BMRB Entry 34488
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34488
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Title: Designing a Granulopoietic Protein by Topological Rescaffolding 2: Moevan
Deposition date: 2020-02-06 Original release date: 2020-03-16
Authors: ElGamacy, M.; Coles, M.
Citation: ElGamacy, M.; Coles, M.. "Designing of novel granulopoietic proteins by topological rescaffolding" . ., .-..
Assembly members:
entity_1, polymer, 138 residues, 15645.854 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: MGSSHHHHHHSSGLVPRGSH
MEAAAAARDESAYLKLQEQM
RKIDADAAALSETRTIEELD
TFKLDVADFVTTVVQLAEEL
EHRFGRNRRGRTEIYKIVKE
VDRKLLDLTDAVLAKEKKGE
DILNMVAEIKALLINIYK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 428 |
| 15N chemical shifts | 89 |
| 1H chemical shifts | 623 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 138 residues - 15645.854 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | GLU | ALA | ALA | ALA | ALA | ALA | ARG | ASP | GLU | ||||
| 4 | SER | ALA | TYR | LEU | LYS | LEU | GLN | GLU | GLN | MET | ||||
| 5 | ARG | LYS | ILE | ASP | ALA | ASP | ALA | ALA | ALA | LEU | ||||
| 6 | SER | GLU | THR | ARG | THR | ILE | GLU | GLU | LEU | ASP | ||||
| 7 | THR | PHE | LYS | LEU | ASP | VAL | ALA | ASP | PHE | VAL | ||||
| 8 | THR | THR | VAL | VAL | GLN | LEU | ALA | GLU | GLU | LEU | ||||
| 9 | GLU | HIS | ARG | PHE | GLY | ARG | ASN | ARG | ARG | GLY | ||||
| 10 | ARG | THR | GLU | ILE | TYR | LYS | ILE | VAL | LYS | GLU | ||||
| 11 | VAL | ASP | ARG | LYS | LEU | LEU | ASP | LEU | THR | ASP | ||||
| 12 | ALA | VAL | LEU | ALA | LYS | GLU | LYS | LYS | GLY | GLU | ||||
| 13 | ASP | ILE | LEU | ASN | MET | VAL | ALA | GLU | ILE | LYS | ||||
| 14 | ALA | LEU | LEU | ILE | ASN | ILE | TYR | LYS |
Samples:
sample_1: Moevan, [U-99% 13C; U-99% 15N], 600 uM; PBS 50 mM
sample_conditions_1: ionic strength: 125 mM; pH: 5.2; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 125 mM; pH: 5.2; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_2 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_2 |
| 3D (H)CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CC(CO)NH | sample_1 | isotropic | sample_conditions_2 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_2 |
| 2D NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CNH-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CNH-NOESY | sample_1 | isotropic | sample_conditions_2 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin, Bruker Biospin - collection
Sparky, Goddard - chemical shift assignment
Rosetta, Baker - structure calculation
CoMAND, in house - refinement
NMR spectrometers:
- Bruker AVANCE III 600 MHz
- Bruker AVANCE III 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts