BMRB Entry 30821
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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/BMR30821
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Title: Solution Structure of the R2ab Repeat Domain from Staph. epidermidis Autolysin (AtlE)
Deposition date: 2020-12-01 Original release date: 2021-12-03
Authors: Yadav, R.; Perera, Y.; Fitzkee, N.
Citation: Perera, Y.; Yadav, R.; South, T.; McConnell, K.; Fitzkee, N.. "Solution Structure of the R2ab Repeat Domain from Staph. epidermidis Autolysin (AtlE)" .
Assembly members:
entity_1, polymer, 152 residues, 16739.672 Da.
Natural source: Common Name: Staphylococcus epidermidis Taxonomy ID: 1282 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus epidermidis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pET15b
Entity Sequences (FASTA):
entity_1: NNQLTVTNNSGVAQINAKNS
GLYTTVYDTKGKTTNQIQRT
LSVTKAATLGDKKFYLVGDY
NTGTNYGWVKQDEVIYNTAK
SPVKINQTYNVKPGVKLHTV
PWGTYNQVAGTVSGKGDQTF
KATKQQQIDKATYLYGTVNG
KSGWISKYYLTA
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 598 |
| 15N chemical shifts | 141 |
| 1H chemical shifts | 894 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 152 residues - 16739.672 Da.
| 1 | ASN | ASN | GLN | LEU | THR | VAL | THR | ASN | ASN | SER | ||||
| 2 | GLY | VAL | ALA | GLN | ILE | ASN | ALA | LYS | ASN | SER | ||||
| 3 | GLY | LEU | TYR | THR | THR | VAL | TYR | ASP | THR | LYS | ||||
| 4 | GLY | LYS | THR | THR | ASN | GLN | ILE | GLN | ARG | THR | ||||
| 5 | LEU | SER | VAL | THR | LYS | ALA | ALA | THR | LEU | GLY | ||||
| 6 | ASP | LYS | LYS | PHE | TYR | LEU | VAL | GLY | ASP | TYR | ||||
| 7 | ASN | THR | GLY | THR | ASN | TYR | GLY | TRP | VAL | LYS | ||||
| 8 | GLN | ASP | GLU | VAL | ILE | TYR | ASN | THR | ALA | LYS | ||||
| 9 | SER | PRO | VAL | LYS | ILE | ASN | GLN | THR | TYR | ASN | ||||
| 10 | VAL | LYS | PRO | GLY | VAL | LYS | LEU | HIS | THR | VAL | ||||
| 11 | PRO | TRP | GLY | THR | TYR | ASN | GLN | VAL | ALA | GLY | ||||
| 12 | THR | VAL | SER | GLY | LYS | GLY | ASP | GLN | THR | PHE | ||||
| 13 | LYS | ALA | THR | LYS | GLN | GLN | GLN | ILE | ASP | LYS | ||||
| 14 | ALA | THR | TYR | LEU | TYR | GLY | THR | VAL | ASN | GLY | ||||
| 15 | LYS | SER | GLY | TRP | ILE | SER | LYS | TYR | TYR | LEU | ||||
| 16 | THR | ALA |
Samples:
sample_1: Autolysin repeat domain (R2ab), [U-15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.02 % w/v
sample_2: Autolysin repeat domain (R2ab), [U-15N; U-13C], 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.02 % w/v
sample_3: Autolysin repeat domain (R2ab), [U-15N; U-13C], 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.02 % w/v
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D (H)C(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_3 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CARA v1.9v1, Keller and Wuthrich - chemical shift assignment, peak picking
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker AVANCE III 600 MHz
- Bruker AVANCE III HD 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts