BMRB Entry 51520
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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/BMR51520
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title: bacteriophage lambda Ea22 C-terminal domain PubMed: 32548406
Deposition date: 2022-07-19 Original release date: 2023-07-19
Authors: Donaldson, Logan
Citation: Tong, Jinge; Nejman-Falenczyk, BoZena; Bloch, Sylwia; Wegrzyn, Alicja; Wegrzyn, Grzegorz; Donaldson, Logan. "Ea22 Proteins from Lambda and Shiga Toxin-Producing Bacteriophages Balance Structural Diversity with Functional Similarity" ACS Omega 5, 12236-12244 (2020).
Assembly members:
entity_1, polymer, 93 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: HHHHHHMSNEVREDGNQFLV
VRHPGKTPVIKHCTGDLEEF
LRQLIEQDPLVTIDIITHRY
YGVGGQWVQDAGEYLHMMSD
AGIRIKGEIETAV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 291 |
| 15N chemical shifts | 64 |
| 1H chemical shifts | 439 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ea22, chain 1 | 1 |
| 2 | ea22, chain 2 | 1 |
Entities:
Entity 1, ea22, chain 1 93 residues - Formula weight is not available
6x-His tagged protein fragment. The last five amino acids IETAV are non-native.
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | MET | SER | ASN | GLU | ||||
| 2 | VAL | ARG | GLU | ASP | GLY | ASN | GLN | PHE | LEU | VAL | ||||
| 3 | VAL | ARG | HIS | PRO | GLY | LYS | THR | PRO | VAL | ILE | ||||
| 4 | LYS | HIS | CYS | THR | GLY | ASP | LEU | GLU | GLU | PHE | ||||
| 5 | LEU | ARG | GLN | LEU | ILE | GLU | GLN | ASP | PRO | LEU | ||||
| 6 | VAL | THR | ILE | ASP | ILE | ILE | THR | HIS | ARG | TYR | ||||
| 7 | TYR | GLY | VAL | GLY | GLY | GLN | TRP | VAL | GLN | ASP | ||||
| 8 | ALA | GLY | GLU | TYR | LEU | HIS | MET | MET | SER | ASP | ||||
| 9 | ALA | GLY | ILE | ARG | ILE | LYS | GLY | GLU | ILE | GLU | ||||
| 10 | THR | ALA | VAL |
Samples:
sample_1: ea22, [U-99% 13C; U-99% 15N], 0.8 mM; TRIS 10 mM; sodium chloride 100 mM; sodium azide 0.05%
sample_conditions_1: ionic strength: 0.1 M; pH: 7.7; pressure: 1 atm; temperature: 305 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 |
| 3D CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 12C-filtered 13C-edited NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe v10.9 Rev 2021.051.13.12 - processing
ANALYSIS v2.52 - data analysis
CYANA v3.0 - structure solution
Rosetta v2021.16.61629 - refinement
NMR spectrometers:
- Bruker AVANCE III 700 MHz
- Varian INOVA 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts