BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

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
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1MSP-P56S DOMAIN/VAPB1

Entities:

Entity 1, MSP-P56S DOMAIN/VAPB 125 residues - 14206.426 Da.

1   METALALYSVALGLUGLNVALLEUSERLEU
2   GLUPROGLNHISGLULEULYSPHEARGGLY
3   PROPHETHRASPVALVALTHRTHRASNLEU
4   LYSLEUGLYASNPROTHRASPARGASNVAL
5   CYSPHELYSVALLYSTHRTHRALAPROARG
6   ARGTYRCYSVALARGSERASNSERGLYILE
7   ILEASPALAGLYALASERILEASNVALSER
8   VALMETLEUGLNPROPHEASPTYRASPPRO
9   ASNGLULYSSERLYSHISLYSPHEMETVAL
10   GLNSERMETPHEALAPROTHRASPTHRSER
11   ASPMETGLUALAVALTRPLYSGLUALALYS
12   PROGLUASPLEUMETASPSERLYSLEUARG
13   CYSVALPHEGLULEU

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:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicpH4_313K
3D 1H-15N TOCSYsample_1isotropicpH4_313K
3D 1H-15N NOESYsample_1isotropicpH4_313K
3D HCCH-TOCSYsample_1isotropicpH4_313K
3D HBHA(CO)NHsample_1isotropicpH4_313K
3D HN(CO)CAsample_1isotropicpH4_313K
3D HNCACBsample_1isotropicpH4_313K
3D HNCOsample_1isotropicpH4_313K
3D C(CO)NHsample_1isotropicpH4_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