BMRB Entry 18849

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18849
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Chemical shift assignments and secondary structure prediction of the C-terminal domain of the response regulator BfmR from Acinetobacter baumannii
Deposition date:
2012-11-20
Original release date:
2012-11-26
Authors:
Olson, Andrew; Thompson, Richele; Melander, Christian; Cavanagh, John
Citation:

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).
PubMed: 23264007

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-16b

Entity Sequences (FASTA):

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