BMRB Entry 19673
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19673
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Title: NMR structure of p75 transmembrane domain in DPC micelles
Deposition date: 2013-12-12 Original release date: 2014-12-22
Authors: Nadezhdin, Kirill; Arseniev, Alexander; Goncharuk, Sergey; Mineev, Konstantin
Citation: Nadezhdin, Kirill; Arseniev, Alexander; Goncharuk, Sergey; Mineev, Konstantin; Vilar, Mar al. "Structure of dimeric p75 neurotrophin receptor transmembrane domain provides insight on neurotrophin signaling" Not known ., .-..
Assembly members:
p75-TM-wt, polymer, 41 residues, 4562.378 Da.
Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free
Entity Sequences (FASTA):
p75-TM-wt: MTRGTTDNLIPVYCSILAAV
VVGLVAYIAFKRWNSSKQNK
Q
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 170 |
15N chemical shifts | 42 |
1H chemical shifts | 291 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | p75 transmembrane domain, 1 | 1 |
2 | p75 transmembrane domain, 2 | 1 |
Entities:
Entity 1, p75 transmembrane domain, 1 41 residues - 4562.378 Da.
1 | MET | THR | ARG | GLY | THR | THR | ASP | ASN | LEU | ILE | ||||
2 | PRO | VAL | TYR | CYS | SER | ILE | LEU | ALA | ALA | VAL | ||||
3 | VAL | VAL | GLY | LEU | VAL | ALA | TYR | ILE | ALA | PHE | ||||
4 | LYS | ARG | TRP | ASN | SER | SER | LYS | GLN | ASN | LYS | ||||
5 | GLN |
Samples:
sample_1: p75-TM-wt, [U-100% 13C; U-100% 15N], 1.9 mM; DPC, [U-98% 2H], 95 mM; sodium phosphate 20 mM; H2O 95%; D2O 5%
sample_conditions_1: pH: 5.9; pressure: 1 atm; temperature: 318 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 15N- and 13C-edited NOESY and 15N,13C-F1-filtered/F3-edited-NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.0, Bruker Biospin - collection, data analysis, processing
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
CARA, Keller, R - chemical shift assignment, data analysis, peak picking
TALOS-N, Yang Shen, and Ad Bax - angles constrains prediction
NMR spectrometers:
- Bruker Avance 800 MHz
- 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