BMRB Entry 15167

Title:
NMR Structure of E. Coli YehR Protein. Northeast Structural Genomics Target ER538.
Deposition date:
2007-03-08
Original release date:
2007-04-11
Authors:
Ding, Keyang; Ramelot, Theresa; Cort, John; Chen, Chen; Jiang, Mei; Cunningham, Kellie; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, Gurla; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Ding, Keyang; Ramelot, Theresa; Cort, John; Jiang, Mei; Xiao, Rong; Swapna, Gurla; Montelione, Gaetano; Kennedy, Michael. "NMR Structure of E. Coli YehR Protein"  .

Assembly members:

Assembly members:
YehR, polymer, 139 residues, 15389.607 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Data typeCount
13C chemical shifts611
15N chemical shifts147
1H chemical shifts974

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YehR1

Entities:

Entity 1, YehR 139 residues - 15389.607 Da.

The C-terminal his-tag LEHHHHHH was included in calculation. The N-terminal 22 residues MKAFNKLFSLVVASVLVFSLAG was not included in the cloning.

1   METGLYASPLYSGLUGLUSERLYSLYSPHE
2   SERALAASNLEUASNGLYTHRGLUILEALA
3   ILETHRTYRVALTYRLYSGLYASPLYSVAL
4   LEULYSGLNSERSERGLUTHRLYSILEGLN
5   PHEALASERILEGLYALATHRTHRLYSGLU
6   ASPALAALALYSTHRLEUGLUPROLEUSER
7   ALALYSTYRLYSASNILEALAGLYVALGLU
8   GLULYSLEUTHRTYRTHRASPTHRTYRALA
9   GLNGLUASNVALTHRILEASPMETGLULYS
10   VALASPPHELYSALALEUGLNGLYILESER
11   GLYILEASNVALSERALAGLUASPALALYS
12   LYSGLYILETHRMETALAGLNMETGLULEU
13   VALMETLYSALAALAGLYPHELYSGLUVAL
14   LYSLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: protein, [U-100% 13C; U-100% 15N], 1 ± 0.2 mM; NH4OAc 20 ± 1 mM; NaCl 100 ± 5 mM; DTT 10 ± 1 mM; CaCl2 5 ± 1 mM; NaN3 0.02 ± 0.001 %; H2O 95 ± 0.001 %; D2O 5 ± 0.001 %

sample_2: protein, [U-5% 13C; U-100% 15N], 1 ± 0.2 mM; NH4OAc 20 ± 1 mM; NaCl 100 ± 5 mM; DTT 10 ± 1 mM; CaCl2 5 ± 1 mM; NaN3 0.02 ± 0.001 %; H2O 95 ± 0.001 %; D2O 5 ± 0.001 %

sample_3: protein, [U-100% 13C; U-100% 15N], 1 ± 0.2 mM; NH4OAc 20 ± 1 mM; NaCl 100 ± 5 mM; DTT 10 ± 1 mM; CaCl2 5 ± 1 mM; NaN3 0.02 ± 0.001 %; D2O 100 ± 0.001 %

sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 283 K

sample_conditions_2: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
3D HNCOsample_1isotropicsample_conditions_2
3D HNCAsample_1isotropicsample_conditions_2
3D HN(CO)CAsample_1isotropicsample_conditions_2
3D CBCA(CO)NHsample_1isotropicsample_conditions_2
3D HNCACBsample_1isotropicsample_conditions_2
3D HBHA(CO)NHsample_1isotropicsample_conditions_2
3D HNHAsample_2isotropicsample_conditions_2
3D C(CO)NHsample_1isotropicsample_conditions_2
3D H(CCO)NHsample_1isotropicsample_conditions_2
3D HCCH-TOCSYsample_1isotropicsample_conditions_2
2D 1H-13C HSQCsample_3isotropicsample_conditions_2
2D 1H-13C (Arom) HSQCsample_1isotropicsample_conditions_2
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N (NH2) HSQCsample_1isotropicsample_conditions_2
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C (Aliph) NOESYsample_1isotropicsample_conditions_1
3D 1H-13C (Arom) NOESYsample_1isotropicsample_conditions_1
3D 1H-13C (Aliph) NOESYsample_3isotropicsample_conditions_2
4D 1H-13C NOESYsample_3isotropicsample_conditions_2
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

X-PLOR NIH v2.15.0, Schwieters, Kuszewski, Tjandra and Clore - structure solution

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

SPARKY v3.1, Goddard - peak picking

NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

AutoStruct v2.1.1, Huang, Swapana, Rajan, Ke, Xia, Shukla, Inouye and Montelione - data analysis

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAB19552 BAB36357 BAE76599 BAG66588 BAG77915
EMBL CAP76626 CAQ32527 CAQ99044 CAR03550 CAR08661
GB AAA60486 AAC75184 AAG57191 AAN43719 AAN81109
PRF 2014253T
REF NP_310961 NP_416627 NP_708012 WP_000293099 WP_000397950
SP P33354
AlphaFold P33354

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