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
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Title: Telokin-like domain (TL-domain) from P22 coat protein PubMed: 22987227
Deposition date: 2012-07-03 Original release date: 2012-11-02
Authors: Rizzo, Alessandro; Fraser, LaTasha; Sheftic, Sarah; Suhanovsky, Margaret; Teschke, Carolyn; Alexandrescu, Andrei
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).
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
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: 273 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
Related Database Links:
PDB | |
DBJ | BAD15215 BAF80720 BAG12603 BAJ35317 BAP06070 |
EMBL | CAR60452 CBG23391 CBY96612 CCR48948 CCT21055 |
GB | AAA72963 AAF75047 AAL15527 AAM81389 AAX21429 |
REF | NP_059630 NP_720329 WP_001196931 WP_001196932 WP_001196933 |
SP | P26747 |
TPG | DAA00987 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts