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 15975

Title: Sequence-specific 1H, 15N, and 13C resonance assignments and relaxation parameters for the whole region 4 of Escherichia coli RNA polymerase sigma70 subunit in 30% TFE   PubMed: 19847776

Authors: Kaczka, Piotr; Poznanski, Jarek

Citation: Kaczka, Piotr; Polkowska-Nowakowska, Agnieszka; Bolewska, Krystyna; Zhukov, Igor; Poznaski, Jarosaw; Wierzchowski, Kazimierz. "Backbone dynamics of TFE-induced native-like fold of region 4 of Escherichia coli RNA polymerase sigma70 subunit."  Proteins 78, 754-768 (2010).

Assembly members:
4_sigma70, polymer, 107 residues, 12032.5 Da.

Natural source:   Common Name: Escherichia coli   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):
4_sigma70: MGSSHHHHHHSSGLVPRGSH MLELPLDSATTESLRAATHD VLAGLTAREAKVLRMRFGID MNTDYTLEEVGKQFDVTRER IRQIEAKALRKLRHPSRSEV LRSFLDD

Data sets:
Data typeCount
13C chemical shifts431
15N chemical shifts104
1H chemical shifts661
heteronuclear NOE values100
T1 relaxation values101
T2 relaxation values101

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
14 sigma701

Entities:

Entity 1, 4 sigma70 107 residues - 12032.5 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METLEUGLULEUPROLEUASPSERALATHR
4   THRGLUSERLEUARGALAALATHRHISASP
5   VALLEUALAGLYLEUTHRALAARGGLUALA
6   LYSVALLEUARGMETARGPHEGLYILEASP
7   METASNTHRASPTYRTHRLEUGLUGLUVAL
8   GLYLYSGLNPHEASPVALTHRARGGLUARG
9   ILEARGGLNILEGLUALALYSALALEUARG
10   LYSLEUARGHISPROSERARGSERGLUVAL
11   LEUARGSERPHELEUASPASP

Samples:

sample_1: 4 sigma70, [U-13C; U-15N], 3 mM

sample_conditions_1: pH: 4.55; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
{1H-} -15N NOEsample_1isotropicsample_conditions_1
{1H-} -15N T1sample_1isotropicsample_conditions_1
{1H-} -15N T2sample_1isotropicsample_conditions_1

Software:

NMRPipe v1.7, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.111, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian UnityPlus 500 MHz

Related Database Links:

BMRB 15930 15936
PDB
DBJ BAB37373 BAE77118 BAG66772 BAG78873 BAH65247
EMBL CAD07736 CAL34114 CAP77541 CAQ33404 CAQ90501
GB AAA24601 AAA27242 AAA89147 AAB60181 AAC76103
PIR AB0893
REF NP_311977 NP_417539 NP_457602 NP_462126 NP_708877
SP P00579 P0A2E3 P0A2E4