BMRB Entry 15324
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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/BMR15324
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Title: A novel domain-swapped solution NMR structure of protein RPA2121 from Rhodopseudomonas palustris
Deposition date: 2007-06-21 Original release date: 2009-10-09
Authors: Wu, Bin; Yee, Adelinda; Lemak, Alexander; Cort, John; Bansal, Sonal; Semest, Anthony; Guido, Valerie; Kennedy, Michael; Prestegard, James; Arrowsmith, Cheryl
Citation: Wu, Bin; Yee, Adelinda; Lemak, Alexander; Cort, John; Bansal, Sonal; Semest, Anthony; Guido, Valerie; Kennedy, Michael; Prestegard, James; Arrowsmith, Cheryl. "A novel domain-swapped solution NMR structure of protein RPA2121 from Rhodopseudomonas palustris" Not known ., .-..
Assembly members:
unknown_function_protein_RPA2121, polymer, 67 residues, Formula weight is not available
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):
unknown_function_protein_RPA2121: MMTASDRLGADPTQAASSPG
GARAVSIVGNQIDSRELFTV
DREIVIAHGDDRYRLRLTSQ
NKLILTK
- assigned_chemical_shifts
- spectral_peak_list
Data type | Count |
13C chemical shifts | 267 |
15N chemical shifts | 64 |
1H chemical shifts | 446 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | subunit 1 | 1 |
2 | subunit 2 | 1 |
Entities:
Entity 1, subunit 1 67 residues - Formula weight is not available
1 | MET | MET | THR | ALA | SER | ASP | ARG | LEU | GLY | ALA | ||||
2 | ASP | PRO | THR | GLN | ALA | ALA | SER | SER | PRO | GLY | ||||
3 | GLY | ALA | ARG | ALA | VAL | SER | ILE | VAL | GLY | ASN | ||||
4 | GLN | ILE | ASP | SER | ARG | GLU | LEU | PHE | THR | VAL | ||||
5 | ASP | ARG | GLU | ILE | VAL | ILE | ALA | HIS | GLY | ASP | ||||
6 | ASP | ARG | TYR | ARG | LEU | ARG | LEU | THR | SER | GLN | ||||
7 | ASN | LYS | LEU | ILE | LEU | THR | LYS |
Samples:
sample_1: unknown function protein RPA2121, [U-99% 13C; U-99% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; sodium azide 0.01%; benzamidine 1 mM
sample_2: unknown function protein RPA2121, [U-7% 13C; U-99% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; sodium azide 0.01%; benzamidine 1 mM
sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
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(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNHA | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
2D IPAP 15N-HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.95, Goddard - data analysis, peak picking
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CNS v1.0, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStruct v2.1.0, Huang, Tejero, Powers and Montelione - Validation
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts