BMRB Entry 17265

Title:
NMR structure of fusion of CtIP (641-685) to LMO4-LIM1 (18-82)
Deposition date:
2010-10-24
Original release date:
2011-06-07
Authors:
Liew, Chu Wai; Stokes, Philippa; Kwan, Ann; Matthews, Jacqui
Citation:

Citation: Liew, Chu Wai; Kwan, Ann; Stokes, Philippa; Mackay, Joel; Matthews, Jacqueline. "(1)H, (15)N and (13)C assignments of an intramolecular LMO4-LIM1/CtIP complex."  Biomol. NMR Assignments 6, 31-34 (2012).
PubMed: 21643835

Assembly members:

Assembly members:
Fusion_protein, polymer, 123 residues, 13075.729 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts429
15N chemical shifts128
1H chemical shifts758

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Fusion_protein1
2ZINC ION_12
3ZINC ION_22

Entities:

Entity 1, Fusion_protein 123 residues - 13075.729 Da.

Initial GS from protease site not included in deposited NMR structure. LMO4 C52S/C64S mutations.

1   GLYSERSERLEUGLNASNASNGLNASPVAL
2   SERPHEGLUASNILEGLNTRPSERILEASP
3   PROGLYALAASPLEUSERGLNTYRLYSMET
4   ASPVALTHRVALILEASPTHRLYSASPGLY
5   SERGLNSERLYSLEUGLYGLYGLYGLYSER
6   GLYGLYHISMETGLYSERGLYGLYLEUSER
7   TRPLYSARGCYSALAGLYCYSGLYGLYLYS
8   ILEALAASPARGPHELEULEUTYRALAMET
9   ASPSERTYRTRPHISSERARGCYSLEULYS
10   CYSSERSERCYSGLNALAGLNLEUGLYASP
11   ILEGLYTHRSERSERTYRTHRLYSSERGLY
12   METILELEUCYSARGASNASPTYRILEARG
13   LEUPHEGLY

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Fusion protein, [U-15N], 150 uM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_2: Fusion protein, [U-99% 13C; U-99% 15N], 500 uM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_3: Fusion protein, [U-99% 13C; U-99% 15N], 300 uM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM; D2O 10%

sample_4: Fusion protein 500 uM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 6; pressure: 1 atm; temperature: 291 K

sample_conditions_2: ionic strength: 150 mM; pH: 6; pressure: 1 atm; temperature: 281 K

sample_conditions_3: ionic strength: 150 mM; pH: 6; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D CCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
2D 1H-1H TOCSYsample_4isotropicsample_conditions_1

Software:

TOPSPIN v1.1-2.1, Bruker - collection

SPARKY v3.114, Goddard - data analysis

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB

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