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 25801

Title: UBL domain of the human DNA damage-inducible protein homolog 2   PubMed: 27461074

Deposition date: 2015-09-08 Original release date: 2016-07-13

Authors: Siva, Monika; Grantz Saskova, Klara; Veverka, Vaclav

Citation: Siva, Monika; Svoboda, Michal; Veverka, Vaclav; Trempe, Jean-Francois; Hofmann, Kay; Kozisek, Milan; Hexnerova, Rozalie; Sedlak, Frantisek; Belza, Jan; Brynda, Jiri; Sacha, Pavel; Hubalek, Martin; Starkova, Jana; Flaisigova, Iva; Konvalinka, Jan; Saskova, Klara Grantz. "Human DNA-Damage-Inducible 2 Protein Is Structurally and Functionally Distinct from Its Yeast Ortholog"  Sci. Rep. 6, 30443-30443 (2016).

Assembly members:
entity, polymer, 97 residues, 11142.557 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):
entity: MGHHHHHHHHHHSSGHIEGR HMLLTVYCVRRDLSEVTFSL QVDADFELHNFRALCELESG IPAAESQIVYAERPLTDNHR SLASYGLKDGDVVILRQ

Data sets:
Data typeCount
13C chemical shifts332
15N chemical shifts83
1H chemical shifts579

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 97 residues - 11142.557 Da.

1   METGLYHISHISHISHISHISHISHISHIS
2   HISHISSERSERGLYHISILEGLUGLYARG
3   HISMETLEULEUTHRVALTYRCYSVALARG
4   ARGASPLEUSERGLUVALTHRPHESERLEU
5   GLNVALASPALAASPPHEGLULEUHISASN
6   PHEARGALALEUCYSGLULEUGLUSERGLY
7   ILEPROALAALAGLUSERGLNILEVALTYR
8   ALAGLUARGPROLEUTHRASPASNHISARG
9   SERLEUALASERTYRGLYLEULYSASPGLY
10   ASPVALVALILELEUARGGLN

Samples:

sample_1: sodium phosphate 25 mM; sodium chloride 100 mM; entity, [U-13C; U-15N], 0.4 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

YASARA, YASARA - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Bruker Avance 600 MHz

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