BMRB Entry 15426

Name: Solution NMR structure of OmpG
Published: 2008-03-14

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15426

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of OmpG

Deposition date:

2007-08-09

Original release date:

2008-03-14

Authors:

Liang, Binyong; Tamm, Lukas

Citation:

Citation: Liang, Binyong; Tamm, Lukas. "Structure of outer membrane protein G by solution NMR spectroscopy." Proc. Natl. Acad. Sci. U.S.A. 104, 16140-16145 (2007).
PubMed: 17911261

Assembly members:

Assembly members:
OmpG, polymer, 280 residues, 32813.707 Da.

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: pT7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OmpG: EERNDWHFNIGAMYEIENVE GYGEDMDGLAEPSVYFNAAN GPWRIALAYYQEGPVDYSAG KRGTWFDRPELEVHYQFLEN DDFSFGLTGGFRNYGYHYVD EPGKDTANMQRWKIAPDWDV KLTDDLRFNGWLSMYKFAND LNTTGYADTRVETETGLQYT FNETVALRVNYYLERGFNMD DSRNNGEFSTQEIRAYLPLT LGNHSVTPYTRIGLDRWSNW DWQDDIEREGHDFNRVGLFY GYDFQNGLSVSLEYAFEWQD HDEGDSDKFHYAGVGVNYSF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	697
15N chemical shifts	226
1H chemical shifts	226

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OmpG	1

Entities:

Entity 1, OmpG 280 residues - 32813.707 Da.

1	GLU	GLU	ARG	ASN	ASP	TRP	HIS	PHE	ASN	ILE
2	GLY	ALA	MET	TYR	GLU	ILE	GLU	ASN	VAL	GLU
3	GLY	TYR	GLY	GLU	ASP	MET	ASP	GLY	LEU	ALA
4	GLU	PRO	SER	VAL	TYR	PHE	ASN	ALA	ALA	ASN
5	GLY	PRO	TRP	ARG	ILE	ALA	LEU	ALA	TYR	TYR
6	GLN	GLU	GLY	PRO	VAL	ASP	TYR	SER	ALA	GLY
7	LYS	ARG	GLY	THR	TRP	PHE	ASP	ARG	PRO	GLU
8	LEU	GLU	VAL	HIS	TYR	GLN	PHE	LEU	GLU	ASN
9	ASP	ASP	PHE	SER	PHE	GLY	LEU	THR	GLY	GLY
10	PHE	ARG	ASN	TYR	GLY	TYR	HIS	TYR	VAL	ASP
11	GLU	PRO	GLY	LYS	ASP	THR	ALA	ASN	MET	GLN
12	ARG	TRP	LYS	ILE	ALA	PRO	ASP	TRP	ASP	VAL
13	LYS	LEU	THR	ASP	ASP	LEU	ARG	PHE	ASN	GLY
14	TRP	LEU	SER	MET	TYR	LYS	PHE	ALA	ASN	ASP
15	LEU	ASN	THR	THR	GLY	TYR	ALA	ASP	THR	ARG
16	VAL	GLU	THR	GLU	THR	GLY	LEU	GLN	TYR	THR
17	PHE	ASN	GLU	THR	VAL	ALA	LEU	ARG	VAL	ASN
18	TYR	TYR	LEU	GLU	ARG	GLY	PHE	ASN	MET	ASP
19	ASP	SER	ARG	ASN	ASN	GLY	GLU	PHE	SER	THR
20	GLN	GLU	ILE	ARG	ALA	TYR	LEU	PRO	LEU	THR
21	LEU	GLY	ASN	HIS	SER	VAL	THR	PRO	TYR	THR
22	ARG	ILE	GLY	LEU	ASP	ARG	TRP	SER	ASN	TRP
23	ASP	TRP	GLN	ASP	ASP	ILE	GLU	ARG	GLU	GLY
24	HIS	ASP	PHE	ASN	ARG	VAL	GLY	LEU	PHE	TYR
25	GLY	TYR	ASP	PHE	GLN	ASN	GLY	LEU	SER	VAL
26	SER	LEU	GLU	TYR	ALA	PHE	GLU	TRP	GLN	ASP
27	HIS	ASP	GLU	GLY	ASP	SER	ASP	LYS	PHE	HIS
28	TYR	ALA	GLY	VAL	GLY	VAL	ASN	TYR	SER	PHE

Samples:

sample_1: OmpG, [U-13C; U-15N; U-2H], 1 mM; DPC15 – 300 mM; Bis-Tris 25 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.3; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D TROSYNOESY	sample_1	isotropic	sample_conditions_1
3D TROSYNOESYTROSY	sample_1	isotropic	sample_conditions_1
2D heteronuclear 1H-15N NOE	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 500 MHz

PDB	2F1C 2IWV 2IWW 2JQY 2WVP 2X9K
DBJ	BAB35321 BAE76401 BAG76895 BAI25168 BAI35617
EMBL	CAP75863 CAQ31824 CAQ98203 CAR02781 CAR07725
GB	AAC34720 AAC74401 AAG56483 AAN80257 ABE07068
REF	NP_309925 NP_415835 WP_000735233 WP_000735234 WP_000735235
SP	P76045
AlphaFold	P76045

1	GLU	GLU	ARG	ASN	ASP	TRP	HIS	PHE	ASN	ILE
2	GLY	ALA	MET	TYR	GLU	ILE	GLU	ASN	VAL	GLU
3	GLY	TYR	GLY	GLU	ASP	MET	ASP	GLY	LEU	ALA
4	GLU	PRO	SER	VAL	TYR	PHE	ASN	ALA	ALA	ASN
5	GLY	PRO	TRP	ARG	ILE	ALA	LEU	ALA	TYR	TYR
6	GLN	GLU	GLY	PRO	VAL	ASP	TYR	SER	ALA	GLY
7	LYS	ARG	GLY	THR	TRP	PHE	ASP	ARG	PRO	GLU
8	LEU	GLU	VAL	HIS	TYR	GLN	PHE	LEU	GLU	ASN
9	ASP	ASP	PHE	SER	PHE	GLY	LEU	THR	GLY	GLY
10	PHE	ARG	ASN	TYR	GLY	TYR	HIS	TYR	VAL	ASP
11	GLU	PRO	GLY	LYS	ASP	THR	ALA	ASN	MET	GLN
12	ARG	TRP	LYS	ILE	ALA	PRO	ASP	TRP	ASP	VAL
13	LYS	LEU	THR	ASP	ASP	LEU	ARG	PHE	ASN	GLY
14	TRP	LEU	SER	MET	TYR	LYS	PHE	ALA	ASN	ASP
15	LEU	ASN	THR	THR	GLY	TYR	ALA	ASP	THR	ARG
16	VAL	GLU	THR	GLU	THR	GLY	LEU	GLN	TYR	THR
17	PHE	ASN	GLU	THR	VAL	ALA	LEU	ARG	VAL	ASN
18	TYR	TYR	LEU	GLU	ARG	GLY	PHE	ASN	MET	ASP
19	ASP	SER	ARG	ASN	ASN	GLY	GLU	PHE	SER	THR
20	GLN	GLU	ILE	ARG	ALA	TYR	LEU	PRO	LEU	THR
21	LEU	GLY	ASN	HIS	SER	VAL	THR	PRO	TYR	THR
22	ARG	ILE	GLY	LEU	ASP	ARG	TRP	SER	ASN	TRP
23	ASP	TRP	GLN	ASP	ASP	ILE	GLU	ARG	GLU	GLY
24	HIS	ASP	PHE	ASN	ARG	VAL	GLY	LEU	PHE	TYR
25	GLY	TYR	ASP	PHE	GLN	ASN	GLY	LEU	SER	VAL
26	SER	LEU	GLU	TYR	ALA	PHE	GLU	TRP	GLN	ASP
27	HIS	ASP	GLU	GLY	ASP	SER	ASP	LYS	PHE	HIS
28	TYR	ALA	GLY	VAL	GLY	VAL	ASN	TYR	SER	PHE

1	GLU	GLU	ARG	ASN	ASP	TRP	HIS	PHE	ASN	ILE
2	GLY	ALA	MET	TYR	GLU	ILE	GLU	ASN	VAL	GLU
3	GLY	TYR	GLY	GLU	ASP	MET	ASP	GLY	LEU	ALA
4	GLU	PRO	SER	VAL	TYR	PHE	ASN	ALA	ALA	ASN
5	GLY	PRO	TRP	ARG	ILE	ALA	LEU	ALA	TYR	TYR
6	GLN	GLU	GLY	PRO	VAL	ASP	TYR	SER	ALA	GLY
7	LYS	ARG	GLY	THR	TRP	PHE	ASP	ARG	PRO	GLU
8	LEU	GLU	VAL	HIS	TYR	GLN	PHE	LEU	GLU	ASN
9	ASP	ASP	PHE	SER	PHE	GLY	LEU	THR	GLY	GLY
10	PHE	ARG	ASN	TYR	GLY	TYR	HIS	TYR	VAL	ASP
11	GLU	PRO	GLY	LYS	ASP	THR	ALA	ASN	MET	GLN
12	ARG	TRP	LYS	ILE	ALA	PRO	ASP	TRP	ASP	VAL
13	LYS	LEU	THR	ASP	ASP	LEU	ARG	PHE	ASN	GLY
14	TRP	LEU	SER	MET	TYR	LYS	PHE	ALA	ASN	ASP
15	LEU	ASN	THR	THR	GLY	TYR	ALA	ASP	THR	ARG
16	VAL	GLU	THR	GLU	THR	GLY	LEU	GLN	TYR	THR
17	PHE	ASN	GLU	THR	VAL	ALA	LEU	ARG	VAL	ASN
18	TYR	TYR	LEU	GLU	ARG	GLY	PHE	ASN	MET	ASP
19	ASP	SER	ARG	ASN	ASN	GLY	GLU	PHE	SER	THR
20	GLN	GLU	ILE	ARG	ALA	TYR	LEU	PRO	LEU	THR
21	LEU	GLY	ASN	HIS	SER	VAL	THR	PRO	TYR	THR
22	ARG	ILE	GLY	LEU	ASP	ARG	TRP	SER	ASN	TRP
23	ASP	TRP	GLN	ASP	ASP	ILE	GLU	ARG	GLU	GLY
24	HIS	ASP	PHE	ASN	ARG	VAL	GLY	LEU	PHE	TYR
25	GLY	TYR	ASP	PHE	GLN	ASN	GLY	LEU	SER	VAL
26	SER	LEU	GLU	TYR	ALA	PHE	GLU	TRP	GLN	ASP
27	HIS	ASP	GLU	GLY	ASP	SER	ASP	LYS	PHE	HIS
28	TYR	ALA	GLY	VAL	GLY	VAL	ASN	TYR	SER	PHE