BMRB Entry 18898

Title:
Backbone and side-chain assignments of a tethered complex between LMO4 and DEAF-1
Deposition date:
2012-12-13
Original release date:
2013-02-21
Authors:
Joseph, Soumya; Kwan, Ann; Mackay, Joel; Cubeddu, Liza; Matthews, Jacqueline
Citation:

Citation: Joseph, Soumya; Kwan, Ann; Mackay, Joel; Cubeddu, Liza; Matthews, Jacqueline. "Backbone and side-chain assignments of a tethered complex between LMO4 and DEAF-1."  Biomol. NMR Assignments ., .-. (2013).
PubMed: 23417771

Assembly members:

Assembly members:
LMO4-DEAF-1, polymer, 96 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-2T

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts354
15N chemical shifts103
1H chemical shifts608

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LMO4-DEAF-1 tethered complex1
2Zn2+, 12
3Zn2+, 22

Entities:

Entity 1, LMO4-DEAF-1 tethered complex 96 residues - Formula weight is not available

G1 and S2 are non-native residues that remain from thrombin cleavage of the affinity tag. Residues Y3-N73 correspond to murine LMO4 residues 77-147. Residues G74-S81 correspond to a synthetic G/S linker peptide. Residues I82-K96 corresond to murine DEAF1 residues 404-418.

1   GLYSERTYRILEARGLEUPHEGLYASNSER
2   GLYALACYSSERALACYSGLYGLNSERILE
3   PROALASERGLULEUVALMETARGALAGLN
4   GLYASNVALTYRHISLEULYSCYSPHETHR
5   CYSSERTHRCYSARGASNARGLEUVALPRO
6   GLYASPARGPHEHISTYRILEASNGLYSER
7   LEUPHECYSGLUHISASPARGPROTHRALA
8   LEUILEASNGLYGLYSERGLYGLYSERGLY
9   SERILEALAPROPHEPROGLUALAALALEU
10   PROTHRSERHISPROLYS

Entity 2, Zn2+, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_LMO4-DEAF-1: LMO4-DEAF-1, [U-13C; U-15N], 0.5 ± 0.2 mM; LMO4-DEAF-1, [U-15N], 0.5 ± 0.2 mM; LMO4-DEAF-1 0.5 ± 0.2 mM; sodium acetate 20 ± 1 mM; sodium chloride 35 ± 1 mM; TCEP 1 ± 0.5 mM; H2O 55 ± 1 M; D2O 5 ± 1 M

condition_LMO4-DEAF-1: ionic strength: 0.1 M; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_LMO4-DEAF-1isotropiccondition_LMO4-DEAF-1
2D 1H-13C HSQCsample_LMO4-DEAF-1isotropiccondition_LMO4-DEAF-1
2D 1H-1H TOCSYsample_LMO4-DEAF-1isotropiccondition_LMO4-DEAF-1
2D DQF-COSYsample_LMO4-DEAF-1isotropiccondition_LMO4-DEAF-1
2D 1H-1H NOESYsample_LMO4-DEAF-1isotropiccondition_LMO4-DEAF-1
3D CBCA(CO)NHsample_LMO4-DEAF-1isotropiccondition_LMO4-DEAF-1
3D HNCOsample_LMO4-DEAF-1isotropiccondition_LMO4-DEAF-1
3D HNCACBsample_LMO4-DEAF-1isotropiccondition_LMO4-DEAF-1
3D H(CCO)NHsample_LMO4-DEAF-1isotropiccondition_LMO4-DEAF-1
3D HCCH-TOCSYsample_LMO4-DEAF-1isotropiccondition_LMO4-DEAF-1
3D 1H-15N NOESYsample_LMO4-DEAF-1isotropiccondition_LMO4-DEAF-1
3D 1H-13C NOESY aliphaticsample_LMO4-DEAF-1isotropiccondition_LMO4-DEAF-1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 19415
PDB
DBJ BAC37938 BAE23609 BAE35210 BAF85267 BAF93844
EMBL CAF90424 CAJ82708
GB AAB51073 AAC62958 AAC83789 AAC98510 AAH03488
REF NP_001004922 NP_001009708 NP_001029923 NP_001087890 NP_001106156
SP P61968 P61969 Q3SWZ8 Q6DJ06
TPG DAA31414
AlphaFold P61968 P61969 Q3SWZ8 Q6DJ06

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks