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BMRB Entry 15265

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15265
MolProbity Validation Chart

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Title: solution structure of NESG target SsR10, Orf c02003 protein

Deposition date: 2007-05-23 Original release date: 2007-07-18

Authors: Wu, Yibing; Singarapu, Kiran Kumar; Zhang, Qi; Eletski, Alex; Xu, Duanxiang; Sukumaran, Dinesh; Parish, David; Wang, Dongyan; Jiang, Mei; Cunningham, Kellie; Maglaqui, Melissa; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael C.; Swapna, G.V.T; Acton, Thomas B.; Rost, Burkhard; Montelione, Gaetano T.; Szyperski, Thomas

Citation: Wu, Yibing; Singarapu, Kiran Kumar; Zhang, Qi; Eletski, Alex; Xu, Duanxiang; Sukumaran, Dinesh; Parish, David; Wang, Dongyan; Jiang, Mei; Cunningham, Kellie; Maglaqui, Melissa; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael C.; Swapna, G.V.T; Acton, Thomas B.; Rost, Burkhard; Montelione, Gaetano T.; Szyperski, Thomas. "solution structure of NESG target SsR10, Orf c02003 protein"  . ., .-..

Assembly members:
Orf c02003 protein, polymer, 129 residues, 15085.357 Da.

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

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

Entity Sequences (FASTA):
Orf c02003 protein: MSISTSAEVYYEEAEEFLSK GDLVQACEKYYKAAEEAIKL LVIENNLKEITNNVKNKGRW KSENLFKASKLLRSNNTEIP ILWKSAWTLHVEGFHELSLN EKEVKKLKEDVRKLVIFAVN SLEHHHHHH

Data typeCount
13C chemical shifts574
15N chemical shifts141
1H chemical shifts946

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Orf c02003 protein1

Entities:

Entity 1, Orf c02003 protein 129 residues - 15085.357 Da.

1   METSERILESERTHRSERALAGLUVALTYR
2   TYRGLUGLUALAGLUGLUPHELEUSERLYS
3   GLYASPLEUVALGLNALACYSGLULYSTYR
4   TYRLYSALAALAGLUGLUALAILELYSLEU
5   LEUVALILEGLUASNASNLEULYSGLUILE
6   THRASNASNVALLYSASNLYSGLYARGTRP
7   LYSSERGLUASNLEUPHELYSALASERLYS
8   LEULEUARGSERASNASNTHRGLUILEPRO
9   ILELEUTRPLYSSERALATRPTHRLEUHIS
10   VALGLUGLYPHEHISGLULEUSERLEUASN
11   GLULYSGLUVALLYSLYSLEULYSGLUASP
12   VALARGLYSLEUVALILEPHEALAVALASN
13   SERLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: entity 1.1 mM

sample_2: entity 1.0 mM

sample_conditions_1: ionic strength: 100 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
4,3D, GFT HNNCABCAsample_1isotropicsample_conditions_1
4,3D, GFT CABCACONNHsample_1isotropicsample_conditions_1
4,3D, GFT HCCH COSYsample_1isotropicsample_conditions_1
3D, 15N-13C RESOLVEDSIMULTANIOUS NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

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

XEASY, Bartels et al. - data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CAA69481
GB AAK42288 ACX92908 AKA74900 AKA77596 AKA80286
REF WP_009990136

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