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 34500

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34500

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Title: Solution structure and dynamics of Zn-Finger HVO_2753 protein   PubMed: 32905660

Deposition date: 2020-03-20 Original release date: 2020-09-14

Authors: Kubatova, N.; Pyper, D.; Schwalbe, H.

Citation: Zahn, Sebastian; Kubatova, Nina; Pyper, Dennis; Cassidy, Liam; Saxena, Krishna; Tholey, Andreas; Schwalbe, Harald; Soppa, Jorg. "Biological functions, genetic and biochemical characterization, and NMR structure determination of the small zinc finger protein HVO_2753 from Haloferax volcanii"  FEBS J. ., .-. (2020).

Assembly members:
entity_1, polymer, 62 residues, 6625.537 Da.

Natural source:   Common Name: Haloferax volcanii   Taxonomy ID: 2246   Superkingdom: Archaea   Kingdom: not available   Genus/species: Haloferax volcanii

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21

Entity Sequences (FASTA):
entity_1: GAMGSESEQRHAHQCVSCGI NIAGMSAATFKCPDCGQEIS RCSKCRKQSNLYECPDCGFM GP

Data typeCount
13C chemical shifts234
15N chemical shifts56
1H chemical shifts351

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 62 residues - 6625.537 Da.

1   GLYALAMETGLYSERGLUSERGLUGLNARG
2   HISALAHISGLNCYSVALSERCYSGLYILE
3   ASNILEALAGLYMETSERALAALATHRPHE
4   LYSCYSPROASPCYSGLYGLNGLUILESER
5   ARGCYSSERLYSCYSARGLYSGLNSERASN
6   LEUTYRGLUCYSPROASPCYSGLYPHEMET
7   GLYPRO

Samples:

sample_1: HVO_2753, [U-15N; U-13C], 1 mM; Bis Tris 25 mM; sodium chloride 200 mM; DTT 3 mM

sample_2: HVO_2753, [U-15N; U-13C], 1 mM; Bis Tris 25 mM; sodium chloride 200 mM; DTT 3 mM

sample_3: HVO_2753, [U-15N], 0.5 mM; Bis Tris 25 mM; sodium chloride 200 mM; DDT 3 mM

sample_conditions_1: ionic strength: 411 mM; pH: 7; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HETNOEsample_3isotropicsample_conditions_1
2D 1H-15N T1sample_3isotropicsample_conditions_1
2D 1H-15N T2sample_3isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

TopSpin v3.5, Bruker Biospin - collection, processing

Sparky v3.114, Goddard - chemical shift assignment, data analysis, peak picking

TALOS vN, Cornilescu, Delaglio and Bax - data analysis

TENSOR v2, Dosset, Marion, Blackledge - data analysis

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

  • Bruker AVANCE 600 MHz
  • Bruker AVANCE 700 MHz
  • Bruker AVANCE 950 MHz
  • Bruker AVANCE 800 MHz

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