Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16069
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Citation: Guzzo, Cristiane; Salinas, Roberto; Andrade, Maxuel; Farah, Chuck. "PILZ protein structure and interactions with PILB and the FIMX EAL domain: implications for control of type IV pilus biogenesis." J. Mol. Biol. 393, 848-866 (2009).
PubMed: 19646999
Assembly members:
PilZ, polymer, 117 residues, Formula weight is not available
Natural source: Common Name: Xanthomonas axonopodis Taxonomy ID: 53413 Superkingdom: Bacteria Kingdom: not available Genus/species: Xanthomonas axonopodis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET3a
Entity Sequences (FASTA):
PilZ: MSAMNARQGILSLALKDKPA
LYSAYMPFVKGGGIFVPTPK
RYMLGDEVFLLLTLPDSSER
LPVAGKVIWTTPAGAQGNRA
AGIGVQFPDGPEGEAVRNKI
ETLLAGLTTSDKPTHTM
| Data type | Count |
| 13C chemical shifts | 184 |
| 15N chemical shifts | 93 |
| 1H chemical shifts | 93 |
| heteronuclear NOE values | 87 |
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PilZ | 1 |
Entity 1, PilZ 117 residues - Formula weight is not available
| 1 | MET | SER | ALA | MET | ASN | ALA | ARG | GLN | GLY | ILE | ||||
| 2 | LEU | SER | LEU | ALA | LEU | LYS | ASP | LYS | PRO | ALA | ||||
| 3 | LEU | TYR | SER | ALA | TYR | MET | PRO | PHE | VAL | LYS | ||||
| 4 | GLY | GLY | GLY | ILE | PHE | VAL | PRO | THR | PRO | LYS | ||||
| 5 | ARG | TYR | MET | LEU | GLY | ASP | GLU | VAL | PHE | LEU | ||||
| 6 | LEU | LEU | THR | LEU | PRO | ASP | SER | SER | GLU | ARG | ||||
| 7 | LEU | PRO | VAL | ALA | GLY | LYS | VAL | ILE | TRP | THR | ||||
| 8 | THR | PRO | ALA | GLY | ALA | GLN | GLY | ASN | ARG | ALA | ||||
| 9 | ALA | GLY | ILE | GLY | VAL | GLN | PHE | PRO | ASP | GLY | ||||
| 10 | PRO | GLU | GLY | GLU | ALA | VAL | ARG | ASN | LYS | ILE | ||||
| 11 | GLU | THR | LEU | LEU | ALA | GLY | LEU | THR | THR | SER | ||||
| 12 | ASP | LYS | PRO | THR | HIS | THR | MET |
sample_1: PilZ, [U-99% 13C; U-99% 15N], 0.5 mM; Tris buffer 5 mM; NaCl 150 mM
sample_2: PilZ, [U-99% 15N], 0.5 ± 0.05 mM; Tris buffer 5 mM; NaCl 150 mM
sample_conditions_1: ionic strength: 0.150 M; pH: 7.0; pressure: 1 atm; temperature: 300 K
sample_conditions_2: ionic strength: 0.150 M; pH: 7.0; temperature: 300 K
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 1H-15N NOE | sample_2 | isotropic | sample_conditions_2 |
Analysis_CCPN v1.0.14, CCPN - chemical shift assignment
| PDB | |
| DBJ | BAE67567 GAE49623 GAE57138 GAE61747 |
| EMBL | CAJ22783 CAP52699 CCF68085 CCG36105 CDF60728 |
| GB | AAM36006 AAM40324 AAW74141 AAY50265 ACD60951 |
| REF | NP_636400 WP_002814313 WP_003483889 WP_007969015 WP_011036225 |
Download HSQC peak lists in one of the following formats:
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