BMRB Entry 34365

Name: Solid-state NMR structure of outer membrane protein AlkL in DMPC lipid bilayers
Published: 2020-03-16

Click here to enlarge.

PDB ID: 6qwr
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34365
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:

Solid-state NMR structure of outer membrane protein AlkL in DMPC lipid bilayers

Deposition date:

2019-03-06

Original release date:

2020-03-16

Authors:

Schubeis, T.; Andreas, L.; Pintacuda, G.

Citation:

Citation: Schubeis, Tobias; Le Marchand, Tanguy; Daday, Csaba; Kopec, Wojciech; Tekwani Movellan, Kumar; Stanek, Jan; Schwarzer, Tom; Castiglione, Kathrin; de Groot, Bert; Pintacuda, Guido; Andreas, Loren. "A beta-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL" Proc. Natl. Acad. Sci. U.S.A. 117, 21014-21021 (2020).
PubMed: 32817429

Assembly members:

Assembly members:
entity_1, polymer, 219 residues, 24087.912 Da.

Natural source:

Natural source: Common Name: Pseudomonas oleovorans Taxonomy ID: 301 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas oleovorans

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MNENYPAKSAGYNQGDWVAS FNFSKVYVGEELGDLNVGGG ALPNADVSIGNDTTLTFDIA YFVSSNIAVDFFVGVPARAK FQGEKSISSLGRVSEVDYGP AILSLQYHYDSFERLYPYVG VGVGRVLFFDKTDGALSSFD IKDKWAPAFQVGLRYDLGNS WMLNSDVRYIPFKTDVTGTL GPVPVSTKIEVDPFILSLGA SYVFKLAAALEHHHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	591
15N chemical shifts	172
1H chemical shifts	804

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 219 residues - 24087.912 Da.

1

MET

ASN

GLU

ASN

TYR

PRO

ALA

LYS

SER

ALA

2

GLY

TYR

ASN

GLN

GLY

ASP

TRP

VAL

ALA

SER

3

PHE

ASN

PHE

SER

LYS

VAL

TYR

VAL

GLY

GLU

4

GLU

LEU

GLY

ASP

LEU

ASN

VAL

GLY

5

ALA

LEU

PRO

ASN

ALA

ASP

VAL

SER

ILE

GLY

6

ASN

ASP

THR

LEU

THR

PHE

ASP

ILE

ALA

7

TYR

PHE

VAL

SER

ASN

ILE

ALA

VAL

ASP

8

PHE

VAL

GLY

VAL

PRO

ALA

ARG

ALA

LYS

9

PHE

GLN

GLY

GLU

LYS

SER

ILE

SER

LEU

10

GLY

ARG

VAL

SER

GLU

VAL

ASP

TYR

GLY

PRO

11

ALA

ILE

LEU

SER

LEU

GLN

TYR

HIS

TYR

ASP

12

SER

PHE

GLU

ARG

LEU

TYR

PRO

TYR

VAL

GLY

13

VAL

GLY

VAL

GLY

ARG

VAL

LEU

PHE

ASP

14

LYS

THR

ASP

GLY

ALA

LEU

SER

PHE

ASP

15

ILE

LYS

ASP

LYS

TRP

ALA

PRO

ALA

PHE

GLN

16

VAL

GLY

LEU

ARG

TYR

ASP

LEU

GLY

ASN

SER

17

TRP

MET

LEU

ASN

SER

ASP

VAL

ARG

TYR

ILE

18

PRO

PHE

LYS

THR

ASP

VAL

THR

GLY

THR

LEU

19

GLY

PRO

VAL

PRO

VAL

SER

THR

LYS

ILE

GLU

20

VAL

ASP

PRO

PHE

ILE

LEU

SER

LEU

GLY

ALA

21

SER

TYR

VAL

PHE

LYS

LEU

ALA

LEU

22

GLU

HIS

Samples:

sample_1: Outer membrane protein AlkL, [U-13C; U-15N], 0.5 w/w

sample_2: Outer membrane protein AlkL, [U-13C; U-15N; U-2H], 0.5 w/w

sample_conditions_1: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D hCANH	sample_1	isotropic	sample_conditions_1
3D hCONH	sample_1	isotropic	sample_conditions_1
3D hcoCAcoNH	sample_1	isotropic	sample_conditions_1
3D hcaCBcaNH	sample_1	isotropic	sample_conditions_1
3D hcaCBcacoNH	sample_1	isotropic	sample_conditions_1
3D hNCAHa	sample_1	isotropic	sample_conditions_1
3D hNcoCAHa	sample_1	isotropic	sample_conditions_1
3D hCOCAHa	sample_1	isotropic	sample_conditions_1
3D hCOnCAHa	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D hCANH	sample_2	isotropic	sample_conditions_1
3D hCONH	sample_2	isotropic	sample_conditions_1
3D hcoCAcoNH	sample_2	isotropic	sample_conditions_1
3D hCOcaNH	sample_2	isotropic	sample_conditions_1
3D hNHH BASS-SD	sample_1	isotropic	sample_conditions_1
3D hNNH BASS-SD	sample_1	isotropic	sample_conditions_1
3D hCCH BASS-SD	sample_1	isotropic	sample_conditions_1
3D hNHH RFDR	sample_1	isotropic	sample_conditions_1
3D hCHH RFDR	sample_1	isotropic	sample_conditions_1
4D HNNH RFDR	sample_2	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Sparky, Goddard - chemical shift assignment

CcpNmr Analysis, CCPN - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker AVANCE III 1000 MHz
Bruker AVANCE III 800 MHz

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