BMRB Entry 27216

Title:
Chemical shift assignments of prothymosin alpha in complex with Histone H1
Deposition date:
2017-08-14
Original release date:
2018-02-12
Authors:
Bugge, Katrine; Kragelund, Birthe; Fernandes, Catarina; Borgia, Alessandro; Borgia, Madeleine; Heidarsson, Petur; Schuler, Benjamin
Citation:

Citation: Borgia, Alessandro; Borgia, Madeleine; Bugge, Katrine; Kissling, Vera; Heidarsson, Petur; Fernandes, Catarina; Sottini, Andrea; Soranno, Andrea; Buholzer, Karin; Nettels, Daniel; Kragelund, Birthe; Best, Robert; Schuler, Benjamin. "Extreme disorder in an ultrahigh-affinity protein complex."  Nature 555, 61-66 (2018).
PubMed: 29466338

Assembly members:

Assembly members:
Prothymosin_alpha, polymer, 112 residues, Formula weight is not available
Histone_H1, polymer, 197 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: pET47b

Data sets:
Data typeCount
13C chemical shifts172
15N chemical shifts102
1H chemical shifts99

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Prothymosin alpha1
2Histone H12

Entities:

Entity 1, Prothymosin alpha 112 residues - Formula weight is not available

GP is leftover from cleavage from a tag, and residue numbering does not include these first two residues.

1   GLYPROMETSERASPALAALAVALASPTHR
2   SERSERGLUILETHRTHRLYSASPLEULYS
3   GLULYSLYSGLUVALVALGLUGLUALAGLU
4   ASNGLYARGASPALAPROALAASNGLYASN
5   ALAASNGLUGLUASNGLYGLUGLNGLUALA
6   ASPASNGLUVALASPGLUGLUGLUGLUGLU
7   GLYGLYGLUGLUGLUGLUGLUGLUGLUGLU
8   GLYASPGLYGLUGLUGLUASPGLYASPGLU
9   ASPGLUGLUALAGLUSERALATHRGLYLYS
10   ARGALAALAGLUASPASPGLUASPASPASP
11   VALASPTHRLYSLYSGLNLYSTHRASPGLU
12   ASPASP

Entity 2, Histone H1 197 residues - Formula weight is not available

1   THRGLUASNSERTHRSERALAPROALAALA
2   LYSPROLYSARGALALYSALASERLYSLYS
3   SERTHRASPHISPROLYSTYRSERASPMET
4   ILEVALALAALAILEGLNALAGLULYSASN
5   ARGALAGLYSERSERARGGLNSERILEGLN
6   LYSTYRILELYSSERHISTYRLYSVALGLY
7   GLUASNALAASPSERGLNILELYSLEUSER
8   ILELYSARGLEUVALTHRTHRGLYVALLEU
9   LYSGLNTHRLYSGLYVALGLYALASERGLY
10   SERPHEARGLEUALALYSSERASPGLUPRO
11   LYSLYSSERVALALAPHELYSLYSTHRLYS
12   LYSGLUILELYSLYSVALALATHRPROLYS
13   LYSALASERLYSPROLYSLYSALAALASER
14   LYSALAPROTHRLYSLYSPROLYSALATHR
15   PROVALLYSLYSALALYSLYSLYSLEUALA
16   ALATHRPROLYSLYSALALYSLYSPROLYS
17   THRVALLYSALALYSPROVALLYSALASER
18   LYSPROLYSLYSALALYSPROVALLYSPRO
19   LYSALALYSSERSERALALYSARGALAGLY
20   LYSLYSLYSGLYGLYPROARG

Samples:

sample_1: Prothymosin alpha, [U-100% 13C; U-100% 15N], 100 uM; Histone H1 80 uM; DSS 0.7 mM; D2O, [U-100% 2H], 10%; EDTA 0.1 mM; TBS buffer 165 mM; Tris-HCl 10 mM; KCl 155 mM

sample_conditions_1: ionic strength: 165 mM; pH: 7.4; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)NNHsample_1isotropicsample_conditions_1

Software:

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

Ccpnmr_Analysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz
  • Varian INOVA 800 MHz

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