BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 6577

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6577

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Title: Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2   PubMed: 16081655

Deposition date: 2005-04-01 Original release date: 2007-11-07

Authors: Wienk, Hans; Tomaselli, Simona; Bernard, Cedric; Spurio, Roberto; Picone, Delia; Gualerzi, Claudio; Boelens, Rolf

Citation: Wienk, Hans; Tomaselli, Simona; Bernard, Cedric; Spurio, Roberto; Picone, Delia; Gualerzi, Claudio; Boelens, Rolf. "Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2."  Protein Sci. 14, 2461-2468 (2005).

Assembly members:
IF2-C1, polymer, 135 residues, 14797 Da.

Natural source:   Common Name: Geobacillus stearothermophilus   Taxonomy ID: 1422   Superkingdom: Eubacteria   Kingdom: Not applicable   Genus/species: Geobacillus stearothermophilus

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
IF2-C1: NEFELGTRGSSRVDLQEQRS VKTRVSLDDLFEQIKQGEMK ELNLIVKADVQGSVEALVAA LQKIDVEGVRVKIIHAAVGA ITESDISLATASNAIVIGFN VRPDANAKRAAESEKVDIRL HRIIYNVIEEIEAAM

Data sets:
Data typeCount
13C chemical shifts425
15N chemical shifts106
1H chemical shifts699
S2 parameters67
T1 relaxation values70
T2 relaxation values70
coupling constants53
heteronuclear NOE values70

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IF2-C1_polypeptide1

Entities:

Entity 1, IF2-C1_polypeptide 135 residues - 14797 Da.

1   ASNGLUPHEGLULEUGLYTHRARGGLYSER
2   SERARGVALASPLEUGLNGLUGLNARGSER
3   VALLYSTHRARGVALSERLEUASPASPLEU
4   PHEGLUGLNILELYSGLNGLYGLUMETLYS
5   GLULEUASNLEUILEVALLYSALAASPVAL
6   GLNGLYSERVALGLUALALEUVALALAALA
7   LEUGLNLYSILEASPVALGLUGLYVALARG
8   VALLYSILEILEHISALAALAVALGLYALA
9   ILETHRGLUSERASPILESERLEUALATHR
10   ALASERASNALAILEVALILEGLYPHEASN
11   VALARGPROASPALAASNALALYSARGALA
12   ALAGLUSERGLULYSVALASPILEARGLEU
13   HISARGILEILETYRASNVALILEGLUGLU
14   ILEGLUALAALAMET

Samples:

sample_1: IF2-C1, [U-13C; U-15N], 0.5 mM; KPi 20 mM; KCl 200 mM; glycerol, d8, 5%; D2O 5%

conditions_1: pH: 6.4; temperature: 307.4 K

Experiments:

NameSampleSample stateSample conditions
1H15N_HSQCsample_1isotropicconditions_1
1H15N13C_HNCAsample_1isotropicconditions_1
1H15N13C_HNCACBsample_1isotropicconditions_1
1H15N13C_CBCACONHsample_1isotropicconditions_1
1H15N13C_HNCOsample_1isotropicconditions_1
1H15N13C_HNCACOsample_1isotropicconditions_1
1H15N13C_HNHAsample_1isotropicconditions_1
1H15N13C_HBHACONHsample_1isotropicconditions_1
1H15N13C_HcCH-TOCSY_2sample_1isotropicconditions_1
1H15N13C_hCCH-TOCSYsample_1isotropicconditions_1
2D_1H1H-NOESYsample_1isotropicconditions_1
3D_1H15N-NOESY-HSQCsample_1isotropicconditions_1
3D_1H13C-NOESY-HSQCsample_1isotropicconditions_1
1H15N_hetNOEsample_1isotropicconditions_1
1H15N_HSQC_R1sample_1isotropicconditions_1
1H15N_CPMG_R2sample_1isotropicconditions_1

Software:

NMRView v5.0.3, Bruce A. johnson; Merck Research Laboratories - assignment

NMRPipe, Frank Delaglio, NIH, NIDDK - processing

NMR spectrometers:

  • Bruker Avance 900.21 MHz
  • Bruker Avance 700.13 MHz
  • Bruker Avance 600.13 MHz

Related Database Links:

BMRB 7088
PDB
DBJ BAD75548 GAD12201 GAJ59418
EMBL CAA27987
GB ACX78663 ADI27260 ADU93636 AEV18768 AGE21726
REF WP_011230763 WP_013145729 WP_013523417 WP_015374430 WP_020959388
SP P04766 Q5L0I8

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