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BMRB Entry 15203

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15203
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Title: NMR Structure of Clostridium Perfringens Protein CPE0013. Northeast Structural Genomics Target CpR31.

Deposition date: 2007-04-04 Original release date: 2007-05-04

Authors: Ding, Keyang; Ramelot, Theresa; Anklin, Clemens; Wang, Huang; Nwosu, Chioma; Cunningham, Kellie; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, Gurla; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael

Citation: Ding, Keyang; Ramelot, Theresa; Wang, Huang; Nwosu, Chioma; Montelione, Gaetano; Kennedy, Michael. "NMR structure of Clostridium perfringens protein CPE0013."  . ., .-..

Assembly members:
CPE0013, polymer, 85 residues, 9683.400 Da.

Natural source:   Common Name: Clostridium perfringens   Taxonomy ID: 1502   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Clostridium perfringens

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

Entity Sequences (FASTA):
CPE0013: MHKDIFTSVVRVRGSKKYNV VPVKSNKPVEISKWIDFSNV LSRLYVGVPTKSGNVVCKNI MNTGVDIICTKNLPKDSLEH HHHHH

Data typeCount
13C chemical shifts347
15N chemical shifts80
1H chemical shifts569

Time Domain Data

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1CPE00131

Entities:

Entity 1, CPE0013 85 residues - 9683.400 Da.

The full sequence is cloned with his-tag LEHHHHHH added at the C-terminal.

1   METHISLYSASPILEPHETHRSERVALVAL
2   ARGVALARGGLYSERLYSLYSTYRASNVAL
3   VALPROVALLYSSERASNLYSPROVALGLU
4   ILESERLYSTRPILEASPPHESERASNVAL
5   LEUSERARGLEUTYRVALGLYVALPROTHR
6   LYSSERGLYASNVALVALCYSLYSASNILE
7   METASNTHRGLYVALASPILEILECYSTHR
8   LYSASNLEUPROLYSASPSERLEUGLUHIS
9   HISHISHISHISHIS

Samples:

sample_1: protein, [U-100% 13C; U-100% 15N], 1 mM; MES 20 mM; NaCl 100 mM; DTT 10 mM; CaCl2 5 mM; NaN3 0.02%; D2O 5%

sample_2: protein, [U-100% 13C; U-100% 15N], 1 mM; MES 20 mM; NaCl 100 mM; DTT 10 mM; CaCl2 5 mM; NaN3 0.02%

sample_3: protein, [U-5% 13C; U-100% 15N], 1 mM; MES 20 mM; NaCl 100 mM; DTT 10 mM; CaCl2 5 mM; NaN3 0.02%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

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

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

AutoStruct, Huang, Swapana, Rajan, Ke, Xia, Shukla, Inouye and Montelione - data analysis

SPARKY, Goddard - peak picking

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

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ BAB79719
EMBL CUO73046
GB ABG83544 ABG87799 ALG47387 EDS80569 EDT15029
REF WP_003450903

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