BMRB Entry 5706
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PDB ID: 1ny9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5706
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Kahmann, Jan; Sass, Hans Juergen; Allan, Martin; Seto, Haruo; Thompson, Charles; Grzesiek, Stephan. "Structural Basis for Antibiotic Recognition by the TipA Class of
Multidrug-resistance Transcriptional Regulators" EMBO J. 22, 1824-1834 (2003).
PubMed: 12682015
Assembly members:
Transcriptional activator tipA, polymer, 143 residues, 16432 Da.
Natural source: Common Name: Streptomyces lividans Taxonomy ID: 1916 Superkingdom: Eubacteria Kingdom: not available Genus/species: Streptomyces lividans
Experimental source: Production method: recombinant tecHology Host organism: Escherichia lividans Vector: pREP4 and pDS8
Entity Sequences (FASTA):
Transcriptional activator tipA: GINLTPEEKFEVFGDFDPDQ
YEEEVRERWGNTDAYRQSKE
KTASYTKEDWQRIQDEADEL
TRRFVALMDAGEPADSEGAM
DAAEDHRQGIARNHYDCGYE
MHTCLGEMYVSDERFTRNID
AAKPGLAAYMRDAILANAVR
HTP
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 473 |
| 13C chemical shifts | 345 |
| 15N chemical shifts | 103 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TipAS | 1 |
Entities:
Entity 1, TipAS 143 residues - 16432 Da.
| 1 | GLY | ILE | ASN | LEU | THR | PRO | GLU | GLU | LYS | PHE | ||||
| 2 | GLU | VAL | PHE | GLY | ASP | PHE | ASP | PRO | ASP | GLN | ||||
| 3 | TYR | GLU | GLU | GLU | VAL | ARG | GLU | ARG | TRP | GLY | ||||
| 4 | ASN | THR | ASP | ALA | TYR | ARG | GLN | SER | LYS | GLU | ||||
| 5 | LYS | THR | ALA | SER | TYR | THR | LYS | GLU | ASP | TRP | ||||
| 6 | GLN | ARG | ILE | GLN | ASP | GLU | ALA | ASP | GLU | LEU | ||||
| 7 | THR | ARG | ARG | PHE | VAL | ALA | LEU | MET | ASP | ALA | ||||
| 8 | GLY | GLU | PRO | ALA | ASP | SER | GLU | GLY | ALA | MET | ||||
| 9 | ASP | ALA | ALA | GLU | ASP | HIS | ARG | GLN | GLY | ILE | ||||
| 10 | ALA | ARG | ASN | HIS | TYR | ASP | CYS | GLY | TYR | GLU | ||||
| 11 | MET | HIS | THR | CYS | LEU | GLY | GLU | MET | TYR | VAL | ||||
| 12 | SER | ASP | GLU | ARG | PHE | THR | ARG | ASN | ILE | ASP | ||||
| 13 | ALA | ALA | LYS | PRO | GLY | LEU | ALA | ALA | TYR | MET | ||||
| 14 | ARG | ASP | ALA | ILE | LEU | ALA | ASN | ALA | VAL | ARG | ||||
| 15 | HIS | THR | PRO |
Related Database Links:
| BMRB | 19421 19422 |
| PDB | 1NY9 2MBZ 2MC0 |
| DBJ | BAD11210 BAD11216 BAD11222 BAD11228 BAD11234 |
| EMBL | CAB42766 |
| GB | AAB27737 AAC13653 AIJ15084 EFD68501 EHN72093 |
| REF | NP_627619 WP_003975420 |
| SP | P0A4T8 P0A4T9 |
| AlphaFold | P0A4T8 P0A4T9 |
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