BMRB Entry 19284

Name: Relaxation data of the delta subunit of RNA polymerase from Bacillus subtilis
Published: 2013-10-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19284

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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:

Relaxation data of the delta subunit of RNA polymerase from Bacillus subtilis

Deposition date:

2013-06-04

Original release date:

2013-10-14

Authors:

Papouskova, Veronika; Zidek, Lukas; Kaderavek, Pavel; Sanderova, Hana; Krasny, Libor; Sklenar, Vladimir

Citation:

Citation: Papoukova, Veronika; Kadeavek, Pavel; Otrusinova, Olga; Rabatinova, Albeta; Sanderova, Hana; Novaek, Jii; Krasny, Libor; Sklena, Vladimir; Zidek, Luka. "Structural Study of the Partially Disordered Full-Length Subunit of RNA Polymerase from Bacillus subtilis." Chembiochem 14, 1772-1779 (2013).
PubMed: 23868186

Assembly members:

Assembly members:
delta, polymer, 172 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Firmicutes Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pFL31

Entity Sequences (FASTA):

Entity Sequences (FASTA):
delta: GIKQYSQEELKEMALVEIAH ELFEEHKKPVPFQELLNEIA SLLGVKKEELGDRIAQFYTD LNIDGRFLALSDQTWGLRSW YPYDQLDEETQPTVKAKKKK AKKAVEEDLDLDEFEEIDED DLDLDEVEEELDLEADDFDE EDLDEDDDDLEIEEDIIDED DEDYDDEEEEIK

Data sets:

heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1

Data type	Count
heteronuclear NOE values	103
T1 relaxation values	105
T2 relaxation values	105

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	delta	1

Entities:

Entity 1, delta 172 residues - Formula weight is not available

1

GLY

ILE

LYS

GLN

TYR

SER

GLN

GLU

LEU

2

LYS

GLU

MET

ALA

LEU

VAL

GLU

ILE

ALA

HIS

3

GLU

LEU

PHE

GLU

HIS

LYS

PRO

VAL

4

PRO

PHE

GLN

GLU

LEU

ASN

GLU

ILE

ALA

5

SER

LEU

GLY

VAL

LYS

GLU

LEU

6

GLY

ASP

ARG

ILE

ALA

GLN

PHE

TYR

THR

ASP

7

LEU

ASN

ILE

ASP

GLY

ARG

PHE

LEU

ALA

LEU

8

SER

ASP

GLN

THR

TRP

GLY

LEU

ARG

SER

TRP

9

TYR

PRO

TYR

ASP

GLN

LEU

ASP

GLU

THR

10

GLN

PRO

THR

VAL

LYS

ALA

LYS

11

ALA

LYS

ALA

VAL

GLU

ASP

LEU

ASP

12

LEU

ASP

GLU

PHE

GLU

ILE

ASP

GLU

ASP

13

ASP

LEU

ASP

LEU

ASP

GLU

VAL

GLU

14

LEU

ASP

LEU

GLU

ALA

ASP

PHE

ASP

GLU

15

GLU

ASP

LEU

ASP

GLU

ASP

LEU

16

GLU

ILE

GLU

ASP

ILE

ASP

GLU

ASP

17

ASP

GLU

ASP

TYR

ASP

GLU

18

ILE

LYS

Samples:

sample_1: delta, [U-100% 15N], 1.1 mM; D2O, [U-99% 2H], 10%; sodium chloride 10 mM; sodium azide 0.05%; phosphate buffer 20 mM; H2O 90%

sample_conditions_1: ionic strength: 20 mM; pH: 6.6; pressure: 1 atm; temperature: 301 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D NOE 15N,1H correlation	sample_1	isotropic	sample_conditions_1
2D R1 15N,1H correlation	sample_1	isotropic	sample_conditions_1
2D R2 15N,1H correlation	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 600 MHz

BMRB	16635 16912 18903
PDB	2KRC 4NC7 4NC8
DBJ	BAM55799 BAM59811
EMBL	CAA89869 CAB15744 CCU60814 CEI59524 CEJ79381
GB	AAA22710 ADM39706 ADV94526 AEP92774 AFI30331
REF	NP_391597 WP_003221959 WP_003227609 WP_003235832 WP_003243661
SP	P12464
AlphaFold	P12464