BMRB Entry 25868
Click here to enlarge.
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/BMR25868
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution NMR Structure of Designed Protein DA05R1, Northeast Structural Genomics Consortium (NESG) Target OR690
Deposition date: 2015-10-27 Original release date: 2015-11-23
Authors: Eletsky, Alexander; Federizon, Jasmin; Xu, Xianzhong; Pulavarti, S.V.S.R. Krishna; Jacobs, Tim; Kuhlman, Brian; Szyperski, Thomas
Citation: Jacobs, Tim; Xu, Xianzhong; Eletsky, Alexander; Federizon, Jasmin; Szyperski, Thomas; Kuhlman, Brian. "Design of Structurally Unique Proteins Using Strategies Inspired by Evolution" Not known ., .-..
Assembly members:
DA05R1, polymer, 208 residues, 23847.180 Da.
Natural source: Common Name: not available Taxonomy ID: not available 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):
DA05R1: ADENIAKFEKAYKKAEELNQ
GELMGRALYNIGLEKNKMGK
AREAAEYFFRAAIVFYKEHD
TDGLRRAAKSLKEAITAIPE
EEGRKEAKEMAKKAEEWLQA
EQNNADENIAKFEKAYKKAE
ELNQGELMGRALYNIGLEKN
KMGKAREAAEYFFRAAIVFY
KEHDTDGLRRAAKSLKEAIT
AIPEEEGRKEAKEMAKKAEE
WLQAEQNN
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 425 |
| 15N chemical shifts | 94 |
| 1H chemical shifts | 689 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DA05R1 | 1 |
Entities:
Entity 1, DA05R1 208 residues - 23847.180 Da.
| 1 | ALA | ASP | GLU | ASN | ILE | ALA | LYS | PHE | GLU | LYS | ||||
| 2 | ALA | TYR | LYS | LYS | ALA | GLU | GLU | LEU | ASN | GLN | ||||
| 3 | GLY | GLU | LEU | MET | GLY | ARG | ALA | LEU | TYR | ASN | ||||
| 4 | ILE | GLY | LEU | GLU | LYS | ASN | LYS | MET | GLY | LYS | ||||
| 5 | ALA | ARG | GLU | ALA | ALA | GLU | TYR | PHE | PHE | ARG | ||||
| 6 | ALA | ALA | ILE | VAL | PHE | TYR | LYS | GLU | HIS | ASP | ||||
| 7 | THR | ASP | GLY | LEU | ARG | ARG | ALA | ALA | LYS | SER | ||||
| 8 | LEU | LYS | GLU | ALA | ILE | THR | ALA | ILE | PRO | GLU | ||||
| 9 | GLU | GLU | GLY | ARG | LYS | GLU | ALA | LYS | GLU | MET | ||||
| 10 | ALA | LYS | LYS | ALA | GLU | GLU | TRP | LEU | GLN | ALA | ||||
| 11 | GLU | GLN | ASN | ASN | ALA | ASP | GLU | ASN | ILE | ALA | ||||
| 12 | LYS | PHE | GLU | LYS | ALA | TYR | LYS | LYS | ALA | GLU | ||||
| 13 | GLU | LEU | ASN | GLN | GLY | GLU | LEU | MET | GLY | ARG | ||||
| 14 | ALA | LEU | TYR | ASN | ILE | GLY | LEU | GLU | LYS | ASN | ||||
| 15 | LYS | MET | GLY | LYS | ALA | ARG | GLU | ALA | ALA | GLU | ||||
| 16 | TYR | PHE | PHE | ARG | ALA | ALA | ILE | VAL | PHE | TYR | ||||
| 17 | LYS | GLU | HIS | ASP | THR | ASP | GLY | LEU | ARG | ARG | ||||
| 18 | ALA | ALA | LYS | SER | LEU | LYS | GLU | ALA | ILE | THR | ||||
| 19 | ALA | ILE | PRO | GLU | GLU | GLU | GLY | ARG | LYS | GLU | ||||
| 20 | ALA | LYS | GLU | MET | ALA | LYS | LYS | ALA | GLU | GLU | ||||
| 21 | TRP | LEU | GLN | ALA | GLU | GLN | ASN | ASN |
Samples:
NC5: DA05R1, [U-5% 13C; U-15N], 660 uM; sodium phosphate 25 mM; sodium chloride 50 mM; sodium azide 0.02%; protein inhibitor cocktail 1 mM; DSS 50 uM
NC: DA05R1, [U-13C; U-15N], 1 mM; sodium phosphate 25 mM; sodium chloride 50 mM; sodium azide 0.02%; protein inhibitor cocktail 1 mM; DSS 50 uM
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D CT 1H-13C HSQC aliphatic | NC | isotropic | sample_conditions_1 |
| 2D CT 1H-13C HSQC aromatic | NC | isotropic | sample_conditions_1 |
| 3D 15N/13C-edited 1H-1H NOESY | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT HCCH-COSY aliphatic | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT HCCH-COSY aromatic | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | NC | isotropic | sample_conditions_1 |
| 3D HNCACB | NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC | isotropic | sample_conditions_1 |
| 2D CT 1H-13C HSQC aliphatic 28 ms | NC5 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | NC5 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | NC5 | isotropic | sample_conditions_1 |
Software:
PROSA v6.4, Guntert - processing
AS-DP v1.0, Huang, Tejero, Powers and Montelione - structure solution
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
XEASY v1.3.13, Bartels et al. - data analysis
VNMRJ v4.0, Varian - collection
TALOS-N, Cornilescu, Delaglio and Bax - geometry optimization
PSVS v1.5, Bhattacharya and Montelione - structure validation
AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts