BMRB Entry 17176

Name: Solution NMR structure of the BT_0084 lipoprotein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR376.
Published: 2010-11-05

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PDB ID: 2l3b
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17176
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution NMR structure of the BT_0084 lipoprotein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR376. PubMed: 22116783

Deposition date: 2010-09-10 Original release date: 2010-11-05

Authors: Ramelot, Theresa; Yang, Yunhuang; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Ramelot, Theresa; Yang, Yunhuang; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of BT_0084, a conjugative transposon lipoprotein from Bacteroides thetaiotamicron." Proteins ., .-. (2011).

Assembly members:
BT_0084, polymer, 130 residues, 15166 Da.

Natural source: Common Name: Bacteroides thetaiotaomicron Taxonomy ID: 818 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacteroides thetaiotaomicron

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

Entity Sequences (FASTA):
BT_0084: MNDDVDIQQSYPFSIETMPV PKKLKVGETAEIRCQLHRDG RFEETKYFIRYFQPDGAGTL KMSDGTVLLPNDLYPLPGET FRLYYTSASTDQQTVDVYFQ DSFGQLQQLTFSFNNDSSKE EELEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	546
15N chemical shifts	128
1H chemical shifts	836

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BT_0084 lipoprotein	1

Entities:

Entity 1, BT_0084 lipoprotein 130 residues - 15166 Da.

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

Samples:

NC_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 1.0 ± .05 mM; H2O 95%; D2O 5%

NC_sample_in_D2O: MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± .25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 1.0 ± .05 mM; D2O 100%

NC5_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± .001 %; protein, [U-5% 13C; U-100% 15N], 1.0 ± .05 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC_sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY aliph	NC_sample	isotropic	sample_conditions_1
4D 1H-13C NOESY	NC_sample_in_D2O	isotropic	sample_conditions_1
3D HNCO	NC_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HNCACB	NC_sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC_sample	isotropic	sample_conditions_1
3D HCCH-COSY	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC5_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY arom	NC_sample	isotropic	sample_conditions_1
(H)CCH-TOCSY	NC_sample_in_D2O	isotropic	sample_conditions_1
3D HNCA	NC_sample	isotropic	sample_conditions_1
3D HN(CO)CA	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-15N HSQC NH2 only	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC5_sample	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC_sample	isotropic	sample_conditions_1

Software:

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

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.4, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.25, Schwieters, Kuszewski, Tjandra and Clore - structure solution

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - structure validation

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

PDBStat v5.0, (PDBStat) R. Tejero, G.T. Montelione - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - data analysis

NMR spectrometers:

Varian INOVA 600 MHz
Bruker AvanceIII 850 MHz

UNP	Q8ABM6
SWS	Q8ABM6_BACTN
PDB	2L3B
GB	AAO75191 EKN16719 EXY66436 KFX73674
REF	NP_808997 WP_011107096 WP_028897891 WP_032582694 WP_044245674

Biological Magnetic Resonance Data Bank