BMRB Entry 11203

Title:
Solution structure of the core domain of calcyclin binding protein; siah-interacting protein (SIP)
Deposition date:
2010-07-22
Original release date:
2011-07-21
Authors:
Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.
Citation:

Citation: Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.. "Solution structure of the core domain of calcyclin binding protein; siah-interacting protein (SIP)"  .

Assembly members:

Assembly members:
CS domain, polymer, 127 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: cell free synthesis   Host organism: E. coli - cell free   Vector: p040329-62

Data sets:
Data typeCount
13C chemical shifts565
15N chemical shifts126
1H chemical shifts890

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CS domain1

Entities:

Entity 1, CS domain 127 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYVALVALALA
2   PROILETHRTHRGLYTYRTHRVALLYSILE
3   SERASNTYRGLYTRPASPGLNSERASPLYS
4   PHEVALLYSILETYRILETHRLEUTHRGLY
5   VALHISGLNVALPROTHRGLUASNVALGLN
6   VALHISPHETHRGLUARGSERPHEASPLEU
7   LEUVALLYSASNLEUASNGLYLYSSERTYR
8   SERMETILEVALASNASNLEULEULYSPRO
9   ILESERVALGLUGLYSERSERLYSLYSVAL
10   LYSTHRASPTHRVALLEUILELEUCYSARG
11   LYSLYSVALGLUASNTHRARGTRPASPTYR
12   LEUTHRGLNVALGLULYSGLUCYSLYSGLU
13   LYSSERGLYPROSERSERGLY

Samples:

sample_1: CS domain, [U-13C; U-15N], 0.98 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9296, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Varian INOVA 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