BMRB Entry 17942
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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/BMR17942
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Title: 1H, 13C and 15N resonance assignment of a complex constisting of hDlg/SAP-97 residues 318-406 and HPV type 51 E6 protein residues 141-151 PubMed: 22392342
Deposition date: 2011-09-15 Original release date: 2012-03-09
Authors: Mischo, Andre; Ohlenschlaeger, Oliver; Goerlach, Matthias
Citation: Mischo, Andre; Ohlenschlager, Oliver; Ramachandran, Ramadurai; Gorlach, Matthias. "NMR assignment of a PDZ domain in complex with a HPV51 E6 derived N-terminally pyroglutamic acid modified peptide." Biomol. NMR Assignments 7, 47-49 (2013).
Assembly members:
hDlg, polymer, 97 residues, Formula weight is not available
E6_protein_fragment_of_HPV_type_51, polymer, 11 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
hDlg: MEIKLIKGPKGLGFSIAGGV
GNQHIPGDNSIYVTKIIEGG
AAHKDGKLQIGDKLLAVNNV
CLEEVTHEEAVTALKNTSDF
VYLKVAKPTGSHHHHHH
E6_protein_fragment_of_HPV_type_51: XRTRQRNETQV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 460 |
| 15N chemical shifts | 111 |
| 1H chemical shifts | 737 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PDZ domain | 1 |
| 2 | peptide | 2 |
Entities:
Entity 1, PDZ domain 97 residues - Formula weight is not available
Sequence starts with M318. Residues 407-411 represent chemical shifts from a linker and hexahistideine tag (starting with GSHH...)
| 1 | MET | GLU | ILE | LYS | LEU | ILE | LYS | GLY | PRO | LYS | ||||
| 2 | GLY | LEU | GLY | PHE | SER | ILE | ALA | GLY | GLY | VAL | ||||
| 3 | GLY | ASN | GLN | HIS | ILE | PRO | GLY | ASP | ASN | SER | ||||
| 4 | ILE | TYR | VAL | THR | LYS | ILE | ILE | GLU | GLY | GLY | ||||
| 5 | ALA | ALA | HIS | LYS | ASP | GLY | LYS | LEU | GLN | ILE | ||||
| 6 | GLY | ASP | LYS | LEU | LEU | ALA | VAL | ASN | ASN | VAL | ||||
| 7 | CYS | LEU | GLU | GLU | VAL | THR | HIS | GLU | GLU | ALA | ||||
| 8 | VAL | THR | ALA | LEU | LYS | ASN | THR | SER | ASP | PHE | ||||
| 9 | VAL | TYR | LEU | LYS | VAL | ALA | LYS | PRO | THR | GLY | ||||
| 10 | SER | HIS | HIS | HIS | HIS | HIS | HIS |
Entity 2, peptide 11 residues - Formula weight is not available
residue 141 (first residue in sequence) exists as pyroglutamic acid (PGL)
| 1 | PCA | ARG | THR | ARG | GLN | ARG | ASN | GLU | THR | GLN | ||||
| 2 | VAL |
Samples:
sample_1: hDlg, [U-100% 13C; U-100% 15N], 0.8 mM; E6 protein fragment of HPV type 51 2 mM; sodium phosphate 20 mM; TCEP 4 mM; sodium azide 0.05%
sample_2: hDlg, [U-100% 13C; U-100% 15N], 0.8 mM; E6 protein fragment of HPV type 51 2 mM; sodium phosphate 20 mM; TCEP 4 mM; sodium azide 0.05%
sample_3: hDlg 3 mM; E6 protein fragment of HPV type 51, [U-100% 13C; U-100% 15N], 1.25 mM; sodium phosphate 20 mM; TCEP 4 mM; sodium azide 0.05%
sample_4: hDlg 3 mM; E6 protein fragment of HPV type 51, [U-100% 13C; U-100% 15N], 1.25 mM; sodium phosphate 20 mM; TCEP 4 mM; sodium azide 0.05%
sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_3 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_4 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_4 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_4 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
CARA, Rochus Keller - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts