BMRB Entry 18712

Name: b-flap domain of RNA polymerase (B. subtilis)
Published: 2014-03-10

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PDB ID: 2ly7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18712
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

b-flap domain of RNA polymerase (B. subtilis)

Deposition date:

2012-09-12

Original release date:

2014-03-10

Authors:

Mobli, Mehdi

Citation:

Citation: Mobli, Mehdi; Yang, Xiao; Ma, Cong; Thomas, Rhiannon; King, Glenn; Lewis, Peter. "NusA binding to the b-flap tip of RNA polymerase determined by NMR." .

Assembly members:

Assembly members:
b-flap, polymer, 149 residues, 15446.424 Da.

Natural source:

Natural source: Common Name: B. subtilis 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: pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
b-flap: MDDVYTSIHIEEYESEARDT KLGPEEITRDIPNVGEDALR NLDDRGVIRIGAEVKDGDLL VGKVTPKGVTELTAEERLLH AIFGEKAREVRDTSLRVPHG GGGIIHDVKVFNREDGDELP PGVNQLVRVYIVQKRKISEG DGTHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	409
15N chemical shifts	138
1H chemical shifts	902

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	b-flap domain of RNA polymerase (B. subtilis)	1

Entities:

Entity 1, b-flap domain of RNA polymerase (B. subtilis) 149 residues - 15446.424 Da.

1

MET

ASP

VAL

TYR

THR

SER

ILE

HIS

ILE

2

GLU

TYR

GLU

SER

GLU

ALA

ARG

ASP

THR

3

LYS

LEU

GLY

PRO

GLU

ILE

THR

ARG

ASP

4

ILE

PRO

ASN

VAL

GLY

GLU

ASP

ALA

LEU

ARG

5

ASN

LEU

ASP

ARG

GLY

VAL

ILE

ARG

ILE

6

GLY

ALA

GLU

VAL

LYS

ASP

GLY

ASP

LEU

7

VAL

GLY

LYS

VAL

THR

PRO

LYS

GLY

VAL

THR

8

GLU

LEU

THR

ALA

GLU

ARG

LEU

HIS

9

ALA

ILE

PHE

GLY

GLU

LYS

ALA

ARG

GLU

VAL

10

ARG

ASP

THR

SER

LEU

ARG

VAL

PRO

HIS

GLY

11

GLY

ILE

HIS

ASP

VAL

LYS

VAL

12

PHE

ASN

ARG

GLU

ASP

GLY

ASP

GLU

LEU

PRO

13

PRO

GLY

VAL

ASN

GLN

LEU

VAL

ARG

VAL

TYR

14

ILE

VAL

GLN

LYS

ARG

LYS

ILE

SER

GLU

GLY

15

ASP

GLY

THR

HIS

Samples:

sample_1: b-flap, [U-100% 13C; U-100% 15N], 500 ± 50 uM; potassium phosphate 20 mM; sodium chloride 150 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

RNMRTK v3, Jeff Hoch, Alan Stern - processing

TALOS v+, Cornilescu, Delaglio and Bax - Dihedral angle generation

TOPSPIN v3, Bruker Biospin - collection

CYANA v3, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 900 MHz

PDB	2LY7
GB	AFQ00666 AFQ00667 AGO57771 AHZ90577 AHZ90582