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PDB ID: 2kl3
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/BMR16382
MolProbity Validation Chart
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NMR-STAR v3 text file.
XML gzip file.
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Citation: Eletsky, Alexander; Belote, Rachel; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Rost, Burkhard; Swapna, G.; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of the Rhodanese-like domain from Anabaena sp Alr3790 protein. Northeast Structural Genomics Consortium Target NsR437A" Proteins: Struct. Funct. Genet. ., .-..
Assembly members:
Alr3790, polymer, 132 residues, 14539.188 Da.
Natural source: Common Name: Anabaena sp. Taxonomy ID: 1167 Superkingdom: Bacteria Kingdom: not available Genus/species: Anabaena sp.
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C
Entity Sequences (FASTA):
Alr3790: MEPQSDAHVLKSRLEWGEPA
FTILDVRDRSTYNDGHIMGA
MAMPIEDLVDRASSSLEKSR
DIYVYGAGDEQTSQAVNLLR
SAGFEHVSELKGGLAAWKAI
GGPTEGIIESRTPAGADDYN
VVSRLEHHHHHH
Data type | Count |
13C chemical shifts | 534 |
15N chemical shifts | 143 |
1H chemical shifts | 857 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Alr3790 | 1 |
Entity 1, Alr3790 132 residues - 14539.188 Da.
Residues 2-124 correspond to the native residues 17-139. Residue 1 corresponds to the new start codon. Residues 125-132 represent a non-native affinity tag.
1 | MET | GLU | PRO | GLN | SER | ASP | ALA | HIS | VAL | LEU | ||||
2 | LYS | SER | ARG | LEU | GLU | TRP | GLY | GLU | PRO | ALA | ||||
3 | PHE | THR | ILE | LEU | ASP | VAL | ARG | ASP | ARG | SER | ||||
4 | THR | TYR | ASN | ASP | GLY | HIS | ILE | MET | GLY | ALA | ||||
5 | MET | ALA | MET | PRO | ILE | GLU | ASP | LEU | VAL | ASP | ||||
6 | ARG | ALA | SER | SER | SER | LEU | GLU | LYS | SER | ARG | ||||
7 | ASP | ILE | TYR | VAL | TYR | GLY | ALA | GLY | ASP | GLU | ||||
8 | GLN | THR | SER | GLN | ALA | VAL | ASN | LEU | LEU | ARG | ||||
9 | SER | ALA | GLY | PHE | GLU | HIS | VAL | SER | GLU | LEU | ||||
10 | LYS | GLY | GLY | LEU | ALA | ALA | TRP | LYS | ALA | ILE | ||||
11 | GLY | GLY | PRO | THR | GLU | GLY | ILE | ILE | GLU | SER | ||||
12 | ARG | THR | PRO | ALA | GLY | ALA | ASP | ASP | TYR | ASN | ||||
13 | VAL | VAL | SER | ARG | LEU | GLU | HIS | HIS | HIS | HIS | ||||
14 | HIS | HIS |
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