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 15793

Title: CopR Repressor Structure   PubMed: 18837698

Authors: Cantini, Francesca; Banci, Lucia; Magnani, David; Solioz, Marc

Citation: Cantini, Francesca; Banci, Lucia; Solioz, Marc. "The copper-responsive repressor CopR of Lactococcus lactis is a 'winged helix' protein"  Biochem. J. ., 493-499 (2009).

Assembly members:
CopR-NTD, polymer, 99 residues, 8064.518 Da.

Natural source:   Common Name: Lactococcus lactis   Taxonomy ID: 1358   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Lactococcus lactis

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

Entity Sequences (FASTA):
CopR-NTD: MSYYHHHHHHDYDIPTTENL YFQGAMNEVEFNVSNAELIV MRVIWSLGEARVDEIYAQIP QELEWSLATVKTLLGRLVKK EMLSTEKEGRKFVYRPLME

Data sets:
Data typeCount
13C chemical shifts230
15N chemical shifts52
1H chemical shifts407
heteronuclear NOE values49
T1 relaxation values49
T2 relaxation values49

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 99 residues - 8064.518 Da.

CopR-NTD with the his tag was a protein of 99 amino acids, consisting of the 25 amino acid tag, MSYYHHHHHHDYDIPTTENLYFQGA, followed by the N-terminal 74 residues of CopR.

1   METSERTYRTYRHISHISHISHISHISHIS
2   ASPTYRASPILEPROTHRTHRGLUASNLEU
3   TYRPHEGLNGLYALAMETASNGLUVALGLU
4   PHEASNVALSERASNALAGLULEUILEVAL
5   METARGVALILETRPSERLEUGLYGLUALA
6   ARGVALASPGLUILETYRALAGLNILEPRO
7   GLNGLULEUGLUTRPSERLEUALATHRVAL
8   LYSTHRLEULEUGLYARGLEUVALLYSLYS
9   GLUMETLEUSERTHRGLULYSGLUGLYARG
10   LYSPHEVALTYRARGPROLEUMETGLU

Samples:

sample_1: CopR-NTD, [U-99% 13C; U-99% 15N], 0.2 ± 0.05 mM; NaPi 50 mM; NaCl 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.25 M; pH: 7.5; pressure: 1 atm; temperature: 298 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 HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CARA v1.8.4, CARA - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ BAL50764 GAM79848
EMBL CAL98303 CDG05267 CDI47235
GB AAK04930 ABJ72438 ADA64579 ADJ60716 ADZ63448
REF NP_266988 WP_003132584 WP_011675785 WP_011835521 WP_033900304