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Biological Magnetic Resonance Data Bank


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BMRB Entry 16102

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16102
MolProbity Validation Chart

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Title: Solution NMR Structure of the Integrase-Like Domain from Bacillus cereus Ordered Locus BC_1272. Northeast Structural Genomics Target BcR268F

Deposition date: 2008-12-31 Original release date: 2009-02-19

Authors: Rossi, Paolo; Lee, Hsiau-Wei; Maglaqui, Melissa; Foote, Erica; Buchwald, William; Jiang, Mei; Gurla, Swapna; Nair, Rajesh; Xiao, Rong; Acton, Thomas; Rost, Burkhard; Prestegard, James; Montelione, Gaetano

Citation: Rossi, Paolo; Lee, Hsiau-Wei; Xiao, Rong; Acton, Thomas; Prestegard, James; Montelione, Gaetano. "Solution NMR Structure of the Integrase-Like Domain from Bacillus cereus Ordered Locus BC_1272. Northeast Structural Genomics Target BcR268F"  Not known ., .-..

Assembly members:
BcR268F, polymer, 118 residues, 13570.846 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):
BcR268F: MEPSKLSYGEYLESWFNTKR HSVGIQTAKVLKGYLNSRII PSLGNIKLAKLTSLHMQNYV NSLRDEGLKRGTIEKIIKVI RNSLEHAIDLELITKNVAAK TKLPKADKEELEHHHHHH

Data sets:
Data typeCount
13C chemical shifts511
15N chemical shifts123
1H chemical shifts840

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BcR268F1

Entities:

Entity 1, BcR268F 118 residues - 13570.846 Da.

1   METGLUPROSERLYSLEUSERTYRGLYGLU
2   TYRLEUGLUSERTRPPHEASNTHRLYSARG
3   HISSERVALGLYILEGLNTHRALALYSVAL
4   LEULYSGLYTYRLEUASNSERARGILEILE
5   PROSERLEUGLYASNILELYSLEUALALYS
6   LEUTHRSERLEUHISMETGLNASNTYRVAL
7   ASNSERLEUARGASPGLUGLYLEULYSARG
8   GLYTHRILEGLULYSILEILELYSVALILE
9   ARGASNSERLEUGLUHISALAILEASPLEU
10   GLULEUILETHRLYSASNVALALAALALYS
11   THRLYSLEUPROLYSALAASPLYSGLUGLU
12   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.986 mM; DSS 50 uM; sodium chloride 200 mM; MES 20 mM; DTT 10 mM; NaN3 0.02%; Calcium Chloride 5 mM

sample_2: entity, [5% 13C; U-100% 15N], 0.953 mM; DSS 50 uM; sodium chloride 200 mM; MES 20 mM; DTT 10 mM; NaN3 0.02%; Calcium Chloride 5 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
N15 T1sample_2isotropicsample_conditions_1
N15 T2sample_2isotropicsample_conditions_1
HET noesample_2isotropicsample_conditions_1
N15 trosy isosample_2isotropicsample_conditions_1
N15 trosy PolyAcrylamide Gelsample_2anisotropicsample_conditions_1
2D 1H-13C HSQC stereomethylssample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

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

SPARKY, Goddard - data analysis

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

CYANA v3.0 beta, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS, Bhattacharya and Montelione - validation

Molmol, Koradi, Billeter and Wuthrich - visualization

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

PDBStat v5.1, Tejero, Montelione - refinement

MolProbity, Richardson - processing

NMR spectrometers:

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

Related Database Links:

PDB
GB AAP08256 EEL12452
REF NP_831055 WP_000678909

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