BMRB Entry 25402
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25402
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Title: Solution structure of the full length sorting nexin 3 PubMed: 25893673
Deposition date: 2014-12-20 Original release date: 2015-08-13
Authors: Lenoir, Marc; Rajesh, Sandya; Gruenberg, Jean; Overduin, Michael; Kaur, Jaswant
Citation: Overduin, Michael; Rajesh, Sandya; Gruenberg, Jean; Lenoir, Marc. "Secondary structure and 1H, 13C, 15N resonance assignments of the endosomal sorting protein sorting nexin 3" Biomol. NMR Assign. 9, 355-358 (2015).
Assembly members:
SNX3FL, polymer, 172 residues, 19924.6031 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):
SNX3FL: MAHHHHHHVGTAETVADTRR
LITKPQNLNDAYGPPSNFLE
IDVSNPQTVGVGRGRFTTYE
IRVKTNLPIFKLKESTVRRR
YSDFEWLRSELERESKVVVP
PLPGKAFLRQLPFRGDDGIF
DDNFIEERKQGLEQFINKVA
GHPLAQNERCLHMFLQDEII
DKSYTPSKIRHA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 729 |
15N chemical shifts | 165 |
1H chemical shifts | 1177 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | SNX3FL | 1 |
Entities:
Entity 1, SNX3FL 172 residues - 19924.6031 Da.
1 | MET | ALA | HIS | HIS | HIS | HIS | HIS | HIS | VAL | GLY | ||||
2 | THR | ALA | GLU | THR | VAL | ALA | ASP | THR | ARG | ARG | ||||
3 | LEU | ILE | THR | LYS | PRO | GLN | ASN | LEU | ASN | ASP | ||||
4 | ALA | TYR | GLY | PRO | PRO | SER | ASN | PHE | LEU | GLU | ||||
5 | ILE | ASP | VAL | SER | ASN | PRO | GLN | THR | VAL | GLY | ||||
6 | VAL | GLY | ARG | GLY | ARG | PHE | THR | THR | TYR | GLU | ||||
7 | ILE | ARG | VAL | LYS | THR | ASN | LEU | PRO | ILE | PHE | ||||
8 | LYS | LEU | LYS | GLU | SER | THR | VAL | ARG | ARG | ARG | ||||
9 | TYR | SER | ASP | PHE | GLU | TRP | LEU | ARG | SER | GLU | ||||
10 | LEU | GLU | ARG | GLU | SER | LYS | VAL | VAL | VAL | PRO | ||||
11 | PRO | LEU | PRO | GLY | LYS | ALA | PHE | LEU | ARG | GLN | ||||
12 | LEU | PRO | PHE | ARG | GLY | ASP | ASP | GLY | ILE | PHE | ||||
13 | ASP | ASP | ASN | PHE | ILE | GLU | GLU | ARG | LYS | GLN | ||||
14 | GLY | LEU | GLU | GLN | PHE | ILE | ASN | LYS | VAL | ALA | ||||
15 | GLY | HIS | PRO | LEU | ALA | GLN | ASN | GLU | ARG | CYS | ||||
16 | LEU | HIS | MET | PHE | LEU | GLN | ASP | GLU | ILE | ILE | ||||
17 | ASP | LYS | SER | TYR | THR | PRO | SER | LYS | ILE | ARG | ||||
18 | HIS | ALA |
Samples:
Assignments: SNX3FL, [U-100% 13C; U-100% 15N], 0.5 mM; NaCl 100 mM; Sodium phosphate 20 mM
CondSet1: ionic strength: 0.100 M; pH: 6.5; pressure: 1.000 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC/HMQC | Assignments | isotropic | CondSet1 |
3D HNCA | Assignments | isotropic | CondSet1 |
3D HN(CO)CA | Assignments | isotropic | CondSet1 |
3D HNCO | Assignments | isotropic | CondSet1 |
3D CBCA(CO)NH | Assignments | isotropic | CondSet1 |
3D HNCACB | Assignments | isotropic | CondSet1 |
3D HNCO | Assignments | isotropic | CondSet1 |
3D HN(CA)CO | Assignments | isotropic | CondSet1 |
3D HCCH-TOCSY | Assignments | isotropic | CondSet1 |
3D 1H-13C NOESY | Assignments | isotropic | CondSet1 |
3D 1H-15N NOESY | Assignments | isotropic | CondSet1 |
2D 1H-13C HSQC | Assignments | isotropic | CondSet1 |
Software:
CcpNmr_Analysis v2.2, CCPN, Linge, O'Donoghue and Nilges - chemical shift calculation, data analysis, structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian UnityInova 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts