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 10049

Title: Solution structure of the N-terminal Domain I of mouse transcription elongation factor S-II protein 3

Deposition date: 2006-11-09 Original release date: 2008-08-13

Authors: Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the N-terminal Domain I of mouse transcription elongation factor S-II protein 3"  . ., .-..

Assembly members:
Domain I, polymer, 103 residues, Formula weight is not available

Natural source:   Common Name: mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: cell free synthesis

Entity Sequences (FASTA):
Domain I: GSSGSSGMGLEEELLRIAKK LEKMVSRKKTEGALDLLKKL NSCQMSIQLLQTTRIGVAVN GVRKHCSDKEVVSLAKVLIK NWKRLLDSPRTTKGERESGP SSG

Data sets:
Data typeCount
13C chemical shifts433
15N chemical shifts100
1H chemical shifts715

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Transcription elongation factor S-II protein 31

Entities:

Entity 1, Transcription elongation factor S-II protein 3 103 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETGLYLEU
2   GLUGLUGLULEULEUARGILEALALYSLYS
3   LEUGLULYSMETVALSERARGLYSLYSTHR
4   GLUGLYALALEUASPLEULEULYSLYSLEU
5   ASNSERCYSGLNMETSERILEGLNLEULEU
6   GLNTHRTHRARGILEGLYVALALAVALASN
7   GLYVALARGLYSHISCYSSERASPLYSGLU
8   VALVALSERLEUALALYSVALLEUILELYS
9   ASNTRPLYSARGLEULEUASPSERPROARG
10   THRTHRLYSGLYGLUARGGLUSERGLYPRO
11   SERSERGLY

Samples:

sample_1: Domain I of TFIIS, [U-13C; U-15N], 1 mM; d-Tris-HCl 20 mM; NaCl 200 mM; d-DTT 2 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 220 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1not availablecondition_1
3D 13C-separated NOESYsample_1not availablecondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delagio, F. - processing

NMRView v5.0.4, Jhonson, B.A. - data analysis

Kujira v0.896, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB25037 BAF80886
EMBL CAA11392
GB AAH10807 AAH91180 EDL29944 EDL80805 EPY82437
REF NP_001015008 NP_035672 XP_003504976 XP_007617250
SP P23881

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