BMRB Entry 19632
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19632
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Title: NMR structure of protein NP_254181.1 from Pseudomonas aeruginosa PA01
Deposition date: 2013-11-22 Original release date: 2013-12-20
Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of protein NP_254181.1 from Pseudomonas aeruginosa PA01" Not known ., .-..
Assembly members:
entity, polymer, 75 residues, 7154.342 Da.
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):
entity: GADDDAPSGEPDVTIRQEGD
KTIQEYRVNGFLYAIKVVPK
HGKPYFLVRADGSDGNFIRS
DQPDKLIPQWEIFSW
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 241 |
| 15N chemical shifts | 73 |
| 1H chemical shifts | 514 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | hypothetical protein BACUNI_03114 from Bacteroides uniformis ATCC 8492 | 1 |
Entities:
Entity 1, hypothetical protein BACUNI_03114 from Bacteroides uniformis ATCC 8492 75 residues - 7154.342 Da.
| 1 | GLY | ALA | ASP | ASP | ASP | ALA | PRO | SER | GLY | GLU | ||||
| 2 | PRO | ASP | VAL | THR | ILE | ARG | GLN | GLU | GLY | ASP | ||||
| 3 | LYS | THR | ILE | GLN | GLU | TYR | ARG | VAL | ASN | GLY | ||||
| 4 | PHE | LEU | TYR | ALA | ILE | LYS | VAL | VAL | PRO | LYS | ||||
| 5 | HIS | GLY | LYS | PRO | TYR | PHE | LEU | VAL | ARG | ALA | ||||
| 6 | ASP | GLY | SER | ASP | GLY | ASN | PHE | ILE | ARG | SER | ||||
| 7 | ASP | GLN | PRO | ASP | LYS | LEU | ILE | PRO | GLN | TRP | ||||
| 8 | GLU | ILE | PHE | SER | TRP |
Samples:
sample_1: entity, [U-99% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM
sample_2: entity, [U-99% 13C; U-98% 15N], 0.6 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; entity, [U-15N; U-2H], 0.6 mM
sample_conditions_1: ionic strength: 0.0798 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| APSY 4D-HACANH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-HACACONH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS, Bruker Biospin, Brunger A. T. et.al. - collection, processing, refinement
CARA, Keller and Wuthrich - chemical shift assignment, data analysis
j-UNIO, Herrmann, Guntert and Wuthrich - chemical shift assignment, data analysis, peak picking
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - collection
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAK93077 BAP25407 BAP54205 BAQ43445 BAR70992 |
| EMBL | CAW30644 CCQ84532 CDH74259 CDH80608 CDI94117 |
| GB | AAG08879 AAT49351 ABJ14880 ABR84127 AEO78092 |
| REF | NP_254181 WP_003096984 WP_003155462 WP_003161101 WP_017002432 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts