BMRB Entry 15991

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15991

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Title:
Structure of the Core Binding Domain of sigma54
Deposition date:
2008-10-19
Original release date:
2009-05-29
Authors:
Hong, Eunmi; Wemmer, David E.
Citation:

Citation: Hong, Eunmi; Douclaff, Michaeleen; Wemmer, David. "Structure of the RNA Polymerase Core-Binding Domain of sigma(54) Reveals a Likely Conformational Fracture Point."  J. Mol. Biol. 390, 70-82 (2009).
PubMed: 19426742

Assembly members:

Assembly members:
Core_Binding_Domain, polymer, 130 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Aquifex aeolicus   Taxonomy ID: 63363   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Aquifex aeolicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21b3-2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Core_Binding_Domain: YTPSELEELQQNIKLELEGK EQELALELLNYLNEKGFLSK SVEEISDVLRCSVEELEKVR QKVLRLEPLGVCSKDVWEFL ELQIEEIYPEEEEILKKALR DLKRGKKLKPEIKGKLSRLR LFPLSSSAEK

Data sets:
Data typeCount
13C chemical shifts419
15N chemical shifts126
1H chemical shifts975

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11

Entities:

Entity 1, subunit 1 130 residues - Formula weight is not available

1   TYRTHRPROSERGLULEUGLUGLULEUGLN
2   GLNASNILELYSLEUGLULEUGLUGLYLYS
3   GLUGLNGLULEUALALEUGLULEULEUASN
4   TYRLEUASNGLULYSGLYPHELEUSERLYS
5   SERVALGLUGLUILESERASPVALLEUARG
6   CYSSERVALGLUGLULEUGLULYSVALARG
7   GLNLYSVALLEUARGLEUGLUPROLEUGLY
8   VALCYSSERLYSASPVALTRPGLUPHELEU
9   GLULEUGLNILEGLUGLUILETYRPROGLU
10   GLUGLUGLUILELEULYSLYSALALEUARG
11   ASPLEULYSARGGLYLYSLYSLEULYSPRO
12   GLUILELYSGLYLYSLEUSERARGLEUARG
13   LEUPHEPROLEUSERSERSERALAGLULYS

Samples:

sample_1: Core Binding Domain, [U-100% 13C; U-100% 15N], 0.6-0.8 mM; Core Binding Domain, [U-100% 15N], 0.6-0.8 mM; H2O 90%; D2O 10%

sample_2: Core Binding Domain, [U-100% 13C; U-100% 15N], 0.6-0.8 mM; D2O 100%

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY v3.114, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DRX 900 MHz

Related Database Links:

BMRB 15990
PDB
GB AAC06814
REF NP_213418 WP_010880356

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