BMRB Entry 15810
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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/BMR15810
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Title: Solution structure of uncharacterized protein PA1076 from Pseudomonas aeruginosa. Northeast Structural Genomics Consortium (NESG) target PaT3, Ontario Center for Structural Proteomics target PA1076.
Deposition date: 2008-06-19 Original release date: 2009-04-23
Authors: Gutmanas, Aleksandras; Lemak, Alexander; Fares, Christophe; Yee, Adelinda; Semesi, Anthony; Arrowsmith, Cheryl
Citation: Gutmanas, Aleksandras; Lemak, Alexander; Fares, Christophe; Yee, Adelinda; Semesi, Anthony; Arrowsmith, Cheryl. "Solution structure of uncharacterized protein PA1076 from Pseudomonas aeruginosa." Not known ., .-..
Assembly members:
PA1076, polymer, 125 residues, 14233.955 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):
PA1076: QGHMFEPGHLHLVSLPGLDQ
QDINIHIRYEVRQNAESGAY
VHFDMDGEIDGKPFSDSFEL
PRDTAFNFASDATRVAQKHG
LHPKFGAITRVHKEYDAMFE
DIRAKLHAHPGEPVDLERII
RHEGS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 500 |
| 15N chemical shifts | 102 |
| 1H chemical shifts | 797 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PA1076 | 1 |
Entities:
Entity 1, PA1076 125 residues - 14233.955 Da.
| 1 | GLN | GLY | HIS | MET | PHE | GLU | PRO | GLY | HIS | LEU | ||||
| 2 | HIS | LEU | VAL | SER | LEU | PRO | GLY | LEU | ASP | GLN | ||||
| 3 | GLN | ASP | ILE | ASN | ILE | HIS | ILE | ARG | TYR | GLU | ||||
| 4 | VAL | ARG | GLN | ASN | ALA | GLU | SER | GLY | ALA | TYR | ||||
| 5 | VAL | HIS | PHE | ASP | MET | ASP | GLY | GLU | ILE | ASP | ||||
| 6 | GLY | LYS | PRO | PHE | SER | ASP | SER | PHE | GLU | LEU | ||||
| 7 | PRO | ARG | ASP | THR | ALA | PHE | ASN | PHE | ALA | SER | ||||
| 8 | ASP | ALA | THR | ARG | VAL | ALA | GLN | LYS | HIS | GLY | ||||
| 9 | LEU | HIS | PRO | LYS | PHE | GLY | ALA | ILE | THR | ARG | ||||
| 10 | VAL | HIS | LYS | GLU | TYR | ASP | ALA | MET | PHE | GLU | ||||
| 11 | ASP | ILE | ARG | ALA | LYS | LEU | HIS | ALA | HIS | PRO | ||||
| 12 | GLY | GLU | PRO | VAL | ASP | LEU | GLU | ARG | ILE | ILE | ||||
| 13 | ARG | HIS | GLU | GLY | SER |
Samples:
sample_H2O: PA1076, [U-100% 13C; U-100% 15N], 0.7-1 mM; TRIS, [U-2H], 10 mM; sodium chloride 300 mM; sodium azide 0.01%; benzamidine 1 mM; inhibitor cocktail 1 x
sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_H2O | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_H2O | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_H2O | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_H2O | isotropic | sample_conditions_1 |
| 3D HNCO | sample_H2O | isotropic | sample_conditions_1 |
| 3D HNCA | sample_H2O | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_H2O | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_H2O | isotropic | sample_conditions_1 |
| 3D H(C)CH-TOCSY | sample_H2O | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_H2O | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_H2O | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_H2O | isotropic | sample_conditions_1 |
| 3D 1H-13C aromatic NOESY | sample_H2O | isotropic | sample_conditions_1 |
| 3D H(C)CH-TOCSY aromatic | sample_H2O | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY aromatic | sample_H2O | isotropic | sample_conditions_1 |
| T1rho array | sample_H2O | isotropic | sample_conditions_1 |
| 3D IPAP E-COSY HNCO | sample_H2O | isotropic | sample_conditions_1 |
| 3D IPAP E-COSY HNCO | sample_H2O | anisotropic | sample_conditions_1 |
Software:
ANALYSIS v1.4, CCPN - chemical shift assignment, peak picking
MDDNMR v1.2c, V. Orekhov, I. Ibraghimov - processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
ABACUS, A. Lemak - chemical shift assignment, NOE assignment
CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
- Bruker Avance 500 MHz
Related Database Links:
| PDB | |
| DBJ | BAK88798 BAP20653 BAP52231 BAQ41330 BAR69178 |
| EMBL | CAW29000 CCQ87961 CDH72383 CDH78643 CDI89206 |
| GB | AAG04465 AAT49383 ABJ10241 ABR82558 AEO76449 |
| REF | NP_249767 WP_003082140 WP_003111391 WP_003149705 WP_023099857 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts