BMRB Entry 15825
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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/BMR15825
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Title: Solution NMR Structure of Putative Lipoprotein from Pseudomonas syringae Gene Locus PSPTO2350. Northeast Structural Genomics Target PsR76A.
Deposition date: 2008-06-25 Original release date: 2008-07-14
Authors: Hang, Dehua; Aramini, James; Rossi, Paolo; Wang, Dongyan; Jiang, Mei; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation: Rossi, Paolo; Aramini, James; Hang, Dehua; Xiao, Rong; Acton, Thomas; Montelione, Gaetano. "Solution NMR Structure of Putative Lipoprotein from Pseudomonas syringae Gene Locus PSPTO2350. Northeast Structural Genomics Target PsR76A" Not known ., .-..
Assembly members:
PsR76A, polymer, 55 residues, 6340.105 Da.
Natural source: Common Name: Pseudomonas syringae Taxonomy ID: 317 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas syringae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PsR76A: MASPTVITLNDGREIQAVDT
PKYDEESGFYEFKQLDGKQT
RINKDQVRTVKDLLE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 246 |
| 15N chemical shifts | 59 |
| 1H chemical shifts | 390 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PsR76A | 1 |
Entities:
Entity 1, PsR76A 55 residues - 6340.105 Da.
truncated lipobox: MKQRTLPAAFLLALSIASLAGC M1 cloning artifact A2 is residue 23 in original sequence
| 1 | MET | ALA | SER | PRO | THR | VAL | ILE | THR | LEU | ASN | ||||
| 2 | ASP | GLY | ARG | GLU | ILE | GLN | ALA | VAL | ASP | THR | ||||
| 3 | PRO | LYS | TYR | ASP | GLU | GLU | SER | GLY | PHE | TYR | ||||
| 4 | GLU | PHE | LYS | GLN | LEU | ASP | GLY | LYS | GLN | THR | ||||
| 5 | ARG | ILE | ASN | LYS | ASP | GLN | VAL | ARG | THR | VAL | ||||
| 6 | LYS | ASP | LEU | LEU | GLU |
Samples:
sample_1: PsR76A, [U-100% 13C; U-100% 15N], 1.07 mM; DSS 50 uM; DTT 10 mM; sodium chloride 100 mM; sodium azide 0.02%; MES 20 mM; calcium chloride 5 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_2: PsR76A, [5% 13C; U-100% 15N], 1.07 mM; DSS 50 uM; DTT 10 mM; sodium chloride 100 mM; sodium azide 0.02%; MES 20 mM; calcium chloride 5 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (aliph) | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC CT ARO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C-15N SIM NOESY | sample_1 | isotropic | sample_conditions_1 |
| N15-T1 | sample_1 | isotropic | sample_conditions_1 |
| N15-T2(CPMG) | sample_1 | isotropic | sample_conditions_1 |
| 3J NHHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CC(CO)NH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H, 15N HETNOE | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC STEREO | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN v2.1, Bruker Biospin - collection
SPARKY v3.113, Goddard - data analysis
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
RPF(AutoStructure) v2.2.1, Huang, Tejero, Powers and Montelione - validation
Molmol, Koradi, Billeter and Wuthrich - visualization
PSVS, Bhattacharya and Montelione - validation
PDBStat v5.0, Tejero R.; Montelione GT - validation
MolProbity, Richardson - validation
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - validation
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| SWS | Q883K7_PSESM |
| PDB | |
| GB | AAZ36497 ALD96182 EFH99818 EFW80354 EFW84604 |
| REF | WP_002553129 WP_044343779 WP_054995082 WP_057446476 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts