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 34334

Title: NMR solution structure of the HVO_2922 protein from Haloferax volcanii

Deposition date: 2018-12-03 Original release date: 2019-06-07

Authors: Kubatova, N.; Jonker, H.; Saxena, K.; Richter, C.; Marchfelder, A.; Schwalbe, H.

Citation: Kubatova, N.; Jonker, H.; Saxena, K.; Richter, C.; Marchfelder, A.; Schwalbe, H.. "Solution structure and dynamics of HVO_2922 protein from Haloferax volcanii"  to be published ., .-..

Assembly members:
entity_1, polymer, 60 residues, 6686.416 Da.

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

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

Entity Sequences (FASTA):
entity_1: MNKAHFEVFVDAADKYRWRL VHDNGNILADSGEGYASKQK AKQGIESVKRNAPDADVIEA

Data sets:
Data typeCount
13C chemical shifts235
15N chemical shifts63
1H chemical shifts399

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21

Entities:

Entity 1, entity_1, 1 60 residues - 6686.416 Da.

1   METASNLYSALAHISPHEGLUVALPHEVAL
2   ASPALAALAASPLYSTYRARGTRPARGLEU
3   VALHISASPASNGLYASNILELEUALAASP
4   SERGLYGLUGLYTYRALASERLYSGLNLYS
5   ALALYSGLNGLYILEGLUSERVALLYSARG
6   ASNALAPROASPALAASPVALILEGLUALA

Samples:

sample_1: HVO_2922, [U-15N], 5.0 mM; sodium phosphate 50 mM; sodium chloride 100 mM; DTT 3 mM

sample_2: HVO_2922, [U-13C; U-15N], 2.0 mM; sodium phosphate 50 mM; sodium chloride 100 mM; DTT 3 mM

sample_conditions_1: ionic strength: 232 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D 1H-15N HETNOEsample_1isotropicsample_conditions_1
2D 1H-15N T1sample_1isotropicsample_conditions_1
2D 1H-15N T2sample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D (H)CC(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C TOCSY aromaticsample_2isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_2isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_2isotropicsample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin - collection, processing

SPARKY v3.114, Goddard and Kneller - chemical shift assignment, data analysis, peak picking

TALOS vN, Shen and Bax - data analysis

TENSOR v2, Dosset, Marion, Blackledge - data analysis

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

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

ARIA v1.2 HJ, Linge, O'Donoghue and Nilges - refinement

NMR spectrometers:

  • Bruker Avance Bruker 600 600 MHz
  • Bruker Avance Bruker 700 700 MHz
  • Bruker Avance Bruker 800 800 MHz

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