BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16001

Title: SOLUTION STRUCTURE OF DNA BINDING DOMAIN OF E. COLI ARAC   PubMed: 19422057

Authors: Rodgers, Michael; Schleif, Robert

Citation: Rodgers, Michael; Schleif, Robert. "Solution Structure of the DNA binding domain of AraC protein"  Proteins 77, 202-208 (2009).

Assembly members:
AraC-DBD, polymer, 107 residues, 12096.795 Da.

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

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

Entity Sequences (FASTA):
AraC-DBD: MDNRVREACQYISDHLADSN FDIASVAQHVCLSPSRLSHL FRQQLGISVLSWREDQRISQ AKLLLSTTRMPIATVGRNVG FDDQLYFSRVFKKCTGASPS EFRAGCE

Data sets:
Data typeCount
13C chemical shifts465
15N chemical shifts114
1H chemical shifts715

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AraC-DBD1

Entities:

Entity 1, AraC-DBD 107 residues - 12096.795 Da.

Residues 175 through 280 of native E. coli AraC

1   METASPASNARGVALARGGLUALACYSGLN
2   TYRILESERASPHISLEUALAASPSERASN
3   PHEASPILEALASERVALALAGLNHISVAL
4   CYSLEUSERPROSERARGLEUSERHISLEU
5   PHEARGGLNGLNLEUGLYILESERVALLEU
6   SERTRPARGGLUASPGLNARGILESERGLN
7   ALALYSLEULEULEUSERTHRTHRARGMET
8   PROILEALATHRVALGLYARGASNVALGLY
9   PHEASPASPGLNLEUTYRPHESERARGVAL
10   PHELYSLYSCYSTHRGLYALASERPROSER
11   GLUPHEARGALAGLYCYSGLU

Samples:

AraC-DBD-1: AraC-DBD, [U-100% 15N], 0.5 – 1.0 mM; PHOSPHATE BUFFER 50 mM; NACL 400 mM; NAN3 0.1 mM

AraC-DBD-2: AraC-DBD, [U-100% 13C; U-100% 15N], 0.5-1.0 mM; PHOSPHATE BUFFER 50 mM; NACL 400 mM; NAN3 0.1 mM

sample_conditions_1: ionic strength: 400 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_13C-SEPARATED_ALI_NOESYAraC-DBD-2isotropicsample_conditions_1
3D_13C-SEPARATED_ARO_NOESYAraC-DBD-2isotropicsample_conditions_1
3D 1H-15N-SEPARATED NOESYAraC-DBD-1isotropicsample_conditions_1
2D 1H-15N HSQCAraC-DBD-1isotropicsample_conditions_1
2D 1H-13C HSQCAraC-DBD-2isotropicsample_conditions_1
3D HNCOAraC-DBD-2isotropicsample_conditions_1
3D HNCAAraC-DBD-2isotropicsample_conditions_1
3D HNCACBAraC-DBD-2isotropicsample_conditions_1
3D HN(CO)CAAraC-DBD-2isotropicsample_conditions_1
3D CBCA(CO)NHAraC-DBD-2isotropicsample_conditions_1
3D HCCH-COSYAraC-DBD-2isotropicsample_conditions_1
3D HCCCONH-TOCSYAraC-DBD-2isotropicsample_conditions_1
3D H_CCCONH-TOCSYAraC-DBD-2isotropicsample_conditions_1

Software:

CYANA v2.0, P.GUNTERT ET AL. - refinement

ATHNOS-CANDID, Herrmann, Guntert and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - structure solution

NMR spectrometers:

  • VARIAN INOVA 800 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAB33491 BAB96633 BAG75588 BAI23427 BAI28943
EMBL CAA23507 CAA23508 CAL59724 CAP74634 CAQ30582
GB AAA23092 AAA23466 AAA27026 AAC53662 AAC73175
REF NP_308095 NP_414606 NP_459109 NP_706017 WP_000840169
SP P03022 P0A9E0 P0A9E1 P11765