BMRB Entry 6658

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6658

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Title:
NMR Solution Structure of a ldb1-LID:Lhx3-LIM complex
Deposition date:
2007-08-03
Original release date:
2005-12-14
Authors:
Lee, Christopher; Nancarrow, Amy; Mackay, Joel; Matthews, Jacqueline
Citation:

Citation: Lee, Christopher; Nancarrow, Amy; Bach, Ingolf; Mackay, Joel; Matthews, Jacqueline. "1H, 15N and 13C Assignments of an Intramolecular Lhx3:ldb1 Complex"  J. Biomol. NMR 33, 198-198 (2005).

Assembly members:

Assembly members:
FLIX3_-_Fusion_of_ldb1-LID_and_Lhx3_LIM_domains, polymer, 182 residues, 20270.156 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: mouse   Taxonomy ID: 10090   Superkingdom: not available   Kingdom: not available   Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FLIX3_-_Fusion_of_ldb1-LID_and_Lhx3_LIM_domains: SSQVPDVMVVGEPTLMGGEF GDEDERLITRLENTQFDAAN GIDDEGGSGGHMGSGGTPEI PMCAGCDQHILDRFILKALD RHWHSKCLKCSDCHVPLAER CFSRGESVYCKDDFFKRFGT KCAACQLGIPPTQVVRRAQD FVYHLHCFACVVCKRQLATG DEFYLMEDSRLVCKADYETA KQ

Data sets:
Data typeCount
13C chemical shifts701
15N chemical shifts183
1H chemical shifts1099

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FLIX3 - Fusion of ldb1-LID and Lhx3 LIM domains1
2ZINC ION_12
3ZINC ION_22
4ZINC ION_32
5ZINC ION_42

Entities:

Entity 1, FLIX3 - Fusion of ldb1-LID and Lhx3 LIM domains 182 residues - 20270.156 Da.

Residues 1-45 represent mouse ldb1 residues 295-339 (Swissprot P70662), residues 46-56 is a linker fusing the two proteins (GGSGGHMGSGG), where the HM is encoded by an NdeI restriction site; and residues 57-182 are from mouse Lhx3 residues 28-153 (Swissprot P50481)

1   SERSERGLNVALPROASPVALMETVALVAL
2   GLYGLUPROTHRLEUMETGLYGLYGLUPHE
3   GLYASPGLUASPGLUARGLEUILETHRARG
4   LEUGLUASNTHRGLNPHEASPALAALAASN
5   GLYILEASPASPGLUGLYGLYSERGLYGLY
6   HISMETGLYSERGLYGLYTHRPROGLUILE
7   PROMETCYSALAGLYCYSASPGLNHISILE
8   LEUASPARGPHEILELEULYSALALEUASP
9   ARGHISTRPHISSERLYSCYSLEULYSCYS
10   SERASPCYSHISVALPROLEUALAGLUARG
11   CYSPHESERARGGLYGLUSERVALTYRCYS
12   LYSASPASPPHEPHELYSARGPHEGLYTHR
13   LYSCYSALAALACYSGLNLEUGLYILEPRO
14   PROTHRGLNVALVALARGARGALAGLNASP
15   PHEVALTYRHISLEUHISCYSPHEALACYS
16   VALVALCYSLYSARGGLNLEUALATHRGLY
17   ASPGLUPHETYRLEUMETGLUASPSERARG
18   LEUVALCYSLYSALAASPTYRGLUTHRALA
19   LYSGLN

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: FLIX3 - Fusion of ldb1-LID and Lhx3 LIM domains, [U-99% 13C; U-99% 15N], 0.75 mM; ZINC ION 3 mM; DSS15 – 30 uM; DTT 1 mM; sodium phosphate 20 mM; sodium chloride 40 mM; D2O, [U-99% 2H], 10%; H2O 90%

sample_3: FLIX3 - Fusion of ldb1-LID and Lhx3 LIM domains 1.2 mM; ZINC ION 4.8 mM; DSS15 – 30 uM; DTT 1 mM; sodium phosphate 20 mM; sodium chloride 40 mM; H2O 90%; D2O, [U-99% 2H], 10%

sample_4: FLIX3 - Fusion of ldb1-LID and Lhx3 LIM domains, [U-10% 13C; U-99% 15N], 0.6 mM; ZINC ION 2.4 mM; DSS15 – 30 uM; DTT 1 mM; sodium phosphate 20 mM; sodium chloride 40 mM; D2O, [U-99% 2H], 90%; H2O 10%

sample_5: FLIX3 - Fusion of ldb1-LID and Lhx3 LIM domains, [U-99% 15N], 0.3 mM; ZINC ION 1.2 mM; DSS15 – 30 uM; DTT 1 mM; sodium phosphate 20 mM; sodium chloride 40 mM; D2O, [U-99% 2H], 90%; H2O 10%

sample_2: FLIX3 - Fusion of ldb1-LID and Lhx3 LIM domains, [U-99% 13C; U-99% 15N], 0.6 mM; ZINC ION 2.4 mM; DSS15 – 30 uM; DTT 1 mM; sodium phosphate 20 mM; sodium chloride 40 mM; D2O, [U-99% 2H], 99%; H2O 1%

sample_conditions_1: ionic strength: 60 mM; pH: 6.8; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
HNCOsample_1isotropicsample_conditions_1
HNCAsample_1isotropicsample_conditions_1
HNCACOsample_1isotropicsample_conditions_1
HNCOCAsample_1isotropicsample_conditions_1
HCCH-TOCSYsample_1isotropicsample_conditions_1
HCCH-COSYsample_1isotropicsample_conditions_1
HNHAsample_1isotropicsample_conditions_1
15N-HSQCsample_1isotropicsample_conditions_1
13C-CT-HSQCsample_1isotropicsample_conditions_1
2D-homonuclear TOCSYsample_1isotropicsample_conditions_1
2D-homonuclear NOESYsample_1isotropicsample_conditions_1
HNCACBsample_1isotropicsample_conditions_1
CBCACONHsample_1isotropicsample_conditions_1
3D 15N-separated NOESYsample_1isotropicsample_conditions_1
3D 13C-separated NOESYsample_1isotropicsample_conditions_1
15N-HSQC (optimised for histidine sidechain J-coupling)sample_1isotropicsample_conditions_1
13C-CT-HSQC (10% 13C sample)sample_1isotropicsample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

ARIA v1.2, Linge, O'Donoghue and Nilges - chemical shift assignment, refinement

SPARKY, Goddard - data analysis, peak picking

TOPSPIN v1.2, Bruker Biospin - collection, processing

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

SWS P50481 P70662

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