BMRB Entry 17026

Name: Solution NMR Structure of protein BT2368 from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR375
Published: 2010-08-23

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PDB ID: 2l02
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17026
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of protein BT2368 from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR375

Deposition date:

2010-06-29

Original release date:

2010-08-23

Authors:

Eletsky, Alexander; Lee, Hsiau-Wei; Wang, Dongyan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Eletsky, Alexander; Lee, Hsiau-Wei; Wang, Dongyan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of protein BT2368 from Bacteroides thetaiotaomicron" To be published ., .-..

Assembly members:

Assembly members:
BtR375, polymer, 82 residues, 9220.528 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BtR375: MDKKIVGANAGKVWHALNEA DGISIPELARKVNLSVESTA LAVGWLARENKVVIERKNGL IEIYNEGHFDFSFGLEHHHH HH

Data sets:

RDCs
- PEG
- PAAG
assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- N
- Cali
- Caro

Data type	Count
13C chemical shifts	334
15N chemical shifts	91
1H chemical shifts	554
residual dipolar couplings	94

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BtR375_1	1
2	BtR375_2	1

Entities:

Entity 1, BtR375_1 82 residues - 9220.528 Da.

Residues 75-82 represent a non-native affinity tag

1

MET

ASP

LYS

ILE

VAL

GLY

ALA

ASN

ALA

2

GLY

LYS

VAL

TRP

HIS

ALA

LEU

ASN

GLU

ALA

3

ASP

GLY

ILE

SER

ILE

PRO

GLU

LEU

ALA

ARG

4

LYS

VAL

ASN

LEU

SER

VAL

GLU

SER

THR

ALA

5

LEU

ALA

VAL

GLY

TRP

LEU

ALA

ARG

GLU

ASN

6

LYS

VAL

ILE

GLU

ARG

LYS

ASN

GLY

LEU

7

ILE

GLU

ILE

TYR

ASN

GLU

GLY

HIS

PHE

ASP

8

PHE

SER

PHE

GLY

LEU

GLU

HIS

9

HIS

Samples:

NC5_PAAG: BtR375, [U-5% 13C; U-100% 15N], 1.2 mM; ammonium acetate 18 mM; sodium chloride 91 mM; calcium chloride 4.6 mM; sodium azide 0.018%; H2O 80%; D2O 20%

NC: BtR375, [U-100% 13C; U-100% 15N], 1.1 mM; ammonium acetate 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.02%; H2O 90%; D2O 10%

NC5: BtR375, [U-5% 13C; U-100% 15N], 1.1 mM; ammonium acetate 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.02%; H2O 90%; D2O 10%

NC5_PEG: BtR375, [U-5% 13C; U-100% 15N], 0.9 mM; ammonium acetate 18 mM; sodium chloride 91 mM; calcium chloride 4.6 mM; sodium azide 0.018%; C12E5 polyethylene glycol 4%; hexanol 4%; H2O 80%; D2O 20%

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aliphatic	NC	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC	isotropic	sample_conditions_1
3D HNCACB	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aromatic	NC	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	NC	isotropic	sample_conditions_1
3D HN(CA)CO	NC	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC	isotropic	sample_conditions_1
3D HCCH-COSY aliphatic	NC	isotropic	sample_conditions_1
3D HCCH-COSY aromatic	NC	isotropic	sample_conditions_1
3D HCCH-TOCSY aliphatic	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC methyl	NC5	isotropic	sample_conditions_1
2D J-modulation 1H-15N HSQC	NC5	isotropic	sample_conditions_1
2D J-modulation 1H-15N HSQC	NC5_PEG	anisotropic	sample_conditions_1
2D J-modulation 1H-15N HSQC	NC5_PAAG	anisotropic	sample_conditions_1
2D 1H-15N LR-HSQC for Histidine	NC	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

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

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

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

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

XEASY v1.3.13, Bartels et al. - data analysis

TOPSPIN v2.1, Bruker Biospin - collection, processing

VNMRJ v2.1B, Varian - collection

TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - geometry optimization

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

PROSA v6.4, Guntert - processing

NMR spectrometers:

Bruker Avance 600 MHz
Varian INOVA 600 MHz
Varian INOVA 750 MHz
Varian INOVA 600 MHz

PDB	2L02
EMBL	CDE77590 CUN18104 CUQ04359 CUQ17116
GB	AAO77475 ALJ40308 EES66434 EFI02088 EOS01101
REF	NP_811281 WP_008763800