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 15678

Title: Chemical Shift assignment of SeR13 from Staphylococcus Epidermidis, North East Structural Genomics Consortium Target SeR13   PubMed: 20589905

Deposition date: 2008-03-05 Original release date: 2008-03-17

Authors: Lee, Hsiau-Wei; Wylie, Greg; Bansal, Sonal; Wang, Xu; Shastry, Ritu; Jiang, Mei; Cunningham, Kellie; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, GVT; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Prestegard, James

Citation: Lee, Hsiau-Wei; Wylie, Greg; Bansal, Sonal; Wang, Xu; Barb, Adam; Macnaughtan, Megan; Ertekin, Asli; Montelione, Gaetano; Prestegard, James. "Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping."  Protein Sci. 19, 1673-1685 (2010).

Assembly members:
SeR13, polymer, 94 residues, 10138.311 Da.

Natural source:   Common Name: Staphylococcus epidermidis   Taxonomy ID: 1282   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus epidermidis

Experimental source:   Production method: recombinant technology   Host organism: Staphylococcus epidermidis

Entity Sequences (FASTA):
SeR13: MEIIAISETPNHNTMKVSLS EPRQDNSFTTYTAAQEGQPE FINRLFEIEGVKSIFYVLDF ISIDKEDNANWNELLPQIEN TFAKSNLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts345
15N chemical shifts85
1H chemical shifts494
residual dipolar couplings106

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SeR131

Entities:

Entity 1, SeR13 94 residues - 10138.311 Da.

LEHHHHHH are at the C-terminal as part of His-Tag

1   METGLUILEILEALAILESERGLUTHRPRO
2   ASNHISASNTHRMETLYSVALSERLEUSER
3   GLUPROARGGLNASPASNSERPHETHRTHR
4   TYRTHRALAALAGLNGLUGLYGLNPROGLU
5   PHEILEASNARGLEUPHEGLUILEGLUGLY
6   VALLYSSERILEPHETYRVALLEUASPPHE
7   ILESERILEASPLYSGLUASPASNALAASN
8   TRPASNGLULEULEUPROGLNILEGLUASN
9   THRPHEALALYSSERASNLEUGLUHISHIS
10   HISHISHISHIS

Samples:

sample_1: SeR13, [U-100% 13C; U-100% 15N], 1.07 mM; sodium azide 0.2%; DTT 100 mM; CaCl2 5 mM; sodium chloride 100 mM; MES 20 mM

GEL_s: SeR13, [U-100% 13C; U-100% 15N], 0.86 mM; sodium azide 0.2%; DTT 100 mM; CaCl2 5 mM; sodium chloride 100 mM; MES 20 mM; Negative Charged Poly Acrylamide Compressed Gel 7%

Bicelle_s: SeR13, [U-100% 13C; U-100% 15N], 0.60 mM; sodium azide 0.2%; DTT 100 mM; CaCl2 5 mM; sodium chloride 100 mM; MES 20 mM; DMPS/DHPC Mixture 7.5%

sample_conditions_1: ionic strength: 100 mM; 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC-TROSYGEL_sanisotropicsample_conditions_1
2D 1H-15N HSQC-TROSYBicelle_sanisotropicsample_conditions_1

Software:

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

X-PLOR NIH v2.18, Schwieters, Kuszewski, Tjandra and Clore - refinement

SPARKY, Goddard - chemical shift assignment

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

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CDM13704
GB AAO04721 AAW54376 AIR82327 AJP24693 EES36166
REF NP_764679 WP_001831110 WP_002489988 WP_002493609 WP_047500344

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