BMRB Entry 19940

Name: Chemical shifts and structural constraints of outer membrane protein A
Published: 2014-04-29

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19940

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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:

Chemical shifts and structural constraints of outer membrane protein A

Deposition date:

2014-04-24

Original release date:

2014-04-29

Authors:

Arora, Ashish; Abildgaard, Frits; Bushweller, John; Cierpicki, Tomasz; Liang, Binyong; Tamm, Lukas

Citation:

Citation: Arora, Ashish; Abildgaard, Frits; Bushweller, John; Tamm, Lukas. "Structure of outer membrane protein A transmembrane domain by NMR spectroscopy" Nat. Struct. Biol. 8, 334-338 (2001).

Assembly members:

Assembly members:
OmpA, polymer, 176 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: pET14b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OmpA: APKDNTWYTGAKLGFSQYHD TGFINNNGPTHENQLGAGAF GGYQVNPYVGFEMGYDFLGR MPYKGSVENGAYKAQGVQLT AKLGYPITDDLDIYTRLGGM VFRADTKSNVYGKNHDTGVS PVFAGGVEYAITPEIATRLE YQFTNNIGDAHTIGTRPDNG MLSLGVSYRFGQGEAA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	463
15N chemical shifts	143
1H chemical shifts	143

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ompa	1

Entities:

Entity 1, ompa 176 residues - Formula weight is not available

1

ALA

PRO

LYS

ASP

ASN

THR

TRP

TYR

THR

GLY

2

ALA

LYS

LEU

GLY

PHE

SER

GLN

TYR

HIS

ASP

3

THR

GLY

PHE

ILE

ASN

GLY

PRO

THR

4

HIS

GLU

ASN

GLN

LEU

GLY

ALA

GLY

ALA

PHE

5

GLY

TYR

GLN

VAL

ASN

PRO

TYR

VAL

GLY

6

PHE

GLU

MET

GLY

TYR

ASP

PHE

LEU

GLY

ARG

7

MET

PRO

TYR

LYS

GLY

SER

VAL

GLU

ASN

GLY

8

ALA

TYR

LYS

ALA

GLN

GLY

VAL

GLN

LEU

THR

9

ALA

LYS

LEU

GLY

TYR

PRO

ILE

THR

ASP

10

LEU

ASP

ILE

TYR

THR

ARG

LEU

GLY

MET

11

VAL

PHE

ARG

ALA

ASP

THR

LYS

SER

ASN

VAL

12

TYR

GLY

LYS

ASN

HIS

ASP

THR

GLY

VAL

SER

13

PRO

VAL

PHE

ALA

GLY

VAL

GLU

TYR

ALA

14

ILE

THR

PRO

GLU

ILE

ALA

THR

ARG

LEU

GLU

15

TYR

GLN

PHE

THR

ASN

ILE

GLY

ASP

ALA

16

HIS

THR

ILE

GLY

THR

ARG

PRO

ASP

ASN

GLY

17

MET

LEU

SER

LEU

GLY

VAL

SER

TYR

ARG

PHE

18

GLY

GLN

GLY

GLU

ALA

Samples:

sample_1: OmpA, [U-13C; U-15N; U-2H], 1 mM; NaCl 50 mM; potassium phosphate 10 mM; NaN3 0.01%

sample_conditions_1: ionic strength: 50 mM; pH: 6.3; pressure: 1 atm; temperature: 323 K

Experiments:

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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

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

NMR spectrometers:

Bruker DMX 750 MHz
Varian INOVA 600 MHz

BMRB	19410
PDB	1G90 2GE4
DBJ	BAA35715 BAB34464 BAG76542 BAI24400 BAI29850
EMBL	CAA23588 CAQ31485 CAR02310 CAR12355 CAU96868
GB	AAC74043 AAF37887 AAG55443 AAP74759 AAQ96072
REF	NP_309068 NP_415477 WP_000315442 WP_000630860 WP_000750416
SP	P0A910 P0A911
AlphaFold	P0A910 P0A911