BMRB Entry 15334

Title:
Solution Structure of the Beryllofluoride-Activated NtrC4 Receiver Domain Dimer
Deposition date:
2007-06-27
Original release date:
2012-08-03
Authors:
Lee, Chul-Jin; Hong, Eunmi; Doucleff, Michaeleen; Pelton, Jeffrey; Wemmer, David
Citation:

Citation: Hastings, Curtis; Lee, Seok-Yong; Cho, Ho; Yan, Dalai; Kustu, Sydney; Wemmer, David. "High-resolution solution structure of the beryllofluoride-activated NtrC receiver domain."  Biochemistry 42, 9081-9090 (2003).
PubMed: 12885241

Assembly members:

Assembly members:
NtrC4 Receiver domain dimer, polymer, 121 residues, 13671.741 Da.

Natural source:

Natural source:   Common Name: AQUIFEX AEOLICUS VF5   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: PET21A

Data sets:
Data typeCount
13C chemical shifts384
15N chemical shifts115
1H chemical shifts821

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NtrC4 Receiver domain 11
2NtrC4 Receiver domain 21

Entities:

Entity 1, NtrC4 Receiver domain 1 121 residues - 13671.741 Da.

1   METLYSARGVALLEUVALVALASPASPGLU
2   GLUSERILETHRSERSERLEUSERALAILE
3   LEUGLUGLUGLUGLYTYRHISPROASPTHR
4   ALALYSTHRLEUARGGLUALAGLULYSLYS
5   ILELYSGLULEUPHEPHEPROVALILEVAL
6   LEUASPVALTRPMETPROASPGLYASPGLY
7   VALASNPHEILEASPPHEILELYSGLUASN
8   SERPROASPSERVALVALILEVALILETHR
9   GLYHISGLYSERVALASPTHRALAVALLYS
10   ALAILELYSLYSGLYALATYRGLUPHELEU
11   GLULYSPROPHESERVALGLUARGPHELEU
12   LEUTHRILELYSHISALAPHEGLUGLUTYR
13   SER

Samples:

sample_1: NtrC4Ra, [U-100% 13C; U-100% 15N], 1 ± 0.2 mM

sample_2: NtrC4Ra, [U-100% 13C], 0.8 mM

sample_3: NtrC4Ra 0.8 mM

sample_conditions_1: ionic strength: 0 M; pH: 8.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
15N-IPAP-HSQCsample_1isotropicsample_conditions_1
[F1] 13C-edited [F3] 13C-filtered HSQC-NOESYsample_2isotropicsample_conditions_1
HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH v2.1.2, Schwieters, Kuszewski, Tjandra and Clore - structure solution

SPARKY v3.12, Goddard - chemical shift assignment

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

NMR spectrometers:

  • Bruker DRX 900 MHz
  • Bruker DRX 800 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB
GB AAC06509
REF NP_213111 WP_010880049

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