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 18850

Title: Solution structure of the Haloferax volcanii HVO_2177 protein   PubMed: 23821306

Deposition date: 2012-11-21 Original release date: 2013-08-05

Authors: Li, Yunfeng; Maciejewski, Mark; Martin, Jonathan; Jin, Kai; Zhang, Yuhang; Lu, Min; Maupin-Furlow, Julie; Hao, Bing

Citation: Li, Yunfeng; Maciejewski, Mark; Martin, Jonathan; Jin, Kai; Zhang, Yuhang; Maupin-Furlow, Julie; Hao, Bing. "Crystal structure of the ubiquitin-like small archaeal modifier protein 2 from Haloferax volcanii."  Protein Sci. 22, 1206-1217 (2013).

Assembly members:
Ubl_protein_HVO_2177, polymer, 106 residues, 11540.825 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

Entity Sequences (FASTA):
Ubl_protein_HVO_2177: GGGRDYKDDDDKGTMELELR FFATFREVVGQKSIYWRVDD DATVGDVLRSLEAEYDGLAG RLIEDGEVKPHVNVLKNGRE VVHLDGMATALDDGDAVSVF PPVAGG

Data sets:
Data typeCount
13C chemical shifts441
15N chemical shifts98
1H chemical shifts678

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Haloferax volcanii HVO_2177 protein1

Entities:

Entity 1, Haloferax volcanii HVO_2177 protein 106 residues - 11540.825 Da.

residues 1-14 represent a non-native affinity tag

1   GLYGLYGLYARGASPTYRLYSASPASPASP
2   ASPLYSGLYTHRMETGLULEUGLULEUARG
3   PHEPHEALATHRPHEARGGLUVALVALGLY
4   GLNLYSSERILETYRTRPARGVALASPASP
5   ASPALATHRVALGLYASPVALLEUARGSER
6   LEUGLUALAGLUTYRASPGLYLEUALAGLY
7   ARGLEUILEGLUASPGLYGLUVALLYSPRO
8   HISVALASNVALLEULYSASNGLYARGGLU
9   VALVALHISLEUASPGLYMETALATHRALA
10   LEUASPASPGLYASPALAVALSERVALPHE
11   PROPROVALALAGLYGLY

Samples:

sample_1: Ubl protein HVO_2177, [U-99% 13C; U-99% 15N], 1 mM; NaCl 500 mM; Na-K phosphate 25 mM; EDTA 0.2 mM; NaN3 0.02%

sample_2: Ubl protein HVO_2177, [U-99% 13C; U-99% 15N], 1 mM; NaCl 500 mM; Na-K phosphate 25 mM; EDTA 0.2 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 0.5 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

XEASY v1.2, Bartels et al. - chemical shift assignment, peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

VNMRJ v3.1, Varian - collection

Rowland NMR Toolkit v3.0, Hoch, Jeffrey C. & Stern, Alan S. - processing

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

TALOS+, Cornilescu, Delaglio and Bax, Shen, Delaglio, Cornilescu, and Bax - torsion angle restraints

NMR spectrometers:

  • Varian VNMRS 600 MHz
  • Varian VNMRS 800 MHz

Related Database Links:

GB 8923994 ADE02783 ELK45920 ELY33406 ELZ55725 ELZ67244
PDB
EMBL CQR48598
REF WP_004042069 WP_006601267
SP D4GVB0

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