BMRB Entry 51821

Title:
Calmodulin bound to a cytosolic domain of the GluN2 subunit of the NMDA Receptor
Deposition date:
2023-02-03
Original release date:
2023-05-23
Authors:
Bej, Aritra; Ames, James
Citation:

Citation: Bej, Aritra; Ames, James. "Chemical shift assignments of calmodulin bound to a cytosolic domain of GluN2A (residues 1004-1024) from the NMDA receptor"  Biomol. NMR Assignments 17, 89-93 (2023).
PubMed: 37029330

Assembly members:

Assembly members:
entity_1, polymer, 149 residues, Formula weight is not available
entity_2, polymer, 20 residues, Formula weight is not available
entity_CA, non-polymer, 40.078 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: pET11b

Data sets:
Data typeCount
13C chemical shifts533
15N chemical shifts141
1H chemical shifts865

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Chain A1
2Chain B2
3Ca ion, 13
4Ca ion, 23
5Ca ion, 33
6Ca ion, 43

Entities:

Entity 1, Chain A 149 residues - Formula weight is not available

1   METALAASPGLNLEUTHRGLUGLUGLNILE
2   ALAGLUPHELYSGLUALAPHESERLEUPHE
3   ASPLYSASPGLYASPGLYTHRILETHRTHR
4   LYSGLULEUGLYTHRVALMETARGSERLEU
5   GLYGLNASNPROTHRGLUALAGLULEUGLN
6   ASPMETILEASNGLUVALASPALAASPGLY
7   ASNGLYTHRILEASPPHEPROGLUPHELEU
8   THRMETMETALAARGLYSMETLYSASPTHR
9   ASPSERGLUGLUGLUILEARGGLUALAPHE
10   ARGVALPHEASPLYSASPGLYASNGLYTYR
11   ILESERALAALAGLULEUARGHISVALMET
12   THRASNLEUGLYGLULYSLEUTHRASPGLU
13   GLUVALASPGLUMETILEARGGLUALAASP
14   ILEASPGLYASPGLYGLNVALASNTYRGLU
15   GLUPHEVALGLNMETMETTHRALALYS

Entity 2, Chain B 20 residues - Formula weight is not available

1   SERLYSALAASNSERARGPROARGGLNLEU
2   TRPLYSLYSSERVALASPSERILEARGGLN

Entity 3, Ca ion, 1 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: Calmodulin, [U-100% 13C; U-100% 15N], 400 uM; GluN2 1 mM; Calcium chloride 1 mM; TRIS, [U-100% 2H], 20 mM

sample_2: Calmodulin, [U-100% 13C; U-100% 15N], 400 uM; GluN2 1 mM; Calcium chloride 1 mM; TRIS, [U-100% 2H], 20 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HDHEsample_1isotropicsample_conditions_1
3D 13C-separated NOESYsample_1isotropicsample_conditions_1
3D 13C-separated NOESYsample_2isotropicsample_conditions_1

Software:

NMRPipe - processing

SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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