BMRB Entry 16805
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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/BMR16805
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Title: Solution NMR of the specialized acyl carrier protein (RPA2022) from Rhodopseudomonas palustris, Northeast Structural Genomics Consortium Target RpR324
Deposition date: 2010-03-30 Original release date: 2010-04-28
Authors: Rossi, P.; Lee, H; Valafar, H.; Lemak, A.; Wang, H.; Ciccosanti, C.; Mao, L.; Rost, B.; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.
Citation: Rossi, Paolo; Lee, Hsiau-Wei; Valafar, Homayoun; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.. "Solution NMR of the specialized acyl carrier protein (RPA2022) from Rhodopseudomonas palustris, Northeast Structural Genomics Consortium Target RpR324" To be published ., .-..
Assembly members:
RpR324, polymer, 101 residues, 11309.831 Da.
Natural source: Common Name: Rhodopseudomonas palustris Taxonomy ID: 1076 Superkingdom: Bacteria Kingdom: not available Genus/species: Rhodopseudomonas palustris
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RpR324: MTSTFDRVATIIAETCDIPR
ETITPESHAIDDLGIDSLDF
LDIAFAIDKAFGIKLPLEKW
TQEVNDGKATTEQYFVLKNL
AARIDELVAAKGALEHHHHH
H
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 428 |
| 15N chemical shifts | 99 |
| 1H chemical shifts | 683 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RpR324 | 1 |
Entities:
Entity 1, RpR324 101 residues - 11309.831 Da.
| 1 | MET | THR | SER | THR | PHE | ASP | ARG | VAL | ALA | THR | ||||
| 2 | ILE | ILE | ALA | GLU | THR | CYS | ASP | ILE | PRO | ARG | ||||
| 3 | GLU | THR | ILE | THR | PRO | GLU | SER | HIS | ALA | ILE | ||||
| 4 | ASP | ASP | LEU | GLY | ILE | ASP | SER | LEU | ASP | PHE | ||||
| 5 | LEU | ASP | ILE | ALA | PHE | ALA | ILE | ASP | LYS | ALA | ||||
| 6 | PHE | GLY | ILE | LYS | LEU | PRO | LEU | GLU | LYS | TRP | ||||
| 7 | THR | GLN | GLU | VAL | ASN | ASP | GLY | LYS | ALA | THR | ||||
| 8 | THR | GLU | GLN | TYR | PHE | VAL | LEU | LYS | ASN | LEU | ||||
| 9 | ALA | ALA | ARG | ILE | ASP | GLU | LEU | VAL | ALA | ALA | ||||
| 10 | LYS | GLY | ALA | LEU | GLU | HIS | HIS | HIS | HIS | HIS | ||||
| 11 | HIS |
Samples:
sample: RpR324, [U-100% 13C; U-100% 15N], 1.1 mM; sodium chloride 0.2 M; DTT 10 mM; DSS 5 uM; sodium azide 0.02%; MES 20 mM; calcium chloride 5 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample | isotropic | sample_conditions_1 |
| 3D HNCO | sample | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample | isotropic | sample_conditions_1 |
| 3D HNCACB | sample | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample | anisotropic | sample_conditions_1 |
| 3D HNCO | sample | anisotropic | sample_conditions_1 |
| 15N T1 | sample | isotropic | sample_conditions_1 |
| 15N T2 CPMG | sample | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinemen, structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
SPARKY, Goddard - data analysis
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PALES, PALES (Zweckstetter, Bax) - geometry optimization
REDCAT, Valafar, Prestegard - geometry optimization
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Varian INOVA 600 MHz
Related Database Links:
| BMRB | 18032 18263 |
| PDB | |
| EMBL | CAE27463 |
| GB | ABD08049 ABE39325 ACF00754 ADU45059 KPF96758 |
| REF | WP_011157577 WP_011442233 WP_054163491 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts