BMRB Entry 25768

Name: Solution NMR structure of Outer Membrane Protein G from Pseudomonas aeruginosa
Published: 2015-12-28

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PDB ID: 2n6l
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25768
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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:

Solution NMR structure of Outer Membrane Protein G from Pseudomonas aeruginosa

Deposition date:

2015-08-26

Original release date:

2015-12-28

Authors:

Kucharska, Iga; Seelheim, Patrick; Edrington, Thomas; Liang, Binyong; Tamm, Lukas

Citation:

Citation: Kucharska, Iga; Seelheim, Patrick; Edrington, Thomas; Liang, Binyong; Tamm, Lukas. "OprG Harnesses the Dynamics of its Extracellular Loops to Transport Small Amino Acids across the Outer Membrane of Pseudomonas aeruginosa" Structure 23, 2234-2245 (2015).
PubMed: 26655471

Assembly members:

Assembly members:
entity, polymer, 215 residues, 22885.924 Da.

Natural source:

Natural source: Common Name: g-proteobacteria Taxonomy ID: 287 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: Pet30a+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MHKAGDFIIRGGFATVDPDD SSSDIKLDGAKQRGTKATVD SDTQLGLTFTYMFADKWGVE LVAATPFNHQVDVKGLGPGL DGKLADIKQLPPTLLLQYYP MGGTNSAFQPYGGLGVNYTT FFDEDLASNRKAQGFSSMKL QDSWGLAGELGFDYMLNEHA LFNMAVWYMDIDTKASINGP SALGVNKTKVDVDVDPWVYM IGFGYKFLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	558
15N chemical shifts	181
1H chemical shifts	181

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 215 residues - 22885.924 Da.

1

MET

HIS

LYS

ALA

GLY

ASP

PHE

ILE

ARG

2

GLY

PHE

ALA

THR

VAL

ASP

PRO

ASP

3

SER

ASP

ILE

LYS

LEU

ASP

GLY

ALA

4

LYS

GLN

ARG

GLY

THR

LYS

ALA

THR

VAL

ASP

5

SER

ASP

THR

GLN

LEU

GLY

LEU

THR

PHE

THR

6

TYR

MET

PHE

ALA

ASP

LYS

TRP

GLY

VAL

GLU

7

LEU

VAL

ALA

THR

PRO

PHE

ASN

HIS

GLN

8

VAL

ASP

VAL

LYS

GLY

LEU

GLY

PRO

GLY

LEU

9

ASP

GLY

LYS

LEU

ALA

ASP

ILE

LYS

GLN

LEU

10

PRO

THR

LEU

GLN

TYR

PRO

11

MET

GLY

THR

ASN

SER

ALA

PHE

GLN

PRO

12

TYR

GLY

LEU

GLY

VAL

ASN

TYR

THR

13

PHE

ASP

GLU

ASP

LEU

ALA

SER

ASN

ARG

14

LYS

ALA

GLN

GLY

PHE

SER

MET

LYS

LEU

15

GLN

ASP

SER

TRP

GLY

LEU

ALA

GLY

GLU

LEU

16

GLY

PHE

ASP

TYR

MET

LEU

ASN

GLU

HIS

ALA

17

LEU

PHE

ASN

MET

ALA

VAL

TRP

TYR

MET

ASP

18

ILE

ASP

THR

LYS

ALA

SER

ILE

ASN

GLY

PRO

19

SER

ALA

LEU

GLY

VAL

ASN

LYS

THR

LYS

VAL

20

ASP

VAL

ASP

VAL

ASP

PRO

TRP

VAL

TYR

MET

21

ILE

GLY

PHE

GLY

TYR

LYS

PHE

LEU

GLU

HIS

22

HIS

Name	Sample	Sample state	Sample conditions
2D 1H 15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCB	sample_1	isotropic	sample_conditions_1
3D HNCA(CO)	sample_1	isotropic	sample_conditions_1
2D 1H 15N TROSY	sample_2	isotropic	sample_conditions_1
3D 15N 1H 1H NOESY TROSY	sample_1	isotropic	sample_conditions_1
4D 15N 1H 15N HSQC NOESY HSQC	sample_1	isotropic	sample_conditions_1

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

BMRB Entry 25768

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: