BMRB Entry 52386

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52386

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Title:
C-terminal EF-hand (EF34) Domain of a-actinin-1 bound to GluN1-C0
Deposition date:
2024-04-03
Original release date:
2024-09-03
Authors:
Bej, Aritra; Ames, James
Citation:

Citation: Bej, Aritra; Hell, Johannes; Ames, James. "Chemical shift assignments of the alpha-actinin C-terminal EF-hand domain bound to a cytosolic C0 domain of GluN1 (residues 841-865) from the NMDA receptor"  Biomol. NMR Assign. ., .-. (2024).
PubMed: 39207574

Assembly members:

Assembly members:
entity_1, polymer, 90 residues, Formula weight is not available
entity_2, polymer, 25 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   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MDTADQVMASFKILAGDKNY ITMDELRRELPPDQAEYCIA RMAPYTGPDSVPGALDYMSF STALYGESDL
entity_2: KDARRKQMQLAFAAVNVWRK NLQDR

Data sets:
Data typeCount
13C chemical shifts195
15N chemical shifts52
1H chemical shifts323

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ACTN1 EF341
2GluN1-C02

Entities:

Entity 1, ACTN1 EF34 90 residues - Formula weight is not available

Residues 1-21 represent non-native affinity tag and cleavage site

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METASPTHRALAASPGLNVALMETALASER
4   PHELYSILELEUALAGLYASPLYSASNTYR
5   ILETHRMETASPGLULEUARGARGGLULEU
6   PROPROASPGLNALAGLUTYRCYSILEALA
7   ARGMETALAPROTYRTHRGLYPROASPSER
8   VALPROGLYALALEUASPTYRMETSERPHE
9   SERTHRALALEUTYRGLYGLUSERASPLEU

Entity 2, GluN1-C0 25 residues - Formula weight is not available

1   LYSASPALAARGARGLYSGLNMETGLNLEU
2   ALAPHEALAALAVALASNVALTRPARGLYS
3   ASNLEUGLNASPARG

Samples:

sample_1: ACTN1 EF34, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-99% 2H], 20 mM; EDTA, [U-99% 2H], 1 mM; DTT, [U-99% 2H], 1 mM; GluN1-C0 0.75 mM

sample_2: ACTN1 EF34, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-99% 2H], 20 mM; EDTA, [U-99% 2H], 1 mM; DTT, [U-99% 2H], 1 mM; GluN1-C0 0.75 mM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 302 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 HBHANHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D 13C-separated NOESYsample_2isotropicsample_conditions_1
2D 13C-filtered NOESYsample_2isotropicsample_conditions_1
3D 13C-filtered 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