BMRB Entry 16995

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16995
MolProbity Validation Chart

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Title:
Solution structure of a bolA protein (ECH_0303) from Ehrlichia chaffeensis, the causative agent of human monocytic ehrlichiosis. Seattle Structural Genomics Center for Infectious Disease (SSGCID) target EhchA.10365.a
Deposition date:
2010-06-10
Original release date:
2010-07-01
Authors:
Garry, Buchko
Citation:

Citation: Buchko, Garry; Hewitt, Stephen; Napuli, Alberto; Van Voorhis, Wesley; Myler, Peter. "Structural characterization of a BolA protein (ECH_0303) from Ehrlichia chaffeensis, the agent responsible for human monocytotropic ehrlichiosis."  .

Assembly members:

Assembly members:
ECH_0303, polymer, 76 residues, Formula weight is not available

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: AVA0421

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ECH_0303: PGSMTVTQSQLELLIRNAFP EAEITVTSLVGDNNHYSIKV ISSQFQGKSKLEQHRMIYKV LDGLNIHAIQIQTGCK

Data sets:
Data typeCount
13C chemical shifts272
15N chemical shifts66
1H chemical shifts447

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1ECH_03031

Entities:

Entity 1, ECH_0303 76 residues - Formula weight is not available

The first three residues, PGS-, are left over after removal of the N-terminal tag. The first native residue is M4.

1   PROGLYSERMETTHRVALTHRGLNSERGLN
2   LEUGLULEULEUILEARGASNALAPHEPRO
3   GLUALAGLUILETHRVALTHRSERLEUVAL
4   GLYASPASNASNHISTYRSERILELYSVAL
5   ILESERSERGLNPHEGLNGLYLYSSERLYS
6   LEUGLUGLNHISARGMETILETYRLYSVAL
7   LEUASPGLYLEUASNILEHISALAILEGLN
8   ILEGLNTHRGLYCYSLYS

Samples:

sample_1: ECH_0303, [U-99% 13C; U-99% 15N], 1.5 ± 0.3 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.2 mM; H2O 90%; D2O 10%

sample_2: ECH_0303, [U-99% 13C; U-99% 15N], 1.0 ± 0.1 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.2 mM; D2O 100%

sample_conditions_1: ionic strength: 0.12 M; pH: 7.1; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

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

FELIX v2007, Accelrys Software Inc. - processing

SPARKY v3.115, Goddard - data analysis

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
GB ABD45544 AHX03418 AHX05861 AHX06852 AHX07132
REF WP_006011371

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