BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25565

Title: Solution structure of the BCOR PUFD

Deposition date: 2015-04-06 Original release date: 2016-04-04

Authors: Wong, Sarah; Gearhart, Micah; Ha, Daniel; Corcoran, Connie; Diaz, Victoria; Taylor, Alexander; Schirf, Virgil; Ilangovan, Udayar; Hinck, Andrew; Demeler, Borries; Hart, P; Bardwell, Vivian; Kim, Chongwoo

Citation: Wong, Sarah; Gearhart, Micah; Ha, Daniel; Corcoran, Connie; Diaz, Victoria; Taylor, Alexander; Schirf, Virgil; Ilangovan, Udayar; Hinck, Andrew; Demeler, Borries; Hart, John; Bardwell, Vivian; Kim, Chongwoo. "Structural basis for the hierarchical assembly of the core of PRC1.1"  .

Assembly members:
BCOR_PUFD, polymer, 115 residues, 13112.839 Da.

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-30a, pET-3c, pCDF-Duet-1

Entity Sequences (FASTA):
BCOR_PUFD: SDVFEFEFSETPLLPSYNIQ VSVAQGPRNWLLLSDVLKKL KMSSRIFRSNFPNVEIVTIA EAEFYRQVSASLLFSSSKDL EAFNPESKELLDLVEFTNEI QTLLGSSVEWLHPSD

Data sets:
Data typeCount
13C chemical shifts446
15N chemical shifts102
1H chemical shifts690

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 115 residues - 13112.839 Da.

1   SERASPVALPHEGLUPHEGLUPHESERGLU
2   THRPROLEULEUPROSERTYRASNILEGLN
3   VALSERVALALAGLNGLYPROARGASNTRP
4   LEULEULEUSERASPVALLEULYSLYSLEU
5   LYSMETSERSERARGILEPHEARGSERASN
6   PHEPROASNVALGLUILEVALTHRILEALA
7   GLUALAGLUPHETYRARGGLNVALSERALA
8   SERLEULEUPHESERSERSERLYSASPLEU
9   GLUALAPHEASNPROGLUSERLYSGLULEU
10   LEUASPLEUVALGLUPHETHRASNGLUILE
11   GLNTHRLEULEUGLYSERSERVALGLUTRP
12   LEUHISPROSERASP

Samples:

sample_1: entity, [U-13C; U-15N], 3 mM; TRIS 10 mM; sodium chloride 50 mM; TCEP 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 30 mM; pH: 8; pressure: 1 atm; temperature: 300 K

Experiments:

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

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, chemical shift calculation, data analysis

TOPSPIN, Bruker Biospin - collection

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

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

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

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