BMRB Entry 25263
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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/BMR25263
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Tripler, Therese; Maciejewski, Mark; Teschke, Carolyn; Alexandrescu, Andrei. "NMR assignments for the insertion domain of bacteriophage CUS-3 coat protein" Biomol. NMR Assign. 9, 333-336 (2015).
PubMed: 25694158
Assembly members:
CUS-3id, polymer, 126 residues, Formula weight is not available
Natural source: Common Name: Viruses Taxonomy ID: 38018 Superkingdom: Viruses Kingdom: not available Genus/species: CUS-3 Bacteriophage
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-21a
Entity Sequences (FASTA):
CUS-3id: MASGSTESLTVSGQPEHKVE
AKDSNGMPVDNRQGTITVSA
SGLQVGDAFTIAGVNSVHQI
TKDTTGQPQVFRVLAVSGTT
VTISPKILPVENTDVASRPY
ANVDAKPAESAAITILNKLE
HHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 461 |
| 15N chemical shifts | 119 |
| 1H chemical shifts | 742 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CUS-3id, chain 1 | 1 |
| 2 | CUS-3id, chain 2 | 1 |
Entities:
Entity 1, CUS-3id, chain 1 126 residues - Formula weight is not available
contains C-terminal 6x his-tag; additional residues: at N-terminus: MAS from vector design and C-terminus: LE
| 1 | MET | ALA | SER | GLY | SER | THR | GLU | SER | LEU | THR | ||||
| 2 | VAL | SER | GLY | GLN | PRO | GLU | HIS | LYS | VAL | GLU | ||||
| 3 | ALA | LYS | ASP | SER | ASN | GLY | MET | PRO | VAL | ASP | ||||
| 4 | ASN | ARG | GLN | GLY | THR | ILE | THR | VAL | SER | ALA | ||||
| 5 | SER | GLY | LEU | GLN | VAL | GLY | ASP | ALA | PHE | THR | ||||
| 6 | ILE | ALA | GLY | VAL | ASN | SER | VAL | HIS | GLN | ILE | ||||
| 7 | THR | LYS | ASP | THR | THR | GLY | GLN | PRO | GLN | VAL | ||||
| 8 | PHE | ARG | VAL | LEU | ALA | VAL | SER | GLY | THR | THR | ||||
| 9 | VAL | THR | ILE | SER | PRO | LYS | ILE | LEU | PRO | VAL | ||||
| 10 | GLU | ASN | THR | ASP | VAL | ALA | SER | ARG | PRO | TYR | ||||
| 11 | ALA | ASN | VAL | ASP | ALA | LYS | PRO | ALA | GLU | SER | ||||
| 12 | ALA | ALA | ILE | THR | ILE | LEU | ASN | LYS | LEU | GLU | ||||
| 13 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: insertion domain, [U-100% 15N], 1.9 mM; insertion domain, [U-100% 13C; U-100% 15N], 1.9 mM; H2O 90%; D2O 10%
sample_2: insertion domain, [U-100% 13C; U-100% 15N], 1.9 mM; D2O 100%
sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-C13 HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_2 | isotropic | sample_conditions_1 |
| 2D TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
Ccpnmr_analysis, CCPN - chemical shift assignment, peak picking
Felix, Accelrys Software Inc. - processing
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks