BMRB Entry 19533

Name: Solution Structure of NusE (S10) from Thermotoga maritima
Published: 2013-11-04

Click here to enlarge.

PDB ID: 2mew
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19533
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:

Solution Structure of NusE (S10) from Thermotoga maritima

Deposition date:

2013-10-01

Original release date:

2013-11-04

Authors:

Droegemueller, Johanna; Schweimer, Kristian; Roesch, Paul

Citation:

Citation: Droegemueller, Johanna; Schweimer, Kristian; Roesch, Paul. "Solution Structure of NusE from Thermotoga maritima" .

Assembly members:

Assembly members:
entity, polymer, 82 residues, 9043.727 Da.

Natural source:

Natural source: Common Name: Thermotoga maritima Taxonomy ID: 2336 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermotoga maritima

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: SMGGQKIRIKLKAYDHELLD ESAKKIVEVAKSTNSKVSGP IPLPTESRVHKRLIDIIDPS PKTIDALMRINLPAGVDVEI KL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	316
15N chemical shifts	68
1H chemical shifts	516

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NusE (S10) from Thermotoga maritima	1

Entities:

Entity 1, NusE (S10) from Thermotoga maritima 82 residues - 9043.727 Da.

construct used for structure determination: Ser1-Met2:Glu46-Ser47-Arg88_Leu88 Ser1 (cloning artefact from protease cleveage site) Met2:Glu46 (corresponds to Met1:Glu45 of wild type sequence Ser47 (replacement of ribosomal binding loop) Arg48:Leu82 (corresponds to Arg68:Leu102 of wild type sequence)

1

SER

MET

GLY

GLN

LYS

ILE

ARG

ILE

LYS

2

LEU

LYS

ALA

TYR

ASP

HIS

GLU

LEU

ASP

3

GLU

SER

ALA

LYS

ILE

VAL

GLU

VAL

ALA

4

LYS

SER

THR

ASN

SER

LYS

VAL

SER

GLY

PRO

5

ILE

PRO

LEU

PRO

THR

GLU

SER

ARG

VAL

HIS

6

LYS

ARG

LEU

ILE

ASP

ILE

ASP

PRO

SER

7

PRO

LYS

THR

ILE

ASP

ALA

LEU

MET

ARG

ILE

8

ASN

LEU

PRO

ALA

GLY

VAL

ASP

VAL

GLU

ILE

9

LYS

LEU

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	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

BMRB Entry 19533

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: