BMRB Entry 15755

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15755

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Title:
NMR Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a repeat sequence of human Sfi1 (R641-T660)
Deposition date:
2008-05-06
Original release date:
2009-11-20
Authors:
Martinez Sanz, Juan; Assairi, Liliane; Blouquit, Yves; Duchambon, Patricia; Mouawad, Liliane; Craescu, Constantin T.
Citation:

Citation: Martinez-Sanz, Juan; Kateb, Fatiha; Assairi, Liliane; Blouquit, Yves; Bodenhausen, Geoffrey; Abergel, Daniel; Mouawad, Liliane; Craescu, Constantin. "Structure, dynamics and thermodynamics of the human centrin 2/hSfi1 complex."  J. Mol. Biol. 395, 191-204 (2010).
PubMed: 19857500

Assembly members:

Assembly members:
C-HsCen2, polymer, 79 residues, 9234.394 Da.
R17-HsSfi1, polymer, 20 residues, 2381.722 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: PET24A(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
C-HsCen2: TQKMSEKDTKEEILKAFKLF DDDETGKISFKNLKRVAKEL GENLTDEELQEMIDEADRDG DGEVSEQEFLRIMKKTSLY
R17-HsSfi1: RADLHHQHSVLHRALQAWVT

Data sets:
Data typeCount
13C chemical shifts76
15N chemical shifts75
1H chemical shifts508

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-HsCen21
2R17-HsSfi12

Entities:

Entity 1, C-HsCen2 79 residues - 9234.394 Da.

1   THRGLNLYSMETSERGLULYSASPTHRLYS
2   GLUGLUILELEULYSALAPHELYSLEUPHE
3   ASPASPASPGLUTHRGLYLYSILESERPHE
4   LYSASNLEULYSARGVALALALYSGLULEU
5   GLYGLUASNLEUTHRASPGLUGLULEUGLN
6   GLUMETILEASPGLUALAASPARGASPGLY
7   ASPGLYGLUVALSERGLUGLNGLUPHELEU
8   ARGILEMETLYSLYSTHRSERLEUTYR

Entity 2, R17-HsSfi1 20 residues - 2381.722 Da.

1   ARGALAASPLEUHISHISGLNHISSERVAL
2   LEUHISARGALALEUGLNALATRPVALTHR

Samples:

sample_1: C-HsCen2, [U-100% 15N], 1 mM; R17-HsSfi1 1 mM; DEUTERATED TRIS/HCL 20 mM; NACL 200 mM; CACL2 1 mM

sample_2: C-HsCen2, [U-100% 13C; U-100% 15N], 1 mM; R17-HsSfi1 1 mM; DEUTERATED TRIS/HCL 20 mM; NACL 200 mM; CACL2 1 mM

sample_3: C-HsCen2 1 mM; R17-HsSfi1 1 mM; DEUTERATED TRIS/HCL 20 mM; NACL 200 mM; CACL2 1 mM

sample_4: C-HsCen2 1 mM; R17-HsSfi1 1 mM; DEUTERATED TRIS/HCL 20 mM; NACL 200 mM; CACL2 1 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D DQF-COSYsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1

Software:

FELIX v2000.1, Accelrys, inc. - chemical shift assignment, peak picking

DISCOVER v2.98, Accelrys Inc. - data analysis, geometry optimization, refinement

NMR spectrometers:

  • Varian Unity 500 MHz
  • Bruker DRX 800 MHz

Related Database Links:

PDB
GB EPY78459 ERE65656 AAH21576 AAI10815 AAI29927 AAI29946 EAW59980
DBJ BAA25468 BAF85097 BAG11202 BAH11642 BAH13949
REF NP_001007468 NP_001245254 NP_001245255 NP_001245256 NP_055590
SP A8K8P3
AlphaFold A8K8P3

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