BMRB Entry 26612

Name: Transmembrane domain of E. coli OmpA in 8 m Urea
Published: 2020-08-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26612

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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:

Transmembrane domain of E. coli OmpA in 8 m Urea

Deposition date:

2015-07-15

Original release date:

2020-08-30

Authors:

Burmann, Bjoern; Hiller, Sebastian

Citation:

Citation: Mas, G.; Burmann, Sebastian; Sharpe, T.; Claudi, B.; Burmann, D.; Hiller, Sebastian. "Regulation of chaperone function by coupled folding and oligomerization" Sci. Adv. ., .-..

Assembly members:

Assembly members:
tOmpA, polymer, 177 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
tOmpA: MAPKDNTWYTGAKLGWSQYH DTGFINNNGPTHENQLGAGA FGGYQVNPYVGFEMGYDWLG RMPYKGSVENGAYKAQGVQL TAKLGYPITDDLDIYTRLGG MVWRADTKSNVYGKNHDTGV SPVFAGGVEYAITPEIATRL EYQWTNNIGDAHTIGTRPDN GMLSLGVSYRFGQGEAA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	487
15N chemical shifts	168
1H chemical shifts	168

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	tOmpA	1

Entities:

Entity 1, tOmpA 177 residues - Formula weight is not available

this is the transmembrane domain of E. coli OmpA (1-177)

1

MET

ALA

PRO

LYS

ASP

ASN

THR

TRP

TYR

THR

2

GLY

ALA

LYS

LEU

GLY

TRP

SER

GLN

TYR

HIS

3

ASP

THR

GLY

PHE

ILE

ASN

GLY

PRO

4

THR

HIS

GLU

ASN

GLN

LEU

GLY

ALA

GLY

ALA

5

PHE

GLY

TYR

GLN

VAL

ASN

PRO

TYR

VAL

6

GLY

PHE

GLU

MET

GLY

TYR

ASP

TRP

LEU

GLY

7

ARG

MET

PRO

TYR

LYS

GLY

SER

VAL

GLU

ASN

8

GLY

ALA

TYR

LYS

ALA

GLN

GLY

VAL

GLN

LEU

9

THR

ALA

LYS

LEU

GLY

TYR

PRO

ILE

THR

ASP

10

ASP

LEU

ASP

ILE

TYR

THR

ARG

LEU

GLY

11

MET

VAL

TRP

ARG

ALA

ASP

THR

LYS

SER

ASN

12

VAL

TYR

GLY

LYS

ASN

HIS

ASP

THR

GLY

VAL

13

SER

PRO

VAL

PHE

ALA

GLY

VAL

GLU

TYR

14

ALA

ILE

THR

PRO

GLU

ILE

ALA

THR

ARG

LEU

15

GLU

TYR

GLN

TRP

THR

ASN

ILE

GLY

ASP

16

ALA

HIS

THR

ILE

GLY

THR

ARG

PRO

ASP

ASN

17

GLY

MET

LEU

SER

LEU

GLY

VAL

SER

TYR

ARG

18

PHE

GLY

GLN

GLY

GLU

ALA

Samples:

sample_1: tOmpA, [U-13C; U-15N; U-2H], 1 mM; D2O 10%; DSS 50 uM; MES 25 mM; NaCl 150 mM; urea 8 M; H2O 90%

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 288.15 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
5D APSY HNCOCACB	sample_1	isotropic	sample_conditions_1
4D APSY HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin, Guntert, Herrmann and Wuthrich, Keller and Wuthrich - chemical shift assignment, collection, processing

NMR spectrometers:

Bruker Ascend 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks