BMRB Entry 30129
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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/BMR30129
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Title: Solution NMR Structure of Denovo Beta Sheet Design Protein, Northeast Structural Genomics Consortium (NESG) Target OR485
Deposition date: 2016-07-04 Original release date: 2016-09-23
Authors: Tang, Y.; Liu, G.; Montelione, G.; Northeast Structural Genomics Consortium (NESG), NESG
Citation: Tang, Y.; Liu, G.; Montelione, G.. "Solution NMR Structure of Denovo Beta Sheet Design Protein, Northeast Structural Genomics Consortium (NESG) Target OR485" . ., .-..
Assembly members:
entity_1, polymer, 85 residues, 10097.393 Da.
Natural source: Common Name: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MPSEEEEKRQVKQVAKEKLL
EQSPNSKVQVRRVQKQGNTI
RVELELRTNGKKENYTVEVE
RQGNTWTVKRITRTVGSLEH
HHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 337 |
| 15N chemical shifts | 80 |
| 1H chemical shifts | 573 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 85 residues - 10097.393 Da.
| 1 | MET | PRO | SER | GLU | GLU | GLU | GLU | LYS | ARG | GLN | ||||
| 2 | VAL | LYS | GLN | VAL | ALA | LYS | GLU | LYS | LEU | LEU | ||||
| 3 | GLU | GLN | SER | PRO | ASN | SER | LYS | VAL | GLN | VAL | ||||
| 4 | ARG | ARG | VAL | GLN | LYS | GLN | GLY | ASN | THR | ILE | ||||
| 5 | ARG | VAL | GLU | LEU | GLU | LEU | ARG | THR | ASN | GLY | ||||
| 6 | LYS | LYS | GLU | ASN | TYR | THR | VAL | GLU | VAL | GLU | ||||
| 7 | ARG | GLN | GLY | ASN | THR | TRP | THR | VAL | LYS | ARG | ||||
| 8 | ILE | THR | ARG | THR | VAL | GLY | SER | LEU | GLU | HIS | ||||
| 9 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: OR485, [U-99% 13C; U-99% 15N], 0.80 ± 0.2 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.5; 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 aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNcoCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D SIMUTANEOUS 13C-AROMATIC, 13-CALIPHATIC,15N EDITED 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-AROMATIC NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
AutoStructure, Huang, Tejero, Powers and Montelione - refinement
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - peak picking
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
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