BMRB Entry 30514
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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/BMR30514
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Title: Human Obscurin Ig57 Domain PubMed: 30289063
Deposition date: 2018-09-13 Original release date: 2019-02-01
Authors: Wright, N.; Whitley, J.
Citation: Letourneau, Allyn; Wright, Nathan. "Structural Insights on the Obscurin-Binding Domains in Titin." Protein Pept. Lett. 25, 973-979 (2018).
Assembly members:
entity_1, polymer, 102 residues, 11098.264 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 BL21
Entity Sequences (FASTA):
entity_1: MAPEVTILEPLQDVQLSEGQ
DASFQCRLSRASGQEARWAL
GGVPLQANEMNDITVEQGTL
HLLTLHKVTLEDAGTVSFHV
GTCSSEAQLKVTAGLEHHHH
HH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 315 |
| 1H chemical shifts | 534 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 102 residues - 11098.264 Da.
| 1 | MET | ALA | PRO | GLU | VAL | THR | ILE | LEU | GLU | PRO | ||||
| 2 | LEU | GLN | ASP | VAL | GLN | LEU | SER | GLU | GLY | GLN | ||||
| 3 | ASP | ALA | SER | PHE | GLN | CYS | ARG | LEU | SER | ARG | ||||
| 4 | ALA | SER | GLY | GLN | GLU | ALA | ARG | TRP | ALA | LEU | ||||
| 5 | GLY | GLY | VAL | PRO | LEU | GLN | ALA | ASN | GLU | MET | ||||
| 6 | ASN | ASP | ILE | THR | VAL | GLU | GLN | GLY | THR | LEU | ||||
| 7 | HIS | LEU | LEU | THR | LEU | HIS | LYS | VAL | THR | LEU | ||||
| 8 | GLU | ASP | ALA | GLY | THR | VAL | SER | PHE | HIS | VAL | ||||
| 9 | GLY | THR | CYS | SER | SER | GLU | ALA | GLN | LEU | LYS | ||||
| 10 | VAL | THR | ALA | GLY | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 11 | HIS | HIS |
Samples:
sample_1: entity_1 mM; TRIS 20 mM; DTT 1 mM; sodium chloride 50 mM
sample_2: entity_1 mM; TRIS 20 mM; DTT 1 mM; sodium chloride 50 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.2; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | 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 H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
SPARKY, Goddard - peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
NMR spectrometers:
- Bruker Avance 600 MHz