BMRB Entry 16156

Title:
Solution Structure of the Coiled-coil Domain of Synphilin-1
Deposition date:
2009-02-02
Original release date:
2009-03-09
Authors:
Xie, Yuanyuan; Zhou, Chenjie; Zhou, Ziren; Hu, Hongyu
Citation:

Citation: Xie, Yuanyuan; Zhou, Chenjie; Zhou, Ziren; Hong, Jing; Lin, Donghai; Hu, Hongyu. "Solution Structure of the Coiled-coil Domain of Synphilin-1"  .

Assembly members:

Assembly members:
Synphilin-1, polymer, 48 residues, 5371.191 Da.

Natural source:

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-32M

Experimental source:

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-32M

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Synphilin-1: GSVETCMSLASQVVKLTKQL KEQTVERVTLQNQLQQFLEA QKSEGKSL

Data sets:
Data typeCount
13C chemical shifts174
15N chemical shifts46
1H chemical shifts271

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Synphilin-11

Entities:

Entity 1, Synphilin-1 48 residues - 5371.191 Da.

1   GLYSERVALGLUTHRCYSMETSERLEUALA
2   SERGLNVALVALLYSLEUTHRLYSGLNLEU
3   LYSGLUGLNTHRVALGLUARGVALTHRLEU
4   GLNASNGLNLEUGLNGLNPHELEUGLUALA
5   GLNLYSSERGLUGLYLYSSERLEU

Samples:

sample_1: entity, [U-15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O 10%; H2O 90%

sample_2: entity, [U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O 10%; H2O 90%

sample_3: entity, [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O 10%; H2O 90%

sample_conditions_1: pH: 6.0; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, peak picking

ARIA, Linge, O'Donoghue and Nilges - refinement, structure solution

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAA91791 BAD19017 BAD19018 BAG51060 BAH12894
GB AAD30362 AAG17478 AAH33743 AAH40552 AAH94759
REF NP_001229864 NP_001295029 NP_001295034 NP_001295035 NP_001295036
SP Q9Y6H5
AlphaFold Q9Y6H5

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