BMRB Entry 34172

Name: NMR structure of the complex formed by an engineered region 2 of sigmaE in complex with GTAAAA
Published: 2018-06-25

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PDB ID: 5or5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34172
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:

NMR structure of the complex formed by an engineered region 2 of sigmaE in complex with GTAAAA

Deposition date:

2017-08-15

Original release date:

2018-06-25

Authors:

Campagne, S.; Vorholt, J.; Allain, F.

Citation:

Citation: Campagne, S.; Vorholt, J.; Allain, F.; Campagne, S.; Marsh, M.; Capitani, G.; Vorholt, J.; Allain, F.. "Engineered promoter selectivity of an ECF sigma factor" J. Mol. Biol. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 95 residues, 10990.592 Da.
entity_2, polymer, 6 residues, 1761.288 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 83333 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSEQLTDQVLVERVQKGDQK AFNLLVVRYQHKVASLVSRY VPSGDVPDVVQEAFIKAYRA LDSFDINRKFSTWLYRIAVN TAKNYLVAQGRRLEL
entity_2: XTAAAA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	405
15N chemical shifts	102
1H chemical shifts	749

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 95 residues - 10990.592 Da.

1

MET

SER

GLU

GLN

LEU

THR

ASP

GLN

VAL

LEU

2

VAL

GLU

ARG

VAL

GLN

LYS

GLY

ASP

GLN

LYS

3

ALA

PHE

ASN

LEU

VAL

ARG

TYR

GLN

4

HIS

LYS

VAL

ALA

SER

LEU

VAL

SER

ARG

TYR

5

VAL

PRO

SER

GLY

ASP

VAL

PRO

ASP

VAL

6

GLN

GLU

ALA

PHE

ILE

LYS

ALA

TYR

ARG

ALA

7

LEU

ASP

SER

PHE

ASP

ILE

ASN

ARG

LYS

PHE

8

SER

THR

TRP

LEU

TYR

ARG

ILE

ALA

VAL

ASN

9

THR

ALA

LYS

ASN

TYR

LEU

VAL

ALA

GLN

GLY

10

ARG

LEU

GLU

LEU

Entity 2, entity_2 6 residues - 1761.288 Da.

1

GNG

DT

DA

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY f2f	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	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
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY f1ff2f	sample_2	isotropic	sample_conditions_1

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BMRB Entry 34172

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: