BMRB Entry 15456

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PDB ID: 2juw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15456
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR Solution Structure of homodimer protein SO_2176 from Shewanella oneidensis. Northeast Structural Genomics Consortium Target SoR77.

Deposition date: 2007-09-03 Original release date: 2007-09-17

Authors: Ramelot, Theresa; John, Cort; Wang, Dongyan; Nwosu, Chioma; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael

Citation: Ramelot, Theresa; Cort, John; Montelione, Gaetano; Kennedy, Michael. "NMR Solution Structure of homodimer protein SO_2176 from Shewanella oneidensis. Northeast Structural Genomics Consortium Target SoR77." Not known ., .-..

Assembly members:
protein, polymer, 80 residues, 8930 Da.

Natural source: Common Name: Shewanella oneidensis Taxonomy ID: 70863 Superkingdom: Bacteria Kingdom: not available Genus/species: Shewanella oneidensis

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

Entity Sequences (FASTA):
protein: MAIQSKYSNTQVESLIAEIL VVLEKHKAPTDLSLMALGNC VTHLLERKVPSESRQAVAEQ FAKALAQSVKSNLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	345
15N chemical shifts	86
1H chemical shifts	556

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	proteinA	1
2	proteinB	1

Entities:

Entity 1, proteinA 80 residues - 8930 Da.

homodimer, 8 non-native C-terminal His-tag (LEHHHHHH)

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

Samples:

sample_NC: protein, [U-100% 13C; U-100% 15N], 1 ± 0.1 mM; sodium chloride 100 ± 10 mM; ammonium acetate 20 ± 2 mM; calcium chloride 5 ± 0.5 mM; DTT 10 ± 1 mM; sodium azide 0.02 ± 0.002 %

sample_NC50: protein, [U-100% 13C; U-100% 15N], 0.5 ± 0.05 mM; protein 0.5 ± 0.05 mM; sodium chloride 100 ± 10 mM; ammonium acetate 20 ± 2 mM; calcium chloride 5 ± 0.5 mM; DTT 10 ± 1 mM; sodium azide 0.02 ± 0.002 %

sample_NC5: protein, [U-5% 13C; U-100% 15N], 1 ± 0.1 mM; sodium chloride 100 ± 10 mM; ammonium acetate 20 ± 2 mM; calcium chloride 5 ± 0.5 mM; DTT 10 ± 1 mM; sodium azide 0.02 ± 0.002 %

sample_NC_in_D2O: protein, [U-100% 13C; U-100% 15N], 1 ± 0.1 mM; sodium chloride 100 ± 10 mM; ammonium acetate 20 ± 2 mM; calcium chloride 5 ± 0.5 mM; DTT 10 ± 1 mM; sodium azide 0.02 ± 0.002 %

sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; 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 1H-15N NOESY	sample_NC	isotropic	sample_conditions_1
3D 1H-13C NOESY (aliph)	sample_NC	isotropic	sample_conditions_1
4D 1H-13C NOESY	sample_NC_in_D2O	isotropic	sample_conditions_1
3D HNCO	sample_NC	isotropic	sample_conditions_1
3D HNCACB	sample_NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_NC	isotropic	sample_conditions_1
3D H(CCO)NH	sample_NC50	isotropic	sample_conditions_1
3D C(CO)NH	sample_NC50	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_NC50	isotropic	sample_conditions_1
3D HCCH-COSY	sample_NC	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_NC5	isotropic	sample_conditions_1
2D 1H-15N HSQC (15 min)	sample_NC_in_D2O	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_NC50	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_NC5	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_NC50	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_NC_in_D2O	isotropic	sample_conditions_1
3D 1H-13C NOESY (arom)	sample_NC	isotropic	sample_conditions_1
2D 1H-15N HSQC (30 min)	sample_NC_in_D2O	isotropic	sample_conditions_1
2D 1H-15N HSQC (1 hr)	sample_NC_in_D2O	isotropic	sample_conditions_1
2D 1H-15N HSQC (24 hr)	sample_NC_in_D2O	isotropic	sample_conditions_1

Software:

NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.15.0, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.1, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - structure validation

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMR spectrometers:

Varian INOVA 750 MHz
Varian INOVA 600 MHz

PDB	2JUW 2QTI
GB	AAN55220 ABI39291 ABI43282 ABK48656 ABN62028
REF	NP_717776 WP_006081998 WP_011072212 WP_023268262 WP_055648424
SP	Q8EF26

Biological Magnetic Resonance Data Bank