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PDB ID: 2ko1
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/BMR16486
MolProbity Validation Chart
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NMR-STAR v3 text file.
XML gzip file.
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Citation: Eletsky, Alexander; Garcia, Erwin; Wang, Huang; Ciccosanti, Colleen; Jiang, Mei; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of the ACT domain from GTP pyrophosphokinase of Chlorobium tepidum." Proteins: Struct. Funct. Genet. ., .-..
Assembly members:
CtR148A, polymer, 88 residues, 10050.751 Da.
Natural source: Common Name: Chlorobium tepidum Taxonomy ID: 194439 Superkingdom: Bacteria Kingdom: not available Genus/species: Chlorobium tepidum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C
Entity Sequences (FASTA):
CtR148A: MTDFLAGIRIVGEDKNGMTN
QITGVISKFDTNIRTIVLNA
KDGIFTCNLMIFVKNTDKLT
TLMDKLRKVQGVFTVERLSN
LEHHHHHH
Data type | Count |
13C chemical shifts | 368 |
15N chemical shifts | 94 |
1H chemical shifts | 630 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
2 | entity_2 | 1 |
Entity 1, entity_1 88 residues - 10050.751 Da.
Residues 2-80 correspond to the 653-731 fragment of the native protein. Residues 81-88 represent a non-native affinity tag. Residue M1 is a result of a new start codon.
1 | MET | THR | ASP | PHE | LEU | ALA | GLY | ILE | ARG | ILE | ||||
2 | VAL | GLY | GLU | ASP | LYS | ASN | GLY | MET | THR | ASN | ||||
3 | GLN | ILE | THR | GLY | VAL | ILE | SER | LYS | PHE | ASP | ||||
4 | THR | ASN | ILE | ARG | THR | ILE | VAL | LEU | ASN | ALA | ||||
5 | LYS | ASP | GLY | ILE | PHE | THR | CYS | ASN | LEU | MET | ||||
6 | ILE | PHE | VAL | LYS | ASN | THR | ASP | LYS | LEU | THR | ||||
7 | THR | LEU | MET | ASP | LYS | LEU | ARG | LYS | VAL | GLN | ||||
8 | GLY | VAL | PHE | THR | VAL | GLU | ARG | LEU | SER | ASN | ||||
9 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
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