BMRB Entry 30421

Name: Solution structure of the Burkholderia thailandensis transcription antitermination protein NusB (BTH_I1529) - Seattle Structural Genomics Center for Infectious Disease target ButhA.17903.a
Published: 2018-03-29

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PDB ID: 6ckq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30421
MolProbity Validation Chart

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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:

Solution structure of the Burkholderia thailandensis transcription antitermination protein NusB (BTH_I1529) - Seattle Structural Genomics Center for Infectious Disease target ButhA.17903.a

Deposition date:

2018-02-28

Original release date:

2018-03-29

Authors:

Buchko, G.; Seattle Structural Genomics Center for Infectious Disease, SSGCID

Citation:

Citation: Buchko, G.; SSGCID, SSGCID. "Solution structure of the Burkholderia thailandensis transcription antitermination protein NusB (BTH_I1529)." .

Assembly members:

Assembly members:
entity_1, polymer, 149 residues, 16301.551 Da.

Natural source:

Natural source: Common Name: Burkholderia thailandensis Taxonomy ID: 271848 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia thailandensis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGSMKKSARRQSRELATQG LYQWLLSNAAPGEIDAQLRG ALGYDKADKTLLDTILHGVI REHATLAEAISPSLDRPIDQ LSPVERAVLLIATYELTHQI ETPYRVIINEAVELAKTFGG SDGYKYVNGVLDKLAVKLRP AETQARRGA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	543
15N chemical shifts	147
1H chemical shifts	825

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 149 residues - 16301.551 Da.

1

GLY

PRO

GLY

SER

MET

LYS

SER

ALA

ARG

2

ARG

GLN

SER

ARG

GLU

LEU

ALA

THR

GLN

GLY

3

LEU

TYR

GLN

TRP

LEU

SER

ASN

ALA

4

PRO

GLY

GLU

ILE

ASP

ALA

GLN

LEU

ARG

GLY

5

ALA

LEU

GLY

TYR

ASP

LYS

ALA

ASP

LYS

THR

6

LEU

ASP

THR

ILE

LEU

HIS

GLY

VAL

ILE

7

ARG

GLU

HIS

ALA

THR

LEU

ALA

GLU

ALA

ILE

8

SER

PRO

SER

LEU

ASP

ARG

PRO

ILE

ASP

GLN

9

LEU

SER

PRO

VAL

GLU

ARG

ALA

VAL

LEU

10

ILE

ALA

THR

TYR

GLU

LEU

THR

HIS

GLN

ILE

11

GLU

THR

PRO

TYR

ARG

VAL

ILE

ASN

GLU

12

ALA

VAL

GLU

LEU

ALA

LYS

THR

PHE

GLY

13

SER

ASP

GLY

TYR

LYS

TYR

VAL

ASN

GLY

VAL

14

LEU

ASP

LYS

LEU

ALA

VAL

LYS

LEU

ARG

PRO

15

ALA

GLU

THR

GLN

ALA

ARG

GLY

ALA

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D Deltas	sample_1	isotropic	sample_conditions_1
deuterium exchange	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

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BMRB Entry 30421

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: