BMRB Entry 15554
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15554
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Title: Structure and Chemical Shift Assignment for the Eps15EH2-Stonin2 complex PubMed: 19636924
Deposition date: 2007-11-12 Original release date: 2008-01-10
Authors: Rumpf, Julia; Simon, Bernd; Jung, Nadja; Maritzen, Tanja; Haucke, Volker; Sattler, Michael; Groemping, Yvonne
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).
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
Entity Sequences (FASTA):
EH2: GPLGSPWAVKPEDKAKYDAI
FDSLSPVNGFLSGDKVKPVL
LNSKLPVDILGRVWELSDID
HDGMLDRDEFAVAMFLVYCA
LEKEPVPMSLPPALVPPSKR
Stonin_peptide: GPLGSPSVTEASPWRATNPF
LNETLQDVQPSPINPFSAFF
EEQER
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 483 |
| 15N chemical shifts | 130 |
| 1H chemical shifts | 996 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | EH2 | 1 |
| 2 | Stonin | 2 |
| 3 | CA | 3 |
Entities:
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 |
Samples:
sample_1: EH2, [U-99% 13C; U-99% 15N], 0.5-1 mM; Stonin peptide 0.5-1 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM
sample_2: EH2 0.5-1 mM; Stonin peptide, [U-99% 13C; U-99% 15N], 0.5-1 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM
sample_3: EH2, [U-99% 13C; U-99% 15N], 0.5-1 mM; Stonin peptide 0.5-1 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM
sample_4: EH2 0.5-1 mM; Stonin peptide, [U-99% 13C; U-99% 15N], 0.5-1 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM
sample_5: EH2 0.6 mM; Stonin peptide 0.6 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 295 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_5 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_4 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRView v5.0.4, Johnson, One Moon Scientific - chemical shift assignment
TOPSPIN v1.3, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
ARIA v1.2, Linge, O, . - structure solution
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker Avance 800 MHz
- Bruker Avance 900 MHz
Related Database Links:
| BMRB | 4184 |
| PDB | |
| GB | ELK26712 AAH69359 AAK57558 AAL47008 |
| REF | NP_001243359 NP_149095 XP_002825044 XP_004624764 XP_005390296 |
| SP | Q8WXE9 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts