BMRB Entry 19613

Title:
Structural insights into the DNA recognition and protein interaction domains reveal fundamental homologous DNA pairing properties of HOP2   PubMed: 24711446
Deposition date:
2013-11-13
Original release date:
2014-04-11
Authors:
Moktan, Hem; Guiraldelli, Michel; Eyter, Craig; Zhao, Weixing; Camerini-Otero, Rafael; Sung, Patrick; Zhou, Donghua; Pezza, Roberto
Citation:

Citation: Moktan, Hem; Guiraldelli, Michel; Eyster, Craig; Zhao, Weixing; Lee, Chih-Ying; Mather, Timothy; Camerini-Otero, R. Daniel; Sung, Patrick; Zhou, Donghua; Pezza, Roberto. "Solution Structure and DNA-binding Properties of the Winged Helix Domain of the Meiotic Recombination HOP2 Protein."  J. Biol. Chem. ., .-. (2014).

Assembly members:

Assembly members:
Hop2, polymer, 84 residues, 7146.221 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b

Experimental source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts310
15N chemical shifts82
1H chemical shifts485

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HOP21

Entities:

Entity 1, HOP2 84 residues - 7146.221 Da.

1   METSERLYSSERARGALAGLUALAALAALA
2   GLYALAPROGLYILEILELEUARGTYRLEU
3   GLNGLUGLNASNARGPROTYRSERALAGLN
4   ASPVALPHEGLYASNLEUGLNLYSGLUHIS
5   GLYLEUGLYLYSALAALAVALVALLYSALA
6   LEUASPGLNLEUALAGLNGLUGLYLYSILE
7   LYSGLULYSTHRTYRGLYLYSGLNLYSILE
8   TYRPHEALAASPGLNASNGLNPHEASPTHR
9   VALSERASPALA

Samples:

sample_1: Hop2, [U-99% 13C; U-99% 15N], 6 mg/mL; D2O, [U-99% 2H], 5%; imidazole 10 mM; sodium chloride 120 mM; glycerol 5%

sample_conditions_1: ionic strength: 120 mM; pH: 7.8; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment, peak picking

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

CS-Rosetta, Shen, Vernon, Baker and Bax - structure solution

RPF, Huang, Powers, Montelione - refinement

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - structure validation

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

NCBI NP_032975.1
PDB
DBJ BAA23155 BAE21670
GB AAH30169 ACR24246 EDL03884
REF NP_032975 XP_005070210 XP_005369097 XP_005369098 XP_012968832
SP O35047
AlphaFold O35047

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