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 15971

Title: SOLUTION STRUCTURE OF THE LSM DOMAIN OF DROSOPHILA MELANOGASTER TRAL (TRAILER HITCH)   PubMed: 18765641

Deposition date: 2008-10-02 Original release date: 2009-03-18

Authors: Tritschler, F.; Coles, M.; Truffault, V.

Citation: Tritschler, F.; Eulalio, A.; Helms, S.; Weichenrieder, O.; Schmidt, S.; Izaurralde, E.; Truffault, V.. "Similar Modes of Interaction Enables Trailer Hitch and Edc3 to Associate with Dcp1 and Me31B in Distinct Protein Complexes"  Mol. Cell. Biol. 28, 6695-6708 (2008).

Assembly members:
DANIO_RERIO_RAP55, polymer, 95 residues, Formula weight is not available

Natural source:   Common Name: Zebra fish   Taxonomy ID: 7955   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Danio rerio

Experimental source:   Production method: recombinant technology   Host organism: CELL-FREE SYNTHESIS

Entity Sequences (FASTA):
DANIO_RERIO_RAP55: GHHHHHHLEDPSGGTPYIGS KISLISKAEIRYEGILYTID TENSTVALAKVRSFGTEDRP TDRPIAPRDETFEYIIFRGS DIKDLTVCEPPKPIM

Data sets:
Data typeCount
13C chemical shifts346
15N chemical shifts80
1H chemical shifts581

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DANIO RERIO RAP551

Entities:

Entity 1, DANIO RERIO RAP55 95 residues - Formula weight is not available

1   GLYHISHISHISHISHISHISLEUGLUASP
2   PROSERGLYGLYTHRPROTYRILEGLYSER
3   LYSILESERLEUILESERLYSALAGLUILE
4   ARGTYRGLUGLYILELEUTYRTHRILEASP
5   THRGLUASNSERTHRVALALALEUALALYS
6   VALARGSERPHEGLYTHRGLUASPARGPRO
7   THRASPARGPROILEALAPROARGASPGLU
8   THRPHEGLUTYRILEILEPHEARGGLYSER
9   ASPILELYSASPLEUTHRVALCYSGLUPRO
10   PROLYSPROILEMET

Samples:

sample_1: DANIO RERIO RAP55, [U-13C; U-15N], 0.8 mM; NACL 100 mM; BIS- TRIS 10 mM; DTT 5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1.0 atm; temperature: 289.0 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-SEPARATED_NOESYsample_1isotropicsample_conditions_1
3D_13C-SEPARATED_NOESYsample_1isotropicsample_conditions_1
HNCOsample_1isotropicsample_conditions_1
HNCACBsample_1isotropicsample_conditions_1
CCCONHsample_1isotropicsample_conditions_1
HCCCONHsample_1isotropicsample_conditions_1
CBCACONHsample_1isotropicsample_conditions_1
HBHACONHsample_1isotropicsample_conditions_1
HCH-TOCSYsample_1isotropicsample_conditions_1
CCH- TOCSYsample_1isotropicsample_conditions_1

Software:

X-PLOR v2.9.4, BRUNGER - refinement

SPARKY, Goddard - structure solution

NMR spectrometers:

  • VARIAN UNITYINOVA 600 MHz

Related Database Links:

PDB
DBJ BAB55259 BAC99045 BAC99046 BAF36055 BAG10232
EMBL CAG31566 CAH93252 CDQ65324 CDQ79842 CDQ84551
GB AAH16842 AAH31521 AAH42251 AAH54659 AAH55387
REF NP_001012796 NP_001029826 NP_001079434 NP_001087507 NP_001107565
SP A0A8M2 Q3MHF8 Q5R4R4 Q6NVR8 Q8AVJ2
TPG DAA19959

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