BMRB Entry 19427

Name: The solution structure of the C-terminal domain of BldD from Streptomyces coelicolor
Published: 2013-11-26

Click here to enlarge.

PDB ID: 2mc4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19427
MolProbity Validation Chart

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:

The solution structure of the C-terminal domain of BldD from Streptomyces coelicolor

Deposition date:

2013-08-14

Original release date:

2013-11-26

Authors:

Kim, Jeong-Mok; Won, Hyung-Sik; Kang, Sa-Ouk

Citation:

Citation: Kim, Jeong-Mok; Won, Hyung-Sik; Kang, Sa-Ouk. "The C-terminal domain of the transcriptional regulator BldD from Streptomyces coelicolor A3(2) constitutes a novel fold of winged-helix domains." Proteins ., .-. (2013).
PubMed: 24356916

Assembly members:

Assembly members:
BldD-CTD, polymer, 89 residues, 9853.219 Da.

Natural source:

Natural source: Common Name: high GC Gram+ Taxonomy ID: 1902 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces coelicolor

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BldD-CTD: MEPPPKLVLDLERLATVPAE KAGPLQRYAATIQSQRGDYN GKVLSIRQDDLRTLAVIYDQ SPSVLTEQLISWGVLDADAR RAVASHDEL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_for_BldD-CTD

Data type	Count
13C chemical shifts	368
15N chemical shifts	88
1H chemical shifts	609

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BldD-CTD	1

Entities:

Entity 1, BldD-CTD 89 residues - 9853.219 Da.

1

MET

GLU

PRO

LYS

LEU

VAL

LEU

ASP

2

LEU

GLU

ARG

LEU

ALA

THR

VAL

PRO

ALA

GLU

3

LYS

ALA

GLY

PRO

LEU

GLN

ARG

TYR

ALA

4

THR

ILE

GLN

SER

GLN

ARG

GLY

ASP

TYR

ASN

5

GLY

LYS

VAL

LEU

SER

ILE

ARG

GLN

ASP

6

LEU

ARG

THR

LEU

ALA

VAL

ILE

TYR

ASP

GLN

7

SER

PRO

SER

VAL

LEU

THR

GLU

GLN

LEU

ILE

8

SER

TRP

GLY

VAL

LEU

ASP

ALA

ASP

ALA

ARG

9

ARG

ALA

VAL

ALA

SER

HIS

ASP

GLU

LEU

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	Conditions_for_BldD-CTD
2D 1H-13C HSQC	sample_1	isotropic	Conditions_for_BldD-CTD
2D 1H-13C HSQC aliphatic	sample_1	isotropic	Conditions_for_BldD-CTD
3D HNCACB	sample_1	isotropic	Conditions_for_BldD-CTD
3D HN(CO)CACB	sample_1	isotropic	Conditions_for_BldD-CTD
3D HNCO	sample_1	isotropic	Conditions_for_BldD-CTD
3D HCCH-TOCSY	sample_1	isotropic	Conditions_for_BldD-CTD
3D HCCH-COSY	sample_1	isotropic	Conditions_for_BldD-CTD
3D 1H-15N TOCSY	sample_1	isotropic	Conditions_for_BldD-CTD
3D 1H-15N NOESY	sample_1	isotropic	Conditions_for_BldD-CTD
3D 1H-13C NOESY	sample_1	isotropic	Conditions_for_BldD-CTD

PDB	2MC4 4OAZ
DBJ	GAP50531
EMBL	CAB93369 CQR65077
GB	AAC38279 AEY88188 AGF62344 AIJ16957 AIR97221
REF	NP_625769 WP_003977337 WP_003988955 WP_004990661 WP_006131213

BMRB Entry 19427

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: