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 17391

Title: A protein from Haloferax volcanii   PubMed: 23818097

Deposition date: 2011-01-03 Original release date: 2012-01-11

Authors: Zhang, Wen; Liao, Shanhui; Fan, Kai; Tu, Xiaoming

Citation: Ye, Kaiqin; Liao, Shanhui; Zhang, Wen; Fan, Kai; Zhang, Xuecheng; Zhang, Jiahai; Xu, Chao; Tu, Xiaoming. "Ionic strength-dependent conformations of a ubiquitin-like small archaeal modifier protein (SAMP1) from Haloferax volcanii."  Protein Sci. 22, 1174-1182 (2013).

Assembly members:
entity, polymer, 174 residues, 17869.711 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):
entity: MEWKLFADLAEVAGSRTVRV DVDGDATVGDALDALVGAHP ALESRVFGDDGELYDHINVL RNGEAAALGEATAAGDELAL FPPVSGGMEWKLFADLAEVA GSRTVRVDVDGDATVGDALD ALVGAHPALESRVFGDDGEL YDHINVLRNGEAAALGEATA AGDELALFPPVSGG

Data sets:
Data typeCount
13C chemical shifts183
15N chemical shifts75
1H chemical shifts409

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein from Haloferax volcanii1

Entities:

Entity 1, protein from Haloferax volcanii 174 residues - 17869.711 Da.

1   METGLUTRPLYSLEUPHEALAASPLEUALA
2   GLUVALALAGLYSERARGTHRVALARGVAL
3   ASPVALASPGLYASPALATHRVALGLYASP
4   ALALEUASPALALEUVALGLYALAHISPRO
5   ALALEUGLUSERARGVALPHEGLYASPASP
6   GLYGLULEUTYRASPHISILEASNVALLEU
7   ARGASNGLYGLUALAALAALALEUGLYGLU
8   ALATHRALAALAGLYASPGLULEUALALEU
9   PHEPROPROVALSERGLYGLYMETGLUTRP
10   LYSLEUPHEALAASPLEUALAGLUVALALA
11   GLYSERARGTHRVALARGVALASPVALASP
12   GLYASPALATHRVALGLYASPALALEUASP
13   ALALEUVALGLYALAHISPROALALEUGLU
14   SERARGVALPHEGLYASPASPGLYGLULEU
15   TYRASPHISILEASNVALLEUARGASNGLY
16   GLUALAALAALALEUGLYGLUALATHRALA
17   ALAGLYASPGLULEUALALEUPHEPROPRO
18   VALSERGLYGLY

Samples:

sample_1: sodium chloride 100 mM; sodium phosphate 20 mM; protein from Haloferax volcanii 0.6 mM; H2O 90%; D2O 10%

sample_2: sodium chloride 100 mM; sodium phosphate 20 mM; protein from Haloferax volcanii 0.6 mM; D2O 100%

sample_conditions_1: ionic strength: 0.12 M; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift calculation

NMR spectrometers:

  • Bruker DMX 500 MHz

Related Database Links:

PDB
GB ADE04519 ELY32526 ELZ76793 ELZ86249 ELZ91068
REF WP_004042720 WP_004969528 WP_007275285
SP D4GUF6

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