BMRB Entry 34844

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34844
MolProbity Validation Chart

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Title:
Characterization of the zinc finger u-protein HVO_0758 from Haloferax volcanii: biological roles, zinc binding, and NMR solution structure
Deposition date:
2023-08-08
Original release date:
2023-12-19
Authors:
Pyper, D.; Schwalbe, H.
Citation:

Citation: Ueresin, D.; Pyper, D.; Borst, A.; Hadjeras, L.; Gelhausen, R.; Backofen, R.; Sharma, C.; Schwalbe, H.; Soppa, J.. "Characterization of the zinc finger mu-protein HVO_0758 from Haloferax volcanii: biological roles, zinc binding, and NMR solution structure"  Front. Microbiol. 14, 1280972-1280972 (2023).
PubMed: 38094630

Assembly members:

Assembly members:
entity_1, polymer, 56 residues, 6495.407 Da.

Natural source:

Natural source:   Common Name: Haloferax volcanii DS2   Taxonomy ID: 309800   Superkingdom: Archaea   Kingdom: not available   Genus/species: Haloferax volcanii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKTTRKGLRDGELEKDTYGR LTCSECGESLKKKNDPDEVF SVRICADCGREWKELR

Data sets:
Data typeCount
13C chemical shifts240
15N chemical shifts54
1H chemical shifts373

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 56 residues - 6495.407 Da.

1   METLYSTHRTHRARGLYSGLYLEUARGASP
2   GLYGLULEUGLULYSASPTHRTYRGLYARG
3   LEUTHRCYSSERGLUCYSGLYGLUSERLEU
4   LYSLYSLYSASNASPPROASPGLUVALPHE
5   SERVALARGILECYSALAASPCYSGLYARG
6   GLUTRPLYSGLULEUARG

Samples:

sample_1: BisTris 25 mM; NaCl 1000 mM; ZnCl2 100 uM; 2-mercaptoethanol 5 mM

sample_conditions_1: ionic strength: 1000 mM; pH: 7; 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 HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSY-HSQCsample_1isotropicsample_conditions_1

Software:

NMRFAM-SPARKY v1.470, Lee, Tonelli, Markley - chemical shift assignment, data analysis, peak picking

TopSpin v4.1.0, Bruker Biospin - collection, processing

TALOS-N, Cornilescu, Delaglio and Bax - data analysis

TENSOR2, Dosset, Marion, Blackledge - data analysis

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

  • Bruker AVANCE NEO 900 MHz
  • Bruker AVANCE III HD 800 MHz
  • Bruker AVANCE III HD 600 MHz

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