BMRB Entry 15922

Title:
Solution structure of the PPIL1 bound to a fragment of SKIP
Deposition date:
2008-08-17
Original release date:
2010-01-11
Authors:
Wang, Xingsheng; Wu, Jihui; Shi, Yunyu
Citation:

Citation: Wang, Xingsheng; Zhang, Shaojie; Zhang, Jiahai; Huang, Xiaojuan; Xu, Chao; Wang, Weiwei; Liu, Zhijun; Wu, Jihui; Shi, Yunyu. "A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR."  J. Biol. Chem. 285, 4951-4963 (2010).
PubMed: 20007319

Assembly members:

Assembly members:
PPIL1/SKIP, polymer, 203 residues, Formula weight is not available

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: pET22b

Data sets:
Data typeCount
13C chemical shifts519
15N chemical shifts186
1H chemical shifts1176

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PPIL1/SKIP1

Entities:

Entity 1, PPIL1/SKIP 203 residues - Formula weight is not available

1   METALAALAILEPROPROASPSERTRPGLN
2   PROPROASNVALTYRLEUGLUTHRSERMET
3   GLYILEILEVALLEUGLULEUTYRTRPLYS
4   HISALAPROLYSTHRCYSLYSASNPHEALA
5   GLULEUALAARGARGGLYTYRTYRASNGLY
6   THRLYSPHEHISARGILEILELYSASPPHE
7   METILEGLNGLYGLYASPPROTHRGLYTHR
8   GLYARGGLYGLYALASERILETYRGLYLYS
9   GLNPHEGLUASPGLULEUHISPROASPLEU
10   LYSPHETHRGLYALAGLYILELEUALAMET
11   ALAASNALAGLYPROASPTHRASNGLYSER
12   GLNPHEPHEVALTHRLEUALAPROTHRGLN
13   TRPLEUASPGLYLYSHISTHRILEPHEGLY
14   ARGVALCYSGLNGLYILEGLYMETVALASN
15   ARGVALGLYMETVALGLUTHRASNSERGLN
16   ASPARGPROVALASPASPVALLYSILEILE
17   LYSALATYRPROSERGLYGLYGLYGLYSER
18   GLYGLYGLYSERGLYGLYGLYSERGLYGLY
19   GLYSERGLYASPGLYGLYALAPHEPROGLU
20   ILEHISVALALAGLNTYRPROLEUASPMET
21   GLYARGLYS

Samples:

sample: D2O 100%; entity_2; phosphate buffer 50 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsampleisotropicsample_conditions_1
3D_13C-separated_NOESsampleisotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ BAB23265 BAE00661 BAE29731 BAE30513 BAE33862
GB AAD34119 AAH03048 AAH58369 AAH99188 AAI02397
REF NP_001014869 NP_001029360 NP_001233365 NP_001271748 NP_057143
SP Q5E992 Q9D0W5 Q9Y3C6
TPG DAA16620
AlphaFold Q5E992 Q9D0W5 Q9Y3C6

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