BMRB Entry 19404

Name: Solution NMR Structure of DE NOVO DESIGNED Top7 Fold Protein Top7m13, Northeast Structural Genomics Consortium (NESG) Target OR33
Published: 2013-11-26

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PDB ID: 2mbl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19404
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of DE NOVO DESIGNED Top7 Fold Protein Top7m13, Northeast Structural Genomics Consortium (NESG) Target OR33

Deposition date:

2013-08-02

Original release date:

2013-11-26

Authors:

Liu, Gaohua; Zanghellini, Alexandre; Chan, Kui; Xiao, Rong; Janjua, Haleema; Kogan, Sam; Maglaqui, Melissa; Ciccosanti, Colleen; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano

Citation:

Citation: Liu, Gaohua; Zanghellini, Alexandre; Chan, Kui; Xiao, Rong; Janjua, Haleema; Kogan, Sam; Maglaqui, Melissa; Ciccosanti, Colleen; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano. "Solution NMR Structure of DE NOVO DESIGNED Top7 Fold Protein Top7m13, Northeast Structural Genomics Consortium (NESG) Target OR33" To be published ., .-..

Assembly members:

Assembly members:
OR33, polymer, 120 residues, 13888.051 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET29b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OR33: MSGKKVEVQVKITCNGKTYE RTYQLYAVRDEELKEKLKKV LNERMDPIKKLGCKRVRISI RVKHSDAAEEKKEAKKFAAI LNKVFAELGYNDSNVTWDGD TVTVEGQLEGVDLEHHHHHH

Data sets:

RDCs
- RDC_list_1
assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	504
15N chemical shifts	110
1H chemical shifts	826
residual dipolar couplings	83

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OR33	1

Entities:

Entity 1, OR33 120 residues - 13888.051 Da.

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

Samples:

sample_NC: OR33, [U-100% 13C; U-100% 15N], 0.69 mM; NaN3 0.02%; NaCl 100 mM; Tris-HCl 10 mM

sample_NC5: OR33, [U-100% 13C; U-100% 15N], 0.69 mM; NaN3 0.02%; NaCl 100 mM; Tris-HCl 10 mM

sample_NC5_RDC: OR33, [U-100% 13C; U-100% 15N], 0.69 mM; NaN3 0.02%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_NC	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_NC	isotropic	sample_conditions_1
3D HNCO	sample_NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_NC	isotropic	sample_conditions_1
3D HNCACB	sample_NC	isotropic	sample_conditions_1
3D 1H-13C arom NOESY	sample_NC	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	sample_NC	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_NC	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_NC5	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_NC5_RDC	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

REDCAT, Valafar, Prestegard - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz
Varian INOVA 600 MHz

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

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