BMRB Entry 19938

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19938
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution NMR structure of a putative thioredoxin (ECH_0218) in the oxidized 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:
2014-04-24
Original release date:
2014-05-12
Authors:
Buchko, Garry
Citation:

Citation: Buchko, Garry; Hewitt, Stephan; Van Voorhis, Wesley; Myler, Peter. "Solution structure of the Ehrlichia chaffeensis thioredoxin ECH_0218 in the reduced and oxidized states: disorder around the CXXC active site"  .

Assembly members:

Assembly members:
entity, polymer, 256 residues, 28706.621 Da.

Natural source:

Natural source:   Common Name: a-proteobacteria   Taxonomy ID: 205920   Superkingdom: Bacteria   Kingdom: not available   Genus/species: EHRLICHIA CHAFFEENSIS

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: AVA0421

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MAHHHHHHMGTLEAQTQGPG SMIEQIGDSEFDNKVTSCND NILILVDFWAPWCGPCRSLE PQLEKLAQQYTENVKIYKIN IEDNQDVATQYGVSAIPTIL MFKNGKKLSQVIGADISKII SEINNNINMAHHHHHHMGTL EAQTQGPGSMIEQIGDSEFD NKVTSCNDNILILVDFWAPW CGPCRSLEPQLEKLAQQYTE NVKIYKINIEDNQDVATQYG VSAIPTILMFKNGKKLSQVI GADISKIISEINNNIN

Data sets:
Data typeCount
13C chemical shifts352
15N chemical shifts117
1H chemical shifts700

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1putative thioredoxin (ECH_0218) in the oxidized state1

Entities:

Entity 1, putative thioredoxin (ECH_0218) in the oxidized state 256 residues - 28706.621 Da.

1   METALAHISHISHISHISHISHISMETGLY
2   THRLEUGLUALAGLNTHRGLNGLYPROGLY
3   SERMETILEGLUGLNILEGLYASPSERGLU
4   PHEASPASNLYSVALTHRSERCYSASNASP
5   ASNILELEUILELEUVALASPPHETRPALA
6   PROTRPCYSGLYPROCYSARGSERLEUGLU
7   PROGLNLEUGLULYSLEUALAGLNGLNTYR
8   THRGLUASNVALLYSILETYRLYSILEASN
9   ILEGLUASPASNGLNASPVALALATHRGLN
10   TYRGLYVALSERALAILEPROTHRILELEU
11   METPHELYSASNGLYLYSLYSLEUSERGLN
12   VALILEGLYALAASPILESERLYSILEILE
13   SERGLUILEASNASNASNILEASNMETALA
14   HISHISHISHISHISHISMETGLYTHRLEU
15   GLUALAGLNTHRGLNGLYPROGLYSERMET
16   ILEGLUGLNILEGLYASPSERGLUPHEASP
17   ASNLYSVALTHRSERCYSASNASPASNILE
18   LEUILELEUVALASPPHETRPALAPROTRP
19   CYSGLYPROCYSARGSERLEUGLUPROGLN
20   LEUGLULYSLEUALAGLNGLNTYRTHRGLU
21   ASNVALLYSILETYRLYSILEASNILEGLU
22   ASPASNGLNASPVALALATHRGLNTYRGLY
23   VALSERALAILEPROTHRILELEUMETPHE
24   LYSASNGLYLYSLYSLEUSERGLNVALILE
25   GLYALAASPILESERLYSILEILESERGLU
26   ILEASNASNASNILEASN

Samples:

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

sample_conditions_1: ionic strength: 0.12 M; pH: 7; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
deuterium exchangesample_1isotropicsample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - final refinement with explicit water, refinement

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

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

Felix v2007, Accelrys Software Inc. - processing

PSVS v1.5, Bhattacharya and Montelione - data analysis

TALOS v+, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian VNMRS 750 MHz
  • Varian VNMRS 800 MHz

Related Database Links:

PDB

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