BMRB Entry 30040
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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/BMR30040
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Title: Cell surface anchoring domain
Deposition date: 2016-03-23 Original release date: 2017-06-22
Authors: Guo, S.; Langelaan, D.
Citation: Guo, S.; Langelaan, D.; Phippen, S.; Smith, S.; Davies, P.. "Structural insight into host cell surface retention of a 1.5-MDa bacterial ice-binding adhesin" . ., .-..
Assembly members:
Antifreeze protein, polymer, 76 residues, 7826.605 Da.
Natural source: Common Name: g-proteobacteria Taxonomy ID: 178399 Superkingdom: Bacteria Kingdom: not available Genus/species: Marinomonas primoryensis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Antifreeze protein: GNAIGFITKLDGSVTVQSIN
GQERVLKLGDPIFFGETVLT
GGSGSVTIAFVDGTDVVIGG
DSIVEMTDEIYNTGDN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 317 |
| 15N chemical shifts | 82 |
| 1H chemical shifts | 490 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 76 residues - 7826.605 Da.
| 1 | GLY | ASN | ALA | ILE | GLY | PHE | ILE | THR | LYS | LEU | ||||
| 2 | ASP | GLY | SER | VAL | THR | VAL | GLN | SER | ILE | ASN | ||||
| 3 | GLY | GLN | GLU | ARG | VAL | LEU | LYS | LEU | GLY | ASP | ||||
| 4 | PRO | ILE | PHE | PHE | GLY | GLU | THR | VAL | LEU | THR | ||||
| 5 | GLY | GLY | SER | GLY | SER | VAL | THR | ILE | ALA | PHE | ||||
| 6 | VAL | ASP | GLY | THR | ASP | VAL | VAL | ILE | GLY | GLY | ||||
| 7 | ASP | SER | ILE | VAL | GLU | MET | THR | ASP | GLU | ILE | ||||
| 8 | TYR | ASN | THR | GLY | ASP | ASN |
Samples:
sample_1: CaCl2 2 mM; MgCl2 2 mM; MpAFP_RINM, [U-13C], 3 mM; TRIS 20 mM; sodium chloride 50 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA, Linge, O'Donoghue and Nilges - refinement
Analysis, CCPN - chemical shift assignment
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMR, Varian - collection
NMR spectrometers:
- 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