BMRB Entry 26689

Name: The chemical shifts (partial) of E. coli DnaC N-terminal domain
Published: 2021-07-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26689

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

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Title:

The chemical shifts (partial) of E. coli DnaC N-terminal domain

Deposition date:

2015-10-12

Original release date:

2021-07-27

Authors:

Nagata, Koji; Horita, Shoichiro; Katayama, Tsutomu; Ueda, Tadashi; Tanokura, Masaru

Citation:

Citation: Nagata, Koji; Okada, Akitoshi; Ohtsuka, Jun; Ohkuri, Takatoshi; Akama, Yusuke; Sakiyama, Yukari; Miyazaki, Erika; Horita, Shoichiro; Katayama, Tsutomu; Ueda, Tadashi; Tanokura, Masaru. "Crystal structure of the complex of the interaction domains of Escherichia coli DnaB helicase and DnaC helicase loader: structural basis implying a distortion-accumulation mechanism for the DnaB ring opening caused by DnaC binding" J. Biochem. 167, 1-14 (2020).
PubMed: 31665315

Assembly members:

Assembly members:
DnaC_NTD, polymer, 52 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-22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DnaC_NTD: MKNVGDLMQRLQKMMPAHIK PAFKTGEELLAWQKEQGAIR SAALERENRAMK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	193
15N chemical shifts	50
1H chemical shifts	301

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DnaC NTD	1

Entities:

Entity 1, DnaC NTD 52 residues - Formula weight is not available

1

MET

LYS

ASN

VAL

GLY

ASP

LEU

MET

GLN

ARG

2

LEU

GLN

LYS

MET

PRO

ALA

HIS

ILE

LYS

3

PRO

ALA

PHE

LYS

THR

GLY

GLU

LEU

4

ALA

TRP

GLN

LYS

GLU

GLN

GLY

ALA

ILE

ARG

5

SER

ALA

LEU

GLU

ARG

GLU

ASN

ARG

ALA

6

MET

LYS

Name	Sample	Sample state	Sample conditions
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D C(CO)NH	sample_3	isotropic	sample_conditions_1
3D H(CCO)NH	sample_3	isotropic	sample_conditions_1
3D HCCH-COSY	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1

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

BMRB Entry 26689

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: