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Biological Magnetic Resonance Data Bank


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BMRB Entry 19452

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19452
MolProbity Validation Chart

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Title: Solution NMR structure of a putative thioredoxin (ECH_0218) in the reduced state from Ehrlichia chaffeensis, the etiological agent responsible for human monocytic ehrlichiosis. Seattle Structural Genomics Center for Infectious Disease target EhchA.00546.a

Deposition date: 2013-08-26 Original release date: 2016-05-26

Authors: Buchko, Garry

Citation: Buchko, Garry; Hewitt, Stephen; Van Voorhis, Wesley; Myler, Peter. "Solution structure of the Ehrlichia chaffeensis thioredoxin ECH_0218 in the reduced state: disorder around the CXXC active site."  Not known ., .-..

Assembly members:
entity, polymer, 120 residues, 14362.317 Da.

Natural source:   Common Name: a-proteobacteria   Taxonomy ID: 205920   Superkingdom: Bacteria   Kingdom: Proteobacteria   Genus/species: Ehrlichia chaffeensis

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

Entity Sequences (FASTA):
entity: MGTLEAQTQGPGSMIEQIGD SEFDNKVTSCNDNILILVDF WAPWCGPCRSLEPQLEKLAQ QYTENVKIYKINIEDNQDVA TQYGVSAIPTILMFKNGKKL SQVIGADISKIISEINNNIN

Data sets:
Data typeCount
13C chemical shifts410
15N chemical shifts109
1H chemical shifts616

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1putative thioredoxin (ECH_0218)1

Entities:

Entity 1, putative thioredoxin (ECH_0218) 120 residues - 14362.317 Da.

1   METGLYTHRLEUGLUALAGLNTHRGLNGLY
2   PROGLYSERMETILEGLUGLNILEGLYASP
3   SERGLUPHEASPASNLYSVALTHRSERCYS
4   ASNASPASNILELEUILELEUVALASPPHE
5   TRPALAPROTRPCYSGLYPROCYSARGSER
6   LEUGLUPROGLNLEUGLULYSLEUALAGLN
7   GLNTYRTHRGLUASNVALLYSILETYRLYS
8   ILEASNILEGLUASPASNGLNASPVALALA
9   THRGLNTYRGLYVALSERALAILEPROTHR
10   ILELEUMETPHELYSASNGLYLYSLYSLEU
11   SERGLNVALILEGLYALAASPILESERLYS
12   ILEILESERGLUILEASNASNASNILEASN

Samples:

sample_1: sodium chloride 100 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.2 mM; entity, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; H2O 93%; D2O 7%

sample_2: sodium chloride 100 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.2 mM; entity, [U-99% 15N], 1 ± 0.2 mM; D2O 100%

sample_conditions_1: ionic strength: 0.12 M; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
deuterium exchangesample_2isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D HBCBCGCDCDHDsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY v3.115, Goddard - data analysis, peak picking

FELIX v2007, Accelrys Software Inc. - processing

PSVS v1.3, Bhattacharya and Montelione - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

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