BMRB Entry 17962

Title:
Solution structure of putative oxidoreductase from Ehrlichia chaffeensis. (Seattle Structural Genomics Center for Infectious Disease (SSGCID))
Deposition date:
2011-09-30
Original release date:
2011-10-26
Authors:
Yang, Fan; Barnwal, Ravi; Varani, Gabriele
Citation:

Citation: Yang, Fan; Barnwal, Ravi; Varani, Gabriele. "Solution structure of putative oxidoreductase from Ehrlichia chaffeensis"  .

Assembly members:

Assembly members:
putative oxidoreductase from Ehrlichia chaffeensis, polymer, 104 residues, 12015.776 Da.

Natural source:

Natural source:   Common Name: Ehrlichia chaffeensis   Taxonomy ID: 945   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Ehrlichia chaffeensis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
putative oxidoreductase from Ehrlichia chaffeensis: MQEQVSNVRARIYKPAKSTM QSGHSKLKAWKLEFEPSCTQ YTEPLMNWTGSHDTKQQVCL SFTTRELAIAYAVAHKIDYT VLQDNPRTIVPKSYADNFTK PRDM

Data sets:
Data typeCount
13C chemical shifts381
15N chemical shifts99
1H chemical shifts471

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1putative oxidoreductase from Ehrlichia chaffeensis1

Entities:

Entity 1, putative oxidoreductase from Ehrlichia chaffeensis 104 residues - 12015.776 Da.

1   METGLNGLUGLNVALSERASNVALARGALA
2   ARGILETYRLYSPROALALYSSERTHRMET
3   GLNSERGLYHISSERLYSLEULYSALATRP
4   LYSLEUGLUPHEGLUPROSERCYSTHRGLN
5   TYRTHRGLUPROLEUMETASNTRPTHRGLY
6   SERHISASPTHRLYSGLNGLNVALCYSLEU
7   SERPHETHRTHRARGGLULEUALAILEALA
8   TYRALAVALALAHISLYSILEASPTYRTHR
9   VALLEUGLNASPASNPROARGTHRILEVAL
10   PROLYSSERTYRALAASPASNPHETHRLYS
11   PROARGASPMET

Samples:

sample_1: oxidoreductase, [U-95% 15N], 0.5 mM; potassium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_2: oxidoreductase, [U-95% 13C; U-95% 15N], 0.5 mM; potassium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - structure display

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB ABD44783 AHX03349 AHX05932 AHX06922 AHX07274
REF WP_006010520

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