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 16146

Title: Backbone resonance assignment of Staphylococcal Enterotoxin H   PubMed: 19888679

Deposition date: 2009-01-29 Original release date: 2009-03-02

Authors: Saline, Maria; Orekhov, Vladislav; Lindkvist-Petersson, Karin; Karlsson, Goran

Citation: Saline, Maria; Orekhov, Vladislav; Lindkvist-Petersson, Karin; Karlsson, B. Goran. "Backbone resonance assignment of Staphylococcal Enterotoxin H."  Biomol. NMR Assignments 4, 1-4 (2010).

Assembly members:
SEH, polymer, 217 residues, 25143.2 Da.

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

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

Entity Sequences (FASTA):
SEH: EDLHDKSELTDLALANAYGQ YNHPFIKENIKSDEISGEKD LIFRNQGDSGNDLRVKFATA DLAQKFKNKNVDIYGASFYY KCEKISENISECLYGGTTLN SEKLAQERVIGANVWVDGIQ KETELIRTNKKNVTLQELDI KIRKILSDKYKIYYKDSEIS KGLIEFDMKTPRDYSFDIYD LKGENDYEIDKIYEDNKTLK SDDISHIDVNLYTKKKV

Data sets:
Data typeCount
13C chemical shifts396
15N chemical shifts207
1H chemical shifts207

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SEH1

Entities:

Entity 1, SEH 217 residues - 25143.2 Da.

1   GLUASPLEUHISASPLYSSERGLULEUTHR
2   ASPLEUALALEUALAASNALATYRGLYGLN
3   TYRASNHISPROPHEILELYSGLUASNILE
4   LYSSERASPGLUILESERGLYGLULYSASP
5   LEUILEPHEARGASNGLNGLYASPSERGLY
6   ASNASPLEUARGVALLYSPHEALATHRALA
7   ASPLEUALAGLNLYSPHELYSASNLYSASN
8   VALASPILETYRGLYALASERPHETYRTYR
9   LYSCYSGLULYSILESERGLUASNILESER
10   GLUCYSLEUTYRGLYGLYTHRTHRLEUASN
11   SERGLULYSLEUALAGLNGLUARGVALILE
12   GLYALAASNVALTRPVALASPGLYILEGLN
13   LYSGLUTHRGLULEUILEARGTHRASNLYS
14   LYSASNVALTHRLEUGLNGLULEUASPILE
15   LYSILEARGLYSILELEUSERASPLYSTYR
16   LYSILETYRTYRLYSASPSERGLUILESER
17   LYSGLYLEUILEGLUPHEASPMETLYSTHR
18   PROARGASPTYRSERPHEASPILETYRASP
19   LEULYSGLYGLUASNASPTYRGLUILEASP
20   LYSILETYRGLUASPASNLYSTHRLEULYS
21   SERASPASPILESERHISILEASPVALASN
22   LEUTYRTHRLYSLYSLYSVAL

Samples:

sample_1: SEH, [U-100% 13C; U-100% 15N; 80% 2H], 0.8 mM; ammonium acetate 300 mM; sodium chloride 150 mM

sample_2: SEH, [U-100% 13C; U-100% 15N], 1.6 mM; TRIS 20 uM; sodium chloride 150 uM

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 313 K

sample_conditions_2: ionic strength: 150 mM; pH: 7.0; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D 1H-15N TOCSYsample_2isotropicsample_conditions_2
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2

Software:

CCPN, CCPN - chemical shift assignment

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

NMR spectrometers:

  • Varian INOVA 900 MHz

Related Database Links:

PDB
DBJ BAB85990 BAB93916
EMBL CAG41819 CAI77676 CAI77677 CDR23430
GB AAA19777 AAQ63188 ABI98810 AII96788 EFB46156
PRF 2023311A
REF WP_000608674 WP_000608675 WP_000608676 WP_047431826
SP P0A0L9 P0A0M0

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