BMRB Entry 51449

Name: Backbone chemical shifts of DNA binding domain of Cytidine Repressor
Published: 2023-07-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51449

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone chemical shifts of DNA binding domain of Cytidine Repressor

Deposition date:

2022-05-19

Original release date:

2023-07-04

Authors:

Kulkarni, Madhurima; Nandi, Bodhisatwa; Munshi, Sneha; Naganathan, Athi; Sekhar, Ashok

Citation:

Citation: Madhurima, Kulkarni; Nandi, Bodhisatwa; Munshi, Sneha; Naganathan, Athi; Sekhar, Ashok. "Functional regulation of an intrinsically disordered protein via a conformationally excited state" Sci. Adv. 9, eadh4591-eadh4591 (2023).
PubMed: 37379390

Assembly members:

Assembly members:
entity_1, polymer, 66 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: pET-29b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKAKKQETAATMKDVALKAK VSTATVSRALMNPDKVSQAT RNRVEKAAREVGYLPQPMGR NVKRNE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	195
15N chemical shifts	59
1H chemical shifts	113

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DNA binding domain of Cytidine Repressor	1

Entities:

Entity 1, DNA binding domain of Cytidine Repressor 66 residues - Formula weight is not available

1

MET

LYS

ALA

LYS

GLN

GLU

THR

ALA

2

THR

MET

LYS

ASP

VAL

ALA

LEU

LYS

ALA

LYS

3

VAL

SER

THR

ALA

THR

VAL

SER

ARG

ALA

LEU

4

MET

ASN

PRO

ASP

LYS

VAL

SER

GLN

ALA

THR

5

ARG

ASN

ARG

VAL

GLU

LYS

ALA

ARG

GLU

6

VAL

GLY

TYR

LEU

PRO

GLN

PRO

MET

GLY

ARG

7

ASN

VAL

LYS

ARG

ASN

GLU

Samples:

sample_1: DNA binding domain of Cytidine Repressor, [U-99% 13C; U-99% 15N], 614 uM; D2O, [U-100% 2H], 10% v/v; H2O 90% v/v; sodium phosphate 20 mM

sample_2: DNA binding domain of Cytidine Repressor, [U-99% 13C; U-99% 15N], 713 uM; D2O, [U-100% 2H], 10% v/v; H2O 90% v/v; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0.043 M; pH: 7; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1

Software:

NMRPipe - processing

SPARKY - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Agilent DRX 600 MHz

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