BMRB Entry 18566
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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/BMR18566
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: Rizzo, Alessandro; Fraser, LaTasha; Sheftic, Sarah; Suhanovsky, Margaret; Teschke, Carolyn; Alexandrescu, Andrei. "NMR assignments for the telokin-like domain of bacteriophage P22 coat protein." Biomol. NMR Assignments 7, 257-260 (2013).
PubMed: 22987227
Assembly members:
TL-domain, polymer, 124 residues, Formula weight is not available
Natural source: Common Name: Enterobacteria phage P22 Taxonomy ID: 10754 Superkingdom: Viruses Kingdom: not available Genus/species: Bacteriophage P22
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET30b
Entity Sequences (FASTA):
TL-domain: GSTATGITVSGAQSFKPVAW
QLDNDGNKVNVDNRFATVTL
SATTGMKRGDKISFAGVKFL
GQMAKNVLAQDATFSVVRVV
DGTHVEITPKPVALDDVSLS
PEQRAYANVNTSLADAMAVN
ILNV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 511 |
| 15N chemical shifts | 119 |
| 1H chemical shifts | 804 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TL-domain | 1 |
Entities:
Entity 1, TL-domain 124 residues - Formula weight is not available
G222 is non-native glycine that was included as part of the thrombin cleavage site. but for the sake of the numbering scheme is included here as 222
| 1 | GLY | SER | THR | ALA | THR | GLY | ILE | THR | VAL | SER | ||||
| 2 | GLY | ALA | GLN | SER | PHE | LYS | PRO | VAL | ALA | TRP | ||||
| 3 | GLN | LEU | ASP | ASN | ASP | GLY | ASN | LYS | VAL | ASN | ||||
| 4 | VAL | ASP | ASN | ARG | PHE | ALA | THR | VAL | THR | LEU | ||||
| 5 | SER | ALA | THR | THR | GLY | MET | LYS | ARG | GLY | ASP | ||||
| 6 | LYS | ILE | SER | PHE | ALA | GLY | VAL | LYS | PHE | LEU | ||||
| 7 | GLY | GLN | MET | ALA | LYS | ASN | VAL | LEU | ALA | GLN | ||||
| 8 | ASP | ALA | THR | PHE | SER | VAL | VAL | ARG | VAL | VAL | ||||
| 9 | ASP | GLY | THR | HIS | VAL | GLU | ILE | THR | PRO | LYS | ||||
| 10 | PRO | VAL | ALA | LEU | ASP | ASP | VAL | SER | LEU | SER | ||||
| 11 | PRO | GLU | GLN | ARG | ALA | TYR | ALA | ASN | VAL | ASN | ||||
| 12 | THR | SER | LEU | ALA | ASP | ALA | MET | ALA | VAL | ASN | ||||
| 13 | ILE | LEU | ASN | VAL |
Samples:
TL-domain-13C_15N: TL-domain, [U-13C; U-15N], 1.5 mM; sodium phosphate 20 mM; sodium azide 0.2 % w/v
TL-domain-13C_15N_in_D2O: TL-domain, [U-13C; U-15N], 1.5 mM; sodium phosphate 20 mM; sodium azide 0.2 % w/v
TL-domain-15N: TL-domain, [U-15N], 1.5 mM; sodium phosphate 20 mM; sodium azide 0.2 % w/v
TL-domain-unlabelled: TL-domain 1.5 mM; sodium phosphate 20 mM; sodium azide 0.2 % w/v
sample_condition_1: ionic strength: 20 mM; pH: 6.00; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | TL-domain-15N | isotropic | sample_condition_1 |
| 2D 1H-13C HSQC | TL-domain-13C_15N_in_D2O | isotropic | sample_condition_1 |
| 2D DQF-COSY | TL-domain-unlabelled | isotropic | sample_condition_1 |
| 2D DQF-TOCSY | TL-domain-unlabelled | isotropic | sample_condition_1 |
| 3D C(CO)NH | TL-domain-13C_15N | isotropic | sample_condition_1 |
| 3D HNCO | TL-domain-13C_15N | isotropic | sample_condition_1 |
| 3D HNCA | TL-domain-13C_15N | isotropic | sample_condition_1 |
| 3D HNCACB | TL-domain-13C_15N | isotropic | sample_condition_1 |
| 3D HN(CO)CA | TL-domain-13C_15N | isotropic | sample_condition_1 |
| 3D H(CCO)NH | TL-domain-13C_15N | isotropic | sample_condition_1 |
| 3D HCCH-TOCSY | TL-domain-13C_15N_in_D2O | isotropic | sample_condition_1 |
| 3D HNHA | TL-domain-15N | isotropic | sample_condition_1 |
| 3D 1H-15N NOESY | TL-domain-15N | isotropic | sample_condition_1 |
| 3D 1H-15N NOESY | TL-domain-15N | isotropic | sample_condition_1 |
| 3D HNHB | TL-domain-15N | isotropic | sample_condition_1 |
| 3D HN(CA)CO | TL-domain-13C_15N | isotropic | sample_condition_1 |
| 2D H-H NOESY (50ms) | TL-domain-unlabelled | isotropic | sample_condition_1 |
| 3D CCH-TOCSY | TL-domain-13C_15N_in_D2O | isotropic | sample_condition_1 |
Software:
FELIX, Accelrys Software Inc. - processing
ANALYSIS, CCPN - chemical shift assignment
VNMRJ, Varian - collection
NMR spectrometers:
- 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