BMRB Entry 15695

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15695
MolProbity Validation Chart

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Title:
Solution NMR structure of the chromobox protein homolog 4
Deposition date:
2008-03-27
Original release date:
2008-03-28
Authors:
Kaustov, Lilia; Lemak, Alexander; Quyang, Hui; Fares, Christophe; Gutmanas, Alexandras; Ravichandran, Mani; Loppnau, Peter; Bountra, Chas; Weigelt, Johan; Edwards, Aled; Min, Jinrong; Arrowsmith, Cheryl
Citation:

Citation: Kaustov, Lilia; Lemak, Alexander; Quyang, Hui; Fares, Christophe; Gutmanas, Alexandras; Ravichandran, Mani; Loppnau, Peter; Bountra, Chas; Weigelt, Johan; Edwards, Aled; Min, Jinrong; Arrowsmith, Cheryl. "Solution NMR structure of the chromobox protein homolog 4"  .

Assembly members:

Assembly members:
cbx4, polymer, 60 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: pET28a-mhl

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cbx4: GSEHVFAVESIEKKRIRKGR VEYLVKWRGWSPKYNTWEPE ENILDPRLLIAFQNRERQEQ

Data typeCount
13C chemical shifts262
15N chemical shifts56
1H chemical shifts429

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1cbx41

Entities:

Entity 1, cbx4 60 residues - Formula weight is not available

1   GLYSERGLUHISVALPHEALAVALGLUSER
2   ILEGLULYSLYSARGILEARGLYSGLYARG
3   VALGLUTYRLEUVALLYSTRPARGGLYTRP
4   SERPROLYSTYRASNTHRTRPGLUPROGLU
5   GLUASNILELEUASPPROARGLEULEUILE
6   ALAPHEGLNASNARGGLUARGGLNGLUGLN

Samples:

sample_1: phosphate 0.5 mM; phosphate 10 mM; sodium chloride 300 mM; DTT 2 mM

sample_conditions_1: ionic strength: 300 mM; pH: 7.4; 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 HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D aromat 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - peak picking

ABACUS, Grishaev - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ BAA33402 BAG73014
GB AAB80718 AAB96874 AAH14967 AAH45162 AAI17802
REF NP_003646 NP_031651 NP_989973 XP_001081757 XP_001149752
SP O00257 O55187
TPG DAA18114
AlphaFold O00257 O55187

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