Click here to enlarge.
PDB ID: 2jxc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15554
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Rumpf, Julia; Simon, Bernd; Groemping, Yvonne; Sattler, Michael. "1H, 13C, and 15N chemical shift assignments for the Eps15-EH2-stonin 2 complex" Biomol. NMR Assignments 2, 55-58 (2008).
PubMed: 19636924
Assembly members:
EH2, polymer, 100 residues, 10985.906 Da.
Stonin_peptide, polymer, 45 residues, 4998.502 Da.
CA, non-polymer, 40.078 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 Vector: pGEX6P1
Entity Sequences (FASTA):
EH2: GPLGSPWAVKPEDKAKYDAI
FDSLSPVNGFLSGDKVKPVL
LNSKLPVDILGRVWELSDID
HDGMLDRDEFAVAMFLVYCA
LEKEPVPMSLPPALVPPSKR
Stonin_peptide: GPLGSPSVTEASPWRATNPF
LNETLQDVQPSPINPFSAFF
EEQER
Data type | Count |
13C chemical shifts | 483 |
15N chemical shifts | 130 |
1H chemical shifts | 996 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | EH2 | 1 |
2 | Stonin | 2 |
3 | CA | 3 |
Entity 1, EH2 100 residues - 10985.906 Da.
residues 1-5 (GPLGS) in NMR structure calculations originate from the expression vector
1 | GLY | PRO | LEU | GLY | SER | PRO | TRP | ALA | VAL | LYS | |
2 | PRO | GLU | ASP | LYS | ALA | LYS | TYR | ASP | ALA | ILE | |
3 | PHE | ASP | SER | LEU | SER | PRO | VAL | ASN | GLY | PHE | |
4 | LEU | SER | GLY | ASP | LYS | VAL | LYS | PRO | VAL | LEU | |
5 | LEU | ASN | SER | LYS | LEU | PRO | VAL | ASP | ILE | LEU | |
6 | GLY | ARG | VAL | TRP | GLU | LEU | SER | ASP | ILE | ASP | |
7 | HIS | ASP | GLY | MET | LEU | ASP | ARG | ASP | GLU | PHE | |
8 | ALA | VAL | ALA | MET | PHE | LEU | VAL | TYR | CYS | ALA | |
9 | LEU | GLU | LYS | GLU | PRO | VAL | PRO | MET | SER | LEU | |
10 | PRO | PRO | ALA | LEU | VAL | PRO | PRO | SER | LYS | ARG |
Entity 2, Stonin 45 residues - 4998.502 Da.
residues 101-105 in NMR structure calculations originate from the expression vector
1 | GLY | PRO | LEU | GLY | SER | PRO | SER | VAL | THR | GLU | ||||
2 | ALA | SER | PRO | TRP | ARG | ALA | THR | ASN | PRO | PHE | ||||
3 | LEU | ASN | GLU | THR | LEU | GLN | ASP | VAL | GLN | PRO | ||||
4 | SER | PRO | ILE | ASN | PRO | PHE | SER | ALA | PHE | PHE | ||||
5 | GLU | GLU | GLN | GLU | ARG |
Entity 3, CA - Ca - 40.078 Da.
1 | CA |
BMRB | 4184 |
PDB | 1EH2 1F8H 1FF1 2JXC |
GB | ELK26712 AAH69359 AAK57558 AAL47008 |
REF | NP_001243359 NP_149095 XP_002825044 XP_004624764 XP_005390296 |
SP | Q8WXE9 |
AlphaFold | Q8WXE9 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks