BMRB Entry 19957

Title:
Assignment of DNA-MC1 protein complex
Deposition date:
2014-05-07
Original release date:
2014-10-14
Authors:
Loth, Karine; Landon, Celine; Paquet, Francoise
Citation:

Citation: Loth, Karine; Landon, Celine; Paquet, Francoise. "Chemical shifts assignments of the archaeal MC1 protein and a strongly bent 15 base pairs DNA duplex in complex"  Biomol. NMR Assignments ., .-. (2014).
PubMed: 25212183

Assembly members:

Assembly members:
MC1, polymer, 93 residues, Formula weight is not available
DNA1, polymer, 15 residues, Formula weight is not available
DNA2, polymer, 15 residues, Formula weight is not available

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: pET24a-mc1

Data typeCount
13C chemical shifts78
15N chemical shifts103
1H chemical shifts873

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MC11
2DNA12
3DNA23

Entities:

Entity 1, MC1 93 residues - Formula weight is not available

1   SERASNTHRARGASNPHEVALLEUARGASP
2   GLUASPGLYASNGLUHISGLYVALPHETHR
3   GLYLYSGLNPROARGGLNALAALALEULYS
4   ALAALAASNARGGLYSERGLYTHRLYSALA
5   ASNPROASPILEILEARGLEUARGGLUARG
6   GLYTHRLYSLYSVALHISVALPHELYSALA
7   TRPLYSGLUILEVALASPALAPROLYSASN
8   ARGPROALATRPMETPROGLULYSILESER
9   LYSPROPHEVALLYSLYSGLUARGILEGLU
10   LYSLEUGLU

Entity 2, DNA1 15 residues - Formula weight is not available

1   DADADADADADCDADCDADC
2   DADCDCDCDA

Entity 3, DNA2 15 residues - Formula weight is not available

1   DTDGDGDGDTDGDTDGDTDG
2   DTDTDTDTDT

Samples:

sample_1: MC1, [U-15N], 1.18 mM; DNA1, [U-13C; U-15N], 1.18 mM; DNA2 1.18 mM; sodium phosphate 10 mM; sodium chloride 100 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 299 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

TOPSPIN, Bruker Biospin - collection

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

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance III HD 700 MHz

Related Database Links:

PDB
GB AKB13417 AKB15948 ALK04717
REF WP_048167444
SP P12770
AlphaFold P12770

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