BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16030

Title: Solution structure of protein BPP2914 from Bordetella parapertussis. Northeast Structural Genomics Consortium target BpR206

Deposition date: 2008-11-14 Original release date: 2009-03-05

Authors: Wu, Yibing; Mills, Jeffrey; Wang, Dongyan; Jiang, Mei; Foote, Erica; Xiao, Rong; Sathyamoorthy, Bharathwaj; Sukumaran, Dinesh; Nair, Rajesh; Everett, John; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas

Citation: Wu, Yibing; Mills, Jeffrey; Wang, Dongyan; Jiang, Mei; Foote, Erica; Xiao, Rong; Sathyamoorthy, Bharathwaj; Sukumaran, Dinesh; Nair, Rajesh; Everett, John; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas. "Solution structure of protein BPP2914 from Bordetella parapertussis. Northeast Structural Genomics Consortium target BpR206"  Not known ., .-..

Assembly members:
BPP, polymer, 115 residues, 13089.824 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
BPP: MQAITERLEAMLAQGTDNML LRFTLGKTYAEHEQFDAALP HLRAALDFDPTYSVAWKWLG KTLQGQGDRAGARQAWESGL AAAQSRGDQQVVKELQVFLR RLAREDALEHHHHHH

Data sets:
Data typeCount
13C chemical shifts376
15N chemical shifts125
1H chemical shifts797

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BPP1

Entities:

Entity 1, BPP 115 residues - 13089.824 Da.

1   METGLNALAILETHRGLUARGLEUGLUALA
2   METLEUALAGLNGLYTHRASPASNMETLEU
3   LEUARGPHETHRLEUGLYLYSTHRTYRALA
4   GLUHISGLUGLNPHEASPALAALALEUPRO
5   HISLEUARGALAALALEUASPPHEASPPRO
6   THRTYRSERVALALATRPLYSTRPLEUGLY
7   LYSTHRLEUGLNGLYGLNGLYASPARGALA
8   GLYALAARGGLNALATRPGLUSERGLYLEU
9   ALAALAALAGLNSERARGGLYASPGLNGLN
10   VALVALLYSGLULEUGLNVALPHELEUARG
11   ARGLEUALAARGGLUASPALALEUGLUHIS
12   HISHISHISHISHIS

Samples:

sample_2: BPP, [U-5% 13C; U-100% 15N], 0.3 mM; H2O 90%; D2O 10%; Ammonium Acetate 20 mM; NaCl 200 mM; CaCl2 5 mM; DTT 10 mM; DSS 50 uM; NaN3 .02%

sample_1: BPP, [U-100% 13C; U-100% 15N], 0.3 mM; H2O 90%; D2O 10%; Ammonium Acetate 20 mM; NaCl 200 mM; CaCl2 5 mM; DTT 10 mM; DSS 50 uM; NaN3 .02%

sample_conditions_1: ionic strength: 0.2 M; pH: 4.5; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
(4,3)D GFT HCCH-COSYsample_2isotropicsample_conditions_1
3D, 15N-13C RESOLVED SIMULTANIOUS NOESYsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

XEASY, Bartels et al. - peak picking

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

PSVS, Bhattacharya and Montelione - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
DBJ BAO69438
EMBL CAE33376 CAE38207 CAE41600 CCJ49952 CCJ52604
GB AEE66689 AIW92849 AIW95226 AJB27345 ALH49899
REF NP_880070 WP_003811313 WP_015039931 WP_029443804 WP_041937430

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