BMRB Entry 15652
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15652
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Title: Solution NMR structure of the uncharacterized protein from Rhodospirillum rubrum gene locus Rru_A0810. Northeast Structural Genomics Target RrR43.
Deposition date: 2008-02-04 Original release date: 2008-02-07
Authors: Rossi, Paolo; Wang, Huang; Jiang, Mei; Foote, Erica; Xiao, Rong; Liu, Jinfeng; Swapna, G.V.T.; Acton, Thomas; Baran, Michael; Rost, Burkhard; Montelione, Gaetano
Citation: Rossi, Paolo; Xiao, Rong; Acton, Thomas; Montelione, Gaetano. "Solution NMR structure of the uncharacterized protein from Rhodospirillum rubrum gene locus Rru_A0810. Northeast Structural Genomics Target RrR43." . ., .-..
Assembly members:
RrR43, polymer, 104 residues, 11870.668 Da.
Natural source: Common Name: Rhodospirillum rubrum Taxonomy ID: 1085 Superkingdom: Bacteria Kingdom: not available Genus/species: Rhodospirillum rubrum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RrR43: MAKAQPIEIAGHEFARKADA
LAFMKVMLNRYRPGDIVSTV
DGAFLVEALKRHPDATSKIG
PGVRNFEVRSADYGTQCFWI
LRTDGSEERFSYKKCVLEHH
HHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 435 |
| 15N chemical shifts | 90 |
| 1H chemical shifts | 677 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RrR43 | 1 |
Entities:
Entity 1, RrR43 104 residues - 11870.668 Da.
97-104 C-term LEHHHHHH Ni affinity tag.
| 1 | MET | ALA | LYS | ALA | GLN | PRO | ILE | GLU | ILE | ALA | ||||
| 2 | GLY | HIS | GLU | PHE | ALA | ARG | LYS | ALA | ASP | ALA | ||||
| 3 | LEU | ALA | PHE | MET | LYS | VAL | MET | LEU | ASN | ARG | ||||
| 4 | TYR | ARG | PRO | GLY | ASP | ILE | VAL | SER | THR | VAL | ||||
| 5 | ASP | GLY | ALA | PHE | LEU | VAL | GLU | ALA | LEU | LYS | ||||
| 6 | ARG | HIS | PRO | ASP | ALA | THR | SER | LYS | ILE | GLY | ||||
| 7 | PRO | GLY | VAL | ARG | ASN | PHE | GLU | VAL | ARG | SER | ||||
| 8 | ALA | ASP | TYR | GLY | THR | GLN | CYS | PHE | TRP | ILE | ||||
| 9 | LEU | ARG | THR | ASP | GLY | SER | GLU | GLU | ARG | PHE | ||||
| 10 | SER | TYR | LYS | LYS | CYS | VAL | LEU | GLU | HIS | HIS | ||||
| 11 | HIS | HIS | HIS | HIS |
Samples:
sample_1: RrR43, [U-5% 13C; U-100% 15N], 1.15 mM; MES 20 mM; DTT 10 mM; sodium azide 0.02%; sodium chloride 100 mM; DSS 50 uM; calcium chloride 5 mM
sample_2: RrR43, [U-100% 13C; U-100% 15N], 1.05 mM; MES 20 mM; DTT 10 mM; sodium azide 0.02%; sodium chloride 100 mM; DSS 50 uM; calcium chloride 5 mM
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 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (aliph) | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (stereomethyl) | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (arom) | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (arom) | sample_1 | 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
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PSVS, Bhattacharya and Montelione - validation
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
TOPSPIN v1.3, Bruker Biospin - collection
SPARKY v3.112, Goddard - data analysis
Molmol v2k2, Koradi, Billeter and Wuthrich - visualization
ProcheckNMR, Laskowski and MacArthur - refinement
MolProbity, Richardson - validation
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts