BMRB Entry 30321
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30321
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of the sorting nexin 25 phox-homology domain PubMed: 30948714
Deposition date: 2017-08-01 Original release date: 2018-07-30
Authors: Chin, Y.; Mas, C.; Mobli, M.; Collins, B.
Citation: Chandra, Mintu; Chin, Yanni K-Y; Mas, Caroline; Feathers, J Ryan; Paul, Blessy; Datta, Sanchari; Chen, Kai-En; Jia, Xinying; Yang, Zhe; Norwood, Suzanne; Mohanty, Biswaranjan; Bugarcic, Andrea; Teasdale, Rohan; Henne, W Mike; Mobli, Mehdi; Collins, Brett. "Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities" Nat. Commun. 10, 1528-1528 (2019).
Assembly members:
entity_1, polymer, 125 residues, 14245.309 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
Entity Sequences (FASTA):
entity_1: GSNLGMWKASITSGEVTEEN
GEQLPCYFVMVSLQEVGGVE
TKNWTVPRRLSEFQNLHRKL
SECVPSLKKVQLPSLSKLPF
KSIDQKFMEKSKNQLNKFLQ
NLLSDERLCQSEALYAFLSP
SPDYL
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 535 |
| 15N chemical shifts | 131 |
| 1H chemical shifts | 886 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 125 residues - 14245.309 Da.
| 1 | GLY | SER | ASN | LEU | GLY | MET | TRP | LYS | ALA | SER | ||||
| 2 | ILE | THR | SER | GLY | GLU | VAL | THR | GLU | GLU | ASN | ||||
| 3 | GLY | GLU | GLN | LEU | PRO | CYS | TYR | PHE | VAL | MET | ||||
| 4 | VAL | SER | LEU | GLN | GLU | VAL | GLY | GLY | VAL | GLU | ||||
| 5 | THR | LYS | ASN | TRP | THR | VAL | PRO | ARG | ARG | LEU | ||||
| 6 | SER | GLU | PHE | GLN | ASN | LEU | HIS | ARG | LYS | LEU | ||||
| 7 | SER | GLU | CYS | VAL | PRO | SER | LEU | LYS | LYS | VAL | ||||
| 8 | GLN | LEU | PRO | SER | LEU | SER | LYS | LEU | PRO | PHE | ||||
| 9 | LYS | SER | ILE | ASP | GLN | LYS | PHE | MET | GLU | LYS | ||||
| 10 | SER | LYS | ASN | GLN | LEU | ASN | LYS | PHE | LEU | GLN | ||||
| 11 | ASN | LEU | LEU | SER | ASP | GLU | ARG | LEU | CYS | GLN | ||||
| 12 | SER | GLU | ALA | LEU | TYR | ALA | PHE | LEU | SER | PRO | ||||
| 13 | SER | PRO | ASP | TYR | LEU |
Samples:
sample_1: DTT 2 mM; HEPES 20 mM; NaCl 100 mM; SNX25, [U-99% 13C; U-99% 15N], 0.8 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | anisotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | anisotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | anisotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | anisotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | anisotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | anisotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | anisotropic | sample_conditions_1 |
Software:
Analysis, CCPN - chemical shift assignment, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation
Rowland NMR ToolKit, Gregory P. Mullen - processing
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker AvanceII 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts