BMRB Entry 15352
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Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15352
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Title: NMR Structure of protein Q6N9A4_RHOPA:Northeast Structural Genomics Consortium Target RpT8
Deposition date: 2007-06-29 Original release date: 2007-08-29
Authors: SINGARAPU, KIRAN KUMAR; WU, YIBING; YEE, ADELINDA; ELETSKY, ALEX; SUKUMARAN, DINESH; GARCIA, MAITE; XIAO, RONG; BANSAL, SONAL; BARAN, MICHAEL; GAETANO, MONTELIONE; JAMES, PRESTEGARD; ARROWSMITH, CHERYL; SZYPERSKI, THOMAS
Citation: SINGARAPU, KIRAN KUMAR; WU, YIBING; YEE, ADELINDA; ELETSKY, ALEX; SUKUMARAN, DINESH; GARCIA, MAITE; XIAO, RONG; BANSAL, SONAL; BARAN, MICHAEL; GAETANO, MONTELIONE; JAMES, PRESTEGARD; ARROWSMITH, CHERYL; SZYPERSKI, THOMAS. "NMR Structure of protein Q6N9A4_RHOPA" . ., .-..
Assembly members:
rpt8 dimer, polymer, 192 residues, 20891.723 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: E. coli - cell free
Entity Sequences (FASTA):
rpt8 dimer: MGSSHHHHHHSSGRENLYFQ
GMTDTAAEDVRKIATALLKT
AIEIVSEEDGGAHNQCKLCG
ASVPWLQTGDEIKHADDCPV
VIAKQILSSRPKLHAVMGSS
HHHHHHSSGRENLYFQGMTD
TAAEDVRKIATALLKTAIEI
VSEEDGGAHNQCKLCGASVP
WLQTGDEIKHADDCPVVIAK
QILSSRPKLHAV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 357 |
| 15N chemical shifts | 87 |
| 1H chemical shifts | 586 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | chain1 | 1 |
| 2 | chain2 | 1 |
Entities:
Entity 1, chain1 192 residues - 20891.723 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | ARG | GLU | ASN | LEU | TYR | PHE | GLN | ||||
| 3 | GLY | MET | THR | ASP | THR | ALA | ALA | GLU | ASP | VAL | ||||
| 4 | ARG | LYS | ILE | ALA | THR | ALA | LEU | LEU | LYS | THR | ||||
| 5 | ALA | ILE | GLU | ILE | VAL | SER | GLU | GLU | ASP | GLY | ||||
| 6 | GLY | ALA | HIS | ASN | GLN | CYS | LYS | LEU | CYS | GLY | ||||
| 7 | ALA | SER | VAL | PRO | TRP | LEU | GLN | THR | GLY | ASP | ||||
| 8 | GLU | ILE | LYS | HIS | ALA | ASP | ASP | CYS | PRO | VAL | ||||
| 9 | VAL | ILE | ALA | LYS | GLN | ILE | LEU | SER | SER | ARG | ||||
| 10 | PRO | LYS | LEU | HIS | ALA | VAL | MET | GLY | SER | SER | ||||
| 11 | HIS | HIS | HIS | HIS | HIS | HIS | SER | SER | GLY | ARG | ||||
| 12 | GLU | ASN | LEU | TYR | PHE | GLN | GLY | MET | THR | ASP | ||||
| 13 | THR | ALA | ALA | GLU | ASP | VAL | ARG | LYS | ILE | ALA | ||||
| 14 | THR | ALA | LEU | LEU | LYS | THR | ALA | ILE | GLU | ILE | ||||
| 15 | VAL | SER | GLU | GLU | ASP | GLY | GLY | ALA | HIS | ASN | ||||
| 16 | GLN | CYS | LYS | LEU | CYS | GLY | ALA | SER | VAL | PRO | ||||
| 17 | TRP | LEU | GLN | THR | GLY | ASP | GLU | ILE | LYS | HIS | ||||
| 18 | ALA | ASP | ASP | CYS | PRO | VAL | VAL | ILE | ALA | LYS | ||||
| 19 | GLN | ILE | LEU | SER | SER | ARG | PRO | LYS | LEU | HIS | ||||
| 20 | ALA | VAL |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 0.5 mM
sample_2: entity, [U-50% 13C; U-50% 15N], 0.5 mM
sample_conditions_1: ionic strength: 300 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D simNOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D filtered NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMR, Varian - collection
CYANA, Guntert, Mumenthaler and Wuthrich - refinement
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
Molmol, Koradi, Billeter and Wuthrich - structure solution
NMR spectrometers:
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
- Bruker DRX 800 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts