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 18849

Title: Chemical shift assignments and secondary structure prediction of the C-terminal domain of the response regulator BfmR from Acinetobacter baumannii   PubMed: 23264007

Deposition date: 2012-11-20 Original release date: 2012-11-26

Authors: Olson, Andrew; Thompson, Richele; Melander, Christian; Cavanagh, John

Citation: Olson, Andrew; Thompson, Richele; Melander, Christian; Cavanagh, John. "Chemical shift assignments and secondary structure prediction of the C-terminal domain of the response regulator BfmR from Acinetobacter baumannii."  Biomol. NMR Assignments ., .-. (2012).

Assembly members:
BfmrC, polymer, 117 residues, Formula weight is not available

Natural source:   Common Name: Acinetobacter baumannii   Taxonomy ID: 470   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Acinetobacter baumannii

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

Entity Sequences (FASTA):
BfmrC: EDEVAQRIEFDDLVIDNGGR SVTLNGELVDFTSAEYDLLW LLASNAGRILSREDIFERLR GIEYDGQDRSIDVRISRIRP KIGDDPENPKRIKTVRSKGY LFVKETNGLLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts420
15N chemical shifts96
1H chemical shifts686

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BfmrC1

Entities:

Entity 1, BfmrC 117 residues - Formula weight is not available

1   GLUASPGLUVALALAGLNARGILEGLUPHE
2   ASPASPLEUVALILEASPASNGLYGLYARG
3   SERVALTHRLEUASNGLYGLULEUVALASP
4   PHETHRSERALAGLUTYRASPLEULEUTRP
5   LEULEUALASERASNALAGLYARGILELEU
6   SERARGGLUASPILEPHEGLUARGLEUARG
7   GLYILEGLUTYRASPGLYGLNASPARGSER
8   ILEASPVALARGILESERARGILEARGPRO
9   LYSILEGLYASPASPPROGLUASNPROLYS
10   ARGILELYSTHRVALARGSERLYSGLYTYR
11   LEUPHEVALLYSGLUTHRASNGLYLEULEU
12   GLUHISHISHISHISHISHIS

Samples:

sample_1: BfmrC, [U-100% 13C; U-100% 15N], 1 mM; Tris-HCl 0.025 M; KCl 0.05 M

sample_2: BfmrC, [U-100% 13C], 1 mM; Tris-HCl 0.025 M; KCl 0.05 M

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Varian INOVA 600 MHz

Related Database Links:

DBJ BAN88679 BAP35785 BAP67858 GAB01456 GAB75315
EMBL CAG67634 CAM87883 CAP02024 CDG76603 CDG77731
GB AAX40744 ABO11188 ACC56017 ACJ40594 ACJ59134
REF WP_000076438 WP_000076439 WP_000076440 WP_000076441 WP_000076442

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