BMRB Entry 16868

Name: Solution structure of the aminoterminal domain of E. coli NusA
Published: 2012-08-02

Click here to enlarge.

PDB ID: 2kwp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16868
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 the aminoterminal domain of E. coli NusA

Deposition date:

2010-04-15

Original release date:

2012-08-02

Authors:

Schweimer, Kristian; Jurk, Marcel; Roesch, Paul

Citation:

Citation: Jurk, Marcel; Schweimer, Kristian; Roesch, Paul. "Solution structure of the aminoterminal domain of E. coli NusA" .

Assembly members:

Assembly members:
NusA, polymer, 129 residues, 14894.971 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NusA: MNKEILAVVEAVSNEKALPR EKIFEALESALATATKKKYE QEIDVRVQIDRKSGDFDTFR RWLVVDEVTQPTKEITLEAA RYEDESLNLGDYVEDQIESV TFDRITTQTAKQVIVQKVRE AERAMLVPR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	508
15N chemical shifts	119
1H chemical shifts	868

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NusA	1

Entities:

Entity 1, NusA 129 residues - 14894.971 Da.

1

MET

ASN

LYS

GLU

ILE

LEU

ALA

VAL

GLU

2

ALA

VAL

SER

ASN

GLU

LYS

ALA

LEU

PRO

ARG

3

GLU

LYS

ILE

PHE

GLU

ALA

LEU

GLU

SER

ALA

4

LEU

ALA

THR

ALA

THR

LYS

TYR

GLU

5

GLN

GLU

ILE

ASP

VAL

ARG

VAL

GLN

ILE

ASP

6

ARG

LYS

SER

GLY

ASP

PHE

ASP

THR

PHE

ARG

7

ARG

TRP

LEU

VAL

ASP

GLU

VAL

THR

GLN

8

PRO

THR

LYS

GLU

ILE

THR

LEU

GLU

ALA

9

ARG

TYR

GLU

ASP

GLU

SER

LEU

ASN

LEU

GLY

10

ASP

TYR

VAL

GLU

ASP

GLN

ILE

GLU

SER

VAL

11

THR

PHE

ASP

ARG

ILE

THR

GLN

THR

ALA

12

LYS

GLN

VAL

ILE

VAL

GLN

LYS

VAL

ARG

GLU

13

ALA

GLU

ARG

ALA

MET

LEU

VAL

PRO

ARG

Samples:

sample_1: NusA, [U-98% 13C; U-98% 15N], 0.4 mM; potassium phosphate 10 mM; sodium chloride 50 mM; EDTA 50 uM; H2O 90%; D2O 10%

sample_2: NusA, [U-98% 13C; U-98% 15N], 0.4 mM; potassium phosphate 10 mM; sodium chloride 50 mM; EDTA 50 uM; D2O 100%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
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
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D CCH-NOESY	sample_2	isotropic	sample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMRView, Johnson, One Moon Scientific - data analysis

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 800 MHz

PDB	2KWP
DBJ	BAB37473 BAE77215 BAG78979 BAI27449 BAI32628
EMBL	CAA25200 CAP77631 CAQ33504 CAQ90641 CAR00133
GB	AAA57972 AAC76203 AAG58305 AAN44677 AAN82367
REF	NP_312077 NP_417638 NP_708970 WP_001031044 WP_001031045
SP	P0AFF6 P0AFF7 P0AFF8 P0AFF9
AlphaFold	P0AFF6 P0AFF7 P0AFF8 P0AFF9