BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16557

Title: Solution Structure Of Protein SOS-response transcriptional repressor, LexA From Eubacterium rectale. Northeast Structural Genomics Consortium Target ErR9A

Deposition date: 2009-10-16 Original release date: 2009-11-18

Authors: Wu, Yibing; Eletsky, Alexander; Lee, Dan; Ghosh, Arindam; Buchwald, William; Zhang, Qi; Janjua, Haleema; Garcia, Erwin; Nair, R.; Sukumaran, Dinesh; Rost, B.; Acton, T.B; Xiao, R.; Everett, J.K.; Montelione, G.T.; Szyperski, Thomas

Citation: Wu, Yibing; Eletsky, Alexander; Lee, Dan; Ghosh, Arindam; Buchwald, William; Zhang, Qi; Janjua, Haleema; Garcia, Erwin; Nair, R.; Sukumaran, Dinesh; Rost, B.; Acton, T.B; Everett, J.K.; Montelione, G.T.; Szyperski, Thomas. "Solution Structure Of Protein SOS-response transcriptional repressor, LexA From Eubacterium rectale. Northeast Structural Genomics Consortium Target ErR9A"  .

Assembly members:
ErR9A, polymer, 94 residues, 10723.338 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21(DE3)+Magic

Entity Sequences (FASTA):
ErR9A: MVKDKQKAIFSENLNSYIAK SEKTQLEIAKSIGVSPQTFN TWCKGIAIPRMGKVQALADY FNINKSDLIEDKKLNIDTVP IESGYTLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts285
15N chemical shifts89
1H chemical shifts607

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ErR9A1

Entities:

Entity 1, ErR9A 94 residues - 10723.338 Da.

1   METVALLYSASPLYSGLNLYSALAILEPHE
2   SERGLUASNLEUASNSERTYRILEALALYS
3   SERGLULYSTHRGLNLEUGLUILEALALYS
4   SERILEGLYVALSERPROGLNTHRPHEASN
5   THRTRPCYSLYSGLYILEALAILEPROARG
6   METGLYLYSVALGLNALALEUALAASPTYR
7   PHEASNILEASNLYSSERASPLEUILEGLU
8   ASPLYSLYSLEUASNILEASPTHRVALPRO
9   ILEGLUSERGLYTYRTHRLEUGLUHISHIS
10   HISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O 10%

sample_2: entity, [U-5% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
4,3D, GFT HNNCABCAsample_1isotropicsample_conditions_1
4,3D, GFT CABCACONNHsample_1isotropicsample_conditions_1
4,3D, GFT HCCH COSYsample_1isotropicsample_conditions_1
3D, 15N-13C RESOLVEDSIMULTANIOUS NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

PSVS, Bhattacharya and Montelione - refinement

TALOS, Cornilescu, Delaglio and Bax - refinement

XEASY, Bartels et al. - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker DMX 800 MHz
  • Bruker DMX 800 MHz

Related Database Links:

PDB
GB ACR75018
REF WP_012742117

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