BMRB Entry 15438
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15438
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Title: Solution structure of IPI* PubMed: 18037438
Deposition date: 2007-08-17 Original release date: 2008-06-26
Authors: Rifat, Dalin; Wright, Nathan; Varney, Kristen; Weber, David; Black, Lindsay
Citation: Rifat, Dalin; Wright, Nathan; Varney, Kristen; Weber, David; Black, Lindsay. "Restriction endonuclease inhibitor IPI* of bacteriophage T4: a novel structure for a dedicated target" J. Mol. Biol. 375, 720-734 (2008).
Assembly members:
IP1*, polymer, 76 residues, 8060.466 Da.
Natural source: Common Name: T4 phage Taxonomy ID: 10665 Superkingdom: Viruses Kingdom: not available Genus/species: T4-like viruses Enterobacteria phage T4 sensu lato
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
IP1*: ATLTSEVIKANKGREGKPMI
SLVDGEEIKGTVYLGDGWSA
KKDGATIVISPAEETALFKA
KHISAAHLKIIAKNLL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 221 |
| 15N chemical shifts | 72 |
| 1H chemical shifts | 452 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | IP1* | 1 |
Entities:
Entity 1, IP1* 76 residues - 8060.466 Da.
| 1 | ALA | THR | LEU | THR | SER | GLU | VAL | ILE | LYS | ALA | ||||
| 2 | ASN | LYS | GLY | ARG | GLU | GLY | LYS | PRO | MET | ILE | ||||
| 3 | SER | LEU | VAL | ASP | GLY | GLU | GLU | ILE | LYS | GLY | ||||
| 4 | THR | VAL | TYR | LEU | GLY | ASP | GLY | TRP | SER | ALA | ||||
| 5 | LYS | LYS | ASP | GLY | ALA | THR | ILE | VAL | ILE | SER | ||||
| 6 | PRO | ALA | GLU | GLU | THR | ALA | LEU | PHE | LYS | ALA | ||||
| 7 | LYS | HIS | ILE | SER | ALA | ALA | HIS | LEU | LYS | ILE | ||||
| 8 | ILE | ALA | LYS | ASN | LEU | LEU |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 500 mM; sodium acetate 20 mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 20 mM; pH: 4.8; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D 15N-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D 13C-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker DMX 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts