR structure of F5/8 type C-terminal domain of a putative chitobiase from Bacteroides thetaiotaomicron. Northeast Structural Genomics Consortium target BtR324B
Deposition date: 2009-01-04 Original release date: 2009-03-02
Authors: Eletsky, Alexander; Mills, Jeffrey; Lee, Hsiau-Wei; Lee, Dong Yup; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Prestegard, James; Szyperski, Thomas
Citation: Eletsky, Alexander; Mills, Jeffrey; Lee, Hsiau-Wei; Lee, Dong Yup; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Prestegard, James; Szyperski, Thomas. "Solution NMR structure of F5/8 type C-terminal domain of a putative chitobiase from Bacteroides thetaiotaomicron." Proteins: Struct. Funct. Genet. ., .-..
Assembly members:
btr324b, polymer, 159 residues, 17550.711 Da.
Natural source: Common Name: Bacteroides 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):
btr324b: MGTTISKSGWEVLSFTTQEA
SGEGAGNGLAKCLIDGDTET
FWHAKWQGGSDPLPYDIVID
MKQNIQIAQVELLPRGRGSN
NPIKVVEFAASEDNVNWTPI
GRFGFTNQDAALEYYVKSIK
ARYIRLTIPDDGGNSTVAAI
RELDVKGTIINLEHHHHHH
- assigned_chemical_shifts
- RDCs
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 669 |
| 15N chemical shifts | 178 |
| 1H chemical shifts | 1129 |
| residual dipolar couplings | 137 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | btr324b | 1 |
Entities:
Entity 1, btr324b 159 residues - 17550.711 Da.
Residues 2-151 correspond to the C-terminal residues 291-440 in the wild-type protein. Residue 1 is due to addition of a start codon. Residues 152-159 represent a non-native affinity tag. A K4T mutation was introduced during cloning
| 1 | MET | GLY | THR | THR | ILE | SER | LYS | SER | GLY | TRP | ||||
| 2 | GLU | VAL | LEU | SER | PHE | THR | THR | GLN | GLU | ALA | ||||
| 3 | SER | GLY | GLU | GLY | ALA | GLY | ASN | GLY | LEU | ALA | ||||
| 4 | LYS | CYS | LEU | ILE | ASP | GLY | ASP | THR | GLU | THR | ||||
| 5 | PHE | TRP | HIS | ALA | LYS | TRP | GLN | GLY | GLY | SER | ||||
| 6 | ASP | PRO | LEU | PRO | TYR | ASP | ILE | VAL | ILE | ASP | ||||
| 7 | MET | LYS | GLN | ASN | ILE | GLN | ILE | ALA | GLN | VAL | ||||
| 8 | GLU | LEU | LEU | PRO | ARG | GLY | ARG | GLY | SER | ASN | ||||
| 9 | ASN | PRO | ILE | LYS | VAL | VAL | GLU | PHE | ALA | ALA | ||||
| 10 | SER | GLU | ASP | ASN | VAL | ASN | TRP | THR | PRO | ILE | ||||
| 11 | GLY | ARG | PHE | GLY | PHE | THR | ASN | GLN | ASP | ALA | ||||
| 12 | ALA | LEU | GLU | TYR | TYR | VAL | LYS | SER | ILE | LYS | ||||
| 13 | ALA | ARG | TYR | ILE | ARG | LEU | THR | ILE | PRO | ASP | ||||
| 14 | ASP | GLY | GLY | ASN | SER | THR | VAL | ALA | ALA | ILE | ||||
| 15 | ARG | GLU | LEU | ASP | VAL | LYS | GLY | THR | ILE | ILE | ||||
| 16 | ASN | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
NC5_peg: btr324b, [U-5% 13C; U-100% 15N], 1.1 mM; ammonium acetate 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02 mM
NC: btr324b, [U-100% 13C; U-100% 15N], 1.1 mM; ammonium acetate 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02 mM
NC5: btr324b, [U-5% 13C; U-100% 15N], 1.1 mM; ammonium acetate 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02 mM
NC5_paag: btr324b, [U-5% 13C; U-100% 15N], 1.1 mM; ammonium acetate 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02 mM
sample_conditions_1: ionic strength: 215 mM; pH: 4.5; pressure: 1.0 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC ali | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC ali | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC aro | NC | isotropic | sample_conditions_1 |
| 1D 1H-15N HSQC T1 | NC | isotropic | sample_conditions_1 |
| 1D 1H-15N HSQC T2 | 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 |
| 3D HBHA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSY ali | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY ali | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSY aro | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY aro | NC | isotropic | sample_conditions_1 |
| 2D 1H-15N LR-HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-15N MEXICO | NC | isotropic | sample_conditions_1 |
| 3D 1H-15N/13Cali/13Caro NOESY | NC | isotropic | sample_conditions_1 |
| 3D 1H-13Cali NOESY | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC methyl LV | NC5 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | NC5 | isotropic | sample_conditions_1 |
| 2D 1H-13C TROSY | NC5 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | NC5_paag | anisotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | NC5_paag | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | NC5_peg | anisotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | NC5_peg | anisotropic | sample_conditions_1 |
Software:
VNMRJ v2.1B, Varian - collection
TOPSPIN v2.1, Bruker Biospin - collection, processing
PROSA v6.0.2, Guntert - processing
CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
TALOS v2007.068.09.07, Cornilescu, Delaglio and Bax - data analysis
CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
PSVS v1.3, Bhattacharya and Montelione - structure validation
NMR spectrometers:
- Bruker Avance 900 MHz
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| EMBL | CDE80156 CUM72398 CUO89228 CUP77803 |
| GB | AAO75972 ALJ42041 EES70459 EOS01998 |
| REF | NP_809778 WP_008765703 WP_011107501 WP_016267553 WP_048697480 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts