BMRB Entry 19489
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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/BMR19489
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Title: NMR SOLUTION STRUCTURE OF MSP-P56S DOMAIN/VAPB in DPC PubMed: 23333387
Deposition date: 2013-09-11 Original release date: 2013-10-18
Authors: Qin, Haina; Lim, Liang Zhong; Song, Jianxing
Citation: Qin, Haina; Wang, Wei; Song, Jianxing. "ALS-causing P56S mutation and splicing variation on the hVAPB MSP domain transform its -sandwich fold into lipid-interacting helical conformations." Biochem. Biophys. Res. Commun. 431, 398-403 (2013).
Assembly members:
entity, polymer, 125 residues, 14206.426 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: MAKVEQVLSLEPQHELKFRG
PFTDVVTTNLKLGNPTDRNV
CFKVKTTAPRRYCVRSNSGI
IDAGASINVSVMLQPFDYDP
NEKSKHKFMVQSMFAPTDTS
DMEAVWKEAKPEDLMDSKLR
CVFEL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 230 |
| 15N chemical shifts | 118 |
| 1H chemical shifts | 620 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MSP-P56S DOMAIN/VAPB | 1 |
Entities:
Entity 1, MSP-P56S DOMAIN/VAPB 125 residues - 14206.426 Da.
| 1 | MET | ALA | LYS | VAL | GLU | GLN | VAL | LEU | SER | LEU | ||||
| 2 | GLU | PRO | GLN | HIS | GLU | LEU | LYS | PHE | ARG | GLY | ||||
| 3 | PRO | PHE | THR | ASP | VAL | VAL | THR | THR | ASN | LEU | ||||
| 4 | LYS | LEU | GLY | ASN | PRO | THR | ASP | ARG | ASN | VAL | ||||
| 5 | CYS | PHE | LYS | VAL | LYS | THR | THR | ALA | PRO | ARG | ||||
| 6 | ARG | TYR | CYS | VAL | ARG | SER | ASN | SER | GLY | ILE | ||||
| 7 | ILE | ASP | ALA | GLY | ALA | SER | ILE | ASN | VAL | SER | ||||
| 8 | VAL | MET | LEU | GLN | PRO | PHE | ASP | TYR | ASP | PRO | ||||
| 9 | ASN | GLU | LYS | SER | LYS | HIS | LYS | PHE | MET | VAL | ||||
| 10 | GLN | SER | MET | PHE | ALA | PRO | THR | ASP | THR | SER | ||||
| 11 | ASP | MET | GLU | ALA | VAL | TRP | LYS | GLU | ALA | LYS | ||||
| 12 | PRO | GLU | ASP | LEU | MET | ASP | SER | LYS | LEU | ARG | ||||
| 13 | CYS | VAL | PHE | GLU | LEU |
Samples:
sample_1: MSP-P56S DOMAIN/VAPB, [U-13C; U-15N], mM; DPC 20 mM
pH4_313K: pH: 4; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D CBCA(CO)NH | sample_1 | isotropic | pH4_313K |
| 3D 1H-15N TOCSY | sample_1 | isotropic | pH4_313K |
| 3D 1H-15N NOESY | sample_1 | isotropic | pH4_313K |
| 3D HCCH-TOCSY | sample_1 | isotropic | pH4_313K |
| 3D HBHA(CO)NH | sample_1 | isotropic | pH4_313K |
| 3D HN(CO)CA | sample_1 | isotropic | pH4_313K |
| 3D HNCACB | sample_1 | isotropic | pH4_313K |
| 3D HNCO | sample_1 | isotropic | pH4_313K |
| 3D C(CO)NH | sample_1 | isotropic | pH4_313K |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAC56577 BAE89665 BAG51174 BAI47207 |
| EMBL | CAN13351 |
| GB | AAD13577 AAD13578 AAH01712 AAI33498 AAP88813 |
| REF | NP_001075892 NP_001116685 NP_001182606 NP_001244417 NP_001274609 |
| SP | A2VDZ9 A5GFS8 O95292 |
| TPG | DAA23133 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts