BMRB Entry 51519
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51519
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Khan, Naushaba; Graham, Tavawn; Franciszkiewicz, Katarzyna; Bloch, Sylwia; Nejman-Falenczyk, Bozena; Wegrzyn, Alicja; Donaldson, Logan. "The NMR structure of the Orf63 lytic developmental protein from lambda bacteriophage" Sci. Rep. 14, 3793-3793 (2024).
PubMed: 38360900
Assembly members:
entity_1, polymer, 77 residues, Formula weight is not available
Natural source: Common Name: Bacteriophage sp. Taxonomy ID: 38018 Superkingdom: Viruses Kingdom: not available Genus/species: lambda bacteriophage lambda bacteriophage
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pD441NH
Entity Sequences (FASTA):
entity_1: HHHHHHMDYKDDDDKHKASS
VELRTSIEMAHSLAQIGIRF
VPIPVETDEEFHTLAASLSQ
KLEMMVAKAEADERNQV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 183 |
| 15N chemical shifts | 41 |
| 1H chemical shifts | 266 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | orf63 | 1 |
Entities:
Entity 1, orf63 77 residues - Formula weight is not available
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | MET | ASP | TYR | LYS | ||||
| 2 | ASP | ASP | ASP | ASP | LYS | HIS | LYS | ALA | SER | SER | ||||
| 3 | VAL | GLU | LEU | ARG | THR | SER | ILE | GLU | MET | ALA | ||||
| 4 | HIS | SER | LEU | ALA | GLN | ILE | GLY | ILE | ARG | PHE | ||||
| 5 | VAL | PRO | ILE | PRO | VAL | GLU | THR | ASP | GLU | GLU | ||||
| 6 | PHE | HIS | THR | LEU | ALA | ALA | SER | LEU | SER | GLN | ||||
| 7 | LYS | LEU | GLU | MET | MET | VAL | ALA | LYS | ALA | GLU | ||||
| 8 | ALA | ASP | GLU | ARG | ASN | GLN | VAL |
Samples:
sample_1: orf63, [U-99% 13C; U-99% 15N], 0.6 mM; TRIS 10 mM; sodium chloride 100 mM; sodium azide 0.05%
sample_conditions_1: pH: 7.6; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-12C filtered 1H-13C edited NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
ANALYSIS v2.52 - data analysis
NMRPipe v10.9 Rev 2021.051.13.12 - processing
CYANA v3.0 - structure solution
Rosetta v2021.16.6162 - structure solution
NMR spectrometers:
- Bruker AVANCE III 700 MHz
- Varian INOVA 600 MHz
Related Database Links:
| NCBI | NP_040614.1 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks