BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17267

Title: Solution Structure of an Uncharacterized Thioredoin-like Protein from Clostridium perfringens

Deposition date: 2010-10-26 Original release date: 2010-11-08

Authors: Harris, R.; Foti, R.; Seidel, R.; Bonanno, J.; Freeman, J.; Bain, K.; Sauder, J.; Burley, S.; Girvin, M.; Almo, S.

Citation: Harris, R.; Foti, R.; Seidel, R.; Bonanno, J.; Freeman, J.; Bain, K.; Sauder, J.; Burley, S.; Girvin, M.; Almo, S.. "Solution Structure of an Uncharacterized Thioredoin-like Protein from Clostridium perfringens"  To be published ., .-..

Assembly members:
uncharacterized_thiredoxin-like_protein, polymer, 126 residues, 14739.896 Da.

Natural source:   Common Name: Clostridium perfringens   Taxonomy ID: 1502   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Clostridium perfringens

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

Entity Sequences (FASTA):
uncharacterized_thiredoxin-like_protein: MSLEGIKQINFQSINVVENL EEAKEGIPTIIMFKTDTCPY CVEMQKELSYVSKEREGKFN IYYARLEEEKNIDLAYKYDA NIVPTTVFLDKEGNKFYVHQ GLMRKNNIETILNSLGVKEG HHHHHH

Data sets:
Data typeCount
13C chemical shifts552
15N chemical shifts129
1H chemical shifts891

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1uncharacterized thiredoxin-like protein1

Entities:

Entity 1, uncharacterized thiredoxin-like protein 126 residues - 14739.896 Da.

residues 3-118 in the construct correspond to residues 28-142 of Uniprot entry Q0TMB4

1   METSERLEUGLUGLYILELYSGLNILEASN
2   PHEGLNSERILEASNVALVALGLUASNLEU
3   GLUGLUALALYSGLUGLYILEPROTHRILE
4   ILEMETPHELYSTHRASPTHRCYSPROTYR
5   CYSVALGLUMETGLNLYSGLULEUSERTYR
6   VALSERLYSGLUARGGLUGLYLYSPHEASN
7   ILETYRTYRALAARGLEUGLUGLUGLULYS
8   ASNILEASPLEUALATYRLYSTYRASPALA
9   ASNILEVALPROTHRTHRVALPHELEUASP
10   LYSGLUGLYASNLYSPHETYRVALHISGLN
11   GLYLEUMETARGLYSASNASNILEGLUTHR
12   ILELEUASNSERLEUGLYVALLYSGLUGLY
13   HISHISHISHISHISHIS

Samples:

sample_1: uncharacterized thiredoxin-like protein, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; DTT 1 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_2: uncharacterized thiredoxin-like protein, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; D2O 100%

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
15N HSQCsample_1isotropicsample_conditions_1
15N NOESY-HSQCsample_1isotropicsample_conditions_1
13C HSQCsample_2isotropicsample_conditions_1
aromatic 13C HSQCsample_2isotropicsample_conditions_1
13C NOESY-HSQCsample_2isotropicsample_conditions_1
13C aromatic NOESY-HSQCsample_2isotropicsample_conditions_1
HNCOsample_1isotropicsample_conditions_1
HNCACOsample_1isotropicsample_conditions_1
HNCAsample_1isotropicsample_conditions_1
HNCOCAsample_1isotropicsample_conditions_1
HNCACBsample_1isotropicsample_conditions_1
CBCACONHsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

  • Varian Inova 600 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB82244
EMBL CUO58703
GB ABG83276 ABG85509 ALG50133 EDS80627 EDT15421
REF WP_003450575 WP_003456683 WP_003473610

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