BMRB Entry 15296

Title:
Chemical assignments of Ca-S100A1 bound to RyRP12
Deposition date:
2007-06-08
Original release date:
2008-06-25
Authors:
Wright, Nathan; Varney, Kristen; Weber, David
Citation:

Citation: Prosser, Benjamin; Wright, Nathan; Hernandez-Ochoa, Erick; Varney, Kristen; Liu, Yewei; Zimmer, Danna; Olojo, R; Weber, David; Schneider, Martin. "S100A1 binds to the calmodulin-binding site of ryanodine receptor and modulates skeletal muscle excitation-contraction coupling"  J. Biol. Chem. 283, 5046-5057 (2008).
PubMed: 18089560

Assembly members:

Assembly members:
S100A1-RyR, polymer, 94 residues, Formula weight is not available
RyRP12, polymer, 12 residues, Formula weight is not available
CA, non-polymer, Formula weight is not available

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET16

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts371
15N chemical shifts89
1H chemical shifts585

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1S100A11
2RyRP122
3CALCIUM ION, 13
4CALCIUM ION, 23
5CALCIUM ION, 33
6CALCIUM ION, 43

Entities:

Entity 1, S100A1 94 residues - Formula weight is not available

1   METGLYSERGLULEUGLUTHRALAMETGLU
2   THRLEUILEASNVALPHEHISALAHISSER
3   GLYLYSGLUGLYASPLYSTYRLYSLEUSER
4   LYSLYSGLULEULYSASPLEULEUGLNTHR
5   GLULEUSERSERPHELEUASPVALGLNLYS
6   ASPALAASPALAVALASPLYSILEMETLYS
7   GLULEUASPGLUASNGLYASPGLYGLUVAL
8   ASPPHEGLNGLUPHEVALVALLEUVALALA
9   ALALEUTHRVALALACYSASNASNPHEPHE
10   TRPGLUASNSER

Entity 2, RyRP12 12 residues - Formula weight is not available

1   LYSLYSALAVALTRPHISLYSLEULEUSER
2   LYSGLN

Entity 3, CALCIUM ION, 1 - Formula weight is not available

1   CA

Samples:

sample_1: S100A1, [U-99% 13C; U-99% 15N], 0.5 – 1.2 mM; RyRP120.35 – 3 mM; D2O 10%; DTT 15 mM; TRIS 15 mM; sodium chloride 15 mM; calcium chloride 10 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.2; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 15N NOESYsample_1isotropicsample_conditions_1
4D 15N, 13C NOESYsample_1isotropicsample_conditions_1
4D 14N, 15N NOESYsample_1isotropicsample_conditions_1
HC(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 16050 4285
PDB
GB AAB20539 AAB53657 EDM00555
REF NP_001007637 XP_006232665
SP P35467
AlphaFold P35467

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