BMRB Entry 25556

Title:
Solution structure of the MRG15-MRGBP complex
Deposition date:
2015-03-27
Original release date:
2015-05-26
Authors:
Xie, Tao; Zmysloski, Adam; Zhang, Yongbo; Radhakrishnan, Ishwar
Citation:

Citation: Xie, Tao; Zmysloski, Adam; Zhang, Yongbo; Radhakrishnan, Ishwar. "Structural Basis for Multi-specificity of MRG Domains"  Structure 23, 1049-1057 (2015).
PubMed: 25960410

Assembly members:

Assembly members:
entity_1, polymer, 54 residues, 6284.132 Da.
entity_2, polymer, 172 residues, 19842.887 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: pMCSG7

Data sets:
Data typeCount
13C chemical shifts925
15N chemical shifts217
1H chemical shifts1476

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MRGBP1
2MRG152

Entities:

Entity 1, MRGBP 54 residues - 6284.132 Da.

1   SERASNALAGLYARGGLNVALPROSERLYS
2   VALILETRPASPHISLEUSERTHRMETTYR
3   ASPMETGLNALALEUHISGLUSERGLUILE
4   LEUPROPHEPROASNPROGLUARGASNPHE
5   VALLEUPROGLUGLUILEILEGLNGLUVAL
6   ARGGLUGLYLYS

Entity 2, MRG15 172 residues - 19842.887 Da.

1   SERASNALAGLUVALLYSVALLYSILEPRO
2   GLUGLULEULYSPROTRPLEUVALASPASP
3   TRPASPLEUILETHRARGGLNLYSGLNLEU
4   PHETYRLEUPROALALYSLYSASNVALASP
5   SERILELEUGLUASPTYRALAASNTYRLYS
6   LYSSERARGGLYASNTHRASPASNLYSGLU
7   TYRALAVALASNGLUVALVALALAGLYILE
8   LYSGLUTYRPHEASNVALMETLEUGLYTHR
9   GLNLEULEUTYRLYSPHEGLUARGPROGLN
10   TYRALAGLUILELEUALAASPHISPROASP
11   ALAPROMETSERGLNVALTYRGLYALAPRO
12   HISLEULEUARGLEUPHEVALARGILEGLY
13   ALAMETLEUALATYRTHRPROLEUASPGLU
14   LYSSERLEUALALEULEULEUASNTYRLEU
15   HISASPPHELEULYSTYRLEUALALYSASN
16   SERALATHRLEUPHESERALASERASPTYR
17   GLUVALALAPROPROGLUTYRHISARGLYS
18   ALAVAL

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.8 mM; entity_2 0.8 mM; sodium phosphate 50 mM; dithiothreitol-d10 3 mM; NaN3 0.2%

sample_2: entity_1, [U-100% 13C; U-100% 15N], 0.8 mM; entity_2 0.8 mM; sodium phosphate 50 mM; dithiothreitol-d10 3 mM; NaN3 0.2%

sample_3: entity_1 0.9 mM; entity_2, [U-100% 13C; U-100% 15N], 0.9 mM; sodium phosphate 50 mM; dithiothreitol-d10 3 mM; NaN3 0.2%

sample_4: entity_1 0.9 mM; entity_2, [U-100% 13C; U-100% 15N], 0.9 mM; sodium phosphate 50 mM; dithiothreitol-d10 3 mM; NaN3 0.2%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.9; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D double half-filtered 1H-1H NOESYsample_2isotropicsample_conditions_1
3D 15N,13C-filtered, 15N,13C-edited 1H-1H NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_4isotropicsample_conditions_1
2D double half-filtered 1H-1H NOESYsample_4isotropicsample_conditions_1
3D 15N,13C-filtered, 15N,13C-edited 1H-1H NOESYsample_4isotropicsample_conditions_1

Software:

ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

Felix, Accelrys Software Inc. - processing

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Agilent INOVA 600 MHz

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