BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19489

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

Data sets:
Data typeCount
13C chemical shifts230
15N chemical shifts118
1H chemical shifts620

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Related Database Links:

PDB 2MDK 3IKK
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