BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17026

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

Natural source:   Common Name: B. 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):
BtR375: MDKKIVGANAGKVWHALNEA DGISIPELARKVNLSVESTA LAVGWLARENKVVIERKNGL IEIYNEGHFDFSFGLEHHHH HH

Data sets:
Data typeCount
13C chemical shifts334
15N chemical shifts91
1H chemical shifts554
residual dipolar couplings94

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1BtR375_11
2BtR375_21

Entities:

Entity 1, BtR375_1 82 residues - 9220.528 Da.

Residues 75-82 represent a non-native affinity tag

1   METASPLYSLYSILEVALGLYALAASNALA
2   GLYLYSVALTRPHISALALEUASNGLUALA
3   ASPGLYILESERILEPROGLULEUALAARG
4   LYSVALASNLEUSERVALGLUSERTHRALA
5   LEUALAVALGLYTRPLEUALAARGGLUASN
6   LYSVALVALILEGLUARGLYSASNGLYLEU
7   ILEGLUILETYRASNGLUGLYHISPHEASP
8   PHESERPHEGLYLEUGLUHISHISHISHIS
9   HISHIS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticNCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYNCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D HCCH-COSY aliphaticNCisotropicsample_conditions_1
3D HCCH-COSY aromaticNCisotropicsample_conditions_1
3D HCCH-TOCSY aliphaticNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC methylNC5isotropicsample_conditions_1
2D J-modulation 1H-15N HSQCNC5isotropicsample_conditions_1
2D J-modulation 1H-15N HSQCNC5_PEGanisotropicsample_conditions_1
2D J-modulation 1H-15N HSQCNC5_PAAGanisotropicsample_conditions_1
2D 1H-15N LR-HSQC for HistidineNCisotropicsample_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

Related Database Links:

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

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts