BMRB Entry 34154
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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/BMR34154
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Title: NMR spatial structure of HER2 TM domain dimer in DPC micelles PubMed: 29063258
Deposition date: 2017-06-26 Original release date: 2017-11-17
Authors: Mineev, K.; Arseniev, A.
Citation: Lesovoy, D.; Mineev, K.; Bragin, P.; Bocharova, O.; Bocharov, E.; Arseniev, A.. "NMR relaxation parameters of methyl groups as a tool to map the interfaces of helix-helix interactions in membrane proteins." J. Biomol. NMR 69, 165-179 (2017).
Assembly members:
entity_1, polymer, 44 residues, 4734.805 Da.
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 BL21(DE3)
Entity Sequences (FASTA):
entity_1: GCPAEQRASPLTSIISAVVG
ILLVVVLGVVFGILIKRRQQ
KIRK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 202 |
| 15N chemical shifts | 47 |
| 1H chemical shifts | 339 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1, 1 | 1 |
| 2 | entity_1, 2 | 1 |
Entities:
Entity 1, entity_1, 1 44 residues - 4734.805 Da.
| 1 | GLY | CYS | PRO | ALA | GLU | GLN | ARG | ALA | SER | PRO | ||||
| 2 | LEU | THR | SER | ILE | ILE | SER | ALA | VAL | VAL | GLY | ||||
| 3 | ILE | LEU | LEU | VAL | VAL | VAL | LEU | GLY | VAL | VAL | ||||
| 4 | PHE | GLY | ILE | LEU | ILE | LYS | ARG | ARG | GLN | GLN | ||||
| 5 | LYS | ILE | ARG | LYS |
Samples:
sample_1: DPC, [U-99% 2H], 200 mM; HER2TM 2.5 mM; HER2TM_label, [U-100% 13C; U-100% 15N], 2.5 mM; potassium phosphate 20 mM; sodium azide 0.01%
sample_conditions_1: ionic strength: 30 mM; pH: 6.0; pressure: 1 Pa; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-filtered NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation
TOPSPIN, Bruker Biospin - processing
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker av600 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts