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PDB ID: 2kd7
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
MolProbity Validation Chart
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NMR-STAR v3 text file.
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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 Vector: pET 21-23C
Data type | Count |
13C chemical shifts | 669 |
15N chemical shifts | 178 |
1H chemical shifts | 1129 |
residual dipolar couplings | 137 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | btr324b | 1 |
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 |
PDB | 2KD7 3GGL |
EMBL | CDE80156 CUM72398 CUO89228 CUP77803 |
GB | AAO75972 ALJ42041 EES70459 EOS01998 |
REF | NP_809778 WP_008765703 WP_011107501 WP_016267553 WP_048697480 |
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