BMRB Entry 18228
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18228
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Title: Backbone and side chain assignment of TpbA PubMed: 22392344
Deposition date: 2012-01-27 Original release date: 2012-03-08
Authors: Koveal, Dorothy; Peti, Wolfgang; Page, Rebecca
Citation: Koveal, Dorothy; Jayasundera, Thusitha; Wood, Thomas; Peti, Wolfgang; Page, Rebecca. "Backbone and sidechain (1)H, (15)N and (13)C assignments of Tyrosine Phosphatase related to Biofilm formation A (TpbA) of Pseudomonas aeruginosa." Biomol. NMR Assignments 7, 57-59 (2013).
Assembly members:
TpbA, polymer, 193 residues, Formula weight is not available
Natural source: Common Name: Pseudomonas aeruginosa Taxonomy ID: 287 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas aeruginosa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
TpbA: GHMAETAAPRSPAWAQAVDP
SINLYRMSPTLYRSALPNAQ
SVALLQRLQVKTVVSFIKDD
DRAWLGQAPVRVVSLPTHAD
RVDDAEVLSVLRQLQAAERE
GPVLMHCKHGNNRTGLFAAM
YRIVVQGWDKQAALEEMQRG
GFGDEDDMRDASAYVRGADV
DGLRLAMANGECSPSRFALC
HVREWMAQALDRP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 542 |
| 15N chemical shifts | 172 |
| 1H chemical shifts | 1205 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TpbA monomer | 1 |
Entities:
Entity 1, TpbA monomer 193 residues - Formula weight is not available
G26, H27 and M28 are cloning artifacts.
| 1 | GLY | HIS | MET | ALA | GLU | THR | ALA | ALA | PRO | ARG | ||||
| 2 | SER | PRO | ALA | TRP | ALA | GLN | ALA | VAL | ASP | PRO | ||||
| 3 | SER | ILE | ASN | LEU | TYR | ARG | MET | SER | PRO | THR | ||||
| 4 | LEU | TYR | ARG | SER | ALA | LEU | PRO | ASN | ALA | GLN | ||||
| 5 | SER | VAL | ALA | LEU | LEU | GLN | ARG | LEU | GLN | VAL | ||||
| 6 | LYS | THR | VAL | VAL | SER | PHE | ILE | LYS | ASP | ASP | ||||
| 7 | ASP | ARG | ALA | TRP | LEU | GLY | GLN | ALA | PRO | VAL | ||||
| 8 | ARG | VAL | VAL | SER | LEU | PRO | THR | HIS | ALA | ASP | ||||
| 9 | ARG | VAL | ASP | ASP | ALA | GLU | VAL | LEU | SER | VAL | ||||
| 10 | LEU | ARG | GLN | LEU | GLN | ALA | ALA | GLU | ARG | GLU | ||||
| 11 | GLY | PRO | VAL | LEU | MET | HIS | CYS | LYS | HIS | GLY | ||||
| 12 | ASN | ASN | ARG | THR | GLY | LEU | PHE | ALA | ALA | MET | ||||
| 13 | TYR | ARG | ILE | VAL | VAL | GLN | GLY | TRP | ASP | LYS | ||||
| 14 | GLN | ALA | ALA | LEU | GLU | GLU | MET | GLN | ARG | GLY | ||||
| 15 | GLY | PHE | GLY | ASP | GLU | ASP | ASP | MET | ARG | ASP | ||||
| 16 | ALA | SER | ALA | TYR | VAL | ARG | GLY | ALA | ASP | VAL | ||||
| 17 | ASP | GLY | LEU | ARG | LEU | ALA | MET | ALA | ASN | GLY | ||||
| 18 | GLU | CYS | SER | PRO | SER | ARG | PHE | ALA | LEU | CYS | ||||
| 19 | HIS | VAL | ARG | GLU | TRP | MET | ALA | GLN | ALA | LEU | ||||
| 20 | ASP | ARG | PRO |
Samples:
sample_1: TpbA, [U-15N], 1.1 mM; TRIS 10 mM; sodium chloride 100 mM; TCEP 0.5 mM
sample_2: TpbA, [U-13C, U-15N], 1.0 mM; TRIS 10 mM; sodium chloride 100 mM; TCEP 0.5 mM
sample_3: TpbA 1.0 mM; TRIS 10 mM; sodium chloride 100 mM; TCEP 0.5 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 18977 |
| PDB | |
| DBJ | BAK91895 BAP20213 BAP49072 BAQ37900 BAR66014 |
| EMBL | CDH75498 CDM50177 CDO83381 CEI03735 CEI78250 |
| GB | AAG07272 AAT49761 ABJ13157 AFM63275 AGI79981 |
| REF | NP_252574 WP_003092976 WP_003105672 WP_003111594 WP_003118289 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts