BMRB Entry 25627
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25627
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Title: Solution structure of the meiosis-expressed gene 1 (Meig1) PubMed: 26726850
Deposition date: 2015-05-16 Original release date: 2016-01-19
Authors: Williams, David; Walavalkar, Ninad; Buchwald, William
Citation: Li, Wei; Walavalkar, Ninad; Buchwald, William; Teves, Maria; Zhang, Ling; Liu, Junping; Bilinovich, S.; Peterson, Darrell; Strauss, Jerome; Williams, David; Zhang, Zhibing. "Dissecting the structural basis of MEIG1 interaction with PACRG" Sci. Rep. 6, 18278-18278 (2016).
Assembly members:
entity, polymer, 92 residues, 11256.876 Da.
Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
entity: GSHMMATSDVKPKSISRAKK
WSEEIENLYRFQQAGYRDEI
EYKQVKQVAMVDRWPETGYV
KKLQRRDNTFFYYNKERECE
DKEVHKVKVYVY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 410 |
| 15N chemical shifts | 99 |
| 1H chemical shifts | 623 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 92 residues - 11256.876 Da.
| 1 | GLY | SER | HIS | MET | MET | ALA | THR | SER | ASP | VAL | ||||
| 2 | LYS | PRO | LYS | SER | ILE | SER | ARG | ALA | LYS | LYS | ||||
| 3 | TRP | SER | GLU | GLU | ILE | GLU | ASN | LEU | TYR | ARG | ||||
| 4 | PHE | GLN | GLN | ALA | GLY | TYR | ARG | ASP | GLU | ILE | ||||
| 5 | GLU | TYR | LYS | GLN | VAL | LYS | GLN | VAL | ALA | MET | ||||
| 6 | VAL | ASP | ARG | TRP | PRO | GLU | THR | GLY | TYR | VAL | ||||
| 7 | LYS | LYS | LEU | GLN | ARG | ARG | ASP | ASN | THR | PHE | ||||
| 8 | PHE | TYR | TYR | ASN | LYS | GLU | ARG | GLU | CYS | GLU | ||||
| 9 | ASP | LYS | GLU | VAL | HIS | LYS | VAL | LYS | VAL | TYR | ||||
| 10 | VAL | TYR |
Samples:
sample_1: sodium phosphate 10 mM; Meig1, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 40 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | 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 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D IPAP-HSQC | sample_1 | anisotropic | sample_conditions_1 |
| 2D IPAP-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CcpNMR, CCPN - data analysis
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts