BMRB Entry 17455

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for human TrJ disease-related mutant form of PMP22
Deposition date:
2011-02-10
Original release date:
2011-08-17
Authors:
Sakakura, Masayoshi; Hadziselimovic, Arina; Wang, Zhen; Schey, Kevin; Sanders, Charles
Citation:

Citation: Sakakura, Masayoshi; Hadziselimovic, Arina; Wang, Zhen; Schey, Kevin; Sanders, Charles. "Structural basis for the trembler-j phenotype of charcot-marie-tooth disease."  Structure 19, 1160-1169 (2011).
PubMed: 21827951

Assembly members:

Assembly members:
TrJ-PMP22, polymer, 173 residues, 19260.56 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pAH13.1

Data sets:
Data typeCount
13C chemical shifts82
15N chemical shifts74
1H chemical shifts74

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1membrane protein1

Entities:

Entity 1, membrane protein 173 residues - 19260.56 Da.

Residues 1-13 represent a non-native tag

1   GLYSERGLYTRPSERHISPROGLNPHEGLU
2   LYSGLYSERMETLEULEULEULEULEUSER
3   ILEILEVALLEUHISVALALAVALPROVAL
4   LEULEUPHEVALSERTHRILEVALSERGLN
5   TRPILEVALGLYASNGLYHISALATHRASP
6   LEUTRPGLNASNCYSSERTHRSERSERSER
7   GLYASNVALHISHISCYSPHESERSERSER
8   PROASNGLUTRPLEUGLNSERVALGLNALA
9   THRMETILELEUSERILEILEPHESERILE
10   LEUSERLEUPHELEUPHEPHECYSGLNLEU
11   PHETHRLEUTHRLYSGLYGLYARGPHETYR
12   ILETHRGLYILEPHEGLNILELEUALAGLY
13   LEUCYSVALMETSERALAALAALAILETYR
14   THRVALARGHISPROGLUTRPHISLEUASN
15   SERASPTYRSERTYRGLYPHEALATYRILE
16   LEUALATRPVALALAPHEPROLEUALALEU
17   LEUSERGLYVALILETYRVALILELEUARG
18   LYSARGGLU

Samples:

sample_1: TrJ-PMP22, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; D2O, [U-100% 2H], 5%; H2O 95%; sodium acetate 10 mM; EDTA 1 mM; DTT 10 mM; tetradecylphosphocholine 216 mM

sample_conditions_1: ionic strength: 0.01 M; pH: 5; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3 and 2.1, Bruker Biospin - collection (v1.3), processing (v2.1)

SPARKY v3.114, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks