BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25677

Title: Solution NMR structure of CBX8 in complex with AF9 (CBX8-AF9)

Deposition date: 2015-06-30 Original release date: 2016-07-18

Authors: Kuntimaddi, Aravinda; Leach, Benjamin; Bushweller, John

Citation: Kuntimaddi, Aravinda; Leach, Benjamin; Bushweller, John. "Solution NMR Structure of CBX8 in complex with AF9 (CBX8-AF9)"  Not known ., .-..

Assembly members:
Chromobox_protein_homolog_8, polymer, 24 residues, 2577.936 Da.
Protein_AF-9, polymer, 70 residues, 8278.482 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

Entity Sequences (FASTA):
Chromobox_protein_homolog_8: TQGGRPSLIARIPVARILGD PEEE
Protein_AF-9: MDKAYLDELVELHRRLMTLR ERHILQQIVNLIEETGHFHI TNTTFDFDLCSLDKTTVRKL QSYLETSGTS

Data sets:
Data typeCount
13C chemical shifts406
15N chemical shifts88
1H chemical shifts542

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 24 residues - 2577.936 Da.

RESIDUES 327-349

1   THRGLNGLYGLYARGPROSERLEUILEALA
2   ARGILEPROVALALAARGILELEUGLYASP
3   PROGLUGLUGLU

Entity 2, entity_2 70 residues - 8278.482 Da.

RESIDUES 500-568

1   METASPLYSALATYRLEUASPGLULEUVAL
2   GLULEUHISARGARGLEUMETTHRLEUARG
3   GLUARGHISILELEUGLNGLNILEVALASN
4   LEUILEGLUGLUTHRGLYHISPHEHISILE
5   THRASNTHRTHRPHEASPPHEASPLEUCYS
6   SERLEUASPLYSTHRTHRVALARGLYSLEU
7   GLNSERTYRLEUGLUTHRSERGLYTHRSER

Samples:

sample_1: Chromobox protein homolog 8, [U-100% 13C; U-100% 15N], 750 uM; Protein AF-9, [U-100% 13C; U-100% 15N], 750 uM; BIS-TRIS 9.5 mM; MES 15.8 mM; sodium chloride 100 mM; DTT 1 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 100 mM; pH: 6; pressure: 1 atm; temperature: 298 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 HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CCPNMR_Analysis, CCPN - peak picking

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

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP Q9HC52 P42568

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