BMRB Entry 6689

Title:
1H and 15N Chemical Shift Assignments for N-terminal domain of human centrin 1
Deposition date:
2005-06-15
Original release date:
2006-04-20
Authors:
Yang, Ao; Miron, Simona; Duchambon, Patricia; Assairi, Liliane; Blouquit, Yves; Craescu, Constantin
Citation:

Citation: Yang, Ao; Miron, Simona; Duchambon, Patricia; Assairi, Liliane; Blouquit, Yves; Craescu, Constantin. "The N-terminal domain of human centrin 2 has a closed structure, binds calcium with a very low affinity, and plays a role in the protein self-assembly"  Biochemistry 45, 880-889 (2006).
PubMed: 16411764

Assembly members:

Assembly members:
N-HsCen1, polymer, 97 residues, Formula weight is not available

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

Data sets:
Data typeCount
15N chemical shifts82
1H chemical shifts533

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human centrin 11

Entities:

Entity 1, human centrin 1 97 residues - Formula weight is not available

1   METALASERGLYPHELYSLYSPROSERALA
2   ALASERTHRGLYGLNLYSARGLYSVALALA
3   PROLYSPROGLULEUTHRGLUASPGLNLYS
4   GLNGLUVALARGGLUALAPHEASPLEUPHE
5   ASPVALASPGLYSERGLYTHRILEASPALA
6   LYSGLULEULYSVALALAMETARGALALEU
7   GLYPHEGLUPROARGLYSGLUGLUMETLYS
8   LYSMETILESERGLUVALASPARGGLUGLY
9   THRGLYLYSILESERPHEASNASPPHELEU
10   ALAVALMETTHRGLNLYSMET

Samples:

sample_1: N-HsCen1, [U-15N], 1.0 – 1.3 mM

conditions_1: pH: 6.5; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
Cosy DQFsample_1not availableconditions_1
TOCSYsample_1not availableconditions_1
NOESYsample_1not availableconditions_1
2D (15N-1H) HSQCsample_1not availableconditions_1
3D NOESy-HSQCsample_1not availableconditions_1
TOCSY-HSQCsample_1not availableconditions_1

Software:

No software information available

NMR spectrometers:

  • Varian Unity 500 MHz

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