BMRB Entry 17234

Title:
NMR structure of the DNA-binding domain of E.coli Lrp
Deposition date:
2010-10-01
Original release date:
2011-02-24
Authors:
Kawamura, Tetsuya; Zhou, Hongjun; Dahlquist, Frederick
Citation:

Citation: Kawamura, Tetsuya; Vartanian, Armand; Zhou, Hongjun; Dahlquist, Frederick. "The Design Involved in PapI and Lrp Regulation of the pap Operon."  J. Mol. Biol. 409, 311-332 (2011).
PubMed: 21338611

Assembly members:

Assembly members:
Lrp_DNA-binding_domain, polymer, 66 residues, 7621.872 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Lrp_DNA-binding_domain: MVDSKKRPGKDLDRIDRNIL NELQKDGRISNVELSKRVGL SPTPCLERVRRLERQGFIQG YTALLN

Data sets:
Data typeCount
13C chemical shifts275
15N chemical shifts62
1H chemical shifts451

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Lrp_DNA-binding_domain1

Entities:

Entity 1, Lrp_DNA-binding_domain 66 residues - 7621.872 Da.

1   METVALASPSERLYSLYSARGPROGLYLYS
2   ASPLEUASPARGILEASPARGASNILELEU
3   ASNGLULEUGLNLYSASPGLYARGILESER
4   ASNVALGLULEUSERLYSARGVALGLYLEU
5   SERPROTHRPROCYSLEUGLUARGVALARG
6   ARGLEUGLUARGGLNGLYPHEILEGLNGLY
7   TYRTHRALALEULEUASN

Samples:

sample_1: Lrp DNA-binding domain, [U-99% 13C; U-99% 15N], 2 mM; potassium phosphate 50 mM; beta-mercaptoethanol 5 mM; H2O 90%; D2O 10%

sample_2: Lrp DNA-binding domian, [U-99% 13C; U-99% 15N], 2 mM; potassium phosphate 50 mM; DTT 2 mM; D2O 100%

sample_3: Lrp DNA-biinding domain, [U-99% 13C; U-99% 15N], 80 – 150 uM; potassium phosphate 30 mM; beta-mercaptoethanol 2 mM; potassium chloride 20 mM; H2O 90%; D2O 10%

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
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
4D 15N-13C edited NOESYsample_1isotropicsample_conditions_1
4D 13C-131C edited NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1

Software:

ANSIG v3.3, Kraulis - chemical shift assignment

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

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

X-PLOR, Brunger - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA01880 BAA35614 BAB34397 BAE74382 BAG76471
EMBL CAA76565 CAD05359 CAG75548 CAP75362 CAQ31417
GB AAA24089 AAA75439 AAA75465 AAA75466 AAA75467
PIR AE0611
REF NP_309001 NP_415409 NP_455447 NP_459935 NP_706774
SP P0A2S0 P0ACJ0 P0ACJ1 P0ACJ2 P0ACJ3
AlphaFold P0A2S0 P0ACJ0 P0ACJ1 P0ACJ2 P0ACJ3

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