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 15850

Title: Solution NMR Structure of Putative Lipoprotein from Bacillus cereus Ordered Locus BC_2438. Northeast Structural Genomics Target BcR103A.

Authors: Conover, Kenith; Swapna, G.V.T.; Rossi, Paolo; Wang, Dongyan; Janjua, Haleema; Owens, Leah; Xiao, Rong; Liu, Jingfeng; Baran, Michael; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation: Conover, Kenith; Swapna, G.V.T.; Rossi, Paolo; Wang, Dongyan; Janjua, Haleema; Owens, Leah; Xiao, Rong; Liu, Jingfeng; Baran, Michael; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "Solution NMR Structure of Putative Lipoprotein from Bacillus cereus Ordered Locus BC_2438. Northeast Structural Genomics Target BcR103A."  Not known ., .-..

Assembly members:
BcR103A, polymer, 117 residues, 13091.908 Da.

Natural source:   Common Name: Bacillus cereus   Taxonomy ID: 1396   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus cereus

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

Entity Sequences (FASTA):
BcR103A: MERASLNRIGKDVYYMQIKG EGTIEKVDGRNLRNYTLPAY DEDGVKKQITFRSTKKENDH KLNKYAFLRLYVDQDDNSKN EISSIEVKSYEEIQKADLPE KVKDKFTIKLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts436
15N chemical shifts95
1H chemical shifts680

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BcR103A1

Entities:

Entity 1, BcR103A 117 residues - 13091.908 Da.

21 residues lipobox was removed.

1   METGLUARGALASERLEUASNARGILEGLY
2   LYSASPVALTYRTYRMETGLNILELYSGLY
3   GLUGLYTHRILEGLULYSVALASPGLYARG
4   ASNLEUARGASNTYRTHRLEUPROALATYR
5   ASPGLUASPGLYVALLYSLYSGLNILETHR
6   PHEARGSERTHRLYSLYSGLUASNASPHIS
7   LYSLEUASNLYSTYRALAPHELEUARGLEU
8   TYRVALASPGLNASPASPASNSERLYSASN
9   GLUILESERSERILEGLUVALLYSSERTYR
10   GLUGLUILEGLNLYSALAASPLEUPROGLU
11   LYSVALLYSASPLYSPHETHRILELYSLEU
12   GLUHISHISHISHISHISHIS

Samples:

sample_1: BcR103A, [U-100% 13C; U-100% 15N], 0.6 mM; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; MES 20 mM; calcium chloride 5 mM; sodium chloride 100 mM

sample_2: BcR103A, [5% 13C; U-100% 15N], 1.37 mM; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; MES 20 mM; calcium chloride 5 mM; sodium chloride 100 mM

sample_3: BcR103A, [U-100% 13C; U-100% 15N], 0.5 mM; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; MES 20 mM; calcium chloride 5 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY AROsample_1isotropicsample_conditions_1
3D 1H-13C-15N SIM NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC stereosample_2isotropicsample_conditions_1
HETNOEsample_2isotropicsample_conditions_1
slow exch 1H-15N HSQCsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

TOPSPIN v2.1, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - refinement

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

SPARKY v3.113, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - validation

PDBStat v5.1, Tejero R.; Montelione GT - validation

Molmol v2k2, Koradi, Billeter and Wuthrich - visualization

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - validation

MolProbity, Richardson - Validation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
EMBL CGG02256 CJA31281 CJB35032 CJC25384 CJC28010
GB AAP09401 ADH07006 EEL11492 EJR35492 EJR82496
REF NP_832200 WP_000713860 WP_000713863