BMRB Entry 18614
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18614
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: NMR solution structure of Myo10 anti-CC PubMed: 23012428
Deposition date: 2012-07-25 Original release date: 2012-09-24
Authors: Ye, Fei; Lu, Qing; Zhang, Mingjie
Citation: Lu, Qing; Ye, Fei; Wei, Zhiyi; Wen, Zilong; Zhang, Mingjie. "Antiparallel coiled-coil-mediated dimerization of myosin X." Proc. Natl. Acad. Sci. U.S.A. 109, 17388-17393 (2012).
Assembly members:
entity, polymer, 51 residues, 6339.12 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: ENKQVEEILRLEKEIEDLQR
MKEQQELSLTEASLQKLQER
RDQELRRLEEE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 155 |
| 15N chemical shifts | 51 |
| 1H chemical shifts | 329 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Myo10 anti-CC, 1 | 1 |
| 2 | Myo10 anti-CC, 2 | 1 |
Entities:
Entity 1, Myo10 anti-CC, 1 51 residues - 6339.12 Da.
| 1 | GLU | ASN | LYS | GLN | VAL | GLU | GLU | ILE | LEU | ARG | ||||
| 2 | LEU | GLU | LYS | GLU | ILE | GLU | ASP | LEU | GLN | ARG | ||||
| 3 | MET | LYS | GLU | GLN | GLN | GLU | LEU | SER | LEU | THR | ||||
| 4 | GLU | ALA | SER | LEU | GLN | LYS | LEU | GLN | GLU | ARG | ||||
| 5 | ARG | ASP | GLN | GLU | LEU | ARG | ARG | LEU | GLU | GLU | ||||
| 6 | GLU |
Samples:
sample_1: Myo10_anti-CC, [U-100% 13C; U-100% 15N], 0.8 mM; D2O 100%
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | 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_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
SPARKY, Goddard - chemical shift assignment
PIPP, Garrett - chemical shift assignment
Molmol, Koradi, Billeter and Wuthrich - structure solution
NMR spectrometers:
- Varian INOVA 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAA34519 BAG10382 BAH12170 BAH14509 |
| EMBL | CAH10611 |
| GB | AAF36524 AAF37875 AAF68025 AAI37169 AAI50286 |
| REF | NP_036466 XP_001175408 XP_002745141 XP_002804360 XP_003263225 |
| SP | Q9HD67 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts