BMRB Entry 19415

Title:
LMO4-LIM2 in complex with DEAF-1 (404-418)
Deposition date:
2013-08-05
Original release date:
2014-02-13
Authors:
Joseph, Soumya; Matthews, Jacqui; Kwan, Ann; Mackay, Joel; Cubeddu, Liza; Foo, Priscilla
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 8, 141-144 (2014).
PubMed: 23417771

Assembly members:

Assembly members:
DIC4, polymer, 96 residues, 10142.522 Da.
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

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
1entity_11
2ZINC ION_12
3ZINC ION_22

Entities:

Entity 1, entity_1 96 residues - 10142.522 Da.

G1-S2 remain as an artefact of cleavage 77-147 LMO4 901-908 artificial G/S linker 404-418 DEAF-1 603-604 ZN2+ of LMO4-LIM2

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

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: DIC4, [U-99% 13C; U-99% 15N], 0.3 – 0.7 mM; acetic acid 20 ± 1 mM; sodium chloride 35 ± 1 mM; DTT 1 ± .1 mM; DSS .067 ± .01 mM

sample_conditions_1: ionic strength: 0.13 M; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 18898
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 Q6DJ06 P61969 Q3SWZ8

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