BMRB Entry 18562

Name: Backbone and side-chain assignments of an effector membrane localization domain from Vibrio vulnificus MARTX toxin
Published: 2014-02-11

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PDB ID: 2n9w
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18562
MolProbity Validation Chart

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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:

Backbone and side-chain assignments of an effector membrane localization domain from Vibrio vulnificus MARTX toxin

Deposition date:

2012-06-30

Original release date:

2014-02-11

Authors:

Brothers, Michael; Geissler, Brett; Hsiao, Grant; Wilson, Brenda; Satchell, Karla; Rienstra, Chad

Citation:

Citation: Brothers, Michael; Geissler, Brett; Hisao, Grant; Wilson, Brenda; Satchell, Karla; Rienstra, Chad. "Backbone and side-chain assignments of an effector membrane localization domain from Vibrio vulnificus MARTX toxin." Biomol. NMR Assignments ., .-. (2013).
PubMed: 23765285

Assembly members:

Assembly members:
VvMARTX_MLD, polymer, 90 residues, Formula weight is not available

Natural source:

Natural source: Common Name: g-proteobacteria Taxonomy ID: 672 Superkingdom: Bacteria Kingdom: not available Genus/species: Vibrio Vulnificus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VvMARTX_MLD: MGQIFTVQELKERAKVFAKP IGASYQGILDQLDLVHQAKG RDQIAASFELNKKINDYIAE HPTSGRNQALTQLKEQVTSA LGLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	323
15N chemical shifts	73
1H chemical shifts	427

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	VvMARTX MLD	1

Entities:

Entity 1, VvMARTX MLD 90 residues - Formula weight is not available

1	MET	GLY	GLN	ILE	PHE	THR	VAL	GLN	GLU	LEU
2	LYS	GLU	ARG	ALA	LYS	VAL	PHE	ALA	LYS	PRO
3	ILE	GLY	ALA	SER	TYR	GLN	GLY	ILE	LEU	ASP
4	GLN	LEU	ASP	LEU	VAL	HIS	GLN	ALA	LYS	GLY
5	ARG	ASP	GLN	ILE	ALA	ALA	SER	PHE	GLU	LEU
6	ASN	LYS	LYS	ILE	ASN	ASP	TYR	ILE	ALA	GLU
7	HIS	PRO	THR	SER	GLY	ARG	ASN	GLN	ALA	LEU
8	THR	GLN	LEU	LYS	GLU	GLN	VAL	THR	SER	ALA
9	LEU	GLY	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

PDB	4ERR
GB	AIS39496 AIS39497 AIS39498 AIS39499 AIS39500

BMRB Entry 18562

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

1	MET	GLY	GLN	ILE	PHE	THR	VAL	GLN	GLU	LEU
2	LYS	GLU	ARG	ALA	LYS	VAL	PHE	ALA	LYS	PRO
3	ILE	GLY	ALA	SER	TYR	GLN	GLY	ILE	LEU	ASP
4	GLN	LEU	ASP	LEU	VAL	HIS	GLN	ALA	LYS	GLY
5	ARG	ASP	GLN	ILE	ALA	ALA	SER	PHE	GLU	LEU
6	ASN	LYS	LYS	ILE	ASN	ASP	TYR	ILE	ALA	GLU
7	HIS	PRO	THR	SER	GLY	ARG	ASN	GLN	ALA	LEU
8	THR	GLN	LEU	LYS	GLU	GLN	VAL	THR	SER	ALA
9	LEU	GLY	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

1	MET	GLY	GLN	ILE	PHE	THR	VAL	GLN	GLU	LEU
2	LYS	GLU	ARG	ALA	LYS	VAL	PHE	ALA	LYS	PRO
3	ILE	GLY	ALA	SER	TYR	GLN	GLY	ILE	LEU	ASP
4	GLN	LEU	ASP	LEU	VAL	HIS	GLN	ALA	LYS	GLY
5	ARG	ASP	GLN	ILE	ALA	ALA	SER	PHE	GLU	LEU
6	ASN	LYS	LYS	ILE	ASN	ASP	TYR	ILE	ALA	GLU
7	HIS	PRO	THR	SER	GLY	ARG	ASN	GLN	ALA	LEU
8	THR	GLN	LEU	LYS	GLU	GLN	VAL	THR	SER	ALA
9	LEU	GLY	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

1	MET	GLY	GLN	ILE	PHE	THR	VAL	GLN	GLU	LEU
2	LYS	GLU	ARG	ALA	LYS	VAL	PHE	ALA	LYS	PRO
3	ILE	GLY	ALA	SER	TYR	GLN	GLY	ILE	LEU	ASP
4	GLN	LEU	ASP	LEU	VAL	HIS	GLN	ALA	LYS	GLY
5	ARG	ASP	GLN	ILE	ALA	ALA	SER	PHE	GLU	LEU
6	ASN	LYS	LYS	ILE	ASN	ASP	TYR	ILE	ALA	GLU
7	HIS	PRO	THR	SER	GLY	ARG	ASN	GLN	ALA	LEU
8	THR	GLN	LEU	LYS	GLU	GLN	VAL	THR	SER	ALA
9	LEU	GLY	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS