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 16576

Title: Solution Structure Of Protein BH0266 From Bacillus halodurans. Northeast Structural Genomics Consortium Target BhR97a   PubMed: 21154411

Deposition date: 2009-10-23 Original release date: 2010-01-07

Authors: Wu, Yibing; Eletsky, Alexander; Lee, Dan; Sathyamoorthy, Bharathwaj; Buchwald, William; Hua, Jia; Ciccosanti, Colleen; He, Yunfen; Hamilton, Keith; Acton, T.B.; Xiao, R.; Everett, J.K.; Lee, Hsiau-Wei; Prestegard, Jim; Montelione, G.T.; Szyperski, Thomas

Citation: Barb, Adam; Cort, John; Seetharaman, Jayaraman; Lew, Scott; Lee, Hsiau-Wei; Acton, Thomas; Xiao, Rong; Kennedy, Michael; Tong, Liang; Montelione, Gaetano; Prestegard, James. "Structures of domains I and IV from YbbR are representative of a widely distributed protein family"  Protein Sci. 20, 396-405 (2011).

Assembly members:
BH0266, polymer, 119 residues, 13589.194 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):
BH0266: MPTFDHGNLSLGELELTVLY DEERYDIVEQTETVQVDLEG PRGVLTVFRFARPSYEVFVD LTEAGEGSHTVDVEHRGFPG DLAVTVEPRMARVQLEERQT VSVPVTVEMINLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts358
15N chemical shifts113
1H chemical shifts763

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BH02661

Entities:

Entity 1, BH0266 119 residues - 13589.194 Da.

1   METPROTHRPHEASPHISGLYASNLEUSER
2   LEUGLYGLULEUGLULEUTHRVALLEUTYR
3   ASPGLUGLUARGTYRASPILEVALGLUGLN
4   THRGLUTHRVALGLNVALASPLEUGLUGLY
5   PROARGGLYVALLEUTHRVALPHEARGPHE
6   ALAARGPROSERTYRGLUVALPHEVALASP
7   LEUTHRGLUALAGLYGLUGLYSERHISTHR
8   VALASPVALGLUHISARGGLYPHEPROGLY
9   ASPLEUALAVALTHRVALGLUPROARGMET
10   ALAARGVALGLNLEUGLUGLUARGGLNTHR
11   VALSERVALPROVALTHRVALGLUMETILE
12   ASNLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O 10%

sample_2: entity, [U-5% 13C; U-99% 15N], 1.0 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
simNOESYsample_1isotropicsample_conditions_1

Software:

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

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

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

XEASY, Bartels et al. - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker DMX 800 MHz

Related Database Links:

PDB
DBJ BAB03985
GB KOO36863
REF WP_010896448 WP_053432100

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