BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15642

Title: Solution structure of the aminoterminal domain of E. coli NusG   PubMed: 19500594

Authors: Schweimer, Kristian; Scheckenhofer, Ulrich; Roesch, Paul

Citation: Mooney, Rachel Anne; Schweimer, Kristian; Roesch, Paul; Gottesman, Max; Landick, Robert. "Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators."  J. Mol. Biol. 391, 341-358 (2009).

Assembly members:
NusG, polymer, 123 residues, 14096.366 Da.

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

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

Entity Sequences (FASTA):
NusG: MSEAPKKRWYVVQAFSGFEG RVATSLREHIKLHNMEDLFG EVMVPTEEVVEIRGGQRRKS ERKFFPGYVLVQMVMNDASW HLVRSVPRVMGFIGGTSDRP APISDKEVDAIMNRLQQVGD KPR

Data sets:
Data typeCount
13C chemical shifts498
15N chemical shifts122
1H chemical shifts790

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NusG1

Entities:

Entity 1, NusG 123 residues - 14096.366 Da.

1   METSERGLUALAPROLYSLYSARGTRPTYR
2   VALVALGLNALAPHESERGLYPHEGLUGLY
3   ARGVALALATHRSERLEUARGGLUHISILE
4   LYSLEUHISASNMETGLUASPLEUPHEGLY
5   GLUVALMETVALPROTHRGLUGLUVALVAL
6   GLUILEARGGLYGLYGLNARGARGLYSSER
7   GLUARGLYSPHEPHEPROGLYTYRVALLEU
8   VALGLNMETVALMETASNASPALASERTRP
9   HISLEUVALARGSERVALPROARGVALMET
10   GLYPHEILEGLYGLYTHRSERASPARGPRO
11   ALAPROILESERASPLYSGLUVALASPALA
12   ILEMETASNARGLEUGLNGLNVALGLYASP
13   LYSPROARG

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 0.4 mM; potassium phosphate 10 mM; sodium chloride 50 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 15490
PDB
DBJ BAB38328 BAE73404 BAE77338 BAG79793 BAH61119
EMBL CAD09492 CAG73137 CAH19518 CAL10413 CAL22339
GB AAA24622 AAC43080 AAC76956 AAF33495 AAG59178
PIR AB0934
REF NP_312932 NP_418409 NP_457922 NP_463017 NP_709777
SP P0AA01 P0AA02 P0AA03 P0AFG0 P0AFG1